ES2899227T3 - Anticuerpos anti sortilina y métodos de uso de los mismos - Google Patents
Anticuerpos anti sortilina y métodos de uso de los mismos Download PDFInfo
- Publication number
- ES2899227T3 ES2899227T3 ES16777311T ES16777311T ES2899227T3 ES 2899227 T3 ES2899227 T3 ES 2899227T3 ES 16777311 T ES16777311 T ES 16777311T ES 16777311 T ES16777311 T ES 16777311T ES 2899227 T3 ES2899227 T3 ES 2899227T3
- Authority
- ES
- Spain
- Prior art keywords
- sortilin
- seq
- hvr
- amino acid
- antibodies
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 238000000034 method Methods 0.000 title claims description 87
- 230000007423 decrease Effects 0.000 claims abstract description 9
- 241000282414 Homo sapiens Species 0.000 claims description 149
- 150000001413 amino acids Chemical class 0.000 claims description 104
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 57
- 239000012634 fragment Substances 0.000 claims description 46
- 102000005962 receptors Human genes 0.000 claims description 43
- 201000010099 disease Diseases 0.000 claims description 39
- -1 M 2 p 70 Proteins 0.000 claims description 32
- 238000000338 in vitro Methods 0.000 claims description 23
- 150000007523 nucleic acids Chemical class 0.000 claims description 21
- 102000039446 nucleic acids Human genes 0.000 claims description 20
- 108020004707 nucleic acids Proteins 0.000 claims description 20
- 239000013598 vector Substances 0.000 claims description 20
- 208000035475 disorder Diseases 0.000 claims description 18
- 208000014674 injury Diseases 0.000 claims description 11
- 206010012289 Dementia Diseases 0.000 claims description 10
- 239000002253 acid Substances 0.000 claims description 10
- 208000020431 spinal cord injury Diseases 0.000 claims description 9
- 230000006378 damage Effects 0.000 claims description 7
- 208000006011 Stroke Diseases 0.000 claims description 6
- 108060008682 Tumor Necrosis Factor Proteins 0.000 claims description 6
- 150000007513 acids Chemical class 0.000 claims description 6
- 239000000126 substance Substances 0.000 claims description 6
- 229910052717 sulfur Inorganic materials 0.000 claims description 6
- 208000027418 Wounds and injury Diseases 0.000 claims description 5
- 230000001154 acute effect Effects 0.000 claims description 5
- 230000007850 degeneration Effects 0.000 claims description 5
- 230000012010 growth Effects 0.000 claims description 5
- 201000006417 multiple sclerosis Diseases 0.000 claims description 5
- 229910052727 yttrium Inorganic materials 0.000 claims description 5
- 108010065805 Interleukin-12 Proteins 0.000 claims description 4
- 102000013462 Interleukin-12 Human genes 0.000 claims description 4
- 108090001005 Interleukin-6 Proteins 0.000 claims description 4
- 229910052698 phosphorus Inorganic materials 0.000 claims description 4
- 239000002699 waste material Substances 0.000 claims description 4
- 108010071134 CRM197 (non-toxic variant of diphtheria toxin) Proteins 0.000 claims description 3
- 230000003376 axonal effect Effects 0.000 claims description 3
- 230000028709 inflammatory response Effects 0.000 claims description 3
- 229910052796 boron Inorganic materials 0.000 claims description 2
- 150000002500 ions Chemical class 0.000 claims description 2
- 230000001228 trophic effect Effects 0.000 claims description 2
- 230000029663 wound healing Effects 0.000 claims description 2
- 101100208721 Mus musculus Usp5 gene Proteins 0.000 claims 4
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 claims 2
- 239000004308 thiabendazole Substances 0.000 claims 2
- 102100021503 ATP-binding cassette sub-family B member 6 Human genes 0.000 claims 1
- 206010008190 Cerebrovascular accident Diseases 0.000 claims 1
- 235000017274 Diospyros sandwicensis Nutrition 0.000 claims 1
- 101000677883 Homo sapiens ATP-binding cassette sub-family B member 6 Proteins 0.000 claims 1
- 108010002352 Interleukin-1 Proteins 0.000 claims 1
- 241000282838 Lama Species 0.000 claims 1
- 208000003926 Myelitis Diseases 0.000 claims 1
- 239000004268 Sodium erythorbin Substances 0.000 claims 1
- 102100040247 Tumor necrosis factor Human genes 0.000 claims 1
- 230000007845 axonopathy Effects 0.000 claims 1
- 230000004888 barrier function Effects 0.000 claims 1
- 208000026106 cerebrovascular disease Diseases 0.000 claims 1
- 230000035939 shock Effects 0.000 claims 1
- 108010014657 sortilin Proteins 0.000 abstract description 552
- 102100032889 Sortilin Human genes 0.000 abstract description 549
- 108010012809 Progranulins Proteins 0.000 abstract description 219
- 102000019204 Progranulins Human genes 0.000 abstract description 216
- 125000003275 alpha amino acid group Chemical group 0.000 abstract description 215
- 210000004027 cell Anatomy 0.000 abstract description 148
- 101000868139 Homo sapiens Sortilin Proteins 0.000 abstract description 92
- 230000027455 binding Effects 0.000 description 193
- 125000000539 amino acid group Chemical group 0.000 description 184
- 235000001014 amino acid Nutrition 0.000 description 116
- 108010025020 Nerve Growth Factor Proteins 0.000 description 109
- 108090000623 proteins and genes Proteins 0.000 description 108
- 230000003993 interaction Effects 0.000 description 100
- 108090000765 processed proteins & peptides Proteins 0.000 description 87
- 102000004169 proteins and genes Human genes 0.000 description 87
- 239000000427 antigen Substances 0.000 description 84
- 235000018102 proteins Nutrition 0.000 description 84
- 229940024606 amino acid Drugs 0.000 description 83
- 108091007433 antigens Proteins 0.000 description 83
- 102000036639 antigens Human genes 0.000 description 83
- 230000000875 corresponding effect Effects 0.000 description 75
- 102000015336 Nerve Growth Factor Human genes 0.000 description 68
- 229940053128 nerve growth factor Drugs 0.000 description 68
- 102000004196 processed proteins & peptides Human genes 0.000 description 64
- 241000699670 Mus sp. Species 0.000 description 55
- 230000001413 cellular effect Effects 0.000 description 54
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 53
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 53
- 230000014509 gene expression Effects 0.000 description 50
- 108060003951 Immunoglobulin Proteins 0.000 description 47
- 102000018358 immunoglobulin Human genes 0.000 description 47
- 238000011282 treatment Methods 0.000 description 46
- 108020003175 receptors Proteins 0.000 description 42
- 238000006467 substitution reaction Methods 0.000 description 42
- 102000007072 Nerve Growth Factors Human genes 0.000 description 41
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 38
- 102100029470 Apolipoprotein E Human genes 0.000 description 38
- 101710095339 Apolipoprotein E Proteins 0.000 description 38
- 108010013563 Lipoprotein Lipase Proteins 0.000 description 37
- 102100022119 Lipoprotein lipase Human genes 0.000 description 37
- 101800001814 Neurotensin Proteins 0.000 description 37
- 102400001103 Neurotensin Human genes 0.000 description 37
- PCJGZPGTCUMMOT-ISULXFBGSA-N neurotensin Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1NC(=O)CC1)C1=CC=C(O)C=C1 PCJGZPGTCUMMOT-ISULXFBGSA-N 0.000 description 37
- 101710137189 Amyloid-beta A4 protein Proteins 0.000 description 36
- 102100022704 Amyloid-beta precursor protein Human genes 0.000 description 36
- 101710151993 Amyloid-beta precursor protein Proteins 0.000 description 36
- 230000009467 reduction Effects 0.000 description 36
- 238000006722 reduction reaction Methods 0.000 description 36
- 229920001184 polypeptide Polymers 0.000 description 35
- 210000002966 serum Anatomy 0.000 description 35
- 108090000715 Brain-derived neurotrophic factor Proteins 0.000 description 34
- 102000004219 Brain-derived neurotrophic factor Human genes 0.000 description 34
- 229940077737 brain-derived neurotrophic factor Drugs 0.000 description 34
- DZHSAHHDTRWUTF-SIQRNXPUSA-N amyloid-beta polypeptide 42 Chemical compound C([C@@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)NCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(O)=O)[C@@H](C)CC)C(C)C)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C(C)C)C1=CC=CC=C1 DZHSAHHDTRWUTF-SIQRNXPUSA-N 0.000 description 33
- 102100029946 Sialic acid-binding Ig-like lectin 7 Human genes 0.000 description 32
- 101710187830 Tumor necrosis factor receptor superfamily member 1B Proteins 0.000 description 32
- 210000004556 brain Anatomy 0.000 description 31
- 239000002158 endotoxin Substances 0.000 description 30
- 229920006008 lipopolysaccharide Polymers 0.000 description 30
- 238000003556 assay Methods 0.000 description 29
- 108090000099 Neurotrophin-4 Proteins 0.000 description 26
- 102100038955 Proprotein convertase subtilisin/kexin type 9 Human genes 0.000 description 24
- 101710180553 Proprotein convertase subtilisin/kexin type 9 Proteins 0.000 description 24
- 238000004519 manufacturing process Methods 0.000 description 24
- 230000035772 mutation Effects 0.000 description 23
- 230000002829 reductive effect Effects 0.000 description 23
- 101000868164 Mus musculus Sortilin Proteins 0.000 description 22
- 230000000694 effects Effects 0.000 description 22
- 108010071619 Apolipoproteins Proteins 0.000 description 21
- 102000007592 Apolipoproteins Human genes 0.000 description 21
- 230000006870 function Effects 0.000 description 21
- 210000004408 hybridoma Anatomy 0.000 description 21
- 108090000742 Neurotrophin 3 Proteins 0.000 description 20
- 201000011240 Frontotemporal dementia Diseases 0.000 description 19
- 102000004230 Neurotrophin 3 Human genes 0.000 description 19
- 229940032018 neurotrophin 3 Drugs 0.000 description 19
- 230000000770 proinflammatory effect Effects 0.000 description 19
- 238000010494 dissociation reaction Methods 0.000 description 18
- 230000005593 dissociations Effects 0.000 description 18
- 230000004048 modification Effects 0.000 description 18
- 238000012986 modification Methods 0.000 description 18
- 230000015556 catabolic process Effects 0.000 description 17
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 16
- 238000006731 degradation reaction Methods 0.000 description 16
- 230000001965 increasing effect Effects 0.000 description 16
- 210000002569 neuron Anatomy 0.000 description 16
- 208000024827 Alzheimer disease Diseases 0.000 description 15
- 241000699666 Mus <mouse, genus> Species 0.000 description 15
- 238000001727 in vivo Methods 0.000 description 15
- 241001465754 Metazoa Species 0.000 description 14
- 102000003683 Neurotrophin-4 Human genes 0.000 description 14
- 230000030833 cell death Effects 0.000 description 14
- 238000005516 engineering process Methods 0.000 description 14
- 229940097998 neurotrophin 4 Drugs 0.000 description 14
- 108020004414 DNA Proteins 0.000 description 13
- 108010087819 Fc receptors Proteins 0.000 description 13
- 102000009109 Fc receptors Human genes 0.000 description 13
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 13
- 201000004810 Vascular dementia Diseases 0.000 description 13
- 230000003143 atherosclerotic effect Effects 0.000 description 13
- 208000019553 vascular disease Diseases 0.000 description 13
- 102100033857 Neurotrophin-4 Human genes 0.000 description 12
- 230000032683 aging Effects 0.000 description 12
- 230000009286 beneficial effect Effects 0.000 description 12
- 125000003729 nucleotide group Chemical group 0.000 description 12
- 208000024891 symptom Diseases 0.000 description 12
- 238000002965 ELISA Methods 0.000 description 11
- 230000004071 biological effect Effects 0.000 description 11
- 230000012202 endocytosis Effects 0.000 description 11
- 230000005764 inhibitory process Effects 0.000 description 11
- 239000003446 ligand Substances 0.000 description 11
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 11
- 206010010904 Convulsion Diseases 0.000 description 10
- 108060003393 Granulin Proteins 0.000 description 10
- 210000001744 T-lymphocyte Anatomy 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 10
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 10
- 102000017941 granulin Human genes 0.000 description 10
- 239000002773 nucleotide Substances 0.000 description 10
- 230000002265 prevention Effects 0.000 description 10
- 230000032258 transport Effects 0.000 description 10
- 108010001831 LDL receptors Proteins 0.000 description 9
- 206010035226 Plasma cell myeloma Diseases 0.000 description 9
- 208000030886 Traumatic Brain injury Diseases 0.000 description 9
- 102100033725 Tumor necrosis factor receptor superfamily member 16 Human genes 0.000 description 9
- 230000006907 apoptotic process Effects 0.000 description 9
- 238000013459 approach Methods 0.000 description 9
- 230000000903 blocking effect Effects 0.000 description 9
- 239000012636 effector Substances 0.000 description 9
- 239000007924 injection Substances 0.000 description 9
- 238000002347 injection Methods 0.000 description 9
- 239000000203 mixture Substances 0.000 description 9
- 201000000050 myeloid neoplasm Diseases 0.000 description 9
