CA3067057A1 - Methods for aiding in the diagnosis and evaluation of a subject who has sustained an orthopedic injury and that has or may have sustained an injury to the head, such as mild traumatic brain injury (tbi), using glial fibrillary acidic protein (gfap) and/or ubiquitin carboxy-terminal hydrolase l1 (uch-l1) - Google Patents
Methods for aiding in the diagnosis and evaluation of a subject who has sustained an orthopedic injury and that has or may have sustained an injury to the head, such as mild traumatic brain injury (tbi), using glial fibrillary acidic protein (gfap) and/or ubiquitin carboxy-terminal hydrolase l1 (uch-l1)Info
- Publication number
- CA3067057A1 CA3067057A1 CA3067057A CA3067057A CA3067057A1 CA 3067057 A1 CA3067057 A1 CA 3067057A1 CA 3067057 A CA3067057 A CA 3067057A CA 3067057 A CA3067057 A CA 3067057A CA 3067057 A1 CA3067057 A1 CA 3067057A1
- Authority
- CA
- Canada
- Prior art keywords
- gfap
- uch
- reference level
- sample
- subject
- 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.)
- Pending
Links
- 102000053171 Glial Fibrillary Acidic Human genes 0.000 title claims abstract description 659
- 101710193519 Glial fibrillary acidic protein Proteins 0.000 title claims abstract description 658
- 210000005046 glial fibrillary acidic protein Anatomy 0.000 title claims abstract description 656
- 238000000034 method Methods 0.000 title claims abstract description 365
- 208000014674 injury Diseases 0.000 title claims abstract description 281
- 230000006378 damage Effects 0.000 title claims abstract description 268
- 208000027418 Wounds and injury Diseases 0.000 title claims abstract description 266
- 230000002459 sustained effect Effects 0.000 title claims abstract description 245
- 230000000399 orthopedic effect Effects 0.000 title claims abstract description 112
- 102000005918 Ubiquitin Thiolesterase Human genes 0.000 title claims abstract description 42
- 108010005656 Ubiquitin Thiolesterase Proteins 0.000 title claims abstract description 42
- 238000003745 diagnosis Methods 0.000 title claims abstract description 16
- 208000007333 Brain Concussion Diseases 0.000 title abstract description 35
- 238000011156 evaluation Methods 0.000 title abstract description 24
- 101150057182 GFAP gene Proteins 0.000 title description 3
- 208000030886 Traumatic Brain injury Diseases 0.000 claims abstract description 299
- 230000009529 traumatic brain injury Effects 0.000 claims abstract description 297
- 238000003325 tomography Methods 0.000 claims abstract description 9
- 238000003556 assay Methods 0.000 claims description 288
- 230000035945 sensitivity Effects 0.000 claims description 167
- 239000000427 antigen Substances 0.000 claims description 134
- 108091007433 antigens Proteins 0.000 claims description 130
- 102000036639 antigens Human genes 0.000 claims description 130
- 239000012634 fragment Substances 0.000 claims description 100
- 238000001514 detection method Methods 0.000 claims description 83
- 206010010071 Coma Diseases 0.000 claims description 72
- 238000002591 computed tomography Methods 0.000 claims description 51
- 238000003018 immunoassay Methods 0.000 claims description 38
- 238000011282 treatment Methods 0.000 claims description 29
- 239000000203 mixture Substances 0.000 claims description 26
- 210000002966 serum Anatomy 0.000 claims description 23
- 210000004369 blood Anatomy 0.000 claims description 21
- 239000008280 blood Substances 0.000 claims description 21
- 230000008733 trauma Effects 0.000 claims description 21
- 238000004557 single molecule detection Methods 0.000 claims description 16
- 210000002381 plasma Anatomy 0.000 claims description 15
- 238000012544 monitoring process Methods 0.000 claims description 14
- 210000001175 cerebrospinal fluid Anatomy 0.000 claims description 9
- 238000004880 explosion Methods 0.000 claims description 9
- 206010017076 Fracture Diseases 0.000 claims description 8
- 230000001154 acute effect Effects 0.000 claims description 8
- 208000010392 Bone Fractures Diseases 0.000 claims description 7
- 206010039203 Road traffic accident Diseases 0.000 claims description 7
- 208000025978 Athletic injury Diseases 0.000 claims description 5
- 206010041738 Sports injury Diseases 0.000 claims description 5
- 238000003384 imaging method Methods 0.000 abstract description 16
- 239000012472 biological sample Substances 0.000 abstract description 10
- 230000008901 benefit Effects 0.000 abstract description 6
- 239000000523 sample Substances 0.000 description 356
- 235000001014 amino acid Nutrition 0.000 description 99
- 229940024606 amino acid Drugs 0.000 description 97
- 150000001413 amino acids Chemical class 0.000 description 97
- 238000009739 binding Methods 0.000 description 88
- 230000027455 binding Effects 0.000 description 87
- 210000004027 cell Anatomy 0.000 description 82
- 239000012491 analyte Substances 0.000 description 77
- 210000003128 head Anatomy 0.000 description 77
- 230000009870 specific binding Effects 0.000 description 56
- 108090000623 proteins and genes Proteins 0.000 description 53
- 108090000765 processed proteins & peptides Proteins 0.000 description 46
- 108060003951 Immunoglobulin Proteins 0.000 description 42
- 102000018358 immunoglobulin Human genes 0.000 description 42
- 238000012360 testing method Methods 0.000 description 37
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 35
- 102000004169 proteins and genes Human genes 0.000 description 35
- 235000018102 proteins Nutrition 0.000 description 33
- 102000004196 processed proteins & peptides Human genes 0.000 description 32
- 210000004408 hybridoma Anatomy 0.000 description 28
- 229920001184 polypeptide Polymers 0.000 description 28
- 102000023732 binding proteins Human genes 0.000 description 27
- 108091008324 binding proteins Proteins 0.000 description 27
- 241001465754 Metazoa Species 0.000 description 24
- 230000002596 correlated effect Effects 0.000 description 23
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 23
- 201000010099 disease Diseases 0.000 description 22
- 125000003275 alpha amino acid group Chemical group 0.000 description 21
- 239000000126 substance Substances 0.000 description 21
- -1 MnAs Inorganic materials 0.000 description 20
- 238000004458 analytical method Methods 0.000 description 19
- 208000029028 brain injury Diseases 0.000 description 19
- 239000003795 chemical substances by application Substances 0.000 description 19
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 18
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 18
- 238000005516 engineering process Methods 0.000 description 18
- 229940079593 drug Drugs 0.000 description 17
- 239000003814 drug Substances 0.000 description 17
- 239000013604 expression vector Substances 0.000 description 16
- 239000013598 vector Substances 0.000 description 15
- 238000002595 magnetic resonance imaging Methods 0.000 description 14
- 238000004611 spectroscopical analysis Methods 0.000 description 14
- 210000001519 tissue Anatomy 0.000 description 14
- 239000000047 product Substances 0.000 description 13
- 238000003259 recombinant expression Methods 0.000 description 13
- 206010019196 Head injury Diseases 0.000 description 12
- 238000012216 screening Methods 0.000 description 12
- 239000007787 solid Substances 0.000 description 12
- 230000009261 transgenic effect Effects 0.000 description 12
- 239000001963 growth medium Substances 0.000 description 11
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 10
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 10
- 206010035226 Plasma cell myeloma Diseases 0.000 description 10
- 208000003443 Unconsciousness Diseases 0.000 description 10
- 210000004556 brain Anatomy 0.000 description 10
- 230000005291 magnetic effect Effects 0.000 description 10
- 238000004519 manufacturing process Methods 0.000 description 10
- 102000040430 polynucleotide Human genes 0.000 description 10
- 108091033319 polynucleotide Proteins 0.000 description 10
- 239000002157 polynucleotide Substances 0.000 description 10
- 230000004044 response Effects 0.000 description 10
- 208000024891 symptom Diseases 0.000 description 10
- 108020004414 DNA Proteins 0.000 description 9
- 241000196324 Embryophyta Species 0.000 description 9
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- 241000700159 Rattus Species 0.000 description 9
- 238000003776 cleavage reaction Methods 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 238000004128 high performance liquid chromatography Methods 0.000 description 9
- 201000000050 myeloid neoplasm Diseases 0.000 description 9
- 230000007017 scission Effects 0.000 description 9
- 238000006467 substitution reaction Methods 0.000 description 9
- 238000002965 ELISA Methods 0.000 description 8
- 241000699666 Mus <mouse, genus> Species 0.000 description 8
- 239000011324 bead Substances 0.000 description 8
- 238000004587 chromatography analysis Methods 0.000 description 8
- 230000004927 fusion Effects 0.000 description 8
- 238000002731 protein assay Methods 0.000 description 8
- 230000002159 abnormal effect Effects 0.000 description 7
- 230000004071 biological effect Effects 0.000 description 7
- 230000006870 function Effects 0.000 description 7
- 230000003053 immunization Effects 0.000 description 7
- 238000000760 immunoelectrophoresis Methods 0.000 description 7
- 229940072221 immunoglobulins Drugs 0.000 description 7
- 238000000338 in vitro Methods 0.000 description 7
- 238000004811 liquid chromatography Methods 0.000 description 7
- 238000004895 liquid chromatography mass spectrometry Methods 0.000 description 7
- 238000005259 measurement Methods 0.000 description 7
- 230000035772 mutation Effects 0.000 description 7
- 238000002823 phage display Methods 0.000 description 7
- 230000000144 pharmacologic effect Effects 0.000 description 7
- 238000000730 protein immunoprecipitation Methods 0.000 description 7
- 238000001711 protein immunostaining Methods 0.000 description 7
- 210000003625 skull Anatomy 0.000 description 7
- 238000001890 transfection Methods 0.000 description 7
- 238000001262 western blot Methods 0.000 description 7
- 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 6
- 108091035707 Consensus sequence Proteins 0.000 description 6
- 208000006011 Stroke Diseases 0.000 description 6
- 108090000848 Ubiquitin Proteins 0.000 description 6
- 102000044159 Ubiquitin Human genes 0.000 description 6
