HUE032518T2 - Vizsgálati eljárás endoszomális transzport vizsgálatára - Google Patents
Vizsgálati eljárás endoszomális transzport vizsgálatára Download PDFInfo
- Publication number
- HUE032518T2 HUE032518T2 HUE13785585A HUE13785585A HUE032518T2 HU E032518 T2 HUE032518 T2 HU E032518T2 HU E13785585 A HUE13785585 A HU E13785585A HU E13785585 A HUE13785585 A HU E13785585A HU E032518 T2 HUE032518 T2 HU E032518T2
- Authority
- HU
- Hungary
- Prior art keywords
- molecule
- cell
- assay
- cells
- kia
- Prior art date
Links
- 238000003556 assay Methods 0.000 title description 66
- 210000004027 cell Anatomy 0.000 claims description 105
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 69
- 239000003112 inhibitor Substances 0.000 claims description 20
- 230000015572 biosynthetic process Effects 0.000 claims description 4
- FGUUSXIOTUKUDN-IBGZPJMESA-N C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 Chemical compound C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 FGUUSXIOTUKUDN-IBGZPJMESA-N 0.000 claims 1
- 241000288673 Chiroptera Species 0.000 claims 1
- 239000002131 composite material Substances 0.000 claims 1
- 239000011521 glass Substances 0.000 claims 1
- 239000011435 rock Substances 0.000 claims 1
- 239000010454 slate Substances 0.000 claims 1
- 239000002002 slurry Substances 0.000 claims 1
- 238000010998 test method Methods 0.000 claims 1
- 238000012360 testing method Methods 0.000 description 104
- 210000001163 endosome Anatomy 0.000 description 90
- 210000000172 cytosol Anatomy 0.000 description 55
- 102000004169 proteins and genes Human genes 0.000 description 26
- 108090000623 proteins and genes Proteins 0.000 description 26
- 241000206602 Eukaryota Species 0.000 description 23
- 238000011534 incubation Methods 0.000 description 19
- 230000008685 targeting Effects 0.000 description 19
- 210000004379 membrane Anatomy 0.000 description 16
- 108091005804 Peptidases Proteins 0.000 description 15
- 239000004365 Protease Substances 0.000 description 15
- 238000001514 detection method Methods 0.000 description 15
- 239000012528 membrane Substances 0.000 description 14
- 231100000065 noncytotoxic Toxicity 0.000 description 14
- 230000002020 noncytotoxic effect Effects 0.000 description 14
- 108030001720 Bontoxilysin Proteins 0.000 description 13
- 239000000095 Growth Hormone-Releasing Hormone Substances 0.000 description 12
- 101710142969 Somatoliberin Proteins 0.000 description 12
- 102100022831 Somatoliberin Human genes 0.000 description 12
- 230000008859 change Effects 0.000 description 12
- 238000004458 analytical method Methods 0.000 description 11
- 239000012099 Alexa Fluor family Substances 0.000 description 10
- 210000004940 nucleus Anatomy 0.000 description 10
- 108090000765 processed proteins & peptides Proteins 0.000 description 10
- 241000283973 Oryctolagus cuniculus Species 0.000 description 9
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 9
- 102000000583 SNARE Proteins Human genes 0.000 description 9
- 108010041948 SNARE Proteins Proteins 0.000 description 9
- 231100001103 botulinum neurotoxin Toxicity 0.000 description 9
- 230000012202 endocytosis Effects 0.000 description 9
- 238000002866 fluorescence resonance energy transfer Methods 0.000 description 9
- 102000004196 processed proteins & peptides Human genes 0.000 description 9
- 239000003053 toxin Substances 0.000 description 9
- 231100000765 toxin Toxicity 0.000 description 9
- 108700012359 toxins Proteins 0.000 description 9
- 230000005945 translocation Effects 0.000 description 9
- 241000283707 Capra Species 0.000 description 8
- 241001465754 Metazoa Species 0.000 description 8
- 238000002952 image-based readout Methods 0.000 description 8
- 239000003446 ligand Substances 0.000 description 8
- 108010055044 Tetanus Toxin Proteins 0.000 description 7
- 108010082025 cyan fluorescent protein Proteins 0.000 description 7
- 231100000433 cytotoxic Toxicity 0.000 description 7
- 230000001472 cytotoxic effect Effects 0.000 description 7
- 239000000975 dye Substances 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 238000000034 method Methods 0.000 description 7
- 239000002581 neurotoxin Substances 0.000 description 7
- 102000005962 receptors Human genes 0.000 description 7
- 108020003175 receptors Proteins 0.000 description 7
- 108091005957 yellow fluorescent proteins Proteins 0.000 description 7