- 238000001543 one-way ANOVA Methods 0.000 description 9
- 102000040430 polynucleotide Human genes 0.000 description 9
- 108091033319 polynucleotide Proteins 0.000 description 9
- 239000002157 polynucleotide Substances 0.000 description 9
- 239000002243 precursor Substances 0.000 description 9
- 235000000346 sugar Nutrition 0.000 description 9
- 210000001519 tissue Anatomy 0.000 description 9
- 230000009529 traumatic brain injury Effects 0.000 description 9
- 102000004190 Enzymes Human genes 0.000 description 8
- 108090000790 Enzymes Proteins 0.000 description 8
- 101000801254 Homo sapiens Tumor necrosis factor receptor superfamily member 16 Proteins 0.000 description 8
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 8
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 8
- 208000032578 Inherited retinal disease Diseases 0.000 description 8
- 102100024640 Low-density lipoprotein receptor Human genes 0.000 description 8
- 241001529936 Murinae Species 0.000 description 8
- 239000002202 Polyethylene glycol Substances 0.000 description 8
- 208000032430 Retinal dystrophy Diseases 0.000 description 8
- 229940088598 enzyme Drugs 0.000 description 8
- 201000006321 fundus dystrophy Diseases 0.000 description 8
- 208000017532 inherited retinal dystrophy Diseases 0.000 description 8
- 238000003780 insertion Methods 0.000 description 8
- 230000037431 insertion Effects 0.000 description 8
- 230000016273 neuron death Effects 0.000 description 8
- 229920001223 polyethylene glycol Polymers 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 208000018737 Parkinson disease Diseases 0.000 description 7
- 206010002026 amyotrophic lateral sclerosis Diseases 0.000 description 7
- 206010003246 arthritis Diseases 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 238000004113 cell culture Methods 0.000 description 7
- 239000003795 chemical substances by application Substances 0.000 description 7
- 125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 7
- 230000001086 cytosolic effect Effects 0.000 description 7
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 7
- 230000004927 fusion Effects 0.000 description 7
- 230000013595 glycosylation Effects 0.000 description 7
- 238000006206 glycosylation reaction Methods 0.000 description 7
- 230000003834 intracellular effect Effects 0.000 description 7
- 238000002823 phage display Methods 0.000 description 7
- 229920000642 polymer Polymers 0.000 description 7
- 238000012545 processing Methods 0.000 description 7
- 230000002035 prolonged effect Effects 0.000 description 7
- 230000004083 survival effect Effects 0.000 description 7
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 7
- YMWUJEATGCHHMB-UHFFFAOYSA-N Dichloromethane Chemical compound ClCCl YMWUJEATGCHHMB-UHFFFAOYSA-N 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 208000001089 Multiple system atrophy Diseases 0.000 description 6
- 238000010162 Tukey test Methods 0.000 description 6
- 239000002671 adjuvant Substances 0.000 description 6
- 239000005557 antagonist Substances 0.000 description 6
- 238000000423 cell based assay Methods 0.000 description 6
- 230000001684 chronic effect Effects 0.000 description 6
- 238000004132 cross linking Methods 0.000 description 6
- 210000001163 endosome Anatomy 0.000 description 6
- 239000013604 expression vector Substances 0.000 description 6
- 230000001900 immune effect Effects 0.000 description 6
- 229940072221 immunoglobulins Drugs 0.000 description 6
- 238000011813 knockout mouse model Methods 0.000 description 6
- 210000004379 membrane Anatomy 0.000 description 6
- 239000012528 membrane Substances 0.000 description 6
- 108010091748 peptide A Proteins 0.000 description 6
- 230000002093 peripheral effect Effects 0.000 description 6
- 210000002381 plasma Anatomy 0.000 description 6
- 230000028327 secretion Effects 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- 230000008733 trauma Effects 0.000 description 6
- 108010090849 Amyloid beta-Peptides Proteins 0.000 description 5
- 102000013455 Amyloid beta-Peptides Human genes 0.000 description 5
- 102100032367 C-C motif chemokine 5 Human genes 0.000 description 5
- 241000588724 Escherichia coli Species 0.000 description 5
- 208000010412 Glaucoma Diseases 0.000 description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 5
- 102100034221 Growth-regulated alpha protein Human genes 0.000 description 5
- 101000797762 Homo sapiens C-C motif chemokine 5 Proteins 0.000 description 5
- 101001069921 Homo sapiens Growth-regulated alpha protein Proteins 0.000 description 5
- 101001027324 Homo sapiens Progranulin Proteins 0.000 description 5
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 5
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 5
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 description 5
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 5
- 101001027325 Mus musculus Progranulin Proteins 0.000 description 5
- 102000007339 Nerve Growth Factor Receptors Human genes 0.000 description 5
- 108010076504 Protein Sorting Signals Proteins 0.000 description 5
- 241000700159 Rattus Species 0.000 description 5
- 101000868166 Rattus norvegicus Sortilin Proteins 0.000 description 5
- 108010033576 Transferrin Receptors Proteins 0.000 description 5
- 102100026144 Transferrin receptor protein 1 Human genes 0.000 description 5
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 5
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 5
- 230000004913 activation Effects 0.000 description 5
- 238000001994 activation Methods 0.000 description 5
- 206010064930 age-related macular degeneration Diseases 0.000 description 5
- 230000004075 alteration Effects 0.000 description 5
- 210000004369 blood Anatomy 0.000 description 5
- 239000008280 blood Substances 0.000 description 5
- 230000008499 blood brain barrier function Effects 0.000 description 5
- 210000001218 blood-brain barrier Anatomy 0.000 description 5
- 210000004899 c-terminal region Anatomy 0.000 description 5
- 239000001913 cellulose Substances 0.000 description 5
- 229920002678 cellulose Polymers 0.000 description 5
- 210000003169 central nervous system Anatomy 0.000 description 5
- 238000012217 deletion Methods 0.000 description 5
- 230000037430 deletion Effects 0.000 description 5
- 230000001419 dependent effect Effects 0.000 description 5
- 238000011161 development Methods 0.000 description 5
- 230000018109 developmental process Effects 0.000 description 5
- 231100000673 dose–response relationship Toxicity 0.000 description 5
- 239000001963 growth medium Substances 0.000 description 5
- 230000002209 hydrophobic effect Effects 0.000 description 5
- 230000003053 immunization Effects 0.000 description 5
- 230000016784 immunoglobulin production Effects 0.000 description 5
- 208000015181 infectious disease Diseases 0.000 description 5
- 238000001802 infusion Methods 0.000 description 5
- 230000002401 inhibitory effect Effects 0.000 description 5
- 230000037041 intracellular level Effects 0.000 description 5
- 125000005647 linker group Chemical group 0.000 description 5
- 210000004698 lymphocyte Anatomy 0.000 description 5
- 208000002780 macular degeneration Diseases 0.000 description 5
- 239000003900 neurotrophic factor Substances 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 238000000159 protein binding assay Methods 0.000 description 5
- 150000008163 sugars Chemical class 0.000 description 5
- 230000001225 therapeutic effect Effects 0.000 description 5
- 108090000672 Annexin A5 Proteins 0.000 description 4
- 102000004121 Annexin A5 Human genes 0.000 description 4
- 102100021943 C-C motif chemokine 2 Human genes 0.000 description 4
- 108010004103 Chylomicrons Proteins 0.000 description 4
- 102000003886 Glycoproteins Human genes 0.000 description 4
- 108090000288 Glycoproteins Proteins 0.000 description 4
- 241000282412 Homo Species 0.000 description 4
- 101000897480 Homo sapiens C-C motif chemokine 2 Proteins 0.000 description 4
- 208000023105 Huntington disease Diseases 0.000 description 4
- 108010091358 Hypoxanthine Phosphoribosyltransferase Proteins 0.000 description 4
- 206010022489 Insulin Resistance Diseases 0.000 description 4
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 4
- 102000004895 Lipoproteins Human genes 0.000 description 4
- 108090001030 Lipoproteins Proteins 0.000 description 4
- 102100029185 Low affinity immunoglobulin gamma Fc region receptor III-B Human genes 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- 241000124008 Mammalia Species 0.000 description 4
- 208000008589 Obesity Diseases 0.000 description 4
- 241000283973 Oryctolagus cuniculus Species 0.000 description 4
- 108020004511 Recombinant DNA Proteins 0.000 description 4
- 201000007737 Retinal degeneration Diseases 0.000 description 4
- 241000283984 Rodentia Species 0.000 description 4
- 150000001720 carbohydrates Chemical class 0.000 description 4
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 4
- 235000010980 cellulose Nutrition 0.000 description 4
- 235000012000 cholesterol Nutrition 0.000 description 4
- 230000001054 cortical effect Effects 0.000 description 4
- 235000018417 cysteine Nutrition 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 210000004602 germ cell Anatomy 0.000 description 4
- 238000002649 immunization Methods 0.000 description 4
- 230000008676 import Effects 0.000 description 4
- 230000001976 improved effect Effects 0.000 description 4
- 230000001939 inductive effect Effects 0.000 description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 4
- 210000000265 leukocyte Anatomy 0.000 description 4
- 210000003712 lysosome Anatomy 0.000 description 4
- 230000001868 lysosomic effect Effects 0.000 description 4
- 210000002540 macrophage Anatomy 0.000 description 4
- 238000013507 mapping Methods 0.000 description 4
- 230000007246 mechanism Effects 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 235000020824 obesity Nutrition 0.000 description 4
- 210000000056 organ Anatomy 0.000 description 4
- 239000002245 particle Substances 0.000 description 4
- 230000007170 pathology Effects 0.000 description 4
- 210000003024 peritoneal macrophage Anatomy 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 201000002212 progressive supranuclear palsy Diseases 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 238000003127 radioimmunoassay Methods 0.000 description 4
- 238000003259 recombinant expression Methods 0.000 description 4
- 230000001105 regulatory effect Effects 0.000 description 4
- 230000004258 retinal degeneration Effects 0.000 description 4
- 230000009885 systemic effect Effects 0.000 description 4
- 230000009261 transgenic effect Effects 0.000 description 4
- 238000013519 translation Methods 0.000 description 4
- 229910052720 vanadium Inorganic materials 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 3
- KZNQNBZMBZJQJO-UHFFFAOYSA-N 1-(2-azaniumylacetyl)pyrrolidine-2-carboxylate Chemical compound NCC(=O)N1CCCC1C(O)=O KZNQNBZMBZJQJO-UHFFFAOYSA-N 0.000 description 3
- 102100027165 Alpha-2-macroglobulin receptor-associated protein Human genes 0.000 description 3
- 239000004475 Arginine Substances 0.000 description 3
- 208000009137 Behcet syndrome Diseases 0.000 description 3
- 108091026890 Coding region Proteins 0.000 description 3
- 206010009900 Colitis ulcerative Diseases 0.000 description 3
- 108091035707 Consensus sequence Proteins 0.000 description 3
- 208000020406 Creutzfeldt Jacob disease Diseases 0.000 description 3
- 208000003407 Creutzfeldt-Jakob Syndrome Diseases 0.000 description 3
- 208000010859 Creutzfeldt-Jakob disease Diseases 0.000 description 3
- 208000011231 Crohn disease Diseases 0.000 description 3
- 206010067889 Dementia with Lewy bodies Diseases 0.000 description 3
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 3
- 208000001860 Eye Infections Diseases 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 102100029098 Hypoxanthine-guanine phosphoribosyltransferase Human genes 0.000 description 3
- 108010073807 IgG Receptors Proteins 0.000 description 3
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 3
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 3
- 208000022559 Inflammatory bowel disease Diseases 0.000 description 3
- 108010001127 Insulin Receptor Proteins 0.000 description 3
- 102100036721 Insulin receptor Human genes 0.000 description 3
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 3
- 201000002832 Lewy body dementia Diseases 0.000 description 3
- 230000004988 N-glycosylation Effects 0.000 description 3
- 206010028980 Neoplasm Diseases 0.000 description 3
- 108010032605 Nerve Growth Factor Receptors Proteins 0.000 description 3
- 230000004989 O-glycosylation Effects 0.000 description 3
- 108010067902 Peptide Library Proteins 0.000 description 3
- 241000288906 Primates Species 0.000 description 3
- 102100021923 Prolow-density lipoprotein receptor-related protein 1 Human genes 0.000 description 3