- 125000000539 amino acid group Chemical group 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 6
- 230000000875 corresponding effect Effects 0.000 description 6
- 230000006735 deficit Effects 0.000 description 6
- 230000001419 dependent effect Effects 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 210000004602 germ cell Anatomy 0.000 description 6
- 230000028993 immune response Effects 0.000 description 6
- 210000004698 lymphocyte Anatomy 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 239000002245 particle Substances 0.000 description 6
- 238000000746 purification Methods 0.000 description 6
- 239000007790 solid phase Substances 0.000 description 6
- 201000009032 substance abuse Diseases 0.000 description 6
- 239000003053 toxin Substances 0.000 description 6
- 231100000765 toxin Toxicity 0.000 description 6
- 108700012359 toxins Proteins 0.000 description 6
- 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 5
- 102100029727 Enteropeptidase Human genes 0.000 description 5
- 108010013369 Enteropeptidase Proteins 0.000 description 5
- 101000888419 Homo sapiens Glial fibrillary acidic protein Proteins 0.000 description 5
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 5
- 241001494479 Pecora Species 0.000 description 5
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 5
- 230000009824 affinity maturation Effects 0.000 description 5
- 210000001130 astrocyte Anatomy 0.000 description 5
- 230000001588 bifunctional effect Effects 0.000 description 5
- 230000008827 biological function Effects 0.000 description 5
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 5
- 238000012875 competitive assay Methods 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 238000012258 culturing Methods 0.000 description 5
- 238000012217 deletion Methods 0.000 description 5
- 230000037430 deletion Effects 0.000 description 5
- 230000009977 dual effect Effects 0.000 description 5
- 230000002255 enzymatic effect Effects 0.000 description 5
- 239000012530 fluid Substances 0.000 description 5
- 230000036541 health Effects 0.000 description 5
- 102000051520 human GFAP Human genes 0.000 description 5
- 238000002649 immunization Methods 0.000 description 5
- 230000016784 immunoglobulin production Effects 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 239000011859 microparticle Substances 0.000 description 5
- 150000007523 nucleic acids Chemical group 0.000 description 5
- 239000013612 plasmid Substances 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 238000002818 protein evolution Methods 0.000 description 5
- 238000011084 recovery Methods 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 238000001356 surgical procedure Methods 0.000 description 5
- 238000011830 transgenic mouse model Methods 0.000 description 5
- 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 4
- 241000283690 Bos taurus Species 0.000 description 4
- 241000283707 Capra Species 0.000 description 4
- AOJJSUZBOXZQNB-TZSSRYMLSA-N Doxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 description 4
- 241000282412 Homo Species 0.000 description 4
- 101000759926 Homo sapiens Ubiquitin carboxyl-terminal hydrolase isozyme L1 Proteins 0.000 description 4
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 4
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 4
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 4
- 241000699670 Mus sp. Species 0.000 description 4
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 4
- 239000002671 adjuvant Substances 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 239000001506 calcium phosphate Substances 0.000 description 4
- 229960001714 calcium phosphate Drugs 0.000 description 4
- 229910000389 calcium phosphate Inorganic materials 0.000 description 4
- 235000011010 calcium phosphates Nutrition 0.000 description 4
- 230000002490 cerebral effect Effects 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 230000009514 concussion Effects 0.000 description 4
- 239000007857 degradation product Substances 0.000 description 4
- 239000012636 effector Substances 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- 210000003527 eukaryotic cell Anatomy 0.000 description 4
- 238000000605 extraction Methods 0.000 description 4
- 102000057986 human UCHL1 Human genes 0.000 description 4
- 230000005847 immunogenicity Effects 0.000 description 4
- 230000001965 increasing effect Effects 0.000 description 4
- 238000002955 isolation Methods 0.000 description 4
- 230000033001 locomotion Effects 0.000 description 4
- 210000004962 mammalian cell Anatomy 0.000 description 4
- 238000002483 medication Methods 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 229910052751 metal Inorganic materials 0.000 description 4
- 239000002184 metal Substances 0.000 description 4
- 229960000485 methotrexate Drugs 0.000 description 4
- 239000000178 monomer Substances 0.000 description 4
- 238000001556 precipitation Methods 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 238000003127 radioimmunoassay Methods 0.000 description 4
- 230000009257 reactivity Effects 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- MRMOZBOQVYRSEM-UHFFFAOYSA-N tetraethyllead Chemical compound CC[Pb](CC)(CC)CC MRMOZBOQVYRSEM-UHFFFAOYSA-N 0.000 description 4
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 4
- 230000002792 vascular Effects 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- BZTDTCNHAFUJOG-UHFFFAOYSA-N 6-carboxyfluorescein Chemical compound C12=CC=C(O)C=C2OC2=CC(O)=CC=C2C11OC(=O)C2=CC=C(C(=O)O)C=C21 BZTDTCNHAFUJOG-UHFFFAOYSA-N 0.000 description 3
- 208000000044 Amnesia Diseases 0.000 description 3
- 206010002653 Anosmia Diseases 0.000 description 3
- 102000004127 Cytokines Human genes 0.000 description 3
- 108090000695 Cytokines Proteins 0.000 description 3
- 206010019233 Headaches Diseases 0.000 description 3
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 3
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 3
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 3
- 241000124008 Mammalia Species 0.000 description 3
- 241000699660 Mus musculus Species 0.000 description 3
- 244000061176 Nicotiana tabacum Species 0.000 description 3
- 235000002637 Nicotiana tabacum Nutrition 0.000 description 3
- 108090000526 Papain Proteins 0.000 description 3
- 102000057297 Pepsin A Human genes 0.000 description 3
- 108090000284 Pepsin A Proteins 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 108090000829 Ribosome Inactivating Proteins Proteins 0.000 description 3
- 108010039491 Ricin Proteins 0.000 description 3
- 208000010040 Sprains and Strains Diseases 0.000 description 3
- 238000012452 Xenomouse strains Methods 0.000 description 3
- VWQVUPCCIRVNHF-OUBTZVSYSA-N Yttrium-90 Chemical compound [90Y] VWQVUPCCIRVNHF-OUBTZVSYSA-N 0.000 description 3
- QBFNAVMTMIICEI-UHFFFAOYSA-N acridine-9-carboxamide Chemical compound C1=CC=C2C(C(=O)N)=C(C=CC=C3)C3=NC2=C1 QBFNAVMTMIICEI-UHFFFAOYSA-N 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 201000007201 aphasia Diseases 0.000 description 3
- 239000000090 biomarker Substances 0.000 description 3
- 210000000988 bone and bone Anatomy 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 230000015556 catabolic process Effects 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 238000004132 cross linking Methods 0.000 description 3
- 238000002405 diagnostic procedure Methods 0.000 description 3
- 239000007850 fluorescent dye Substances 0.000 description 3
- 239000003292 glue Substances 0.000 description 3
- 231100000869 headache Toxicity 0.000 description 3
- 238000003780 insertion Methods 0.000 description 3
- 230000037431 insertion Effects 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 230000007774 longterm Effects 0.000 description 3
- 238000004020 luminiscence type Methods 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 150000002739 metals Chemical class 0.000 description 3
- 210000003205 muscle Anatomy 0.000 description 3
- 210000002569 neuron Anatomy 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 210000001672 ovary Anatomy 0.000 description 3
- 239000003973 paint Substances 0.000 description 3
- 230000035515 penetration Effects 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 108020001580 protein domains Proteins 0.000 description 3
- 230000002285 radioactive effect Effects 0.000 description 3
- 210000004761 scalp Anatomy 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 210000004989 spleen cell Anatomy 0.000 description 3
- 210000004988 splenocyte Anatomy 0.000 description 3
- 230000002269 spontaneous effect Effects 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 239000013603 viral vector Substances 0.000 description 3
- WUAPFZMCVAUBPE-NJFSPNSNSA-N 188Re Chemical compound [188Re] WUAPFZMCVAUBPE-NJFSPNSNSA-N 0.000 description 2
- STQGQHZAVUOBTE-UHFFFAOYSA-N 7-Cyan-hept-2t-en-4,6-diinsaeure Natural products C1=2C(O)=C3C(=O)C=4C(OC)=CC=CC=4C(=O)C3=C(O)C=2CC(O)(C(C)=O)CC1OC1CC(N)C(O)C(C)O1 STQGQHZAVUOBTE-UHFFFAOYSA-N 0.000 description 2
- 101800000263 Acidic protein Proteins 0.000 description 2
- 244000303258 Annona diversifolia Species 0.000 description 2
- 235000002198 Annona diversifolia Nutrition 0.000 description 2
- 206010003445 Ascites Diseases 0.000 description 2
- 208000023275 Autoimmune disease Diseases 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 208000003174 Brain Neoplasms Diseases 0.000 description 2
- 241000282836 Camelus dromedarius Species 0.000 description 2
- UGFAIRIUMAVXCW-UHFFFAOYSA-N Carbon monoxide Chemical compound [O+]#[C-] UGFAIRIUMAVXCW-UHFFFAOYSA-N 0.000 description 2
- 241000700199 Cavia porcellus Species 0.000 description 2
- 241000282693 Cercopithecidae Species 0.000 description 2
- 208000018652 Closed Head injury Diseases 0.000 description 2
- 108020004635 Complementary DNA Chemical group 0.000 description 2
- 206010010301 Confusion and disorientation Diseases 0.000 description 2
- 206010010904 Convulsion Diseases 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- 241000699802 Cricetulus griseus Species 0.000 description 2
- XFXPMWWXUTWYJX-UHFFFAOYSA-N Cyanide Chemical compound N#[C-] XFXPMWWXUTWYJX-UHFFFAOYSA-N 0.000 description 2
- 101150074155 DHFR gene Proteins 0.000 description 2
- 102000001477 Deubiquitinating Enzymes Human genes 0.000 description 2
- 108010093668 Deubiquitinating Enzymes Proteins 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- 102100024746 Dihydrofolate reductase Human genes 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- RWSOTUBLDIXVET-UHFFFAOYSA-N Dihydrogen sulfide Chemical compound S RWSOTUBLDIXVET-UHFFFAOYSA-N 0.000 description 2