- 102000035195 Peptidases Human genes 0.000 description 6
- 229920001184 polypeptide Polymers 0.000 description 6
- 230000032258 transport Effects 0.000 description 6
- 238000009825 accumulation Methods 0.000 description 5
- 210000000170 cell membrane Anatomy 0.000 description 5
- 230000003834 intracellular effect Effects 0.000 description 5
- 210000000715 neuromuscular junction Anatomy 0.000 description 5
- 210000002569 neuron Anatomy 0.000 description 5
- 231100000618 neurotoxin Toxicity 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- 230000001225 therapeutic effect Effects 0.000 description 5
- 241001112695 Clostridiales Species 0.000 description 4
- 102100033365 Growth hormone-releasing hormone receptor Human genes 0.000 description 4
- 101000997535 Homo sapiens Growth hormone-releasing hormone receptor Proteins 0.000 description 4
- 238000000225 bioluminescence resonance energy transfer Methods 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- 230000005764 inhibitory process Effects 0.000 description 4
- 230000004807 localization Effects 0.000 description 4
- 239000002105 nanoparticle Substances 0.000 description 4
- -1 pyridyl oxazol Chemical compound 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- 230000028327 secretion Effects 0.000 description 4
- QRLVDLBMBULFAL-UHFFFAOYSA-N Digitonin Natural products CC1CCC2(OC1)OC3C(O)C4C5CCC6CC(OC7OC(CO)C(OC8OC(CO)C(O)C(OC9OCC(O)C(O)C9OC%10OC(CO)C(O)C(OC%11OC(CO)C(O)C(O)C%11O)C%10O)C8O)C(O)C7O)C(O)CC6(C)C5CCC4(C)C3C2C QRLVDLBMBULFAL-UHFFFAOYSA-N 0.000 description 3
- 241000196324 Embryophyta Species 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 241000238631 Hexapoda Species 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 229930040373 Paraformaldehyde Natural products 0.000 description 3
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 3
- UVYVLBIGDKGWPX-KUAJCENISA-N digitonin Chemical compound O([C@@H]1[C@@H]([C@]2(CC[C@@H]3[C@@]4(C)C[C@@H](O)[C@H](O[C@H]5[C@@H]([C@@H](O)[C@@H](O[C@H]6[C@@H]([C@@H](O[C@H]7[C@@H]([C@@H](O)[C@H](O)CO7)O)[C@H](O)[C@@H](CO)O6)O[C@H]6[C@@H]([C@@H](O[C@H]7[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O7)O)[C@@H](O)[C@@H](CO)O6)O)[C@@H](CO)O5)O)C[C@@H]4CC[C@H]3[C@@H]2[C@@H]1O)C)[C@@H]1C)[C@]11CC[C@@H](C)CO1 UVYVLBIGDKGWPX-KUAJCENISA-N 0.000 description 3
- UVYVLBIGDKGWPX-UHFFFAOYSA-N digitonine Natural products CC1C(C2(CCC3C4(C)CC(O)C(OC5C(C(O)C(OC6C(C(OC7C(C(O)C(O)CO7)O)C(O)C(CO)O6)OC6C(C(OC7C(C(O)C(O)C(CO)O7)O)C(O)C(CO)O6)O)C(CO)O5)O)CC4CCC3C2C2O)C)C2OC11CCC(C)CO1 UVYVLBIGDKGWPX-UHFFFAOYSA-N 0.000 description 3
- 230000002538 fungal effect Effects 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 210000004962 mammalian cell Anatomy 0.000 description 3
- 238000012544 monitoring process Methods 0.000 description 3
- 229920002866 paraformaldehyde Polymers 0.000 description 3
- 239000007793 ph indicator Substances 0.000 description 3
- 230000010837 receptor-mediated endocytosis Effects 0.000 description 3
- 150000003384 small molecules Chemical class 0.000 description 3
- 210000005253 yeast cell Anatomy 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- UJINBEQCDMOAHM-SFHVURJKSA-N (2s)-1,1,1-trifluoro-2-(4-pyrazol-1-ylphenyl)-3-[5-[[1-(trifluoromethyl)cyclopropyl]methyl]-1h-imidazol-2-yl]propan-2-ol Chemical compound C([C@](O)(C=1C=CC(=CC=1)N1N=CC=C1)C(F)(F)F)C(NC=1)=NC=1CC1(C(F)(F)F)CC1 UJINBEQCDMOAHM-SFHVURJKSA-N 0.000 description 2
- DEQANNDTNATYII-OULOTJBUSA-N (4r,7s,10s,13r,16s,19r)-10-(4-aminobutyl)-19-[[(2r)-2-amino-3-phenylpropanoyl]amino]-16-benzyl-n-[(2r,3r)-1,3-dihydroxybutan-2-yl]-7-[(1r)-1-hydroxyethyl]-13-(1h-indol-3-ylmethyl)-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentazacycloicosane-4-carboxa Chemical compound C([C@@H](N)C(=O)N[C@H]1CSSC[C@H](NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](CC=2C3=CC=CC=C3NC=2)NC(=O)[C@H](CC=2C=CC=CC=2)NC1=O)C(=O)N[C@H](CO)[C@H](O)C)C1=CC=CC=C1 DEQANNDTNATYII-OULOTJBUSA-N 0.000 description 2
- LOBCDGHHHHGHFA-LBPRGKRZSA-N (S)-monastrol Chemical compound CCOC(=O)C1=C(C)NC(=S)N[C@H]1C1=CC=CC(O)=C1 LOBCDGHHHHGHFA-LBPRGKRZSA-N 0.000 description 2
- OBJOZRVSMLPASY-UHFFFAOYSA-N 8-hydroxypyrene-1,3,6-trisulfonic acid Chemical compound C1=C2C(O)=CC(S(O)(=O)=O)=C(C=C3)C2=C2C3=C(S(O)(=O)=O)C=C(S(O)(=O)=O)C2=C1 OBJOZRVSMLPASY-UHFFFAOYSA-N 0.000 description 2