- 208000007014 Retinitis pigmentosa Diseases 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 206010040047 Sepsis Diseases 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- 208000009106 Shy-Drager Syndrome Diseases 0.000 description 3
- 102000004584 Somatomedin Receptors Human genes 0.000 description 3
- 108010017622 Somatomedin Receptors Proteins 0.000 description 3
- 102100025639 Sortilin-related receptor Human genes 0.000 description 3
- 102100040347 TAR DNA-binding protein 43 Human genes 0.000 description 3
- 101710150875 TAR DNA-binding protein 43 Proteins 0.000 description 3
- 208000034799 Tauopathies Diseases 0.000 description 3
- 239000004473 Threonine Substances 0.000 description 3
- 206010044565 Tremor Diseases 0.000 description 3
- 201000006704 Ulcerative Colitis Diseases 0.000 description 3
- 108010062497 VLDL Lipoproteins Proteins 0.000 description 3
- 230000002159 abnormal effect Effects 0.000 description 3
- 208000002552 acute disseminated encephalomyelitis Diseases 0.000 description 3
- 238000007792 addition Methods 0.000 description 3
- 235000004279 alanine Nutrition 0.000 description 3
- 238000000540 analysis of variance Methods 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 210000003719 b-lymphocyte Anatomy 0.000 description 3
- 239000000969 carrier Substances 0.000 description 3
- 210000000170 cell membrane Anatomy 0.000 description 3
- 238000012512 characterization method Methods 0.000 description 3
- 239000002738 chelating agent Substances 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 206010009887 colitis Diseases 0.000 description 3
- 229920001577 copolymer Polymers 0.000 description 3
- 210000003618 cortical neuron Anatomy 0.000 description 3
- 239000003431 cross linking reagent Substances 0.000 description 3
- 239000002254 cytotoxic agent Substances 0.000 description 3
- 229940127089 cytotoxic agent Drugs 0.000 description 3
- 231100000599 cytotoxic agent Toxicity 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 230000007812 deficiency Effects 0.000 description 3
- 230000004069 differentiation Effects 0.000 description 3
- 208000011323 eye infectious disease Diseases 0.000 description 3
- 229910052731 fluorine Inorganic materials 0.000 description 3
- 239000003102 growth factor Substances 0.000 description 3
- 230000036541 health Effects 0.000 description 3
- 238000003018 immunoassay Methods 0.000 description 3
- 230000002163 immunogen Effects 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 208000027866 inflammatory disease Diseases 0.000 description 3
- 238000007912 intraperitoneal administration Methods 0.000 description 3
- 238000006317 isomerization reaction Methods 0.000 description 3
- 230000033001 locomotion Effects 0.000 description 3
- 206010025135 lupus erythematosus Diseases 0.000 description 3
- 201000004792 malaria Diseases 0.000 description 3
- 210000004962 mammalian cell Anatomy 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 208000030159 metabolic disease Diseases 0.000 description 3
- 229910052751 metal Inorganic materials 0.000 description 3
- 239000002184 metal Substances 0.000 description 3
- 150000002739 metals Chemical class 0.000 description 3
- 210000000274 microglia Anatomy 0.000 description 3
- 238000010172 mouse model Methods 0.000 description 3
- 210000000440 neutrophil Anatomy 0.000 description 3
- 201000003077 normal pressure hydrocephalus Diseases 0.000 description 3
- 125000006239 protecting group Chemical group 0.000 description 3
- 230000017854 proteolysis Effects 0.000 description 3
- 201000000306 sarcoidosis Diseases 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 230000011664 signaling Effects 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 230000000451 tissue damage Effects 0.000 description 3
- 231100000827 tissue damage Toxicity 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- GEUFMGZEFYJAEJ-UHFFFAOYSA-N tris(2-methylpropyl)silicon Chemical compound CC(C)C[Si](CC(C)C)CC(C)C GEUFMGZEFYJAEJ-UHFFFAOYSA-N 0.000 description 3
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 3
- 230000003966 vascular damage Effects 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- IVNJKQPHHPMONX-WCCKRBBISA-N 2-aminoacetic acid;(2s)-2-amino-5-(diaminomethylideneamino)pentanoic acid Chemical group NCC(O)=O.OC(=O)[C@@H](N)CCCNC(N)=N IVNJKQPHHPMONX-WCCKRBBISA-N 0.000 description 2
- GANZODCWZFAEGN-UHFFFAOYSA-N 5-mercapto-2-nitro-benzoic acid Chemical compound OC(=O)C1=CC(S)=CC=C1[N+]([O-])=O GANZODCWZFAEGN-UHFFFAOYSA-N 0.000 description 2
- 102000016954 ADP-Ribosylation Factors Human genes 0.000 description 2
- 108010053971 ADP-Ribosylation Factors Proteins 0.000 description 2
- 108010085238 Actins Proteins 0.000 description 2
- 102000007469 Actins Human genes 0.000 description 2
- 244000303258 Annona diversifolia Species 0.000 description 2
- 235000002198 Annona diversifolia Nutrition 0.000 description 2
- 102100040197 Apolipoprotein A-V Human genes 0.000 description 2
- 102100032412 Basigin Human genes 0.000 description 2
- 108010064528 Basigin Proteins 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 208000006547 Central Nervous System Lupus Vasculitis Diseases 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 108010016626 Dipeptides Proteins 0.000 description 2
- 101100393884 Drosophila melanogaster Glut1 gene Proteins 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- 108010021468 Fc gamma receptor IIA Proteins 0.000 description 2
- 108010021472 Fc gamma receptor IIB Proteins 0.000 description 2
- 241000724791 Filamentous phage Species 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 102400001369 Heparin-binding EGF-like growth factor Human genes 0.000 description 2
- 101800001649 Heparin-binding EGF-like growth factor Proteins 0.000 description 2
- 108010046315 IDL Lipoproteins Proteins 0.000 description 2
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 2
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 2
- 102000004877 Insulin Human genes 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- 102100037850 Interferon gamma Human genes 0.000 description 2
- 108010074328 Interferon-gamma Proteins 0.000 description 2
- 102000003777 Interleukin-1 beta Human genes 0.000 description 2
- 108090000193 Interleukin-1 beta Proteins 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- 102000036770 Islet Amyloid Polypeptide Human genes 0.000 description 2
- 108010041872 Islet Amyloid Polypeptide Proteins 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- 238000008214 LDL Cholesterol Methods 0.000 description 2
- 108010003718 LDL-Receptor Related Protein-Associated Protein Proteins 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 108010015340 Low Density Lipoprotein Receptor-Related Protein-1 Proteins 0.000 description 2
- 102100029204 Low affinity immunoglobulin gamma Fc region receptor II-a Human genes 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 102000018697 Membrane Proteins Human genes 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 108010006519 Molecular Chaperones Proteins 0.000 description 2
- 102000005431 Molecular Chaperones Human genes 0.000 description 2
- 108091008604 NGF receptors Proteins 0.000 description 2
- 208000036110 Neuroinflammatory disease Diseases 0.000 description 2
- 101800001607 Neuromedin N Proteins 0.000 description 2
- 108090000189 Neuropeptides Proteins 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 239000004372 Polyvinyl alcohol Substances 0.000 description 2
- 102000029797 Prion Human genes 0.000 description 2
- 108091000054 Prion Proteins 0.000 description 2
- 108010057464 Prolactin Proteins 0.000 description 2
- 102000003946 Prolactin Human genes 0.000 description 2
- NBBJYMSMWIIQGU-UHFFFAOYSA-N Propionic aldehyde Chemical compound CCC=O NBBJYMSMWIIQGU-UHFFFAOYSA-N 0.000 description 2
- 206010060862 Prostate cancer Diseases 0.000 description 2
- 208000000236 Prostatic Neoplasms Diseases 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 108010029485 Protein Isoforms Proteins 0.000 description 2
- 102000001708 Protein Isoforms Human genes 0.000 description 2
- 206010057190 Respiratory tract infections Diseases 0.000 description 2
- 101150058068 SLC2A1 gene Proteins 0.000 description 2
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 2
- 101710126735 Sortilin-related receptor Proteins 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 108010000499 Thromboplastin Proteins 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- 102100030859 Tissue factor Human genes 0.000 description 2
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 2
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 2
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 2
- 230000001594 aberrant effect Effects 0.000 description 2
- DZBUGLKDJFMEHC-UHFFFAOYSA-N acridine Chemical compound C1=CC=CC2=CC3=CC=CC=C3N=C21 DZBUGLKDJFMEHC-UHFFFAOYSA-N 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 230000009824 affinity maturation Effects 0.000 description 2
- 239000000556 agonist Substances 0.000 description 2
- 125000000217 alkyl group Chemical group 0.000 description 2
- FPIPGXGPPPQFEQ-OVSJKPMPSA-N all-trans-retinol Chemical compound OC\C=C(/C)\C=C\C=C(/C)\C=C\C1=C(C)CCCC1(C)C FPIPGXGPPPQFEQ-OVSJKPMPSA-N 0.000 description 2
- 102000003802 alpha-Synuclein Human genes 0.000 description 2
- 108090000185 alpha-Synuclein Proteins 0.000 description 2
- 230000009435 amidation Effects 0.000 description 2
- 238000007112 amidation reaction Methods 0.000 description 2
- 210000004102 animal cell Anatomy 0.000 description 2
- 230000003110 anti-inflammatory effect Effects 0.000 description 2
- 238000003782 apoptosis assay Methods 0.000 description 2
- 230000005756 apoptotic signaling Effects 0.000 description 2
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 2
- 210000001130 astrocyte Anatomy 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 210000004227 basal ganglia Anatomy 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 2
- 230000033228 biological regulation Effects 0.000 description 2
- 210000005013 brain tissue Anatomy 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 208000011235 central nervous system lupus Diseases 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- GBVKRUOMSUTVPW-AHNVSIPUSA-N chembl1089636 Chemical compound N([C@H]([C@@H](OC(=O)CCC(=O)N[C@@H](C(O)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)NCC(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CCCCNC(=O)CCC(=O)O[C@H]([C@@H](NC(=O)C=1C=CC=CC=1)C=1C=CC=CC=1)C(=O)O[C@@H]1C(=C2[C@@H](OC(C)=O)C(=O)[C@]3(C)[C@@H](O)C[C@H]4OC[C@]4([C@H]3[C@H](OC(=O)C=3C=CC=CC=3)[C@](C2(C)C)(O)C1)OC(C)=O)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCCNC(=O)CCC(=O)O[C@H]([C@@H](NC(=O)C=1C=CC=CC=1)C=1C=CC=CC=1)C(=O)O[C@@H]1C(=C2[C@@H](OC(C)=O)C(=O)[C@]3(C)[C@@H](O)C[C@H]4OC[C@]4([C@H]3[C@H](OC(=O)C=3C=CC=CC=3)[C@](C2(C)C)(O)C1)OC(C)=O)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)C(=O)O[C@@H]1C(=C2[C@@H](OC(C)=O)C(=O)[C@]3(C)[C@@H](O)C[C@H]4OC[C@]4([C@H]3[C@H](OC(=O)C=3C=CC=CC=3)[C@](C2(C)C)(O)C1)OC(C)=O)C)C=1C=CC=CC=1)C(=O)C1=CC=CC=C1 GBVKRUOMSUTVPW-AHNVSIPUSA-N 0.000 description 2
- 238000012412 chemical coupling Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000002983 circular dichroism Methods 0.000 description 2
- 238000012875 competitive assay Methods 0.000 description 2
- 230000009137 competitive binding Effects 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 230000021615 conjugation Effects 0.000 description 2
- 239000013068 control sample Substances 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 210000004443 dendritic cell Anatomy 0.000 description 2
- 238000001212 derivatisation Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 238000006471 dimerization reaction Methods 0.000 description 2
- 125000002228 disulfide group Chemical group 0.000 description 2
- 150000004662 dithiols Chemical class 0.000 description 2
- VYFYYTLLBUKUHU-UHFFFAOYSA-N dopamine Chemical compound NCCC1=CC=C(O)C(O)=C1 VYFYYTLLBUKUHU-UHFFFAOYSA-N 0.000 description 2
- 239000003937 drug carrier Substances 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 150000002148 esters Chemical class 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 238000013467 fragmentation Methods 0.000 description 2
- 238000006062 fragmentation reaction Methods 0.000 description 2
- 235000021588 free fatty acids Nutrition 0.000 description 2
- 201000000887 hereditary sensory and autonomic neuropathy type 5 Diseases 0.000 description 2
- 229920001519 homopolymer Polymers 0.000 description 2
- 102000054121 human GRN Human genes 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 2
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
- 238000003384 imaging method Methods 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 238000001114 immunoprecipitation Methods 0.000 description 2
- 230000002637 immunotoxin Effects 0.000 description 2
- 239000002596 immunotoxin Substances 0.000 description 2