- 208000003164 Diplopia Diseases 0.000 description 2
- 241000283086 Equidae Species 0.000 description 2
- 241000283073 Equus caballus Species 0.000 description 2
- 108091029865 Exogenous DNA Proteins 0.000 description 2
- 241000282326 Felis catus Species 0.000 description 2
- 208000032843 Hemorrhage Diseases 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 102000004157 Hydrolases Human genes 0.000 description 2
- 108090000604 Hydrolases Proteins 0.000 description 2
- 206010021143 Hypoxia Diseases 0.000 description 2
- 206010022998 Irritability Diseases 0.000 description 2
- 108090001090 Lectins Chemical group 0.000 description 2
- 102000004856 Lectins Human genes 0.000 description 2
- 206010024453 Ligament sprain Diseases 0.000 description 2
- 208000026139 Memory disease Diseases 0.000 description 2
- 201000009906 Meningitis Diseases 0.000 description 2
- JJWSNOOGIUMOEE-UHFFFAOYSA-N Monomethylmercury Chemical compound [Hg]C JJWSNOOGIUMOEE-UHFFFAOYSA-N 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- 238000005481 NMR spectroscopy Methods 0.000 description 2
- 241000272144 Naja atra Species 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 241000282577 Pan troglodytes Species 0.000 description 2
- 241000283984 Rodentia Species 0.000 description 2
- GKLVYJBZJHMRIY-OUBTZVSYSA-N Technetium-99 Chemical compound [99Tc] GKLVYJBZJHMRIY-OUBTZVSYSA-N 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
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 2
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 2
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 240000008042 Zea mays Species 0.000 description 2
- 235000016383 Zea mays subsp huehuetenangensis Nutrition 0.000 description 2
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- DZBUGLKDJFMEHC-UHFFFAOYSA-N acridine Chemical class C1=CC=CC2=CC3=CC=CC=C3N=C21 DZBUGLKDJFMEHC-UHFFFAOYSA-N 0.000 description 2
- 238000007792 addition Methods 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 210000000628 antibody-producing cell Anatomy 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 239000010425 asbestos Substances 0.000 description 2
- 238000011504 assay standardization Methods 0.000 description 2
- 230000003140 astrocytic effect Effects 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 238000000225 bioluminescence resonance energy transfer Methods 0.000 description 2
- 229960000074 biopharmaceutical Drugs 0.000 description 2
- 238000001574 biopsy Methods 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- JCXGWMGPZLAOME-AKLPVKDBSA-N bismuth-212 Chemical compound [212Bi] JCXGWMGPZLAOME-AKLPVKDBSA-N 0.000 description 2
- 210000004204 blood vessel Anatomy 0.000 description 2
- 210000005013 brain tissue Anatomy 0.000 description 2
- 238000004364 calculation method Methods 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 229910002091 carbon monoxide Inorganic materials 0.000 description 2
- 210000000845 cartilage Anatomy 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 238000010382 chemical cross-linking Methods 0.000 description 2
- 239000013626 chemical specie Substances 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- ZPUCINDJVBIVPJ-LJISPDSOSA-N cocaine Chemical compound O([C@H]1C[C@@H]2CC[C@@H](N2C)[C@H]1C(=O)OC)C(=O)C1=CC=CC=C1 ZPUCINDJVBIVPJ-LJISPDSOSA-N 0.000 description 2
- 208000010877 cognitive disease Diseases 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- STQGQHZAVUOBTE-VGBVRHCVSA-N daunorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(C)=O)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 STQGQHZAVUOBTE-VGBVRHCVSA-N 0.000 description 2
- 230000034994 death Effects 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 108020001096 dihydrofolate reductase Proteins 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 239000003623 enhancer Substances 0.000 description 2
- 238000003094 enzyme-multiplied immunoassay technique Methods 0.000 description 2
- 206010015037 epilepsy Diseases 0.000 description 2
- 210000003743 erythrocyte Anatomy 0.000 description 2
- 210000003414 extremity Anatomy 0.000 description 2
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 2
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 2
- 230000037406 food intake Effects 0.000 description 2
- 239000007789 gas Substances 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 239000000833 heterodimer Substances 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 208000003906 hydrocephalus Diseases 0.000 description 2
- 229910000037 hydrogen sulfide Inorganic materials 0.000 description 2
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
- 230000007954 hypoxia Effects 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 238000003364 immunohistochemistry Methods 0.000 description 2
- 230000008676 import Effects 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 239000002917 insecticide Substances 0.000 description 2
- 210000003963 intermediate filament Anatomy 0.000 description 2
- 238000005304 joining Methods 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 230000008449 language Effects 0.000 description 2
- 239000002523 lectin Chemical group 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 235000009973 maize Nutrition 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 230000006984 memory degeneration Effects 0.000 description 2
- 208000023060 memory loss Diseases 0.000 description 2
- 230000003340 mental effect Effects 0.000 description 2
- RHCSKNNOAZULRK-UHFFFAOYSA-N mescaline Chemical compound COC1=CC(CCN)=CC(OC)=C1OC RHCSKNNOAZULRK-UHFFFAOYSA-N 0.000 description 2
- 208000030159 metabolic disease Diseases 0.000 description 2
- 238000001823 molecular biology technique Methods 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 238000002610 neuroimaging Methods 0.000 description 2
- 230000003472 neutralizing effect Effects 0.000 description 2
- 230000001473 noxious effect Effects 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 239000003960 organic solvent Substances 0.000 description 2
- 210000004197 pelvis Anatomy 0.000 description 2
- 230000000149 penetrating effect Effects 0.000 description 2
- 229940111202 pepsin Drugs 0.000 description 2
- 239000000816 peptidomimetic Substances 0.000 description 2
- 239000000575 pesticide Substances 0.000 description 2
- IEQIEDJGQAUEQZ-UHFFFAOYSA-N phthalocyanine Chemical compound N1C(N=C2C3=CC=CC=C3C(N=C3C4=CC=CC=C4C(=N4)N3)=N2)=C(C=CC=C2)C2=C1N=C1C2=CC=CC=C2C4=N1 IEQIEDJGQAUEQZ-UHFFFAOYSA-N 0.000 description 2
- 239000004033 plastic Substances 0.000 description 2
- 238000002600 positron emission tomography Methods 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 230000006337 proteolytic cleavage Effects 0.000 description 2
- RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 2
- 238000002708 random mutagenesis Methods 0.000 description 2
- 238000010188 recombinant method Methods 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000012340 reverse transcriptase PCR Methods 0.000 description 2
- WUAPFZMCVAUBPE-IGMARMGPSA-N rhenium-186 Chemical compound [186Re] WUAPFZMCVAUBPE-IGMARMGPSA-N 0.000 description 2
- 229910052895 riebeckite Inorganic materials 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 208000037974 severe injury Diseases 0.000 description 2
- 230000009528 severe injury Effects 0.000 description 2
- 238000002603 single-photon emission computed tomography Methods 0.000 description 2
- 208000019116 sleep disease Diseases 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 230000002194 synthesizing effect Effects 0.000 description 2
- 210000002435 tendon Anatomy 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 230000000472 traumatic effect Effects 0.000 description 2
- 102000003390 tumor necrosis factor Human genes 0.000 description 2
- 210000002700 urine Anatomy 0.000 description 2
- 101150084750 1 gene Proteins 0.000 description 1
- PNDPGZBMCMUPRI-HVTJNCQCSA-N 10043-66-0 Chemical compound [131I][131I] PNDPGZBMCMUPRI-HVTJNCQCSA-N 0.000 description 1
- CKRJGDYKYQUNIM-UHFFFAOYSA-N 3-fluoro-2,2-dimethylpropanoic acid Chemical compound FCC(C)(C)C(O)=O CKRJGDYKYQUNIM-UHFFFAOYSA-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
- HUDPLKWXRLNSPC-UHFFFAOYSA-N 4-aminophthalhydrazide Chemical compound O=C1NNC(=O)C=2C1=CC(N)=CC=2 HUDPLKWXRLNSPC-UHFFFAOYSA-N 0.000 description 1
- 102100031126 6-phosphogluconolactonase Human genes 0.000 description 1
- 108010029731 6-phosphogluconolactonase Proteins 0.000 description 1
- 108010066676 Abrin Proteins 0.000 description 1
- 206010063746 Accidental death Diseases 0.000 description 1
- 108010042708 Acetylmuramyl-Alanyl-Isoglutamine Proteins 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 241000272525 Anas platyrhynchos Species 0.000 description 1
- 241000272814 Anser sp. Species 0.000 description 1
- 208000025674 Anterior Cruciate Ligament injury Diseases 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 108020000948 Antisense Oligonucleotides Proteins 0.000 description 1
- 206010002942 Apathy Diseases 0.000 description 1
- 241000228254 Aspergillus restrictus Species 0.000 description 1
- 101000669426 Aspergillus restrictus Ribonuclease mitogillin Proteins 0.000 description 1
- 108090001008 Avidin Proteins 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
- 208000013883 Blast injury Diseases 0.000 description 1
- 201000004569 Blindness Diseases 0.000 description 1
- 208000007774 Broca Aphasia Diseases 0.000 description 1
- UJKPHYRXOLRVJJ-MLSVHJFASA-N CC(O)C1=C(C)/C2=C/C3=N/C(=C\C4=C(CCC(O)=O)C(C)=C(N4)/C=C4\N=C(\C=C\1/N\2)C(C)=C4C(C)O)/C(CCC(O)=O)=C3C Chemical compound CC(O)C1=C(C)/C2=C/C3=N/C(=C\C4=C(CCC(O)=O)C(C)=C(N4)/C=C4\N=C(\C=C\1/N\2)C(C)=C4C(C)O)/C(CCC(O)=O)=C3C UJKPHYRXOLRVJJ-MLSVHJFASA-N 0.000 description 1
- 206010008190 Cerebrovascular accident Diseases 0.000 description 1
- 241000283153 Cetacea Species 0.000 description 1
- 241000251730 Chondrichthyes Species 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 208000028698 Cognitive impairment Diseases 0.000 description 1
- 206010010214 Compression fracture Diseases 0.000 description 1
- 208000012514 Cumulative Trauma disease Diseases 0.000 description 1