- HJWHHQIVUHOBQN-UHFFFAOYSA-N 9-chloro-5-phenyl-3-prop-2-enyl-1,2,4,5-tetrahydro-3-benzazepine-7,8-diol Chemical compound C1N(CC=C)CCC=2C(Cl)=C(O)C(O)=CC=2C1C1=CC=CC=C1 HJWHHQIVUHOBQN-UHFFFAOYSA-N 0.000 description 2
- 244000251953 Agaricus brunnescens Species 0.000 description 2
- 235000001674 Agaricus brunnescens Nutrition 0.000 description 2
- CYGODHVAJQTCBG-UHFFFAOYSA-N Bifeprunox Chemical compound C=12OC(=O)NC2=CC=CC=1N(CC1)CCN1CC(C=1)=CC=CC=1C1=CC=CC=C1 CYGODHVAJQTCBG-UHFFFAOYSA-N 0.000 description 2
- KDXKERNSBIXSRK-RXMQYKEDSA-N D-lysine Chemical compound NCCCC[C@@H](N)C(O)=O KDXKERNSBIXSRK-RXMQYKEDSA-N 0.000 description 2
- 240000005702 Galium aparine Species 0.000 description 2
- 235000014820 Galium aparine Nutrition 0.000 description 2
- 108010002231 IgA-specific serine endopeptidase Proteins 0.000 description 2
- 241000500891 Insecta Species 0.000 description 2
- 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 2
- 231100000911 LD50 test Toxicity 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 108010016076 Octreotide Proteins 0.000 description 2
- 208000033952 Paralysis flaccid Diseases 0.000 description 2
- 108090000445 Parathyroid hormone Proteins 0.000 description 2
- 102000003982 Parathyroid hormone Human genes 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- CQXADFVORZEARL-UHFFFAOYSA-N Rilmenidine Chemical compound C1CC1C(C1CC1)NC1=NCCO1 CQXADFVORZEARL-UHFFFAOYSA-N 0.000 description 2
- 241000519995 Stachys sylvatica Species 0.000 description 2
- 108010090804 Streptavidin Proteins 0.000 description 2
- 230000003187 abdominal effect Effects 0.000 description 2
- 238000012550 audit Methods 0.000 description 2
- 229950009087 bifeprunox Drugs 0.000 description 2
- 229960000074 biopharmaceutical Drugs 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- QWCRAEMEVRGPNT-UHFFFAOYSA-N buspirone Chemical compound C1C(=O)N(CCCCN2CCN(CC2)C=2N=CC=CN=2)C(=O)CC21CCCC2 QWCRAEMEVRGPNT-UHFFFAOYSA-N 0.000 description 2
- 229960002495 buspirone Drugs 0.000 description 2
- 210000003855 cell nucleus Anatomy 0.000 description 2
- 238000002224 dissection Methods 0.000 description 2
- 239000003596 drug target Substances 0.000 description 2
- 102000052116 epidermal growth factor receptor activity proteins Human genes 0.000 description 2
- 108700015053 epidermal growth factor receptor activity proteins Proteins 0.000 description 2
- 208000028331 flaccid paralysis Diseases 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
- 239000007850 fluorescent dye Substances 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 229960000485 methotrexate Drugs 0.000 description 2
- 108091005573 modified proteins Proteins 0.000 description 2
- 102000035118 modified proteins Human genes 0.000 description 2
- YOHYSYJDKVYCJI-UHFFFAOYSA-N n-[3-[[6-[3-(trifluoromethyl)anilino]pyrimidin-4-yl]amino]phenyl]cyclopropanecarboxamide Chemical compound FC(F)(F)C1=CC=CC(NC=2N=CN=C(NC=3C=C(NC(=O)C4CC4)C=CC=3)C=2)=C1 YOHYSYJDKVYCJI-UHFFFAOYSA-N 0.000 description 2
- 229960002700 octreotide Drugs 0.000 description 2
- WRUUGTRCQOWXEG-UHFFFAOYSA-N pamidronate Chemical compound NCCC(O)(P(O)(O)=O)P(O)(O)=O WRUUGTRCQOWXEG-UHFFFAOYSA-N 0.000 description 2
- 229940046231 pamidronate Drugs 0.000 description 2
- 239000000199 parathyroid hormone Substances 0.000 description 2
- 210000000280 pituicyte Anatomy 0.000 description 2
- 230000001817 pituitary effect Effects 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000007026 protein scission Effects 0.000 description 2
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 229960000764 rilmenidine Drugs 0.000 description 2
- 229930182490 saponin Natural products 0.000 description 2
- 150000007949 saponins Chemical class 0.000 description 2
- 230000018448 secretion by cell Effects 0.000 description 2
- 210000000278 spinal cord Anatomy 0.000 description 2
- OGBMKVWORPGQRR-UMXFMPSGSA-N teriparatide Chemical compound C([C@H](NC(=O)[C@H](CCSC)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@@H](N)CO)C(C)C)[C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1N=CNC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1N=CNC=1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CNC=N1 OGBMKVWORPGQRR-UMXFMPSGSA-N 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- KCCDSHMVQWPFBC-QQUOXUDESA-N (2s,3s)-2-[[(2s)-2-[[(2s)-3-(4-hydroxyphenyl)-2-[[(2s)-3-methyl-2-[[(2s)-3-phenyl-2-[[(2s)-pyrrolidine-2-carbonyl]amino]propanoyl]amino]butanoyl]amino]propanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoic acid Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H]1NCCC1)C(C)C)C1=CC=C(O)C=C1 KCCDSHMVQWPFBC-QQUOXUDESA-N 0.000 description 1