- 229940051026 immunotoxin Drugs 0.000 description 2
- 231100000608 immunotoxin Toxicity 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 229940125396 insulin Drugs 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 238000000111 isothermal titration calorimetry Methods 0.000 description 2
- 238000005304 joining Methods 0.000 description 2
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 230000020796 long term synaptic depression Effects 0.000 description 2
- 230000004777 loss-of-function mutation Effects 0.000 description 2
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 230000004060 metabolic process Effects 0.000 description 2
- DFTAZNAEBRBBKP-UHFFFAOYSA-N methyl 4-sulfanylbutanimidate Chemical compound COC(=N)CCCS DFTAZNAEBRBBKP-UHFFFAOYSA-N 0.000 description 2
- 210000001616 monocyte Anatomy 0.000 description 2
- DNIAPMSPPWPWGF-UHFFFAOYSA-N monopropylene glycol Natural products CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 210000004165 myocardium Anatomy 0.000 description 2
- 108010068617 neonatal Fc receptor Proteins 0.000 description 2
- 230000001537 neural effect Effects 0.000 description 2
- 208000015122 neurodegenerative disease Diseases 0.000 description 2
- 230000003959 neuroinflammation Effects 0.000 description 2
- 230000006576 neuronal survival Effects 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 238000011275 oncology therapy Methods 0.000 description 2
- 230000001590 oxidative effect Effects 0.000 description 2
- 108010046239 paclitaxel-Angiopep-2 conjugate Proteins 0.000 description 2
- 230000001575 pathological effect Effects 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- MCYTYTUNNNZWOK-LCLOTLQISA-N penetratin Chemical compound C([C@H](NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CCCNC(N)=N)[C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(N)=O)C1=CC=CC=C1 MCYTYTUNNNZWOK-LCLOTLQISA-N 0.000 description 2
- 108010043655 penetratin Proteins 0.000 description 2
- 230000035515 penetration Effects 0.000 description 2
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 108010011110 polyarginine Proteins 0.000 description 2
- 229920001451 polypropylene glycol Polymers 0.000 description 2
- 229920002451 polyvinyl alcohol Polymers 0.000 description 2
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 2
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 2
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 230000000861 pro-apoptotic effect Effects 0.000 description 2
- 230000005522 programmed cell death Effects 0.000 description 2
- 229940097325 prolactin Drugs 0.000 description 2
- 230000001737 promoting effect Effects 0.000 description 2
- XJMOSONTPMZWPB-UHFFFAOYSA-M propidium iodide Chemical compound [I-].[I-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CCC[N+](C)(CC)CC)=C1C1=CC=CC=C1 XJMOSONTPMZWPB-UHFFFAOYSA-M 0.000 description 2
- 229940076372 protein antagonist Drugs 0.000 description 2
- 230000012743 protein tagging Effects 0.000 description 2
- ZCCUUQDIBDJBTK-UHFFFAOYSA-N psoralen Chemical compound C1=C2OC(=O)C=CC2=CC2=C1OC=C2 ZCCUUQDIBDJBTK-UHFFFAOYSA-N 0.000 description 2
- 230000005180 public health Effects 0.000 description 2
- 230000008707 rearrangement Effects 0.000 description 2
- 210000003370 receptor cell Anatomy 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 201000000980 schizophrenia Diseases 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 210000002027 skeletal muscle Anatomy 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 210000000130 stem cell Anatomy 0.000 description 2
- 230000035882 stress Effects 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 230000002889 sympathetic effect Effects 0.000 description 2
- 210000000225 synapse Anatomy 0.000 description 2
- 230000002195 synergetic effect Effects 0.000 description 2
- 108010026424 tau Proteins Proteins 0.000 description 2
- 210000003412 trans-golgi network Anatomy 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 238000010361 transduction Methods 0.000 description 2
- 230000026683 transduction Effects 0.000 description 2
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 2
- 239000003656 tris buffered saline Substances 0.000 description 2
- 229920003169 water-soluble polymer Polymers 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- KYBXNPIASYUWLN-WUCPZUCCSA-N (2s)-5-hydroxypyrrolidine-2-carboxylic acid Chemical compound OC1CC[C@@H](C(O)=O)N1 KYBXNPIASYUWLN-WUCPZUCCSA-N 0.000 description 1
- TZCPCKNHXULUIY-RGULYWFUSA-N 1,2-distearoyl-sn-glycero-3-phosphoserine Chemical compound CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(=O)OC[C@H](N)C(O)=O)OC(=O)CCCCCCCCCCCCCCCCC TZCPCKNHXULUIY-RGULYWFUSA-N 0.000 description 1
- WNXJIVFYUVYPPR-UHFFFAOYSA-N 1,3-dioxolane Chemical compound C1COCO1 WNXJIVFYUVYPPR-UHFFFAOYSA-N 0.000 description 1
- VILCJCGEZXAXTO-UHFFFAOYSA-N 2,2,2-tetramine Chemical compound NCCNCCNCCN VILCJCGEZXAXTO-UHFFFAOYSA-N 0.000 description 1
- FALRKNHUBBKYCC-UHFFFAOYSA-N 2-(chloromethyl)pyridine-3-carbonitrile Chemical compound ClCC1=NC=CC=C1C#N FALRKNHUBBKYCC-UHFFFAOYSA-N 0.000 description 1
- WYMDDFRYORANCC-UHFFFAOYSA-N 2-[[3-[bis(carboxymethyl)amino]-2-hydroxypropyl]-(carboxymethyl)amino]acetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)CN(CC(O)=O)CC(O)=O WYMDDFRYORANCC-UHFFFAOYSA-N 0.000 description 1
- 125000000979 2-amino-2-oxoethyl group Chemical group [H]C([*])([H])C(=O)N([H])[H] 0.000 description 1
- FJACZYDXMHRUJF-WCCKRBBISA-N 2-aminoacetic acid;(2s)-pyrrolidine-2-carboxylic acid Chemical group NCC(O)=O.OC(=O)[C@@H]1CCCN1 FJACZYDXMHRUJF-WCCKRBBISA-N 0.000 description 1
- VXGRJERITKFWPL-UHFFFAOYSA-N 4',5'-Dihydropsoralen Natural products C1=C2OC(=O)C=CC2=CC2=C1OCC2 VXGRJERITKFWPL-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- PQYGLZAKNWQTCV-HNNXBMFYSA-N 4-[N'-(2-hydroxyethyl)thioureido]-L-benzyl EDTA Chemical compound OCCNC(=S)NC1=CC=C(C[C@@H](CN(CC(O)=O)CC(O)=O)N(CC(O)=O)CC(O)=O)C=C1 PQYGLZAKNWQTCV-HNNXBMFYSA-N 0.000 description 1
- PKERXAQSXFSAIU-GVDBMIGSSA-N 4-[[1-[(2S,3S,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-3-yl]triazol-4-yl]methoxy]benzenesulfonamide Chemical compound CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)CO)N3C=C(N=N3)COC4=CC=C(C=C4)S(=O)(=O)N PKERXAQSXFSAIU-GVDBMIGSSA-N 0.000 description 1
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 1
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 1
- 229940117976 5-hydroxylysine Drugs 0.000 description 1
- 108091007504 ADAM10 Proteins 0.000 description 1
- 108010078606 Adipokines Proteins 0.000 description 1
- 102000014777 Adipokines Human genes 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 208000037259 Amyloid Plaque Diseases 0.000 description 1
- 108010043324 Amyloid Precursor Protein Secretases Proteins 0.000 description 1
- 102000002659 Amyloid Precursor Protein Secretases Human genes 0.000 description 1
- 102000000412 Annexin Human genes 0.000 description 1
- 108050008874 Annexin Proteins 0.000 description 1
- 102000005666 Apolipoprotein A-I Human genes 0.000 description 1
- 108010059886 Apolipoprotein A-I Proteins 0.000 description 1
- 108010061118 Apolipoprotein A-V Proteins 0.000 description 1
- 208000002109 Argyria Diseases 0.000 description 1
- 206010003445 Ascites Diseases 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 102000014461 Ataxins Human genes 0.000 description 1
- 108010078286 Ataxins Proteins 0.000 description 1
- 101800001288 Atrial natriuretic factor Proteins 0.000 description 1
- 102400001282 Atrial natriuretic peptide Human genes 0.000 description 1
- 101800001890 Atrial natriuretic peptide Proteins 0.000 description 1
- 101710192393 Attachment protein G3P Proteins 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 102100035080 BDNF/NT-3 growth factors receptor Human genes 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 208000035143 Bacterial infection Diseases 0.000 description 1
- 206010004153 Basal ganglion degeneration Diseases 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 102100021257 Beta-secretase 1 Human genes 0.000 description 1
- ZOXJGFHDIHLPTG-UHFFFAOYSA-N Boron Chemical compound [B] ZOXJGFHDIHLPTG-UHFFFAOYSA-N 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 201000006474 Brain Ischemia Diseases 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 208000026310 Breast neoplasm Diseases 0.000 description 1
- QCMYYKRYFNMIEC-UHFFFAOYSA-N COP(O)=O Chemical class COP(O)=O QCMYYKRYFNMIEC-UHFFFAOYSA-N 0.000 description 1
- 102400000113 Calcitonin Human genes 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 102000000584 Calmodulin Human genes 0.000 description 1
- 108010041952 Calmodulin Proteins 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 101710169873 Capsid protein G8P Proteins 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 208000005623 Carcinogenesis Diseases 0.000 description 1
- 208000024172 Cardiovascular disease Diseases 0.000 description 1
- 206010008120 Cerebral ischaemia Diseases 0.000 description 1
- 108010012236 Chemokines Proteins 0.000 description 1
- 102000019034 Chemokines Human genes 0.000 description 1
- 108010005939 Ciliary Neurotrophic Factor Proteins 0.000 description 1
- 102100031614 Ciliary neurotrophic factor Human genes 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 102000005853 Clathrin Human genes 0.000 description 1
- 108010019874 Clathrin Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 102000015833 Cystatin Human genes 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 102100039673 Disintegrin and metalloproteinase domain-containing protein 10 Human genes 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 102100031375 Endothelial lipase Human genes 0.000 description 1
- 101710087274 Endothelial lipase Proteins 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- VGGSQFUCUMXWEO-UHFFFAOYSA-N Ethene Chemical compound C=C VGGSQFUCUMXWEO-UHFFFAOYSA-N 0.000 description 1
- 239000005977 Ethylene Substances 0.000 description 1
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 1
- 208000009386 Experimental Arthritis Diseases 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 102100035233 Furin Human genes 0.000 description 1
- 108090001126 Furin Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 102000004878 Gelsolin Human genes 0.000 description 1
- 108090001064 Gelsolin Proteins 0.000 description 1
- 241000699694 Gerbillinae Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- ZWZWYGMENQVNFU-UHFFFAOYSA-N Glycerophosphorylserin Natural products OC(=O)C(N)COP(O)(=O)OCC(O)CO ZWZWYGMENQVNFU-UHFFFAOYSA-N 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 1
- 102000009465 Growth Factor Receptors Human genes 0.000 description 1
- 108010009202 Growth Factor Receptors Proteins 0.000 description 1
- 108010010234 HDL Lipoproteins Proteins 0.000 description 1
- 102000015779 HDL Lipoproteins Human genes 0.000 description 1
- 208000031886 HIV Infections Diseases 0.000 description 1
- 208000037357 HIV infectious disease Diseases 0.000 description 1
- 102000019267 Hepatic lipases Human genes 0.000 description 1
- 108050006747 Hepatic lipases Proteins 0.000 description 1
- 102100026122 High affinity immunoglobulin gamma Fc receptor I Human genes 0.000 description 1
- 102100035108 High affinity nerve growth factor receptor Human genes 0.000 description 1
- 101000836956 Homo sapiens Alpha-2-macroglobulin receptor-associated protein Proteins 0.000 description 1
- 101000889974 Homo sapiens Apolipoprotein A-V Proteins 0.000 description 1
- 101000596896 Homo sapiens BDNF/NT-3 growth factors receptor Proteins 0.000 description 1
- 101000894895 Homo sapiens Beta-secretase 1 Proteins 0.000 description 1
- 101000913074 Homo sapiens High affinity immunoglobulin gamma Fc receptor I Proteins 0.000 description 1
- 101000878605 Homo sapiens Low affinity immunoglobulin epsilon Fc receptor Proteins 0.000 description 1
- 101000917826 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor II-a Proteins 0.000 description 1
- 101000917824 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor II-b Proteins 0.000 description 1
- 101000917858 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor III-A Proteins 0.000 description 1
- 101000917839 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor III-B Proteins 0.000 description 1
- 101001043562 Homo sapiens Low-density lipoprotein receptor-related protein 2 Proteins 0.000 description 1
- 101000963759 Homo sapiens Melanocortin-2 receptor accessory protein Proteins 0.000 description 1
- 101000896414 Homo sapiens Nuclear nucleic acid-binding protein C1D Proteins 0.000 description 1
- 101001043564 Homo sapiens Prolow-density lipoprotein receptor-related protein 1 Proteins 0.000 description 1
- 101000836127 Homo sapiens Sortilin-related receptor Proteins 0.000 description 1
- 101000914514 Homo sapiens T-cell-specific surface glycoprotein CD28 Proteins 0.000 description 1