- 101710112752 Cytotoxin Proteins 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- WEAHRLBPCANXCN-UHFFFAOYSA-N Daunomycin Natural products CCC1(O)CC(OC2CC(N)C(O)C(C)O2)c3cc4C(=O)c5c(OC)cccc5C(=O)c4c(O)c3C1 WEAHRLBPCANXCN-UHFFFAOYSA-N 0.000 description 1
- 208000009881 Decerebrate State Diseases 0.000 description 1
- 241000702421 Dependoparvovirus Species 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 206010061818 Disease progression Diseases 0.000 description 1
- 206010013142 Disinhibition Diseases 0.000 description 1
- 206010013486 Distractibility Diseases 0.000 description 1
- 206010013887 Dysarthria Diseases 0.000 description 1
- 229910052692 Dysprosium Inorganic materials 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 208000027534 Emotional disease Diseases 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 108010008177 Fd immunoglobulins Proteins 0.000 description 1
- 241000724791 Filamentous phage Species 0.000 description 1
- 238000000729 Fisher's exact test Methods 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 101710160621 Fusion glycoprotein F0 Proteins 0.000 description 1
- 108700004714 Gelonium multiflorum GEL Proteins 0.000 description 1
- 108700005000 Glial Fibrillary Acidic Proteins 0.000 description 1
- 108010018962 Glucosephosphate Dehydrogenase Proteins 0.000 description 1
- 229930186217 Glycolipid Natural products 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 102000018997 Growth Hormone Human genes 0.000 description 1
- 206010018852 Haematoma Diseases 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 1
- 101000690301 Homo sapiens Aldo-keto reductase family 1 member C4 Proteins 0.000 description 1
- 101001116548 Homo sapiens Protein CBFA2T1 Proteins 0.000 description 1
- 206010020880 Hypertrophy Diseases 0.000 description 1
- 206010050515 Hyposmia 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
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 208000026350 Inborn Genetic disease Diseases 0.000 description 1
- 102000000588 Interleukin-2 Human genes 0.000 description 1
- 108010002350 Interleukin-2 Proteins 0.000 description 1
- YQEZLKZALYSWHR-UHFFFAOYSA-N Ketamine Chemical compound C=1C=CC=C(Cl)C=1C1(NC)CCCCC1=O YQEZLKZALYSWHR-UHFFFAOYSA-N 0.000 description 1
- 244000207740 Lemna minor Species 0.000 description 1
- 235000006439 Lemna minor Nutrition 0.000 description 1
- 206010065433 Ligament rupture Diseases 0.000 description 1
- 241000883511 Lophophora williamsii Species 0.000 description 1
- 241000282560 Macaca mulatta Species 0.000 description 1
- 206010072970 Meniscus injury Diseases 0.000 description 1
- 206010027374 Mental impairment Diseases 0.000 description 1
- JEYCTXHKTXCGPB-UHFFFAOYSA-N Methaqualone Chemical compound CC1=CC=CC=C1N1C(=O)C2=CC=CC=C2N=C1C JEYCTXHKTXCGPB-UHFFFAOYSA-N 0.000 description 1
- 208000019695 Migraine disease Diseases 0.000 description 1
- 229910016629 MnBi Inorganic materials 0.000 description 1
- 206010027940 Mood altered Diseases 0.000 description 1
- 206010027951 Mood swings Diseases 0.000 description 1
- 206010028813 Nausea Diseases 0.000 description 1
- 101710204212 Neocarzinostatin Proteins 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 208000002193 Pain Diseases 0.000 description 1
- 208000007542 Paresis Diseases 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 241000009328 Perro Species 0.000 description 1
- 206010034703 Perseveration Diseases 0.000 description 1
- 206010034960 Photophobia Diseases 0.000 description 1
- 231100000742 Plant toxin Toxicity 0.000 description 1
- 208000010332 Plantar Fasciitis Diseases 0.000 description 1
- 235000001855 Portulaca oleracea Nutrition 0.000 description 1
- 206010036437 Posturing Diseases 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108700033844 Pseudomonas aeruginosa toxA Proteins 0.000 description 1
- QVDSEJDULKLHCG-UHFFFAOYSA-N Psilocybine Natural products C1=CC(OP(O)(O)=O)=C2C(CCN(C)C)=CNC2=C1 QVDSEJDULKLHCG-UHFFFAOYSA-N 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 208000006265 Renal cell carcinoma Diseases 0.000 description 1
- 208000027790 Rib fracture Diseases 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 208000024288 Rotator Cuff injury Diseases 0.000 description 1
- 238000011579 SCID mouse model Methods 0.000 description 1
- 208000004337 Salivary Gland Neoplasms Diseases 0.000 description 1
- 240000003946 Saponaria officinalis Species 0.000 description 1
- 108010084592 Saporins Proteins 0.000 description 1
- 102000005686 Serum Globulins Human genes 0.000 description 1
- 108010045362 Serum Globulins Proteins 0.000 description 1
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 1
- 208000028979 Skull fracture Diseases 0.000 description 1
- 244000061456 Solanum tuberosum Species 0.000 description 1
- 235000002595 Solanum tuberosum Nutrition 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 208000013201 Stress fracture Diseases 0.000 description 1
- 238000000692 Student's t-test Methods 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 208000002240 Tennis Elbow Diseases 0.000 description 1
- 208000009205 Tinnitus Diseases 0.000 description 1
- 102400001320 Transforming growth factor alpha Human genes 0.000 description 1
- 101800004564 Transforming growth factor alpha Proteins 0.000 description 1
- 102000013394 Troponin I Human genes 0.000 description 1
- 108010065729 Troponin I Proteins 0.000 description 1
- 206010047513 Vision blurred Diseases 0.000 description 1
- 206010047571 Visual impairment Diseases 0.000 description 1
- 241000282485 Vulpes vulpes Species 0.000 description 1
- 208000002579 Wernicke Aphasia Diseases 0.000 description 1
- 238000001793 Wilcoxon signed-rank test Methods 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 210000001015 abdomen Anatomy 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000002730 additional effect Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 229940009456 adriamycin Drugs 0.000 description 1
- 230000016571 aggressive behavior Effects 0.000 description 1
- 239000002776 alpha toxin Substances 0.000 description 1
- REDXJYDRNCIFBQ-UHFFFAOYSA-N aluminium(3+) Chemical compound [Al+3] REDXJYDRNCIFBQ-UHFFFAOYSA-N 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 210000004381 amniotic fluid Anatomy 0.000 description 1
- 239000003263 anabolic agent Substances 0.000 description 1
- 229940070021 anabolic steroids Drugs 0.000 description 1
- 210000003484 anatomy Anatomy 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 210000003423 ankle Anatomy 0.000 description 1
- 235000019558 anosmia Nutrition 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000001773 anti-convulsant effect Effects 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000001961 anticonvulsive agent Substances 0.000 description 1
- 229960003965 antiepileptics Drugs 0.000 description 1
- 229940127248 antinauseant drug Drugs 0.000 description 1
- 239000000074 antisense oligonucleotide Substances 0.000 description 1
- 238000012230 antisense oligonucleotides Methods 0.000 description 1
- 230000004594 appetite change Effects 0.000 description 1
- 230000037007 arousal Effects 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-L aspartate group Chemical group N[C@@H](CC(=O)[O-])C(=O)[O-] CKLJMWTZIZZHCS-REOHCLBHSA-L 0.000 description 1
- 238000002820 assay format Methods 0.000 description 1
- 238000011888 autopsy Methods 0.000 description 1
- VSRXQHXAPYXROS-UHFFFAOYSA-N azanide;cyclobutane-1,1-dicarboxylic acid;platinum(2+) Chemical compound [NH2-].[NH2-].[Pt+2].OC(=O)C1(C(O)=O)CCC1 VSRXQHXAPYXROS-UHFFFAOYSA-N 0.000 description 1
- 229940125717 barbiturate Drugs 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 230000006399 behavior Effects 0.000 description 1
- 229940049706 benzodiazepine Drugs 0.000 description 1
- 150000001557 benzodiazepines Chemical class 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
- 230000033228 biological regulation Effects 0.000 description 1
- 229940088623 biologically active substance Drugs 0.000 description 1
- JCXGWMGPZLAOME-RNFDNDRNSA-N bismuth-213 Chemical compound [213Bi] JCXGWMGPZLAOME-RNFDNDRNSA-N 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 210000001772 blood platelet Anatomy 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 230000036760 body temperature Effects 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- UHYPYGJEEGLRJD-UHFFFAOYSA-N cadmium(2+);selenium(2-) Chemical compound [Se-2].[Cd+2] UHYPYGJEEGLRJD-UHFFFAOYSA-N 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 229960004562 carboplatin Drugs 0.000 description 1
- 208000003295 carpal tunnel syndrome Diseases 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 210000005056 cell body Anatomy 0.000 description 1
- 238000012832 cell culture technique Methods 0.000 description 1
- 230000007910 cell fusion Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000033077 cellular process Effects 0.000 description 1
- 230000005754 cellular signaling Effects 0.000 description 1
- 210000003169 central nervous system Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 208000026106 cerebrovascular disease Diseases 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000013043 chemical agent Substances 0.000 description 1
- 230000003399 chemotactic effect Effects 0.000 description 1
- 238000000546 chi-square test Methods 0.000 description 1
- 239000012504 chromatography matrix Substances 0.000 description 1
- AYTAKQFHWFYBMA-UHFFFAOYSA-N chromium(IV) oxide Inorganic materials O=[Cr]=O AYTAKQFHWFYBMA-UHFFFAOYSA-N 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 229960003920 cocaine Drugs 0.000 description 1
- 230000007278 cognition impairment Effects 0.000 description 1
- 238000009225 cognitive behavioral therapy Methods 0.000 description 1
- 230000003920 cognitive function Effects 0.000 description 1
- 231100000870 cognitive problem Toxicity 0.000 description 1
- 230000001427 coherent effect Effects 0.000 description 1
- 230000006957 competitive inhibition Effects 0.000 description 1
- 230000006835 compression Effects 0.000 description 1
- 238000007906 compression Methods 0.000 description 1
- 238000011961 computed axial tomography Methods 0.000 description 1
- 238000013170 computed tomography imaging Methods 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 230000036461 convulsion Effects 0.000 description 1
- 238000009223 counseling Methods 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