- XDHNQDDQEHDUTM-XJKSCTEHSA-N (3z,5e,7r,8s,9r,11e,13e,15s,16r)-16-[(2s,3r,4s)-4-[(2r,4r,5s,6r)-2,4-dihydroxy-5-methyl-6-propan-2-yloxan-2-yl]-3-hydroxypentan-2-yl]-8-hydroxy-3,15-dimethoxy-5,7,9,11-tetramethyl-1-oxacyclohexadeca-3,5,11,13-tetraen-2-one Chemical compound CO[C@H]1\C=C\C=C(C)\C[C@@H](C)[C@H](O)[C@H](C)\C=C(/C)\C=C(OC)\C(=O)O[C@@H]1[C@@H](C)[C@@H](O)[C@H](C)[C@]1(O)O[C@H](C(C)C)[C@@H](C)[C@H](O)C1 XDHNQDDQEHDUTM-XJKSCTEHSA-N 0.000 description 1
- GNXDRIAMVNVFMO-UHFFFAOYSA-N 1,4-dihydroxycyclohexa-3,5-diene-1,2-dicarbonitrile Chemical compound OC1=CC(C#N)C(O)(C#N)C=C1 GNXDRIAMVNVFMO-UHFFFAOYSA-N 0.000 description 1
- VVZRKVYGKNFTRR-UHFFFAOYSA-N 12h-benzo[a]xanthene Chemical compound C1=CC=CC2=C3CC4=CC=CC=C4OC3=CC=C21 VVZRKVYGKNFTRR-UHFFFAOYSA-N 0.000 description 1
- YKFRFHRHRHPYNI-UHFFFAOYSA-N 2',7'-bis(3-carboxypropyl)-3',6'-dihydroxy-1-oxospiro[2-benzofuran-3,9'-xanthene]-5-carboxylic acid;2',7'-bis(3-carboxypropyl)-3',6'-dihydroxy-3-oxospiro[2-benzofuran-1,9'-xanthene]-5-carboxylic acid Chemical compound O1C(=O)C2=CC(C(O)=O)=CC=C2C21C1=CC(CCCC(O)=O)=C(O)C=C1OC1=C2C=C(CCCC(=O)O)C(O)=C1.O1C(=O)C2=CC=C(C(O)=O)C=C2C21C1=CC(CCCC(O)=O)=C(O)C=C1OC1=C2C=C(CCCC(=O)O)C(O)=C1 YKFRFHRHRHPYNI-UHFFFAOYSA-N 0.000 description 1
- 108010066676 Abrin Proteins 0.000 description 1
- 101000879393 Aplysia californica Synaptobrevin Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 231100000699 Bacterial toxin Toxicity 0.000 description 1
- 101710117542 Botulinum neurotoxin type A Proteins 0.000 description 1
- 101710117524 Botulinum neurotoxin type B Proteins 0.000 description 1
- 101710117515 Botulinum neurotoxin type E Proteins 0.000 description 1
- 101710117520 Botulinum neurotoxin type F Proteins 0.000 description 1
- JQDZUSDVVHXANW-UHFFFAOYSA-N C1=CC(=C23)C4=NC5=CC=CC=C5N4C(=O)C2=CC=CC3=C1NCCN1CCOCC1 Chemical compound C1=CC(=C23)C4=NC5=CC=CC=C5N4C(=O)C2=CC=CC3=C1NCCN1CCOCC1 JQDZUSDVVHXANW-UHFFFAOYSA-N 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 101000933563 Clostridium botulinum Botulinum neurotoxin type G Proteins 0.000 description 1
- 101000985023 Clostridium botulinum C phage Botulinum neurotoxin type C Proteins 0.000 description 1
- 101000985020 Clostridium botulinum D phage Botulinum neurotoxin type D Proteins 0.000 description 1
- 241000193171 Clostridium butyricum Species 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- RPIXXMOFBZXOQR-UHFFFAOYSA-N DND-160 dye Chemical compound C1=CC(OCC(=O)NCCN(C)C)=CC=C1C1=NC=C(C=2C=CN=CC=2)O1 RPIXXMOFBZXOQR-UHFFFAOYSA-N 0.000 description 1
- VLLFXWZDQHOGLC-UHFFFAOYSA-N DND-167 dye Chemical compound C=12C=CC=CC2=C(CN2CCOCC2)C2=CC=CC=C2C=1CN1CCOCC1 VLLFXWZDQHOGLC-UHFFFAOYSA-N 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 229910052693 Europium Inorganic materials 0.000 description 1
- 206010015995 Eyelid ptosis Diseases 0.000 description 1
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 1
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 1
- 241000282414 Homo sapiens Species 0.000 description 1
- 101000851181 Homo sapiens Epidermal growth factor receptor Proteins 0.000 description 1
- 101001135770 Homo sapiens Parathyroid hormone Proteins 0.000 description 1
- 101001135995 Homo sapiens Probable peptidyl-tRNA hydrolase Proteins 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 102000004390 N-Ethylmaleimide-Sensitive Proteins Human genes 0.000 description 1
- 108010081735 N-Ethylmaleimide-Sensitive Proteins Proteins 0.000 description 1
- 101710138657 Neurotoxin Proteins 0.000 description 1
- 206010033799 Paralysis Diseases 0.000 description 1
- 108010088535 Pep-1 peptide Proteins 0.000 description 1
- 231100000742 Plant toxin Toxicity 0.000 description 1
- 108700033844 Pseudomonas aeruginosa toxA Proteins 0.000 description 1
- 102000015799 Qa-SNARE Proteins Human genes 0.000 description 1
- 108010010469 Qa-SNARE Proteins Proteins 0.000 description 1
- 101100068358 Rattus norvegicus Ghrhr gene Proteins 0.000 description 1
- 101000825738 Rattus norvegicus Somatoliberin Proteins 0.000 description 1
- 108010039491 Ricin Proteins 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 102000006384 Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins Human genes 0.000 description 1