- 102000016252 Huntingtin Human genes 0.000 description 1
- 108050004784 Huntingtin Proteins 0.000 description 1
- 208000035150 Hypercholesterolemia Diseases 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 1
- 102100026120 IgG receptor FcRn large subunit p51 Human genes 0.000 description 1
- 101710177940 IgG receptor FcRn large subunit p51 Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 1
- 102000012745 Immunoglobulin Subunits Human genes 0.000 description 1
- 108010079585 Immunoglobulin Subunits Proteins 0.000 description 1
- 208000004575 Infectious Arthritis Diseases 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 1
- 102000014429 Insulin-like growth factor Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 102100020881 Interleukin-1 alpha Human genes 0.000 description 1
- 102000013691 Interleukin-17 Human genes 0.000 description 1
- 108050003558 Interleukin-17 Proteins 0.000 description 1
- 108010082786 Interleukin-1alpha Proteins 0.000 description 1
- 108090001007 Interleukin-8 Proteins 0.000 description 1
- 206010061246 Intervertebral disc degeneration Diseases 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 102000001851 Low Density Lipoprotein Receptor-Related Protein-1 Human genes 0.000 description 1
- 102100038007 Low affinity immunoglobulin epsilon Fc receptor Human genes 0.000 description 1
- 102100029205 Low affinity immunoglobulin gamma Fc region receptor II-b Human genes 0.000 description 1
- 101710136015 Low-density lipoprotein receptor 1 Proteins 0.000 description 1
- 101710136018 Low-density lipoprotein receptor 2 Proteins 0.000 description 1
- 101710172064 Low-density lipoprotein receptor-related protein Proteins 0.000 description 1
- 102100021922 Low-density lipoprotein receptor-related protein 2 Human genes 0.000 description 1
- 102000009151 Luteinizing Hormone Human genes 0.000 description 1
- 108010073521 Luteinizing Hormone Proteins 0.000 description 1
- 208000015439 Lysosomal storage disease Diseases 0.000 description 1
- 241000282553 Macaca Species 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- 101710156564 Major tail protein Gp23 Proteins 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 102400001156 Medin Human genes 0.000 description 1
- 101800003015 Medin Proteins 0.000 description 1
- 102100040147 Melanocortin-2 receptor accessory protein Human genes 0.000 description 1
- 208000026139 Memory disease Diseases 0.000 description 1
- 102100040243 Microtubule-associated protein tau Human genes 0.000 description 1
- 208000019022 Mood disease Diseases 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101100477979 Mus musculus Sort1 gene Proteins 0.000 description 1
- 241000282339 Mustela Species 0.000 description 1
- OVRNDRQMDRJTHS-CBQIKETKSA-N N-Acetyl-D-Galactosamine Chemical compound CC(=O)N[C@H]1[C@@H](O)O[C@H](CO)[C@H](O)[C@@H]1O OVRNDRQMDRJTHS-CBQIKETKSA-N 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 description 1
- MBLBDJOUHNCFQT-UHFFFAOYSA-N N-acetyl-D-galactosamine Natural products CC(=O)NC(C=O)C(O)C(O)C(O)CO MBLBDJOUHNCFQT-UHFFFAOYSA-N 0.000 description 1
- 102100029166 NT-3 growth factor receptor Human genes 0.000 description 1
- 101150111783 NTRK1 gene Proteins 0.000 description 1
- 241001538234 Nala Species 0.000 description 1
- 206010028851 Necrosis Diseases 0.000 description 1
- 102400001104 Neuromedin N Human genes 0.000 description 1
- 102000003797 Neuropeptides Human genes 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 102000019280 Pancreatic lipases Human genes 0.000 description 1
- 108050006759 Pancreatic lipases Proteins 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical group OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 description 1
- 108010001014 Plasminogen Activators Proteins 0.000 description 1
- 102000001938 Plasminogen Activators Human genes 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 108010071690 Prealbumin Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 102000006437 Proprotein Convertases Human genes 0.000 description 1
- 108010044159 Proprotein Convertases Proteins 0.000 description 1
- 102000003890 RNA-binding protein FUS Human genes 0.000 description 1
- 108090000292 RNA-binding protein FUS Proteins 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 102100030086 Receptor tyrosine-protein kinase erbB-2 Human genes 0.000 description 1
- 101710100968 Receptor tyrosine-protein kinase erbB-2 Proteins 0.000 description 1
- 206010039085 Rhinitis allergic Diseases 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 206010040070 Septic Shock Diseases 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 102000054727 Serum Amyloid A Human genes 0.000 description 1
- 108700028909 Serum Amyloid A Proteins 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- 102100027213 T-cell-specific surface glycoprotein CD28 Human genes 0.000 description 1
- WDLRUFUQRNWCPK-UHFFFAOYSA-N Tetraxetan Chemical compound OC(=O)CN1CCN(CC(O)=O)CCN(CC(O)=O)CCN(CC(O)=O)CC1 WDLRUFUQRNWCPK-UHFFFAOYSA-N 0.000 description 1
- RYYWUUFWQRZTIU-UHFFFAOYSA-N Thiophosphoric acid Chemical class OP(O)(S)=O RYYWUUFWQRZTIU-UHFFFAOYSA-N 0.000 description 1
- 108010034949 Thyroglobulin Proteins 0.000 description 1
- 102100033504 Thyroglobulin Human genes 0.000 description 1
- 102100021398 Transforming growth factor-beta-induced protein ig-h3 Human genes 0.000 description 1
- 102000009190 Transthyretin Human genes 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 101710187888 Tumor necrosis factor receptor superfamily member 16 Proteins 0.000 description 1
- 108091005906 Type I transmembrane proteins Proteins 0.000 description 1
- 101150117115 V gene Proteins 0.000 description 1
- 108091034435 VPS10 family Proteins 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- ULHRKLSNHXXJLO-UHFFFAOYSA-L Yo-Pro-1 Chemical compound [I-].[I-].C1=CC=C2C(C=C3N(C4=CC=CC=C4O3)C)=CC=[N+](CCC[N+](C)(C)C)C2=C1 ULHRKLSNHXXJLO-UHFFFAOYSA-L 0.000 description 1
- 125000002015 acyclic group Chemical group 0.000 description 1
- 102000035181 adaptor proteins Human genes 0.000 description 1
- 108091005764 adaptor proteins Proteins 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 239000003329 adenohypophysis hormone Substances 0.000 description 1
- 239000000478 adipokine Substances 0.000 description 1
- 230000004931 aggregating effect Effects 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 238000012867 alanine scanning Methods 0.000 description 1
- 230000001476 alcoholic effect Effects 0.000 description 1
- 125000003342 alkenyl group Chemical group 0.000 description 1
- 239000002168 alkylating agent Substances 0.000 description 1
- 239000011717 all-trans-retinol Substances 0.000 description 1
- 235000019169 all-trans-retinol Nutrition 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- 201000010105 allergic rhinitis Diseases 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
- 229940037003 alum Drugs 0.000 description 1
- 229940059260 amidate Drugs 0.000 description 1
- 150000001412 amines Chemical group 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- PLOPBXQQPZYQFA-AXPWDRQUSA-N amlintide Chemical compound C([C@@H](C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H]1NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CCCCN)CSSC1)[C@@H](C)O)C(C)C)C1=CC=CC=C1 PLOPBXQQPZYQFA-AXPWDRQUSA-N 0.000 description 1
- 108010064539 amyloid beta-protein (1-42) Proteins 0.000 description 1
- 230000000202 analgesic effect Effects 0.000 description 1
- 230000003042 antagnostic effect Effects 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 230000001640 apoptogenic effect Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 208000006673 asthma Diseases 0.000 description 1
- 208000025255 bacterial arthritis Diseases 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 230000003542 behavioural effect Effects 0.000 description 1
- 108010081355 beta 2-Microglobulin Proteins 0.000 description 1
- 102000015736 beta 2-Microglobulin Human genes 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 108700006666 betaIG-H3 Proteins 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 230000009141 biological interaction Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- ZTQSAGDEMFDKMZ-UHFFFAOYSA-N butyric aldehyde Natural products CCCC=O ZTQSAGDEMFDKMZ-UHFFFAOYSA-N 0.000 description 1
- 108091006374 cAMP receptor proteins Proteins 0.000 description 1
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 1
- 229960004015 calcitonin Drugs 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 230000036952 cancer formation Effects 0.000 description 1
- 125000001314 canonical amino-acid group Chemical group 0.000 description 1
- 210000001043 capillary endothelial cell Anatomy 0.000 description 1
- 150000004657 carbamic acid derivatives Chemical class 0.000 description 1
- 125000002837 carbocyclic group Chemical group 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 231100000504 carcinogenesis Toxicity 0.000 description 1
- 230000000747 cardiac effect Effects 0.000 description 1
- NSQLIUXCMFBZME-MPVJKSABSA-N carperitide Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 NSQLIUXCMFBZME-MPVJKSABSA-N 0.000 description 1
- 238000012219 cassette mutagenesis Methods 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 230000009087 cell motility Effects 0.000 description 1
- 230000002032 cellular defenses Effects 0.000 description 1
- 230000007541 cellular toxicity Effects 0.000 description 1
- 230000004700 cellular uptake Effects 0.000 description 1
- 206010008118 cerebral infarction Diseases 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 230000031154 cholesterol homeostasis Effects 0.000 description 1
- 230000010428 chromatin condensation Effects 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000004087 circulation Effects 0.000 description 1
- 229930193282 clathrin Natural products 0.000 description 1
- 230000004186 co-expression Effects 0.000 description 1
- 230000001447 compensatory effect Effects 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 230000024203 complement activation Effects 0.000 description 1
- 239000008139 complexing agent Substances 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 208000029078 coronary artery disease Diseases 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 238000007821 culture assay Methods 0.000 description 1
- 125000000392 cycloalkenyl group Chemical group 0.000 description 1
- 125000000753 cycloalkyl group Chemical group 0.000 description 1
- 108050004038 cystatin Proteins 0.000 description 1
- 230000003436 cytoskeletal effect Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 208000018180 degenerative disc disease Diseases 0.000 description 1
- YSMODUONRAFBET-UHFFFAOYSA-N delta-DL-hydroxylysine Natural products NCC(O)CCC(N)C(O)=O YSMODUONRAFBET-UHFFFAOYSA-N 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 238000010511 deprotection reaction Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 238000000113 differential scanning calorimetry Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 150000002019 disulfides Chemical class 0.000 description 1
- PYZSVQVRHDXQSL-UHFFFAOYSA-N dithianon Chemical compound S1C(C#N)=C(C#N)SC2=C1C(=O)C1=CC=CC=C1C2=O PYZSVQVRHDXQSL-UHFFFAOYSA-N 0.000 description 1
- NAGJZTKCGNOGPW-UHFFFAOYSA-N dithiophosphoric acid Chemical class OP(O)(S)=S NAGJZTKCGNOGPW-UHFFFAOYSA-N 0.000 description 1
- 229960003638 dopamine Drugs 0.000 description 1
- 230000003291 dopaminomimetic effect Effects 0.000 description 1
- 230000002222 downregulating effect Effects 0.000 description 1
- 230000003828 downregulation Effects 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 230000008482 dysregulation Effects 0.000 description 1
- 201000002491 encephalomyelitis Diseases 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- YSMODUONRAFBET-UHNVWZDZSA-N erythro-5-hydroxy-L-lysine Chemical compound NC[C@H](O)CC[C@H](N)C(O)=O YSMODUONRAFBET-UHNVWZDZSA-N 0.000 description 1
- NPUKDXXFDDZOKR-LLVKDONJSA-N etomidate Chemical compound CCOC(=O)C1=CN=CN1[C@H](C)C1=CC=CC=C1 NPUKDXXFDDZOKR-LLVKDONJSA-N 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000005206 flow analysis Methods 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 108091006047 fluorescent proteins Proteins 0.000 description 1
- 102000034287 fluorescent proteins Human genes 0.000 description 1
- 210000005153 frontal cortex Anatomy 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 229930182830 galactose Natural products 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 210000002288 golgi apparatus Anatomy 0.000 description 1
- 230000010005 growth-factor like effect Effects 0.000 description 1
- 239000000833 heterodimer Substances 0.000 description 1
- 230000000971 hippocampal effect Effects 0.000 description 1
- 210000001320 hippocampus Anatomy 0.000 description 1
- 239000000710 homodimer Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 208000033519 human immunodeficiency virus infectious disease Diseases 0.000 description 1