- 238000012926 crystallographic analysis Methods 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 210000004292 cytoskeleton Anatomy 0.000 description 1
- 231100000599 cytotoxic agent Toxicity 0.000 description 1
- 239000002619 cytotoxin Substances 0.000 description 1
- 230000002354 daily effect Effects 0.000 description 1
- 229960000975 daunorubicin Drugs 0.000 description 1
- 230000000991 decompressive effect Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000002059 diagnostic imaging Methods 0.000 description 1
- 238000012631 diagnostic technique Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 238000002598 diffusion tensor imaging Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 230000005750 disease progression Effects 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 238000004821 distillation Methods 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000002934 diuretic Substances 0.000 description 1
- 229940030606 diuretics Drugs 0.000 description 1
- 208000002173 dizziness Diseases 0.000 description 1
- 208000029444 double vision Diseases 0.000 description 1
- 229960004679 doxorubicin Drugs 0.000 description 1
- 210000005069 ears Anatomy 0.000 description 1
- 230000002996 emotional effect Effects 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 239000002158 endotoxin Substances 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 231100000655 enterotoxin Toxicity 0.000 description 1
- 239000002532 enzyme inhibitor Substances 0.000 description 1
- 210000002409 epiglottis Anatomy 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 230000003203 everyday effect Effects 0.000 description 1
- 208000010771 expressive aphasia Diseases 0.000 description 1
- 210000003722 extracellular fluid Anatomy 0.000 description 1
- 230000004424 eye movement Effects 0.000 description 1
- 206010016256 fatigue Diseases 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 230000005293 ferrimagnetic effect Effects 0.000 description 1
- 239000002902 ferrimagnetic material Substances 0.000 description 1
- 230000005294 ferromagnetic effect Effects 0.000 description 1
- 239000003302 ferromagnetic material Substances 0.000 description 1
- 230000003619 fibrillary effect Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- UQSQSQZYBQSBJZ-UHFFFAOYSA-M fluorosulfonate Chemical compound [O-]S(F)(=O)=O UQSQSQZYBQSBJZ-UHFFFAOYSA-M 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000003500 gene array Methods 0.000 description 1
- 230000007274 generation of a signal involved in cell-cell signaling Effects 0.000 description 1
- 208000016361 genetic disease Diseases 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 230000002518 glial effect Effects 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 239000000380 hallucinogen Substances 0.000 description 1
- 208000016354 hearing loss disease Diseases 0.000 description 1
- 229960003569 hematoporphyrin Drugs 0.000 description 1
- 206010019465 hemiparesis Diseases 0.000 description 1
- 230000002949 hemolytic effect Effects 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 230000002962 histologic effect Effects 0.000 description 1
- 102000054751 human RUNX1T1 Human genes 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 210000004754 hybrid cell Anatomy 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 238000012872 hydroxylapatite chromatography Methods 0.000 description 1
- 238000003365 immunocytochemistry Methods 0.000 description 1
- 230000002998 immunogenetic effect Effects 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- APFVFJFRJDLVQX-AHCXROLUSA-N indium-111 Chemical compound [111In] APFVFJFRJDLVQX-AHCXROLUSA-N 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- SZVJSHCCFOBDDC-UHFFFAOYSA-N iron(II,III) oxide Inorganic materials O=[Fe]O[Fe]O[Fe]=O SZVJSHCCFOBDDC-UHFFFAOYSA-N 0.000 description 1
- 210000001503 joint Anatomy 0.000 description 1
- 229960003299 ketamine Drugs 0.000 description 1
- 210000003127 knee Anatomy 0.000 description 1
- 210000002414 leg Anatomy 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 210000003041 ligament Anatomy 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 229920006008 lipopolysaccharide Polymers 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 208000018883 loss of balance Diseases 0.000 description 1
- 231100000863 loss of memory Toxicity 0.000 description 1
- 231100000864 loss of vision Toxicity 0.000 description 1
- 208000018769 loss of vision Diseases 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 210000004880 lymph fluid Anatomy 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 239000006249 magnetic particle Substances 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 240000004308 marijuana Species 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000010339 medical test Methods 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 206010027191 meningioma Diseases 0.000 description 1
- 230000002175 menstrual effect Effects 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
- 229960002803 methaqualone Drugs 0.000 description 1
- 206010027599 migraine Diseases 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000009149 molecular binding Effects 0.000 description 1
- 239000003068 molecular probe Substances 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 230000007510 mood change Effects 0.000 description 1
- 230000004899 motility Effects 0.000 description 1
- 230000008693 nausea Effects 0.000 description 1
- QZGIWPZCWHMVQL-UIYAJPBUSA-N neocarzinostatin chromophore Chemical compound O1[C@H](C)[C@H](O)[C@H](O)[C@@H](NC)[C@H]1O[C@@H]1C/2=C/C#C[C@H]3O[C@@]3([C@@H]3OC(=O)OC3)C#CC\2=C[C@H]1OC(=O)C1=C(O)C=CC2=C(C)C=C(OC)C=C12 QZGIWPZCWHMVQL-UIYAJPBUSA-N 0.000 description 1
- 210000004498 neuroglial cell Anatomy 0.000 description 1
- 230000000926 neurological effect Effects 0.000 description 1
- 230000006764 neuronal dysfunction Effects 0.000 description 1
- 210000000607 neurosecretory system Anatomy 0.000 description 1
- 150000002826 nitrites Chemical class 0.000 description 1
- 230000001254 nonsecretory effect Effects 0.000 description 1
- 238000011580 nude mouse model Methods 0.000 description 1
- 230000000474 nursing effect Effects 0.000 description 1
- 206010029864 nystagmus Diseases 0.000 description 1
- 210000004248 oligodendroglia Anatomy 0.000 description 1
- 229940005483 opioid analgesics Drugs 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 238000004091 panning Methods 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 230000005298 paramagnetic effect Effects 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000001991 pathophysiological effect Effects 0.000 description 1
- 239000013610 patient sample Substances 0.000 description 1
- 238000000059 patterning Methods 0.000 description 1
- 125000001151 peptidyl group Chemical group 0.000 description 1
- 210000003200 peritoneal cavity Anatomy 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 230000002085 persistent effect Effects 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 229940080469 phosphocellulose Drugs 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 238000002428 photodynamic therapy Methods 0.000 description 1
- 239000003504 photosensitizing agent Substances 0.000 description 1
- 108060006184 phycobiliprotein Proteins 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 210000000280 pituicyte Anatomy 0.000 description 1
- 230000003169 placental effect Effects 0.000 description 1
- 239000003123 plant toxin Substances 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 230000000750 progressive effect Effects 0.000 description 1
- 230000004853 protein function Effects 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- QKTAAWLCLHMUTJ-UHFFFAOYSA-N psilocybin Chemical compound C1C=CC(OP(O)(O)=O)=C2C(CCN(C)C)=CN=C21 QKTAAWLCLHMUTJ-UHFFFAOYSA-N 0.000 description 1
- 150000003834 purine nucleoside derivatives Chemical class 0.000 description 1
- 229950010131 puromycin Drugs 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 239000002096 quantum dot Substances 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 208000026759 receptive aphasia Diseases 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000011514 reflex Effects 0.000 description 1
- 230000026416 response to pain Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 238000002702 ribosome display Methods 0.000 description 1
- 238000012502 risk assessment Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 210000004116 schwann cell Anatomy 0.000 description 1
- 210000002955 secretory cell Anatomy 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 230000001953 sensory effect Effects 0.000 description 1
- 230000021317 sensory perception Effects 0.000 description 1
- 230000014860 sensory perception of taste Effects 0.000 description 1
- 238000010008 shearing Methods 0.000 description 1
- 210000002832 shoulder Anatomy 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 208000022925 sleep disturbance Diseases 0.000 description 1
- 230000008454 sleep-wake cycle Effects 0.000 description 1
- 208000026473 slurred speech Diseases 0.000 description 1
- NRHMKIHPTBHXPF-TUJRSCDTSA-M sodium cholate Chemical compound [Na+].C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC([O-])=O)C)[C@@]2(C)[C@@H](O)C1 NRHMKIHPTBHXPF-TUJRSCDTSA-M 0.000 description 1
- 210000004872 soft tissue Anatomy 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 230000003393 splenic effect Effects 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 230000007103 stamina Effects 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 239000012089 stop solution Substances 0.000 description 1
- 238000013517 stratification Methods 0.000 description 1
- 231100000736 substance abuse Toxicity 0.000 description 1
- 208000011117 substance-related disease Diseases 0.000 description 1
- 229940124530 sulfonamide Drugs 0.000 description 1
- 150000003456 sulfonamides Chemical class 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000012353 t test Methods 0.000 description 1
- 229940056501 technetium 99m Drugs 0.000 description 1
- 210000001550 testis Anatomy 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 150000007970 thio esters Chemical class 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 231100000886 tinnitus Toxicity 0.000 description 1
- 230000009258 tissue cross reactivity Effects 0.000 description 1
- 238000012549 training Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 230000008736 traumatic injury Effects 0.000 description 1