- 108010019040 Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins Proteins 0.000 description 1
- 108010057722 Synaptosomal-Associated Protein 25 Proteins 0.000 description 1
- 102000004183 Synaptosomal-Associated Protein 25 Human genes 0.000 description 1
- NAHTXVIXCMUDLF-DUJPAFNYSA-N Toosendanin Natural products O=C(O[C@H]1C(=O)[C@H]2[C@@](C)([C@H](O)C[C@H]3[C@@]4(C)[C@H](O)OC[C@@]23[C@@H](O)C[C@H]4OC(=O)C)[C@@]23[C@]1(C)[C@H](c1cocc1)C[C@H]2O3)C NAHTXVIXCMUDLF-DUJPAFNYSA-N 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 108010057266 Type A Botulinum Toxins Proteins 0.000 description 1
- 102100038388 Vasoactive intestinal polypeptide receptor 1 Human genes 0.000 description 1
- 101710137655 Vasoactive intestinal polypeptide receptor 1 Proteins 0.000 description 1
- 102100035054 Vesicle-fusing ATPase Human genes 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 230000002320 anti-botulinal effect Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 239000012911 assay medium Substances 0.000 description 1
- 239000000688 bacterial toxin Substances 0.000 description 1
- XDHNQDDQEHDUTM-UHFFFAOYSA-N bafliomycin A1 Natural products COC1C=CC=C(C)CC(C)C(O)C(C)C=C(C)C=C(OC)C(=O)OC1C(C)C(O)C(C)C1(O)OC(C(C)C)C(C)C(O)C1 XDHNQDDQEHDUTM-UHFFFAOYSA-N 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 229940053031 botulinum toxin Drugs 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000033077 cellular process Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- DJZCTUVALDDONK-HQMSUKCRSA-N concanamycin A Chemical compound O1C(=O)\C(OC)=C\C(\C)=C\[C@@H](C)[C@@H](O)[C@@H](CC)[C@@H](O)[C@H](C)C\C(C)=C\C=C\[C@H](OC)[C@H]1[C@@H](C)[C@@H](O)[C@H](C)[C@]1(O)O[C@H](\C=C\C)[C@@H](C)[C@H](O[C@@H]2O[C@H](C)[C@@H](OC(N)=O)[C@H](O)C2)C1 DJZCTUVALDDONK-HQMSUKCRSA-N 0.000 description 1
- DJZCTUVALDDONK-UHFFFAOYSA-N concanamycin A Natural products O1C(=O)C(OC)=CC(C)=CC(C)C(O)C(CC)C(O)C(C)CC(C)=CC=CC(OC)C1C(C)C(O)C(C)C1(O)OC(C=CC)C(C)C(OC2OC(C)C(OC(N)=O)C(O)C2)C1 DJZCTUVALDDONK-UHFFFAOYSA-N 0.000 description 1
- 230000036461 convulsion Effects 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- OGPBJKLSAFTDLK-UHFFFAOYSA-N europium atom Chemical compound [Eu] OGPBJKLSAFTDLK-UHFFFAOYSA-N 0.000 description 1
- 238000010228 ex vivo assay Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 229960000556 fingolimod Drugs 0.000 description 1
- KKGQTZUTZRNORY-UHFFFAOYSA-N fingolimod Chemical compound CCCCCCCCC1=CC=C(CCC(N)(CO)CO)C=C1 KKGQTZUTZRNORY-UHFFFAOYSA-N 0.000 description 1
- 125000003983 fluorenyl group Chemical class C1(=CC=CC=2C3=CC=CC=C3CC12)* 0.000 description 1
- 239000005090 green fluorescent protein Substances 0.000 description 1
- 102000045108 human EGFR Human genes 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000010189 intracellular transport Effects 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 108010082117 matrigel Proteins 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- WSFSSNUMVMOOMR-NJFSPNSNSA-N methanone Chemical compound O=[14CH2] WSFSSNUMVMOOMR-NJFSPNSNSA-N 0.000 description 1
- NIHNNTQXNPWCJQ-UHFFFAOYSA-N o-biphenylenemethane Natural products C1=CC=C2CC3=CC=CC=C3C2=C1 NIHNNTQXNPWCJQ-UHFFFAOYSA-N 0.000 description 1
- 210000003105 phrenic nerve Anatomy 0.000 description 1
- 239000003123 plant toxin Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 201000003004 ptosis Diseases 0.000 description 1
- JFINOWIINSTUNY-UHFFFAOYSA-N pyrrolidin-3-ylmethanesulfonamide Chemical compound NS(=O)(=O)CC1CCNC1 JFINOWIINSTUNY-UHFFFAOYSA-N 0.000 description 1
- 230000004044 response 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
- 229930188950 salvinorin Natural products 0.000 description 1
- OBSYBRPAKCASQB-AGQYDFLVSA-N salvinorin A Chemical compound C=1([C@H]2OC(=O)[C@@H]3CC[C@]4(C)[C@@H]([C@]3(C2)C)C(=O)[C@@H](OC(C)=O)C[C@H]4C(=O)OC)C=COC=1 OBSYBRPAKCASQB-AGQYDFLVSA-N 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 239000002109 single walled nanotube Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 229940118376 tetanus toxin Drugs 0.000 description 1
- ANRHNWWPFJCPAZ-UHFFFAOYSA-M thionine Chemical compound [Cl-].C1=CC(N)=CC2=[S+]C3=CC(N)=CC=C3N=C21 ANRHNWWPFJCPAZ-UHFFFAOYSA-M 0.000 description 1
- NAHTXVIXCMUDLF-RFNFAWMESA-N toosendanin Chemical compound C=1([C@H]2[C@]3(C)[C@@H](OC(C)=O)C(=O)[C@H]4[C@@]([C@@]53O[C@@H]5C2)(C)[C@H](O)C[C@H]2[C@@]3(C)[C@H](O)OC[C@]24[C@@H](O)C[C@H]3OC(=O)C)C=COC=1 NAHTXVIXCMUDLF-RFNFAWMESA-N 0.000 description 1