- 229920001477 hydrophilic polymer Polymers 0.000 description 1
- 125000002349 hydroxyamino group Chemical group [H]ON([H])[*] 0.000 description 1
- 238000012872 hydroxylapatite chromatography Methods 0.000 description 1
- 230000002631 hypothermal effect Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 229940124452 immunizing agent Drugs 0.000 description 1
- 229940127121 immunoconjugate Drugs 0.000 description 1
- 230000037449 immunogenic cell death Effects 0.000 description 1
- 108010023260 immunoglobulin Fv Proteins 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000005462 in vivo assay Methods 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 238000005305 interferometry Methods 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 208000021600 intervertebral disc degenerative disease Diseases 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 230000003447 ipsilateral effect Effects 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 208000028867 ischemia Diseases 0.000 description 1
- 238000012933 kinetic analysis Methods 0.000 description 1
- 210000001865 kupffer cell Anatomy 0.000 description 1
- 101150066555 lacZ gene Proteins 0.000 description 1
- 210000001821 langerhans cell Anatomy 0.000 description 1
- 201000010901 lateral sclerosis Diseases 0.000 description 1
- 210000004558 lewy body Anatomy 0.000 description 1
- 238000000670 ligand binding assay Methods 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 230000008604 lipoprotein metabolism Effects 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 230000006738 locomotor deficit Effects 0.000 description 1
- 101150084157 lrp-1 gene Proteins 0.000 description 1
- 229940040129 luteinizing hormone Drugs 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 230000006674 lysosomal degradation Effects 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 150000002671 lyxoses Chemical class 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- FPYJFEHAWHCUMM-UHFFFAOYSA-N maleic anhydride Chemical compound O=C1OC(=O)C=C1 FPYJFEHAWHCUMM-UHFFFAOYSA-N 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 102000006240 membrane receptors Human genes 0.000 description 1
- 108020004084 membrane receptors Proteins 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 230000002025 microglial effect Effects 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 230000000116 mitigating effect Effects 0.000 description 1
- 230000004898 mitochondrial function Effects 0.000 description 1
- 239000003607 modifier Substances 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 150000002759 monoacylglycerols Chemical class 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 1
- 150000002772 monosaccharides Chemical class 0.000 description 1
- 210000002161 motor neuron Anatomy 0.000 description 1
- 208000005264 motor neuron disease Diseases 0.000 description 1
- 238000011201 multiple comparisons test Methods 0.000 description 1
- YIEDSISPYKQADU-UHFFFAOYSA-N n-acetyl-n-[2-methyl-4-[(2-methylphenyl)diazenyl]phenyl]acetamide Chemical compound C1=C(C)C(N(C(C)=O)C(=O)C)=CC=C1N=NC1=CC=CC=C1C YIEDSISPYKQADU-UHFFFAOYSA-N 0.000 description 1
- 230000017074 necrotic cell death Effects 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 210000000653 nervous system Anatomy 0.000 description 1
- 230000004770 neurodegeneration Effects 0.000 description 1
- 230000007472 neurodevelopment Effects 0.000 description 1
- RZMLVIHXZGQADB-YLUGYNJDSA-N neuromedin n Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)[C@@H](N)CCCCN)[C@@H](C)CC)C1=CC=C(O)C=C1 RZMLVIHXZGQADB-YLUGYNJDSA-N 0.000 description 1
- 230000014511 neuron projection development Effects 0.000 description 1
- 230000007996 neuronal plasticity Effects 0.000 description 1
- 230000004112 neuroprotection Effects 0.000 description 1
- 239000002858 neurotransmitter agent Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 238000010606 normalization Methods 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 238000002515 oligonucleotide synthesis Methods 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 201000008482 osteoarthritis Diseases 0.000 description 1
- 210000002997 osteoclast Anatomy 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 229940116369 pancreatic lipase Drugs 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 210000004738 parenchymal cell Anatomy 0.000 description 1
- 230000007310 pathophysiology Effects 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 239000000813 peptide hormone Substances 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 210000001428 peripheral nervous system Anatomy 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 1
- 150000004713 phosphodiesters Chemical class 0.000 description 1
- 230000010399 physical interaction Effects 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 229940127126 plasminogen activator Drugs 0.000 description 1
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
- 229920000191 poly(N-vinyl pyrrolidone) Polymers 0.000 description 1
- 229920001308 poly(aminoacid) Polymers 0.000 description 1
- 229920001583 poly(oxyethylated polyols) Polymers 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 230000006659 positive regulation of apoptotic process Effects 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 230000008741 proinflammatory signaling process Effects 0.000 description 1
- 210000001176 projection neuron Anatomy 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 238000011321 prophylaxis Methods 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 230000004224 protection Effects 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 230000004850 protein–protein interaction Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 210000000449 purkinje cell Anatomy 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 229920005604 random copolymer Polymers 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000004064 recycling Methods 0.000 description 1
- 230000022983 regulation of cell cycle Effects 0.000 description 1
- 230000026267 regulation of growth Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 210000002345 respiratory system Anatomy 0.000 description 1
- 230000003938 response to stress Effects 0.000 description 1
- 210000001525 retina Anatomy 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 238000002702 ribosome display Methods 0.000 description 1
- 238000009738 saturating Methods 0.000 description 1
- 230000037390 scarring Effects 0.000 description 1
- 238000013391 scatchard analysis Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 150000003341 sedoheptuloses Chemical class 0.000 description 1
- 230000001953 sensory effect Effects 0.000 description 1
- 230000036303 septic shock Effects 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- PTLRDCMBXHILCL-UHFFFAOYSA-M sodium arsenite Chemical compound [Na+].[O-][As]=O PTLRDCMBXHILCL-UHFFFAOYSA-M 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000000278 spinal cord Anatomy 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000004960 subcellular localization Effects 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 229940014800 succinic anhydride Drugs 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 102000013498 tau Proteins Human genes 0.000 description 1
- 210000001550 testis Anatomy 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 229960002175 thyroglobulin Drugs 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
- 230000036962 time dependent Effects 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 230000005945 translocation Effects 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- 108010064892 trkC Receptor Proteins 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 229910052721 tungsten Inorganic materials 0.000 description 1
- 230000007332 vesicle formation Effects 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 230000003442 weekly effect Effects 0.000 description 1
- 230000037314 wound repair Effects 0.000 description 1
- 150000003742 xyloses Chemical class 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/70—Carbohydrates; Sugars; Derivatives thereof
- A61K31/7088—Compounds having three or more nucleosides or nucleotides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2863—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for growth factors, growth regulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P21/00—Drugs for disorders of the muscular or neuromuscular system
- A61P21/02—Muscle relaxants, e.g. for tetanus or cramps
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/08—Antiepileptics; Anticonvulsants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/14—Drugs for disorders of the nervous system for treating abnormal movements, e.g. chorea, dyskinesia
- A61P25/16—Anti-Parkinson drugs
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/28—Drugs for disorders of the nervous system for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
- A61P27/06—Antiglaucoma agents or miotics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/286—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against neuromediator receptors, e.g. serotonin receptor, dopamine receptor
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/10—Immunoglobulins specific features characterized by their source of isolation or production
- C07K2317/14—Specific host cells or culture conditions, e.g. components, pH or temperature
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/31—Immunoglobulins specific features characterized by aspects of specificity or valency multispecific
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/32—Fusion polypeptide fusions with soluble part of a cell surface receptor, "decoy receptors"
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Neurology (AREA)
- Biomedical Technology (AREA)
- Immunology (AREA)
- Neurosurgery (AREA)
- Molecular Biology (AREA)
- Ophthalmology & Optometry (AREA)
- Pain & Pain Management (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Physical Education & Sports Medicine (AREA)
- Rheumatology (AREA)
- Epidemiology (AREA)
- Urology & Nephrology (AREA)
- Hospice & Palliative Care (AREA)
- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
- Vascular Medicine (AREA)
- Psychology (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Psychiatry (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201562144270P | 2015-04-07 | 2015-04-07 | |
| PCT/US2016/026519 WO2016164637A1 (en) | 2015-04-07 | 2016-04-07 | Anti-sortilin antibodies and methods of use thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2899227T3 true ES2899227T3 (es) | 2022-03-10 |
Family
ID=57072459
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES16777311T Active ES2899227T3 (es) | 2015-04-07 | 2016-04-07 | Anticuerpos anti sortilina y métodos de uso de los mismos |
Country Status (22)
| Country | Link |
|---|---|
| US (10) | US10087255B2 (OSRAM) |
| EP (2) | EP3280441B1 (OSRAM) |
| JP (4) | JP6999421B2 (OSRAM) |
| CN (1) | CN107708733B (OSRAM) |
| AU (1) | AU2016245807B2 (OSRAM) |
| CA (1) | CA2981851A1 (OSRAM) |
| CY (1) | CY1124771T1 (OSRAM) |
| DK (1) | DK3280441T3 (OSRAM) |
| EA (1) | EA201792221A1 (OSRAM) |
| ES (1) | ES2899227T3 (OSRAM) |
| HR (1) | HRP20211980T1 (OSRAM) |
| HU (1) | HUE057432T2 (OSRAM) |
| IL (1) | IL254887B2 (OSRAM) |
| LT (1) | LT3280441T (OSRAM) |
| MX (1) | MX393951B (OSRAM) |
| PL (1) | PL3280441T3 (OSRAM) |
| PT (1) | PT3280441T (OSRAM) |
| RS (1) | RS62546B1 (OSRAM) |
| SG (2) | SG11201708220RA (OSRAM) |
| SI (1) | SI3280441T1 (OSRAM) |
| SM (1) | SMT202200065T1 (OSRAM) |
| WO (1) | WO2016164637A1 (OSRAM) |
Families Citing this family (53)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US10053513B2 (en) | 2009-11-30 | 2018-08-21 | Janssen Biotech, Inc. | Antibody Fc mutants with ablated effector functions |
| JP6999421B2 (ja) | 2015-04-07 | 2022-02-04 | アレクトル エルエルシー | 抗ソルチリン抗体及びその使用方法 |
| US10849992B1 (en) | 2015-04-07 | 2020-12-01 | Alector Llc | Methods of screening for sortilin binding antagonists |
| GB201512215D0 (en) | 2015-07-13 | 2015-08-19 | Lundbeck & Co As H | Agents,uses and methods |
| PL3380495T3 (pl) * | 2015-11-24 | 2021-12-13 | Transfert Plus, S.E.C. | Związki peptydowe i koniugaty peptydowe do leczenia nowotworu poprzez chemioterapię receptorową |
| KR20180104036A (ko) | 2016-01-22 | 2018-09-19 | 머크 샤프 앤드 돔 코포레이션 | 항-응고 인자 xi 항체 |
| US11542332B2 (en) | 2016-03-26 | 2023-01-03 | Bioatla, Inc. | Anti-CTLA4 antibodies, antibody fragments, their immunoconjugates and uses thereof |
| TWI802193B (zh) | 2016-06-14 | 2023-05-11 | 美商默沙東有限責任公司 | 抗凝血因子ｘｉ抗體 |
| US20200095327A1 (en) * | 2017-02-08 | 2020-03-26 | Dragonfly Therapeutics, Inc. | Antibody heavy chain variable domains targeting the nkg2d receptor |
| CA3221995C (en) | 2017-02-08 | 2024-05-28 | Dragonfly Therapeutics, Inc. | Multi-specific binding proteins for activation of natural killer cells and therapeutic uses thereof to treat cancer |