- 229940121358 tyrosine kinase inhibitor Drugs 0.000 description 1
- 239000005483 tyrosine kinase inhibitor Substances 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- 230000004393 visual impairment Effects 0.000 description 1
- 230000001755 vocal effect Effects 0.000 description 1
- 230000002747 voluntary effect Effects 0.000 description 1
- 210000000707 wrist Anatomy 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
- 229950009268 zinostatin Drugs 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y301/00—Hydrolases acting on ester bonds (3.1)
- C12Y301/02—Thioester hydrolases (3.1.2)
- C12Y301/02015—Ubiquitin thiolesterase (3.1.2.15)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/46—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans from vertebrates
- G01N2333/47—Assays involving proteins of known structure or function as defined in the subgroups
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/916—Hydrolases (3) acting on ester bonds (3.1), e.g. phosphatases (3.1.3), phospholipases C or phospholipases D (3.1.4)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
- G01N2800/2871—Cerebrovascular disorders, e.g. stroke, cerebral infarct, cerebral haemorrhage, transient ischemic event
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/52—Predicting or monitoring the response to treatment, e.g. for selection of therapy based on assay results in personalised medicine; Prognosis
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Hematology (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Urology & Nephrology (AREA)
- General Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Medicinal Chemistry (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biotechnology (AREA)
- Cell Biology (AREA)
- General Physics & Mathematics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Pathology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Microbiology (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Peptides Or Proteins (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Magnetic Resonance Imaging Apparatus (AREA)
Applications Claiming Priority (7)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201762596805P | 2017-12-09 | 2017-12-09 | |
| US62/596,805 | 2017-12-09 | ||
| US201762611707P | 2017-12-29 | 2017-12-29 | |
| US62/611,707 | 2017-12-29 | ||
| US201862652734P | 2018-04-04 | 2018-04-04 | |
| US62/652,734 | 2018-04-04 | ||
| PCT/US2018/064587 WO2019113525A2 (en) | 2017-12-09 | 2018-12-07 | Methods for aiding in the diagnosis and evaluation of a subject who has sustained an orthopedic injury and that has or may have sustained an injury to the head, such as mild traumatic brain injury (tbi), using glial fibrillary acidic protein (gfap) and/or ubiquitin carboxy-terminal hydrolase l1 (uch-l1) |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA3067057A1 true CA3067057A1 (en) | 2019-06-13 |
Family
ID=64901115
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA3067057A Pending CA3067057A1 (en) | 2017-12-09 | 2018-12-07 | Methods for aiding in the diagnosis and evaluation of a subject who has sustained an orthopedic injury and that has or may have sustained an injury to the head, such as mild traumatic brain injury (tbi), using glial fibrillary acidic protein (gfap) and/or ubiquitin carboxy-terminal hydrolase l1 (uch-l1) |
Country Status (8)
| Country | Link |
|---|---|
| US (3) | US11022617B2 (enExample) |
| EP (1) | EP3721233A2 (enExample) |
| JP (1) | JP7344801B2 (enExample) |
| CN (1) | CN111094983A (enExample) |
| AU (1) | AU2018378971B9 (enExample) |
| BR (1) | BR112019028254A2 (enExample) |
| CA (1) | CA3067057A1 (enExample) |
| WO (1) | WO2019113525A2 (enExample) |
Families Citing this family (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU2009282117B2 (en) * | 2008-08-11 | 2016-05-12 | Banyan Biomarkers, Inc. | Biomarker detection process and assay of neurological condition |
| CA3052513A1 (en) | 2017-03-23 | 2018-09-27 | Abbott Laboratories | Methods for aiding in the diagnosis and determination of the extent of traumatic brain injury in a human subject using the early biomarker ubiquitin carboxy-terminal hydrolase l1 |
| AU2018250688B2 (en) | 2017-04-15 | 2024-07-04 | Abbott Laboratories | Methods for aiding in the hyperacute diagnosis and determination of traumatic brain injury in a human subject using early biomarkers |
| AU2018256845B2 (en) | 2017-04-28 | 2024-03-14 | Abbott Laboratories | Methods for aiding in the hyperacute diagnosis and determination of traumatic brain injury using early biomarkers on at least two samples from the same human subject |
| EP3631465A1 (en) | 2017-05-25 | 2020-04-08 | Abbott Laboratories | Methods for aiding in the determination of whether to perform imaging on a human subject who has sustained or may have sustained an injury to the head using early biomarkers |
| AU2018275236B2 (en) | 2017-05-30 | 2024-11-07 | Abbott Laboratories | Methods for aiding in diagnosing and evaluating a mild traumatic brain injury in a human subject using cardiac troponin I |
| JP7454945B2 (ja) | 2017-07-03 | 2024-03-25 | アボット・ラボラトリーズ | 血液中のユビキチンカルボキシ末端ヒドロラーゼｌ１レベルを測定するための、改善された方法 |
| EP3721233A2 (en) | 2017-12-09 | 2020-10-14 | Abbott Laboratories | Methods for aiding in the diagnosis and evaluation of a subject who has sustained an orthopedic injury and that has or may have sustained an injury to the head, such as mild traumatic brain injury (tbi), using glial fibrillary acidic protein (gfap) and/or ubiquitin carboxy-terminal hydrolase l1 (uch-l1) |
| CA3067055A1 (en) * | 2017-12-09 | 2019-06-13 | Abbott Laboratories | Methods for aiding in diagnosing and evaluating a traumatic brain injury in a human subject using a combination of gfap and uch-l1 |
| US20190383832A1 (en) | 2017-12-29 | 2019-12-19 | Abbott Laboratories | Novel biomarkers and methods for diagnosing and evaluating traumatic brain injury |
| US20240012012A1 (en) * | 2020-12-01 | 2024-01-11 | Meredith Hay | Biomarker and treatment for vascular cognitive impairment and related conditions |
| BR112023024169A2 (pt) * | 2021-05-18 | 2024-02-06 | Abbott Lab | Métodos para avaliar lesão cerebral em um indivíduo pediátrico |
| EP4528280A3 (en) * | 2021-06-14 | 2025-07-02 | Abbott Laboratories | Methods of diagnosing or aiding in diagnosis of brain injury caused by acoustic energy, electromagnetic energy, an over pressurization wave, and/or blast wind |
| WO2023034777A1 (en) * | 2021-08-31 | 2023-03-09 | Abbott Laboratories | Methods and systems of diagnosing brain injury |
| CN118715440A (zh) * | 2021-08-31 | 2024-09-27 | 雅培实验室 | 诊断脑损伤的方法和系统 |
| EP4409294A1 (en) * | 2021-09-30 | 2024-08-07 | Abbott Laboratories | Methods and systems of diagnosing brain injury |
| FI130340B (en) * | 2022-02-22 | 2023-06-29 | Medicortex Finland Oy | Procedure for the diagnosis of traumatic brain injury |
| WO2024006876A1 (en) | 2022-06-29 | 2024-01-04 | Abbott Laboratories | Magnetic point-of-care systems and assays for determining gfap in biological samples |
| CN118707112B (zh) * | 2024-08-28 | 2024-12-13 | 浙江格物致知生物科技有限公司 | 一种gfap、nfl和uch-l1联合检测试剂盒及其用于脑创伤早期检测 |
Family Cites Families (152)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4554101A (en) | 1981-01-09 | 1985-11-19 | New York Blood Center, Inc. | Identification and preparation of epitopes on antigens and allergens on the basis of hydrophilicity |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| DE3590766C2 (enExample) | 1985-03-30 | 1991-01-10 | Marc Genf/Geneve Ch Ballivet | |
| US6492107B1 (en) | 1986-11-20 | 2002-12-10 | Stuart Kauffman | Process for obtaining DNA, RNA, peptides, polypeptides, or protein, by recombinant DNA technique |
| US5618920A (en) | 1985-11-01 | 1997-04-08 | Xoma Corporation | Modular assembly of antibody genes, antibodies prepared thereby and use |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US5635600A (en) | 1986-07-07 | 1997-06-03 | Trustees Of Dartmouth College | Bifunctional and heteroantibodies specific for the high affinity Fc receptor for immunoglobulin G on human mononuclear phagocytes |
| US4704692A (en) | 1986-09-02 | 1987-11-03 | Ladner Robert C | Computer based system and method for determining and displaying possible chemical structures for converting double- or multiple-chain polypeptides to single-chain polypeptides |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| DE3750503T2 (de) | 1986-10-22 | 1995-02-09 | Abbott Lab | Chemilumineszierende Acridinium- und Phenantridiniumsalze. |
| EP0279582A3 (en) | 1987-02-17 | 1989-10-18 | Pharming B.V. | Dna sequences to target proteins to the mammary gland for efficient secretion |
| US5258498A (en) | 1987-05-21 | 1993-11-02 | Creative Biomolecules, Inc. | Polypeptide linkers for production of biosynthetic proteins |
| US4873316A (en) | 1987-06-23 | 1989-10-10 | Biogen, Inc. | Isolation of exogenous recombinant proteins from the milk of transgenic mammals |
| US5006309A (en) | 1988-04-22 | 1991-04-09 | Abbott Laboratories | Immunoassay device with liquid transfer between wells by washing |
| US5089424A (en) | 1988-06-14 | 1992-02-18 | Abbott Laboratories | Method and apparatus for heterogeneous chemiluminescence assay |
| AU4308689A (en) | 1988-09-02 | 1990-04-02 | Protein Engineering Corporation | Generation and selection of recombinant varied binding proteins |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| US5241070A (en) | 1988-09-26 | 1993-08-31 | Ciba Corning Diagnostics Corp. | Nucleophilic polysubstituted aryl acridinium esters and uses thereof |
| US5063081A (en) | 1988-11-14 | 1991-11-05 | I-Stat Corporation | Method of manufacturing a plurality of uniform microfabricated sensing devices having an immobilized ligand receptor |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5028535A (en) | 1989-01-10 | 1991-07-02 | Biosite Diagnostics, Inc. | Threshold ligand-receptor assay |
| US5939272A (en) | 1989-01-10 | 1999-08-17 | Biosite Diagnostics Incorporated | Non-competitive threshold ligand-receptor assays |
| DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| US5780225A (en) | 1990-01-12 | 1998-07-14 | Stratagene | Method for generating libaries of antibody genes comprising amplification of diverse antibody DNAs and methods for using these libraries for the production of diverse antigen combining molecules |