- 239000008488 toosendanin Substances 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 238000011282 treatment Methods 0.000 description 1
- 238000011269 treatment regimen Methods 0.000 description 1
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 1
- ATCJTYORYKLVIA-SRXJVYAUSA-N vamp regimen Chemical compound O=C1C=C[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1.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.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.C([C@H](C[C@]1(C(=O)OC)C=2C(=CC3=C(C45[C@H]([C@@]([C@H](OC(C)=O)[C@]6(CC)C=CCN([C@H]56)CC4)(O)C(=O)OC)N3C=O)C=2)OC)C[C@@](C2)(O)CC)N2CCC2=C1NC1=CC=CC=C21 ATCJTYORYKLVIA-SRXJVYAUSA-N 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
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
- G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
- G01N33/502—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics for testing non-proliferative effects
-
- 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
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
- G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
-
- 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
-
- 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
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
- G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
- G01N33/5076—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics involving cell organelles, e.g. Golgi complex, endoplasmic reticulum
-
- 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)
- G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
- G01N2333/95—Proteinases, i.e. endopeptidases (3.4.21-3.4.99)
- G01N2333/952—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from bacteria
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Chemical & Material Sciences (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Food Science & Technology (AREA)
- Biochemistry (AREA)
- Cell Biology (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Microbiology (AREA)
- General Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Toxicology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Claims (2)
- I igém* pSSOOik \ Vizsgálat; optas tesz»obl®kbla mlos/oman tWs/abôdh<S hépesaégés'ièk vtxs^áisii^ ahoi a nns/ünolekula viourlchtms ereddé nensvaoKm vagy t«sat«eláh, samt cuoíosífeug|íi-öíeá?. (l'argajssl ipcretlon inhibitor''; ia*g« >> s>ok»«.\'K^ » M< u\}, »snoiyiton .¾ net» mtíhoxíktts pmteaac SvmspMtas ikbídképessége köíopand vagv îa!ge?àlô moleknisuv*;/ lk'/..madás;áyal soddoskva lett. és nhoi a tesaamoiekois képe* hNáRE felvírjvi |K«kvohttk^s»$*«ÄmM feakiiviW; uíiaíiy vizsgálati eljárás tastaksnszzas & kévelke/óket: I? eukarkrt« nejt erimice/k-tes* }cs»tto«lck«^vak ntnoKösk etsiókaátodt ΜνζοΙΡΙΒά fcépéÂfÉ sî/ -Άνη > ahol «. ί ids« ,'-sn sca sOtatow a Mp M'gnn'O'.bíáamh'afk hbl>aS tvlviton pen Ιον o kotdhehst jarkdmazé Míjhnembránh is.! a ieszimeiekuki mkrshäläs» a/, eokanóm aejnd, ezáltal a következők lehetővé tétele: a'> i tes.öOOtekois kínodesn a/ ónkat tata mjíojí jogodevé kötöhedylrez sh; kötött kompié*. kép?Me*e„ miábal lehetővé válik, hogy a kötött kosnphts; etidoetkszissal belépj«»tsz-«»«kariös»-telibe, b) egy vagy több enöns.zionts képződése. & sejten bellik ahol :8¾ egy Vágy több tasehmslekdág és v> a ivsztismfekt.de a/. egy vágy több emtoszöm» ersdosaomáb* tnembtliojáts ás lépve belep ez eukasiása .svjl eásoá/s.-yábSi, «10 ö feleslegben lévik az etíkatiöss sgjMest jéfapjévê: Röiéhapkte mm m®Ëʧ iesÄmiektdik eMvoMiása, sv; elése meghat&Äii. idiy alán m égy -vagy- lifeb ®a$#e$bmáb&8 jélggigvö issÄdtgköläk iíMonylálpáek megbasátétáss vagy az eekedida sejk aoMayiséptiel; tmeghatámzáss; vj « ív) légistes. mepÄdzdd îeszimolekelâ-esîefîoysvég ö.ssaehasoöikás& kesurobésaekkp. dte ;# köteídléslék az egy vagy· tilde esiddteateso jeiealávd tesztssteeknlák snennyísege vagy d edoszothab ijeieísléyíksesgtssyíleksdákfiteííisiyiíségeíís: iv> lépés elétk vl) 8: ieszimojekala essílnsgíkss^a^jelsssbsílíílásí: éridkdadk kiszátsdtása az egy -·Ρ|^··^$Ι» .V ! V λ I s' k )vi) y V S' ν’ ' s η * » t h λ s s Z s 5 ii s s*» Sstut λ \ u η*' os m} dimzotjâbanjeimtéyô lesáiraoíéítóák ínvn«ysségébe« bekövetkezett relatív vábazás snegtostdriszasayzh ahol a (sv) lépés isfísilínazz® a les./t«notektth« ksemtaiázát fhtoresxcent: jsddtes aik<dí)iazá?áy;d.