| SG11201907646YA (en) | 2017-02-20 | 2019-09-27 | Dragonfly Therapeutics Inc | Proteins binding her2, nkg2d and cd16 |
| WO2018195302A1 (en) | 2017-04-19 | 2018-10-25 | Bluefin Biomedicine, Inc. | Anti-vtcn1 antibodies and antibody drug conjugates |
| US20200157151A1 (en) * | 2017-05-24 | 2020-05-21 | Transfert Plus, S.E.C. | Peptide compounds, conjugate compounds and uses thereof for treating inflammatory diseases |
| AU2018275359C1 (en) | 2017-06-02 | 2022-02-03 | Pfizer Inc. | Antibodies specific for FLT3 and their uses |
| US10894833B2 (en) * | 2017-07-20 | 2021-01-19 | H. Lundbeck A/S | Agents, uses and methods for treatment |
| WO2019083944A2 (en) * | 2017-10-23 | 2019-05-02 | The Brigham And Women's Hospital, Inc. | MATERIALS AND METHODS FOR DISEASES ASSOCIATED WITH EXTRACELLULAR VESICLES |
| WO2019084067A1 (en) * | 2017-10-24 | 2019-05-02 | Magenta Therapeutics, Inc. | ANTI-CD117 ANTIBODIES AND METHODS OF USE |
| JP7280254B2 (ja) | 2017-10-24 | 2023-05-23 | マジェンタ セラピューティクス インコーポレイテッド | Ｃｄ１１７＋細胞を減少させるための組成物及び方法 |
| TW201922782A (zh) | 2017-10-24 | 2019-06-16 | 美商麥珍塔治療學股份有限公司 | 去除cd117+細胞之組合物及方法 |
| AU2019205330B2 (en) | 2018-01-04 | 2025-09-11 | Iconic Therapeutics Llc | Anti-tissue factor antibodies, antibody-drug conjugates, and related methods |
| KR20200118824A (ko) | 2018-02-08 | 2020-10-16 | 드래곤플라이 쎄라퓨틱스, 인크. | 자연 살해 세포를 활성화시키는 다중-특이성 결합 단백질을 수반하는 암의 병용 요법 |
| PT3749346T (pt) | 2018-02-08 | 2024-09-05 | Dragonfly Therapeutics Inc | Combinações de domínios variáveis de anticorpos dirigidas ao receptor nkg2d |
| CA3091424A1 (en) | 2018-02-20 | 2019-08-29 | Dragonfly Therapeutics, Inc. | Multi-specific binding proteins that bind cd33, nkg2d, and cd16, and methods of use |
| MX2020008683A (es) * | 2018-02-20 | 2020-12-07 | Dragonfly Therapeutics Inc | Dominios variables de anticuerpo que se dirigen a cd33 y sus usos. |
| US12173030B2 (en) * | 2018-03-27 | 2024-12-24 | Aztherapies, Inc. | CAR-Treg-based therapies for treating neurodegenerative diseases |
| US20210284702A1 (en) * | 2018-06-18 | 2021-09-16 | Denali Therapeutics Inc. | Fusion proteins comprising progranulin |
| KR102530517B1 (ko) | 2018-07-13 | 2023-05-09 | 알렉터 엘엘씨 | 항-소틸린 항체 및 이들의 사용 방법 |
| CA3108646A1 (en) | 2018-08-08 | 2020-02-13 | Dragonfly Therapeutics, Inc. | Proteins binding nkg2d, cd16 and a tumor-associated antigen |
| AU2019318083A1 (en) | 2018-08-08 | 2021-02-25 | Dragonfly Therapeutics, Inc. | Multi-specific binding proteins that bind BCMA, NKG2D and CD16, and methods of use |
| EA202091888A1 (ru) | 2018-08-08 | 2020-10-23 | Драгонфлай Терапьютикс, Инк. | Вариабельные домены антител, нацеленные на рецептор nkg2d |
| US11591390B2 (en) | 2018-09-27 | 2023-02-28 | Celgene Corporation | SIRP-α binding proteins and methods of use thereof |
| PE20211491A1 (es) | 2018-09-27 | 2021-08-11 | Celgene Corp | PROTEINAS DE FIJACION A SIRPa Y METODOS DE USO DE ESTAS |
| MX2021015212A (es) * | 2019-06-11 | 2022-04-06 | Alector Llc | Anticuerpos antisortilina para uso en terapia. |
| WO2021003074A1 (en) * | 2019-07-03 | 2021-01-07 | Crystal Bioscience Inc. | Anti-cd38 antibody and methods of use thereof |
| EA202193309A1 (ru) * | 2019-07-03 | 2022-03-28 | Айконик Терапьютикс, Инк. | Конъюгаты антитело к тканевому фактору-лекарственное средство и связанные способы |
| US20230044608A1 (en) * | 2019-12-10 | 2023-02-09 | Aarhus Universitet | Compounds for treatment of eye diseases |
| US20230212266A1 (en) * | 2020-04-27 | 2023-07-06 | Fred Hutchinson Cancer Center | Neutralizing monoclonal antibodies against covid19 |
| MX2022013944A (es) | 2020-05-06 | 2022-11-30 | Dragonfly Therapeutics Inc | Proteinas que se unen al receptor activador de celulas asesinas naturales grupo 2 miembro d (nkg2d), cumulo de diferenciacion (cd16) y miembro a de la familia de dominios de lectina tipo c 12 (clec12a). |
| IL299329A (en) * | 2020-06-24 | 2023-02-01 | Prothena Biosciences Ltd | Antibodies recognizing sortilin |
| EP3981394A1 (en) * | 2020-10-07 | 2022-04-13 | Insusense ApS | A sortilin antagonist for use in the prevention or treatment of hearing loss. |
| CA3198606A1 (en) | 2020-10-14 | 2022-04-21 | Denali Therapeutics Inc. | Methods for treating and monitoring frontotemporal dementia |
| KR20230117169A (ko) | 2020-12-02 | 2023-08-07 | 알렉터 엘엘씨 | 항-소르틸린 항체의 사용 방법 |
| WO2022120423A1 (en) * | 2020-12-08 | 2022-06-16 | James Cook University | Peptides and uses thereof |
| JP2024508894A (ja) | 2021-03-03 | 2024-02-28 | ドラゴンフライ セラピューティクス， インコーポレイテッド | Ｎｋｇ２ｄ、ｃｄ１６、及び腫瘍関連抗原に結合する多特異性結合タンパク質を使用して癌を治療する方法 |
| AU2022277698A1 (en) * | 2021-05-19 | 2023-12-14 | Biohaven Therapeutics Ltd. | Antibody drug conjugates using mates technology for delivering cytotoxic agents |
| IL310535A (en) * | 2021-08-10 | 2024-03-01 | Byomass Inc | Anti-gdf15 antibodies, compositions and uses thereof |
| SE545408C2 (en) | 2021-12-02 | 2023-09-05 | Sortina Pharma Ab | Sortilin inhibitors |
| CA3242070A1 (en) * | 2021-12-23 | 2023-06-29 | Andriani IOANNOU | Antibodies recognizing sortilin |
| CA3251522A1 (en) * | 2022-05-03 | 2023-11-09 | Mbrace Therapeutics, Inc. | PROCESSES FOR THE PRODUCTION OF RECOMBINANT ANTIBODIES AND ASSOCIATED CELL SYSTEMS |
| IL317511A (en) * | 2022-06-16 | 2025-02-01 | Cephalon Llc | IL-2 immunoconjugates attenuated by anti-PD-1 antibody and their uses |
| CN119403786A (zh) | 2022-06-23 | 2025-02-07 | 德罗普尼尔生物有限公司 | 选择性诱导细胞外靶标在溶酶体中降解的双功能分子 |
| WO2024245719A1 (en) | 2023-05-26 | 2024-12-05 | Charité - Universitätsmedizin Berlin | Sortilin inhibitors for treatment of patients with functional neuroendocrine tumors |
| WO2025166073A1 (en) * | 2024-01-31 | 2025-08-07 | Alector Llc | Compositions comprising anti-sortilin antibodies and uses thereof |
Family Cites Families (137)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| USRE30985E (en) | 1978-01-01 | 1982-06-29 | Serum-free cell culture media | |
| US4657760A (en) | 1979-03-20 | 1987-04-14 | Ortho Pharmaceutical Corporation | Methods and compositions using monoclonal antibody to human T cells |
| US4560655A (en) | 1982-12-16 | 1985-12-24 | Immunex Corporation | Serum-free cell culture medium and process for making same |
| US4657866A (en) | 1982-12-21 | 1987-04-14 | Sudhir Kumar | Serum-free, synthetic, completely chemically defined tissue culture media |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4767704A (en) | 1983-10-07 | 1988-08-30 | Columbia University In The City Of New York | Protein-free culture medium |
| US5206344A (en) | 1985-06-26 | 1993-04-27 | Cetus Oncology Corporation | Interleukin-2 muteins and polymer conjugation thereof |
| GB8516415D0 (en) | 1985-06-28 | 1985-07-31 | Celltech Ltd | Culture of animal cells |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| US6548640B1 (en) | 1986-03-27 | 2003-04-15 | Btg International Limited | Altered antibodies |
| US4927762A (en) | 1986-04-01 | 1990-05-22 | Cell Enterprises, Inc. | Cell culture medium with antioxidant |
| US5567610A (en) | 1986-09-04 | 1996-10-22 | Bioinvent International Ab | Method of producing human monoclonal antibodies and kit therefor |
| EP0308936B1 (en) | 1987-09-23 | 1994-07-06 | Bristol-Myers Squibb Company | Antibody heteroconjugates for the killing of HIV-infected cells |
| EP0435911B1 (en) | 1988-09-23 | 1996-03-13 | Cetus Oncology Corporation | Cell culture medium for enhanced cell growth, culture longevity and product expression |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| FI903489A0 (fi) | 1988-11-11 | 1990-07-10 | Medical Res Council | Ligander med en enda sektion, receptorer innehaollande naemnda ligander, foerfaranden foer deras framstaellning samt anvaendning av liganderna och receptorerna. |
| US5175384A (en) | 1988-12-05 | 1992-12-29 | Genpharm International | Transgenic mice depleted in mature t-cells and methods for making transgenic mice |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| AU641673B2 (en) | 1989-06-29 | 1993-09-30 | Medarex, Inc. | Bispecific reagents for aids therapy |
| US5225212A (en) | 1989-10-20 | 1993-07-06 | Liposome Technology, Inc. | Microreservoir liposome composition and method |
| US5959177A (en) | 1989-10-27 | 1999-09-28 | The Scripps Research Institute | Transgenic plants expressing assembled secretory antibodies |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| DE69133566T2 (de) | 1990-01-12 | 2007-12-06 | Amgen Fremont Inc. | Bildung von xenogenen Antikörpern |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5229275A (en) | 1990-04-26 | 1993-07-20 | Akzo N.V. | In-vitro method for producing antigen-specific human monoclonal antibodies |
| AU8295491A (en) | 1990-06-29 | 1992-01-23 | Biosource Technologies Incorporated | Melanin production by transformed microorganisms |
| WO1992003918A1 (en) | 1990-08-29 | 1992-03-19 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5122469A (en) | 1990-10-03 | 1992-06-16 | Genentech, Inc. | Method for culturing Chinese hamster ovary cells to improve production of recombinant proteins |
| DK0564531T3 (da) | 1990-12-03 | 1998-09-28 | Genentech Inc | Berigelsesfremgangsmåde for variantproteiner med ændrede bindingsegenskaber |
| US5571894A (en) | 1991-02-05 | 1996-11-05 | Ciba-Geigy Corporation | Recombinant antibodies specific for a growth factor receptor |
| CA2102511A1 (en) | 1991-05-14 | 1992-11-15 | Paul J. Higgins | Heteroconjugate antibodies for treatment of hiv infection |
| CA2103059C (en) | 1991-06-14 | 2005-03-22 | Paul J. Carter | Method for making humanized antibodies |
| GB9114948D0 (en) | 1991-07-11 | 1991-08-28 | Pfizer Ltd | Process for preparing sertraline intermediates |
| CA2116774C (en) | 1991-09-19 | 2003-11-11 | Paul J. Carter | Expression in e. coli antibody fragments having at least a cysteine present as a free thiol. use for the production of bifunctional f(ab') 2 antibodies |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| FI941572L (fi) | 1991-10-07 | 1994-05-27 | Oncologix Inc | Anti-erbB-2-monoklonaalisten vasta-aineiden yhdistelmä ja käyttömenetelmä |
| WO1993008829A1 (en) | 1991-11-04 | 1993-05-13 | The Regents Of The University Of California | Compositions that mediate killing of hiv-infected cells |
| DK1136556T3 (da) | 1991-11-25 | 2005-10-03 | Enzon Inc | Fremgangsmåde til fremstilling af multivalente antigen-bindende proteiner |
| US5869619A (en) | 1991-12-13 | 1999-02-09 | Xoma Corporation | Modified antibody variable domains |
| EP1291360A1 (en) | 1991-12-13 | 2003-03-12 | Xoma Corporation | Methods and materials for preparation of modified antibody variable domains and therapeutic uses thereof |
| DE69333807T2 (de) | 1992-02-06 | 2006-02-02 | Chiron Corp., Emeryville | Marker für krebs und biosynthetisches bindeprotein dafür |
| US5573905A (en) | 1992-03-30 | 1996-11-12 | The Scripps Research Institute | Encoded combinatorial chemical libraries |
| CA2140280A1 (en) | 1992-08-17 | 1994-03-03 | Avi J. Ashkenazi | Bispecific immunoadhesins |
| US5789199A (en) | 1994-11-03 | 1998-08-04 | Genentech, Inc. | Process for bacterial production of polypeptides |
| US5840523A (en) | 1995-03-01 | 1998-11-24 | Genetech, Inc. | Methods and compositions for secretion of heterologous polypeptides |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| US5641870A (en) | 1995-04-20 | 1997-06-24 | Genentech, Inc. | Low pH hydrophobic interaction chromatography for antibody purification |
| US5869046A (en) | 1995-04-14 | 1999-02-09 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US5739277A (en) | 1995-04-14 | 1998-04-14 | Genentech Inc. | Altered polypeptides with increased half-life |
| ATE390933T1 (de) | 1995-04-27 | 2008-04-15 | Amgen Fremont Inc | Aus immunisierten xenomäusen stammende menschliche antikörper gegen il-8 |
| WO1996034096A1 (en) | 1995-04-28 | 1996-10-31 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| WO1997011971A1 (en) | 1995-09-28 | 1997-04-03 | Alexion Pharmaceuticals, Inc. | Porcine cell interaction proteins |
| DE19544393A1 (de) | 1995-11-15 | 1997-05-22 | Hoechst Schering Agrevo Gmbh | Synergistische herbizide Mischungen |
| CA2722378C (en) | 1996-12-03 | 2015-02-03 | Amgen Fremont Inc. | Human antibodies that bind tnf.alpha. |
| US6040498A (en) | 1998-08-11 | 2000-03-21 | North Caroline State University | Genetically engineered duckweed |
| US6610833B1 (en) | 1997-11-24 | 2003-08-26 | The Institute For Human Genetics And Biochemistry | Monoclonal human natural antibodies |
| EP1034298B1 (en) | 1997-12-05 | 2011-11-02 | The Scripps Research Institute | Humanization of murine antibody |
| GB9809951D0 (en) | 1998-05-08 | 1998-07-08 | Univ Cambridge Tech | Binding molecules |
| ES2248127T3 (es) | 1999-10-04 | 2006-03-16 | Medicago Inc. | Metodo para regular la transcripcion de genes foraneos en presencia de nigtrogeno. |
| US7125978B1 (en) | 1999-10-04 | 2006-10-24 | Medicago Inc. | Promoter for regulating expression of foreign genes |