| AU7247191A (en) | 1990-01-11 | 1991-08-05 | Molecular Affinities Corporation | Production of antibodies using gene libraries |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| ATE356869T1 (de) | 1990-01-12 | 2007-04-15 | Amgen Fremont Inc | Bildung von xenogenen antikörpern |
| US5922615A (en) | 1990-03-12 | 1999-07-13 | Biosite Diagnostics Incorporated | Assay devices comprising a porous capture membrane in fluid-withdrawing contact with a nonabsorbent capillary network |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| ES2139598T3 (es) | 1990-07-10 | 2000-02-16 | Medical Res Council | Procedimientos para la produccion de miembros de parejas de union especifica. |
| EP0542810A1 (en) | 1990-08-02 | 1993-05-26 | B.R. Centre Limited | Methods for the production of proteins with a desired function |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| WO1992005282A1 (en) | 1990-09-14 | 1992-04-02 | Biosite Diagnostics, Inc. | Antibodies to complexes of ligand receptors and ligands and their utility in ligand-receptor assays |
| US5698426A (en) | 1990-09-28 | 1997-12-16 | Ixsys, Incorporated | Surface expression libraries of heteromeric receptors |
| WO1992009690A2 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| ES2330052T3 (es) | 1991-03-01 | 2009-12-03 | Dyax Corporation | Proteina quimerica que comprende micro-proteinas que tienen dos o mas puentes disulfuro y relaizaciones de las mismas. |
| CA2107899A1 (en) | 1991-04-10 | 1992-10-11 | Gunars Edwin Valkirs | Novel conjugates and assays for simultaneous detection of multiple ligands |
| FI934437L (fi) | 1991-04-10 | 1993-11-22 | Biosite Diagnostics Inc | Crosstalk-inhibitorer och deras anvaendning |
| ATE414768T1 (de) | 1991-04-10 | 2008-12-15 | Scripps Research Inst | Bibliotheken heterodimerer rezeptoren mittels phagemiden |
| CA2069530A1 (en) | 1991-06-03 | 1992-12-04 | Cass J. Grandone | Reagent pack for immunoassays |
| AU2238292A (en) | 1991-06-14 | 1993-01-12 | Xoma Corporation | Microbially-produced antibody fragments and their conjugates |
| DE4122599C2 (de) | 1991-07-08 | 1993-11-11 | Deutsches Krebsforsch | Phagemid zum Screenen von Antikörpern |
| EP1136556B1 (en) | 1991-11-25 | 2005-06-08 | Enzon, Inc. | Method of producing multivalent antigen-binding proteins |
| ES2227512T3 (es) | 1991-12-02 | 2005-04-01 | Medical Research Council | Produccion de anticuerpos contra auto-antigenos a partir de repertorios de segmentos de anticuerpos fijados en un fago. |
| EP1291360A1 (en) | 1991-12-13 | 2003-03-12 | Xoma Corporation | Methods and materials for preparation of modified antibody variable domains and therapeutic uses thereof |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| US5352803A (en) | 1992-03-30 | 1994-10-04 | Abbott Laboratories | 5(6)-methyl substituted fluorescein derivatives |
| ES2198823T3 (es) | 1992-03-30 | 2004-02-01 | Abbott Laboratories | Reactivos que permiten la deteccion y la cuantificacion de la tiroxina en muestras de fluido. |
| US6143576A (en) | 1992-05-21 | 2000-11-07 | Biosite Diagnostics, Inc. | Non-porous diagnostic devices for the controlled movement of reagents |
| US6019944A (en) | 1992-05-21 | 2000-02-01 | Biosite Diagnostics, Inc. | Diagnostic devices and apparatus for the controlled movement of reagents without membranes |
| SG48760A1 (en) | 1992-07-24 | 2003-03-18 | Abgenix Inc | Generation of xenogenetic antibodies |
| US5824799A (en) | 1993-09-24 | 1998-10-20 | Biosite Diagnostics Incorporated | Hybrid phthalocyanine derivatives and their uses |
| JPH09506262A (ja) | 1993-12-08 | 1997-06-24 | ジェンザイム・コーポレイション | 特異的抗体の製造方法 |
| US5827690A (en) | 1993-12-20 | 1998-10-27 | Genzyme Transgenics Corporatiion | Transgenic production of antibodies in milk |
| PT1231268E (pt) | 1994-01-31 | 2005-11-30 | Univ Boston | Bancos de anticorpos policlonais |
| DK0749325T3 (da) | 1994-03-07 | 2002-10-07 | Medarex Inc | Bispecifikke molekyler med klinisk anvendelse |
| US5516637A (en) | 1994-06-10 | 1996-05-14 | Dade International Inc. | Method involving display of protein binding pairs on the surface of bacterial pili and bacteriophage |
| US6111166A (en) | 1994-09-19 | 2000-08-29 | Medarex, Incorporated | Transgenic mice expressing human Fcα and β receptors |
| US6130364A (en) | 1995-03-29 | 2000-10-10 | Abgenix, Inc. | Production of antibodies using Cre-mediated site-specific recombination |
| US6091001A (en) | 1995-03-29 | 2000-07-18 | Abgenix, Inc. | Production of antibodies using Cre-mediated site-specific recombination |
| EP0826034A4 (en) | 1995-04-21 | 2002-06-19 | Cell Genesys Inc | PRODUCTION OF LARGE GENOMIC DNA DELETIONS |
| ATE390933T1 (de) | 1995-04-27 | 2008-04-15 | Amgen Fremont Inc | Aus immunisierten xenomäusen stammende menschliche antikörper gegen il-8 |
| AU2466895A (en) | 1995-04-28 | 1996-11-18 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US6410690B1 (en) | 1995-06-07 | 2002-06-25 | Medarex, Inc. | Therapeutic compounds comprised of anti-Fc receptor antibodies |
| JP2978435B2 (ja) | 1996-01-24 | 1999-11-15 | チッソ株式会社 | アクリロキシプロピルシランの製造方法 |
| BRPI9707379C8 (pt) | 1996-02-09 | 2017-12-12 | Abbott Biotech Ltd | composições farmacêuticas compreendendo anticorpo humano recombinante geneticamente engenheirado, e anticorpo humano recombinante geneticamente engenheirado. |
| US5714352A (en) | 1996-03-20 | 1998-02-03 | Xenotech Incorporated | Directed switch-mediated DNA recombination |
| US6699658B1 (en) | 1996-05-31 | 2004-03-02 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US5922845A (en) | 1996-07-11 | 1999-07-13 | Medarex, Inc. | Therapeutic multispecific compounds comprised of anti-Fcα receptor antibodies |
| US5916771A (en) | 1996-10-11 | 1999-06-29 | Abgenix, Inc. | Production of a multimeric protein by cell fusion method |
| US6113855A (en) | 1996-11-15 | 2000-09-05 | Biosite Diagnostics, Inc. | Devices comprising multiple capillarity inducing surfaces |
| EP2314625B1 (en) | 1996-12-03 | 2014-05-07 | Amgen Fremont Inc. | Transgenic mammals having human Ig loci including plural VH and Vkappa regions and antibodies produced therefrom |
| US6017517A (en) | 1996-12-18 | 2000-01-25 | The Dial Corporation | Method for treating human nails |
| CA2278786C (en) | 1997-01-21 | 2010-07-20 | The General Hospital Corporation | Selection of proteins using rna-protein fusions |
| US5947124A (en) | 1997-03-11 | 1999-09-07 | Biosite Diagnostics Incorporated | Diagnostic for determining the time of a heart attack |
| US6235883B1 (en) | 1997-05-05 | 2001-05-22 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
| EP1044263A2 (en) | 1997-12-02 | 2000-10-18 | Medarex, Inc. | CELLS EXPRESSING ANTI-Fc RECEPTOR BINDING COMPONENTS |
| JP2002505097A (ja) | 1998-03-03 | 2002-02-19 | アブジェニックス インク． | 治療薬としてのｃｄ１４７結合分子 |
| US20020029391A1 (en) | 1998-04-15 | 2002-03-07 | Claude Geoffrey Davis | Epitope-driven human antibody production and gene expression profiling |
| WO2000009560A2 (en) | 1998-08-17 | 2000-02-24 | Abgenix, Inc. | Generation of modified molecules with increased serum half-lives |
| EP1135498B1 (en) | 1998-11-18 | 2008-01-23 | Genentech, Inc. | Antibody variants with higher binding affinity compared to parent antibodies |
| CA2356215C (en) | 1998-12-23 | 2015-11-24 | Pfizer Inc. | Human monoclonal antibodies to ctla-4 |
| US6231768B1 (en) | 1999-01-19 | 2001-05-15 | Nalco Chemical Company | Rheology modification of settled solids in mineral processing |
| US6914128B1 (en) | 1999-03-25 | 2005-07-05 | Abbott Gmbh & Co. Kg | Human antibodies that bind human IL-12 and methods for producing |
| CN101333256A (zh) | 1999-03-25 | 2008-12-31 | 艾博特股份有限两合公司 | 结合人il-12的人抗体及其生产方法 |
| WO2001014424A2 (en) | 1999-08-24 | 2001-03-01 | Medarex, Inc. | Human ctla-4 antibodies and their uses |
| US6438498B1 (en) | 2000-02-10 | 2002-08-20 | I-Stat Corporation | System, method and computer implemented process for assaying coagulation in fluid samples |
| HUP0300423A3 (en) | 2000-02-10 | 2008-07-28 | Abbott Lab | Antibodies that bind human interleukin-18 and methods of making and using |
| IL153567A0 (en) | 2000-06-29 | 2003-07-06 | Abbott Lab | Dual specificity antibodies and methods of making and using |
| US20030199000A1 (en) | 2001-08-20 | 2003-10-23 | Valkirs Gunars E. | Diagnostic markers of stroke and cerebral injury and methods of use thereof |
| DK1438400T3 (da) | 2001-10-01 | 2009-10-05 | Dyax Corp | Flerkædede eukaryote display-vektorer og anvendelser deraf |
| US7419821B2 (en) | 2002-03-05 | 2008-09-02 | I-Stat Corporation | Apparatus and methods for analyte measurement and immunoassay |
| US20060134713A1 (en) | 2002-03-21 | 2006-06-22 | Lifescan, Inc. | Biosensor apparatus and methods of use |
| US20040018577A1 (en) | 2002-07-29 | 2004-01-29 | Emerson Campbell John Lewis | Multiple hybrid immunoassay |
| US7682833B2 (en) | 2003-09-10 | 2010-03-23 | Abbott Point Of Care Inc. | Immunoassay device with improved sample closure |
| US7723099B2 (en) | 2003-09-10 | 2010-05-25 | Abbott Point Of Care Inc. | Immunoassay device with immuno-reference electrode |
| EP2357477B1 (en) | 2003-09-20 | 2017-11-08 | Electrophoretics Limited | Diagnostic method for brain damage-related disorders based on the detection of NDKA |
| ES2367311T3 (es) | 2004-04-15 | 2011-11-02 | University Of Florida Research Foundation, Inc. | Productos de degradación proteolítica de map-2 como biomarcadores de diagnóstico para las lesiones neurales. |
| WO2005106038A2 (en) | 2004-04-15 | 2005-11-10 | University Of Florida Research Foundation, Inc. | Neural proteins as biomarkers for nervous system injury and other neural disorders |
| US8492107B2 (en) | 2004-04-15 | 2013-07-23 | University Of Florida Research Foundation, Inc. | Neural proteins as biomarkers for nervous system injury and other neural disorders |
| US20140303041A1 (en) | 2004-04-15 | 2014-10-09 | University Of Florida Research Foundation Inc. | In vitro diagnostic devices for nervous system injury and other neural disorders |
| JP2008526251A (ja) | 2005-01-18 | 2008-07-24 | バイオセプト インコーポレイティッド | パターン化されたポストを有するマイクロチャネルを用いた細胞分離 |
| RU2423073C2 (ru) | 2005-07-14 | 2011-07-10 | Нано-Дайтек Корпорейшн | Микрофлюидные устройства и способы их подготовки и применения |
| US7612181B2 (en) | 2005-08-19 | 2009-11-03 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| EP2500352A1 (en) | 2005-08-19 | 2012-09-19 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| AU2009212463A1 (en) | 2008-02-04 | 2009-08-13 | Banyan Biomarkers, Inc. | Process to diagnose or treat brain injury |