- .2. Λκ \ igiisyps>ßksäm;lbll vssssgaka; eh«»*, ahol az s?akíoksís seb sSlea/hHejt. sssvasseg, gernice:. ssipje, eoslfeejs. obvényt pbPigwfeaplíkbáÖI von kiváksszíyá, à. A? ekv.í'i ipayimosok. Mmselj ike stennts vjgsgálssi après, «bol a si) hikobikiás lépés é peíísta > mpig s»«6 ideig zajsik. pekkksl lekl Uén .u vssya _M0 órán ál vsg) 4- k fkán út vagy ö-k hsán út. d, Aoelözb Igétsyptíslekhásvaejylke sesslssti vizsgálati eljárj ahol a Iv) lidyeld 5 pete és J dvalkdgíbl Pgezzllik, péktáai 1M4Ö peeeel vagy iChldd peseaPkypp dfelJd pbisseekd »f lépésa kPveiéess Jv. ¥!xspáli eíjáíás iáíoíó («olélsiá ifctt áejtbég :tiiPkÂpîts® ldpí«íi Pdö: batlsamák yszsgllálára. almi ^vissgáíátíipdáíiilólossz^i^P Λ ivp >Or>4S6Bi ijetikariota sejt án«tlorM<*é*& ksiotroilmolekolaval, &«éiy az eakanélts sejí le Isz mén jelenlévő kötőhelyhez kötődik, ahoi, g kmitudhmA4.oli slsUtuhnttt ctsakan beieskoart va-sg rettagsutît, ovm siîouvstktt- privés (" I aggévá Ss-vrenott bibihlîo!·", tstgetáh sashtädos inhibitor), awiybeo » oeot dtotftsiktn p rovás teateílszsaes kôtbképéïsege kStôHg&nd vagy iargeîâh) mtáekstksrese hozzáadásával robâoshva kik és ahoi a seseisnolekoia kepes SNARE U'k'iVs potttvht ko^ao ktsdatt! 0' tiukntahn alstb a konhsdimö rhtiia « koVisrlHH Kotoîî htnrtpieset képes. eodadtAsissisi belép tt.t. eukarióíasejtbe, meiv nék sbrâo & koötnálmolekoiát kml^axôsndosxèo^ k«pddk>Je ahol a kotthoilmulekstia &z $«<È<»xètms «hdôm«à!i^ stemhrásíáa átlépve belép ax enk&rkvta sois ciólxoljálk· il) a hstwrolknolekaia iokaPSlsa as «ukMiéta sejtlek ezáltal s következők lehetővé tétele: as a kowoodoíoiokola a. sakaikna .e'ten jekavsA hötbhélvhs-z kofoshk >'a kototi k^.Wt kV. z v< V, e "Akai lehetne lesSk bags a Mo« kstmpies etiàt\ áozsssaS belépjen a? rakat îssia sep he, bj RSV vagy több et>áos«rónut képződik s sejten bellii, ahol as egy vagy több enâosiùm* tartalmaz·»* a ieszPsnslékulák és ë) ;t ks>mroi!moiek«la as egy s agy több ertdoszóstta etRlossomdUs membránján átlépve belép as to.ikafiőtn sejt dtosssájába. sht sa cukatíOta sejt enrtUvtsk'ae tnhbstot tesstmok'kol&vai, amelynek vizsgáknak! a IVpsvsege a. K n tíolbookkokik emkiajV! 'át\>' vaíö crsles/om&lk feissabadalavdt'Rtk |ál;lsMra> ívj előre atiegkttttesob iá#, vstat! a> egy vagy több «nsl-vszómában joíeolévö kortirftlimoiékulák oáShnylaégépék thégbátátöss&í vagy as '.I ke -,\t 'V t e őst sxáj abats p'lt 'leső irek^o tk«-o fitvegének meghatarozasa; V í <, X i'p"0\"» Vsgbö' ot Ό \ > ikhtvhm a on '< s sOg 'h wmlhavt kontvhzrVkKd, vhsd 4 ki's'ífohaoak áí .g··. s v> töb'' sváomooi ,;\a jelenő ,o htm, olhnoäekbhk so^rjiv \ \ *g> a eaoaaok'bt Vizniévő m:..o molekulát. tnenoyiSsge a ki) la mo, ölöd. V >) gatkta ebök ji.'i f.vfujO*' ö -' m? mb it <,»r tevüt'tfkki 'altos az , >s v agy több m'Jo'Xos töm -.. lenktö \t" uolb' ok'ktskn ' o 3nt begebt' Kk-oa, v fj «ο\> λ t > totá'k o-vg« n nveavat , \om s m ká> kbn sei ehoseoljábajt jeiettlétó koatroilmoleknlök oteoroiségébeí; bekövtnkeseb felstlv váilosA;; njegtistar^eátávak ahoi Üst? k'pín Óságában ivgbna o koní»oik«n ki íí'..; katste aavo ib;.n<-vmem. n-lblév alLdous^av.b b. As: 5, igéajfpjtît tseràtî* vn'ëgàïab kjáfát; o.hol as enlarlóla tok élesztőse}^ rovarsejr. gernmos sejtje, en'ílósvs'is, obv.pyi sejt év g<imbâsoj! tos.oä tan kivälsastva ' A» ' tagt b í.?ö!s.\ps''Íít s »· V -ιΆϋί <. a<t\ ,íkj a in si kibamo- k'pèo s pm cist. - ngt >. t->tö nkng sajbkj pékkkíl I - III 6?An A· vagy k >0 à;An à! vagy 4-8 yitán át vagy t; h sátán a?. Ί As 5-7. igénypontok bánnék: ke mm inti vimgaksí! e;járást eltol <t ívj megbattlrosás lápéin :t bk lejtést követő A pmc óv 5 óra ko/nu végessük. pstlöasi 15-241? petvcel vagy·1 30-I8O pert cél vagy 45-1.50 peres t-:i n III.! íépój* követőét!. ^ \i s.H >»e?ts^Atvti'\ bats s ''U v^i tts' vt sitiit elitta., tM '! stíotkesUK.' kos tat' hsksíbáelón lépés kiáltását kövs-to 5 pere A; 5 óra kősói! vegesank, paláén! Üíl pass és 12 óta közöti vagy >0 pety és : ti óra kozott vagy .10 pert: és 5 Otrs kozott vagy |-g s>sa kősöb a ti) htkssbtlcittv léjkts iodltását .köy.íf'öérs. ...../ I
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB1219024.5A GB201219024D0 (en) | 2012-10-23 | 2012-10-23 | Assay |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| HUE032518T2 true HUE032518T2 (hu) | 2017-09-28 |