| MXPA02010011A (es) | 2000-04-11 | 2003-04-25 | Genentech Inc | Anticuerpos multivalentes y usos para los mismos. |
| US7064191B2 (en) | 2000-10-06 | 2006-06-20 | Kyowa Hakko Kogyo Co., Ltd. | Process for purifying antibody |
| US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
| US6596541B2 (en) | 2000-10-31 | 2003-07-22 | Regeneron Pharmaceuticals, Inc. | Methods of modifying eukaryotic cells |
| DE60131456T2 (de) | 2000-11-30 | 2008-07-10 | Medarex, Inc., Milpitas | Transchromosomale transgen-nagetiere zur herstellung von humanen antikörpern |
| PL213948B1 (pl) | 2001-10-25 | 2013-05-31 | Genentech Inc | Kompozycje zawierajace glikoproteine, czasteczka kwasu nukleinowego kodujaca te glikoproteine, komórka gospodarza, sposób wytwarzania glikoproteiny, kompozycja do zastosowania do leczenia, zastosowanie kompozycji i zestaw zawierajacy kompozycje |
| US20040093621A1 (en) | 2001-12-25 | 2004-05-13 | Kyowa Hakko Kogyo Co., Ltd | Antibody composition which specifically binds to CD20 |
| PL373256A1 (en) | 2002-04-09 | 2005-08-22 | Kyowa Hakko Kogyo Co, Ltd. | Cells with modified genome |
| US7749753B2 (en) | 2002-04-09 | 2010-07-06 | Kyowa Hakko Kirin Co., Ltd | Cells in which activity of the protein involved in transportation of GDP-fucose is reduced or lost |
| JPWO2003084569A1 (ja) | 2002-04-09 | 2005-08-11 | 協和醗酵工業株式会社 | 抗体組成物含有医薬 |
| US20040132140A1 (en) | 2002-04-09 | 2004-07-08 | Kyowa Hakko Kogyo Co., Ltd. | Production process for antibody composition |
| CA2502413A1 (en) | 2002-11-01 | 2004-05-21 | The Regents Of The University Of Colorado, A Body Corporate | Quantitative analysis of protein isoforms using matrix-assisted laser desorption/ionization time of flight mass spectrometry |
| ES2380055T3 (es) | 2002-12-20 | 2012-05-08 | H. Lundbeck A/S | Modulación de la actividad de neurotrofinas; método de escrutinio |
| EP1682170A2 (en) | 2003-11-07 | 2006-07-26 | Lay Line Genomics SpA | Compositions able to prevent neurodegenerative processes and methods of assaying the same |
| BRPI0508761A (pt) | 2004-03-31 | 2007-08-14 | Genentech Inc | anticorpo humanizado, composição que compreende um anticorpo humanizado, ácido nucléico isolado, vetor, célula hospedeira, processo de produção de anticorpo humanizado, método de tratamento de disfunção tgf-beta, método de detecção de tgf-beta, artigo industrializado e método de tratamento de cáncer |
| MX2007008017A (es) | 2004-12-31 | 2007-09-12 | Genentech Inc | Polipeptidos que se ligan a br3 y usos de los mismos. |
| US7700099B2 (en) | 2005-02-14 | 2010-04-20 | Merck & Co., Inc. | Non-immunostimulatory antibody and compositions containing the same |
| US8877714B2 (en) | 2005-06-14 | 2014-11-04 | Raptor Pharmaceutical Inc. | Compositions comprising receptor-associated protein (RAP) variants specific for LRP2 and uses thereof |
| CN104356236B (zh) * | 2005-07-01 | 2020-07-03 | E.R.施贵宝&圣斯有限责任公司 | 抗程序性死亡配体1(pd-l1)的人单克隆抗体 |
| WO2007035716A2 (en) | 2005-09-16 | 2007-03-29 | Raptor Pharmaceutical Inc. | Compositions comprising receptor-associated protein (rap) variants specific for cr-containing proteins and uses thereof |
| FR2896881B1 (fr) | 2006-01-31 | 2008-04-18 | Biomerieux Sa | Procede de dosage du prongf pour le diagnostic in vitro du cancer du sein et utilisation du prongf en therapie |
| EP3124029A1 (en) | 2006-03-15 | 2017-02-01 | Alexion Pharmaceuticals, Inc. | Treatment of paroxysmal nocturnal hemoglobinuria patients by an inhibitor of complement |
| WO2007134050A2 (en) | 2006-05-09 | 2007-11-22 | Genentech, Inc. | Binding polypeptides with optimized scaffolds |
| WO2008027236A2 (en) | 2006-08-30 | 2008-03-06 | Genentech, Inc. | Multispecific antibodies |
| WO2008036682A2 (en) | 2006-09-18 | 2008-03-27 | Raptor Pharmaceutical Inc. | Treatment of liver disorders by administration of receptor-associated protein (rap)-conjugates |
| WO2008052016A2 (en) | 2006-10-23 | 2008-05-02 | Columbia University | The sortilin-related receptor sorl1 is functionally and genetically associated with alzheimer's disease |
| US20100028333A1 (en) * | 2006-12-15 | 2010-02-04 | Getty Krista L | Receptor for amyloid beta and uses thereof |
| UY30776A1 (es) | 2006-12-21 | 2008-07-03 | Medarex Inc | Anticuerpos cd44 |
| SI3225251T1 (sl) | 2006-12-21 | 2020-03-31 | H. Lundbeck A/S | Modulacija aktivnosti pronevrotrofinov |
| WO2008086452A2 (en) | 2007-01-10 | 2008-07-17 | Columbia University | Treatment and prevention of alzheimer's disease |
| CN100592373C (zh) | 2007-05-25 | 2010-02-24 | 群康科技(深圳)有限公司 | 液晶显示面板驱动装置及其驱动方法 |
| CA2697193C (en) | 2007-09-14 | 2017-06-06 | Adimab, Inc. | Rationally designed, synthetic antibody libraries and uses therefor |
| US8877688B2 (en) | 2007-09-14 | 2014-11-04 | Adimab, Llc | Rationally designed, synthetic antibody libraries and uses therefor |
| PT2235064E (pt) | 2008-01-07 | 2016-03-01 | Amgen Inc | Método de preparação de moléculas heterodiméricas de fc de anticorpos utilizando efeitos de indução eletrostática |
| JP5715045B2 (ja) * | 2008-04-27 | 2015-05-07 | ハー・ルンドベック・アクチエゼルスカベット | ソルチリンに対する特異的リガンドの設計 |
| DK2282728T3 (en) | 2008-05-22 | 2015-04-20 | Lundbeck & Co As H | Modulation at Vps10p domain receptors |
| US20160359907A1 (en) | 2015-06-02 | 2016-12-08 | Vmware, Inc. | Automatically auditing virtual machines for security hardening compliance |
| EP2307042B1 (en) | 2008-06-25 | 2014-03-26 | H. Lundbeck A/S | Modulation of the trpv : vps10p-domain receptor system for the treatment of pain |
| UA106354C2 (ru) * | 2008-07-16 | 2014-08-26 | Инститьют Фо Рисерч Ин Байомедсин | Антитела, нейтрализующие цитомегаловирус человека, и их применение |
| US20120039865A1 (en) * | 2008-08-19 | 2012-02-16 | Yale University | Identification of sortilin as a neuronal receptor for the frontotemporal dementia protein, progranulin |
| CA2736460A1 (en) | 2008-09-08 | 2010-03-11 | Mayo Foundation For Medical Education And Research | Methods and devices for ligating tubular structures |
| EP3165537A1 (en) | 2008-12-19 | 2017-05-10 | H. Lundbeck A/S | Modulation of the vps 10-domain receptor family for the treatment of mental and behavioural disorders |
| FR2945538B1 (fr) | 2009-05-12 | 2014-12-26 | Sanofi Aventis | Anticorps humanises specifiques de la forme protofibrillaire du peptide beta-amyloide. |
| BR112012007137A2 (pt) | 2009-09-30 | 2015-09-15 | Harvard College | metodos para modulacao da autofagia por meio da modulacao de produtos genicos inibidores da autofagia |
| WO2011159762A1 (en) | 2010-06-15 | 2011-12-22 | Cornell University | Methods of limiting microvascular damage following acute myocardial ischemia |
| MX360336B (es) | 2010-07-16 | 2018-10-30 | Adimab Llc Star | Colecciones de anticuerpos. |
| WO2012068332A2 (en) | 2010-11-17 | 2012-05-24 | Cornell University | Methods for treating early stage or mild neurological disorders |
| MX343580B (es) * | 2011-06-13 | 2016-11-10 | Csl Ltd | Anticuerpos contra el g-csfr y sus usos. |
| US9822366B2 (en) | 2012-11-02 | 2017-11-21 | The Brigham And Women's Hospital, Inc. | Sortilin 1 is a novel inducer of vascular calcification |
| US10156574B2 (en) | 2013-04-29 | 2018-12-18 | Adimab, Llc | Polyspecificity reagents, methods for their preparation and use |
| BR112016000106B1 (pt) * | 2013-07-09 | 2023-11-21 | Annexon, Inc. | Anticorpos anti-c1q e usos dos mesmos, célula de hibridoma, composição farmacêutica e métodos de detecção de sinapses em uma amostra biológica referências cruzadas a pedidos relacionados |
| JP2017510623A (ja) | 2014-02-04 | 2017-04-13 | ニューヨーク ユニバーシティ | リソソーム蓄積症の診断および治療のためのプログラニュリン（ｐｇｒｎ）およびその誘導体 |
| HK1232289A1 (zh) | 2014-02-12 | 2018-01-05 | H. Lundbeck A/S | 分拣蛋白作为针对情感/心境障碍的生物标记的用途 |
| US20170096486A1 (en) | 2014-03-26 | 2017-04-06 | Goran Landberg | Agents inhibiting granulin for treatment of cancer |
| EP3193942B1 (en) | 2014-08-11 | 2020-03-25 | Shire Human Genetic Therapies, Inc. | Lysosomal targeting and uses thereof |
| US10849992B1 (en) * | 2015-04-07 | 2020-12-01 | Alector Llc | Methods of screening for sortilin binding antagonists |
| JP6999421B2 (ja) | 2015-04-07 | 2022-02-04 | アレクトル エルエルシー | 抗ソルチリン抗体及びその使用方法 |
| US20160331746A1 (en) | 2015-05-12 | 2016-11-17 | University Of South Florida | Sortilin-Binding Small Molecules for Increasing Glucose Uptake |
| GB201512215D0 (en) * | 2015-07-13 | 2015-08-19 | Lundbeck & Co As H | Agents,uses and methods |
| WO2017024137A1 (en) | 2015-08-04 | 2017-02-09 | New York University | Progranulin (pgrn) fragments and derivatives for treatment or alleviation of lysosomal storage diseases |
| US10085969B1 (en) | 2016-02-12 | 2018-10-02 | University Of South Florida | Sortilin binding compounds, formulations, and uses thereof |
| US10894833B2 (en) | 2017-07-20 | 2021-01-19 | H. Lundbeck A/S | Agents, uses and methods for treatment |
| WO2019083944A2 (en) | 2017-10-23 | 2019-05-02 | The Brigham And Women's Hospital, Inc. | MATERIALS AND METHODS FOR DISEASES ASSOCIATED WITH EXTRACELLULAR VESICLES |
| US20210284702A1 (en) | 2018-06-18 | 2021-09-16 | Denali Therapeutics Inc. | Fusion proteins comprising progranulin |
| KR102530517B1 (ko) | 2018-07-13 | 2023-05-09 | 알렉터 엘엘씨 | 항-소틸린 항체 및 이들의 사용 방법 |
| EP3844190A4 (en) | 2018-08-24 | 2022-06-08 | Transfert Plus, S.E.C. | Methods and compounds for targeting sortilin receptors and inhibiting vasculogenic mimicry |
| WO2020051624A1 (en) | 2018-09-11 | 2020-03-19 | Grophin Pty Ltd | Methods and compositions for improving recovery from a brain injury |
| EP3666281A1 (en) | 2018-12-14 | 2020-06-17 | Insusense ApS | Compositions comprising sortilin-1 |
| WO2020191212A1 (en) | 2019-03-20 | 2020-09-24 | President And Fellows Of Harvard College | Antisense oligonucleotide-based progranulin augmentation therapy in neurodegenerative diseases |
| MX2021015212A (es) | 2019-06-11 | 2022-04-06 | Alector Llc | Anticuerpos antisortilina para uso en terapia. |
-
2016
- 2016-04-07 JP JP2017552831A patent/JP6999421B2/ja active Active
- 2016-04-07 CA CA2981851A patent/CA2981851A1/en active Pending
- 2016-04-07 RS RS20211389A patent/RS62546B1/sr unknown
- 2016-04-07 CN CN201680032832.9A patent/CN107708733B/zh active Active
- 2016-04-07 MX MX2017012802A patent/MX393951B/es unknown
- 2016-04-07 LT LTEPPCT/US2016/026519T patent/LT3280441T/lt unknown
- 2016-04-07 EP EP16777311.8A patent/EP3280441B1/en active Active
- 2016-04-07 DK DK16777311.8T patent/DK3280441T3/da active
- 2016-04-07 WO PCT/US2016/026519 patent/WO2016164637A1/en not_active Ceased
- 2016-04-07 HR HRP20211980TT patent/HRP20211980T1/hr unknown
- 2016-04-07 EP EP21191834.7A patent/EP3991748A3/en active Pending
- 2016-04-07 SI SI201631423T patent/SI3280441T1/sl unknown
- 2016-04-07 SG SG11201708220RA patent/SG11201708220RA/en unknown
- 2016-04-07 EA EA201792221A patent/EA201792221A1/ru unknown
- 2016-04-07 AU AU2016245807A patent/AU2016245807B2/en active Active
- 2016-04-07 IL IL254887A patent/IL254887B2/en unknown
- 2016-04-07 SM SM20220065T patent/SMT202200065T1/it unknown
- 2016-04-07 HU HUE16777311A patent/HUE057432T2/hu unknown
- 2016-04-07 PT PT167773118T patent/PT3280441T/pt unknown
- 2016-04-07 SG SG10201912087SA patent/SG10201912087SA/en unknown
- 2016-04-07 PL PL16777311T patent/PL3280441T3/pl unknown
- 2016-04-07 ES ES16777311T patent/ES2899227T3/es active Active
- 2016-10-04 US US15/285,359 patent/US10087255B2/en active Active
-
2018
- 2018-01-10 US US15/867,609 patent/US10308718B2/en active Active
- 2018-08-08 US US16/058,817 patent/US11339223B2/en active Active
- 2018-08-20 US US15/999,627 patent/US10428150B2/en active Active
- 2018-09-18 US US16/134,830 patent/US11208488B2/en active Active
-
2020
- 2020-01-13 US US16/741,658 patent/US11186645B2/en active Active
- 2020-08-04 JP JP2020132534A patent/JP2020202842A/ja active Pending
-
2021
- 2021-11-23 US US17/534,291 patent/US20220185899A1/en not_active Abandoned
- 2021-11-23 US US17/534,270 patent/US20220185898A1/en not_active Abandoned
- 2021-12-06 CY CY20211101067T patent/CY1124771T1/el unknown
-
2022
- 2022-04-14 US US17/721,112 patent/US20240309097A2/en not_active Abandoned
- 2022-11-24 JP JP2022187671A patent/JP7648584B2/ja active Active
-
2024
- 2024-11-22 US US18/957,413 patent/US20250092144A1/en active Pending
-
2025
- 2025-03-06 JP JP2025035592A patent/JP2025087841A/ja active Pending
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2899227T3 (es) | Anticuerpos anti sortilina y métodos de uso de los mismos | |
| US20230295297A1 (en) | Anti-trem2 antibodies and methods of use thereof | |
| EP3322722B1 (en) | Agents, uses and methods for the treatment of synucleinopathy | |
| US20210403540A1 (en) | Anti-apoe4 antigen-binding proteins and methods of use thereof | |
| TW201702273A (zh) | 用於治療的藥劑、用途及方法 | |
| EA043015B1 (ru) | Антитела против сортилина и способы их применения | |
| WO2023238869A1 (ja) | 筋萎縮性側索硬化症、パーキンソン病、ハンチントン病、脊髄小脳失調症、老化に関連する変性疾患若しくは神経疾患、脳老化、あるいは脳老化を伴う疾患の予防剤又は治療剤 | |
| HK1249445B (en) | Anti-sortilin antibodies and methods of use thereof |