| US20140342381A1 (en) | 2008-08-11 | 2014-11-20 | Banyan Biomarkers, Inc. | Devices and methods for biomarker detection process and assay of neurological condition |
| AU2009282117B2 (en) * | 2008-08-11 | 2016-05-12 | Banyan Biomarkers, Inc. | Biomarker detection process and assay of neurological condition |
| PL2403645T3 (pl) | 2009-03-06 | 2017-05-31 | President And Fellows Of Harvard College | Mikroprzepływowe, elektrochemiczne urządzenia |
| US20170315136A9 (en) | 2009-06-19 | 2017-11-02 | Banyan Biomarkers, Inc. | Biomarker assay of neurological condition |
| CA2766057A1 (en) * | 2009-06-19 | 2010-12-23 | Banyan Biomarkers, Inc. | Biomarker assay of neurological condition |
| US20120202231A1 (en) | 2009-07-18 | 2012-08-09 | Kevin Ka-Wang Wang | Synergistic biomarker assay of neurological condition using s-100b |
| JP5909447B2 (ja) | 2009-09-14 | 2016-04-26 | バンヤン・バイオマーカーズ・インコーポレーテッド | ニューロン損傷診断のためのマイクロｒｎａ、自己抗体およびタンパク質マーカー |
| WO2011160096A2 (en) | 2010-06-17 | 2011-12-22 | Banyan Biomarkers, Inc. | Glial fibrillary acidic protein, autoantigens and autoantibodies thereto as biomarkers of neural injury or neurological disorder or condition |
| US9746481B2 (en) | 2010-10-14 | 2017-08-29 | The Johns Hopkins University | Biomarkers of brain injury |
| WO2012170998A1 (en) | 2011-06-10 | 2012-12-13 | Cornell University | Immobilized protein system for rapid and enhanced multiplexed diagnostics |
| US20120322682A1 (en) | 2011-06-20 | 2012-12-20 | William Marsh Rice University | Brain injury biomarker panel |
| US20140370531A1 (en) | 2011-12-14 | 2014-12-18 | University Of Rochester | Method of diagnosing mild traumatic brain injury |
| WO2014124174A2 (en) | 2013-02-08 | 2014-08-14 | Children's Hospital Los Angeles | Circulating bmec and related cells as biomarkers of cns diseases associated with the blood-brain-barrier disorders |
| US9157910B2 (en) | 2013-03-15 | 2015-10-13 | Abbott Laboratories | Assay with increased dynamic range |
| WO2014194329A1 (en) | 2013-05-31 | 2014-12-04 | Banyan Biomarkers, Inc. | NEURAL SPECIFIC S100β FOR BIOMARKER ASSAYS AND DEVICES FOR DETECTION OF A NEUROLOGICAL CONDITION |
| US9265441B2 (en) | 2013-07-12 | 2016-02-23 | Siemens Aktiengesellschaft | Assessment of traumatic brain injury |
| EP3022322A4 (en) * | 2013-07-17 | 2017-05-17 | The Johns Hopkins University | A multi-protein biomarker assay for brain injury detection and outcome |
| WO2015066211A1 (en) | 2013-10-29 | 2015-05-07 | Banyan Biomarkers, Inc. | Uch-l1 isoforms, assays and devices for detection of a neurological condition |
| US20150224499A1 (en) | 2014-02-13 | 2015-08-13 | SFC Fluidics, Inc. | Automated Microfluidic Sample Analyzer Platforms for Point of Care |
| WO2015157300A1 (en) * | 2014-04-07 | 2015-10-15 | Iron Horse Diagnostics, Inc | Traumatic brain injury and neurodegenerative biomarkers, methods, and systems |
| BR112017005252B1 (pt) | 2014-09-22 | 2023-12-26 | Japan Science And Technology Agency | Método para detecção de molécula alvo e kit para utilização no referido método |
| AU2015330355B2 (en) * | 2014-10-06 | 2021-09-23 | Fundacio Hospital Universitari Vall D'hebron - Institut De Recerca | Markers and their use in brain injury |
| CN107690582B (zh) | 2015-04-03 | 2023-10-20 | 雅培制药有限公司 | 用于样品分析的装置和方法 |
| RU2712610C2 (ru) | 2015-04-03 | 2020-01-29 | Эбботт Лэборетриз | Устройства и способы для анализа образца |
| FI20155280L (fi) | 2015-04-15 | 2016-10-16 | Medicortex Finland Oy | Aivovamman prognostisia ja diagnostisia glykaanipohjaisia biomarkkereita |
| WO2016196522A1 (en) | 2015-05-29 | 2016-12-08 | Cedars-Sinai Medical Center | Correlated peptides for quantitative mass spectrometry |
| CN105085629A (zh) | 2015-08-12 | 2015-11-25 | 浙江聚康生物工程有限公司 | 人gfap抗原决定簇多肽、抗体及其体外诊断试剂盒 |
| JP2019535015A (ja) | 2016-10-03 | 2019-12-05 | アボット・ラボラトリーズＡｂｂｏｔｔ Ｌａｂｏｒａｔｏｒｉｅｓ | 患者サンプルにおけるｇｆａｐ状況を評価する改善された方法 |
| WO2018081649A1 (en) | 2016-10-28 | 2018-05-03 | Banyan Biomarkers, Inc. | Antibodies to ubiquitin c-terminal hydrolase l1 (uch-l1) and glial fibrillary acidic protein (gfap) and related methods |
| WO2018136825A1 (en) | 2017-01-19 | 2018-07-26 | Cedars-Sinai Medical Center | Highly multiplexed and mass spectrometry based methods to measuring 72 human proteins |
| CA3052513A1 (en) | 2017-03-23 | 2018-09-27 | Abbott Laboratories | Methods for aiding in the diagnosis and determination of the extent of traumatic brain injury in a human subject using the early biomarker ubiquitin carboxy-terminal hydrolase l1 |
| AU2018250688B2 (en) * | 2017-04-15 | 2024-07-04 | Abbott Laboratories | Methods for aiding in the hyperacute diagnosis and determination of traumatic brain injury in a human subject using early biomarkers |
| AU2018256845B2 (en) * | 2017-04-28 | 2024-03-14 | Abbott Laboratories | Methods for aiding in the hyperacute diagnosis and determination of traumatic brain injury using early biomarkers on at least two samples from the same human subject |
| EP3630804A4 (en) | 2017-05-23 | 2021-06-16 | Brainbox Solutions, Inc. | BIOMARKER CONCENTRATIONS AND NEURO IMAGING FOR DETECTION, MONITORING AND TREATMENT OF BRAIN INJURY OR TRAUMA |
| EP3631465A1 (en) | 2017-05-25 | 2020-04-08 | Abbott Laboratories | Methods for aiding in the determination of whether to perform imaging on a human subject who has sustained or may have sustained an injury to the head using early biomarkers |
| AU2018275236B2 (en) | 2017-05-30 | 2024-11-07 | Abbott Laboratories | Methods for aiding in diagnosing and evaluating a mild traumatic brain injury in a human subject using cardiac troponin I |
| CN107202890A (zh) * | 2017-05-31 | 2017-09-26 | 湖州华远生物技术有限公司 | 用于轻中度脑损伤的快速诊断试剂及含有该试剂的试剂盒及该试剂盒的制备和检测方法 |
| US20190091687A1 (en) | 2017-09-28 | 2019-03-28 | Maha Abdullah A. Alhasnani | Safe blood pregnancy test at home |
| EP3721233A2 (en) | 2017-12-09 | 2020-10-14 | Abbott Laboratories | Methods for aiding in the diagnosis and evaluation of a subject who has sustained an orthopedic injury and that has or may have sustained an injury to the head, such as mild traumatic brain injury (tbi), using glial fibrillary acidic protein (gfap) and/or ubiquitin carboxy-terminal hydrolase l1 (uch-l1) |
| CA3067055A1 (en) | 2017-12-09 | 2019-06-13 | Abbott Laboratories | Methods for aiding in diagnosing and evaluating a traumatic brain injury in a human subject using a combination of gfap and uch-l1 |
| US20190383832A1 (en) | 2017-12-29 | 2019-12-19 | Abbott Laboratories | Novel biomarkers and methods for diagnosing and evaluating traumatic brain injury |
| US20190302127A1 (en) | 2018-03-30 | 2019-10-03 | Sysmex Corporation | Method for diagnosing traumatic brain injury |
| WO2019199871A1 (en) | 2018-04-10 | 2019-10-17 | Quanterix Corporation | Quantification of neurofilament light chain in physiological samples |
| WO2021026261A1 (en) | 2019-08-05 | 2021-02-11 | Auer Precision Company, Inc. | Microfluidic passive plasma separation device and method |
| KR102464243B1 (ko) | 2020-04-01 | 2022-11-08 | 프리시젼바이오 주식회사 | 외상성 뇌손상 바이오마커 검출용 시분해 형광분석 측방유동 분석장치 및 이를 이용한 외상성 뇌손상 바이오마커 측정방법 |
-
2018
- 2018-12-07 EP EP18826899.9A patent/EP3721233A2/en not_active Withdrawn
- 2018-12-07 JP JP2019572018A patent/JP7344801B2/ja active Active
- 2018-12-07 BR BR112019028254-8A patent/BR112019028254A2/pt unknown
- 2018-12-07 WO PCT/US2018/064587 patent/WO2019113525A2/en not_active Ceased
- 2018-12-07 US US16/213,898 patent/US11022617B2/en active Active
- 2018-12-07 AU AU2018378971A patent/AU2018378971B9/en active Active
- 2018-12-07 CA CA3067057A patent/CA3067057A1/en active Pending
- 2018-12-07 CN CN201880044557.1A patent/CN111094983A/zh active Pending
-
2021
- 2021-05-10 US US17/316,267 patent/US12105098B2/en active Active
-
2024
- 2024-08-14 US US18/804,253 patent/US20250020666A1/en active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| US20210356477A1 (en) | 2021-11-18 |
| JP7344801B2 (ja) | 2023-09-14 |
| WO2019113525A3 (en) | 2019-07-11 |
| US11022617B2 (en) | 2021-06-01 |
| AU2018378971B9 (en) | 2025-04-17 |
| BR112019028254A2 (pt) | 2020-07-14 |
| US12105098B2 (en) | 2024-10-01 |
| US20250020666A1 (en) | 2025-01-16 |
| AU2018378971A1 (en) | 2020-01-02 |
| EP3721233A2 (en) | 2020-10-14 |
| WO2019113525A2 (en) | 2019-06-13 |
| CN111094983A (zh) | 2020-05-01 |
| US20190242906A1 (en) | 2019-08-08 |
| JP2021505843A (ja) | 2021-02-18 |
| AU2018378971B2 (en) | 2025-04-03 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US12105100B2 (en) | Methods for aiding in diagnosing and evaluating a traumatic brain injury in a human subject using a combination of GFAP and UCH-L1 | |
| US20250020665A1 (en) | Methods for aiding in the determination of whether to perform imaging on a human subject who has sustained or may have sustained an injury to the head using early biomarkers | |
| US20250020672A1 (en) | Methods for aiding in the hyperacute diagnosis and determination of traumatic brain injury in a human subject using early biomarkers | |
| US12105098B2 (en) | Methods for aiding in the diagnosis and evaluation of a subject who has sustained an orthopedic injury and that has or may have sustained an injury to the head, such as mild traumatic brain injury (TBI), using glial fibrillary acidic protein (GFAP) and/or ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) | |
| US20250020649A1 (en) | Methods for aiding in the hyperacute diagnosis and determination of traumatic brain injury using early biomarkers on at least two samples from the same human subject | |
| CA3059601A1 (en) | Methods for aiding in diagnosing and evaluating a mild traumatic brain injury in a human subject using cardiac troponin i and early biomarkers | |
| EP4396587A1 (en) | Methods and systems of diagnosing brain injury | |
| US20220381796A1 (en) | Methods of evaluating brain injury in a pediatric subject | |
| CA3053409C (en) | Methods for aiding in the hyperacute diagnosis and determination of traumatic brain injury in a human subject using early biomarkers |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |
Effective date: 20220124 |
|
| EEER | Examination request |
Effective date: 20220124 |
|
| EEER | Examination request |
Effective date: 20220124 |
|
| EEER | Examination request |
Effective date: 20220124 |
|
| EEER | Examination request |
Effective date: 20220124 |
|
| EEER | Examination request |
Effective date: 20220124 |
|
| EEER | Examination request |
Effective date: 20220124 |