Family
ID=47359328
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| HUE13785585A HUE032518T2 (hu) | 2012-10-23 | 2013-10-23 | Vizsgálati eljárás endoszomális transzport vizsgálatára |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US9170252B2 (hu) |
| EP (2) | EP2912456B1 (hu) |
| JP (1) | JP6302475B2 (hu) |
| CN (1) | CN104718452B (hu) |
| DK (1) | DK2912456T3 (hu) |
| ES (1) | ES2618521T3 (hu) |
| GB (1) | GB201219024D0 (hu) |
| HK (2) | HK1208527A1 (hu) |
| HU (1) | HUE032518T2 (hu) |
| PL (1) | PL2912456T3 (hu) |
| PT (1) | PT2912456T (hu) |
| RU (1) | RU2673086C2 (hu) |
| WO (1) | WO2014064442A1 (hu) |
Family Cites Families (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9305735D0 (en) | 1993-03-19 | 1993-05-05 | North John R | Novel agent for controlling cell activity |
| GB9411138D0 (en) | 1994-06-03 | 1994-07-27 | Microbiological Res Authority | Toxin assay |
| GB9508204D0 (en) | 1995-04-21 | 1995-06-07 | Speywood Lab Ltd | A novel agent able to modify peripheral afferent function |
| GB9617671D0 (en) | 1996-08-23 | 1996-10-02 | Microbiological Res Authority | Recombinant toxin fragments |
| US6277479B1 (en) | 1997-12-19 | 2001-08-21 | Kimberly-Clark Worldwide, Inc. | Microporous films having zoned breathability |
| US7183066B2 (en) * | 2002-09-27 | 2007-02-27 | Allergan, Inc. | Cell-based fluorescence resonance energy transfer (FRET) assays for clostridial toxins |
| WO2005014798A2 (en) * | 2003-03-31 | 2005-02-17 | Boston Medical Center Corporation | Novel compositions and methods for promoting, inhibiting, and detecting protein entry into cells |
| GB0321344D0 (en) * | 2003-09-11 | 2003-10-15 | Health Prot Agency | Re-targeted toxin conjugates |
| CN101063657A (zh) * | 2006-04-29 | 2007-10-31 | 中国科学院上海生命科学研究院 | 在活体细胞中筛选配体与受体结合的方法和系统 |
| HUE033007T2 (hu) * | 2006-06-23 | 2017-11-28 | Engeneic Molecular Delivery Pty Ltd | Gyógyszer, terápiás nukleinsavak és funkcionális nukleinsavak célzott szolgáltatása emlõs sejtekhez sértetlen elölt bakteriális sejtek útján |
| CN101070547B (zh) * | 2007-05-15 | 2010-12-22 | 中国人民解放军军事医学科学院军事兽医研究所 | 主动运载外源基因的重组蛋白载体PEAⅡ-HPhA及其制备方法和应用 |
| WO2009041633A1 (ja) * | 2007-09-28 | 2009-04-02 | Kyoto University | コイルドコイルを利用した膜タンパク質標識方法 |
| US8492109B2 (en) * | 2009-01-20 | 2013-07-23 | Trustees Of Tufts College | Methods for the delivery of toxins or enzymatically active portions thereof |
| US8450282B2 (en) * | 2009-07-23 | 2013-05-28 | The University Of Tokyo | Anionic polymer, polyion complex and ternary polymer composite using anionic polymer, and pharmaceutical composition |
| US9441181B2 (en) * | 2009-07-23 | 2016-09-13 | International Technology Center | Lubricant and synergistic additive formulation |
| CN102625812A (zh) | 2009-08-12 | 2012-08-01 | 医药研究协会 | 复合系统 |
| US9149666B2 (en) | 2009-08-17 | 2015-10-06 | East Carolina University | Fast acting SNARE-cleaving enzymes |
-
2012
- 2012-10-23 GB GBGB1219024.5A patent/GB201219024D0/en not_active Ceased
-
2013
- 2013-10-23 EP EP13785585.4A patent/EP2912456B1/en active Active
- 2013-10-23 PT PT137855854T patent/PT2912456T/pt unknown
- 2013-10-23 US US14/429,668 patent/US9170252B2/en not_active Expired - Fee Related
- 2013-10-23 WO PCT/GB2013/052765 patent/WO2014064442A1/en active Application Filing
- 2013-10-23 CN CN201380053659.7A patent/CN104718452B/zh not_active Expired - Fee Related
- 2013-10-23 HU HUE13785585A patent/HUE032518T2/hu unknown
- 2013-10-23 JP JP2015538567A patent/JP6302475B2/ja not_active Expired - Fee Related
- 2013-10-23 ES ES13785585.4T patent/ES2618521T3/es active Active
- 2013-10-23 RU RU2015119539A patent/RU2673086C2/ru active
- 2013-10-23 EP EP17150909.4A patent/EP3217174A1/en not_active Withdrawn
- 2013-10-23 DK DK13785585.4T patent/DK2912456T3/en active
- 2013-10-23 PL PL13785585T patent/PL2912456T3/pl unknown
-
2015
- 2015-09-16 HK HK15109066.3A patent/HK1208527A1/xx not_active IP Right Cessation
-
2018
- 2018-03-13 HK HK18103514.1A patent/HK1244060A1/zh unknown
Also Published As
| Publication number | Publication date |
|---|---|
| ES2618521T3 (es) | 2017-06-21 |
| US9170252B2 (en) | 2015-10-27 |
| PL2912456T3 (pl) | 2017-07-31 |
| EP2912456A1 (en) | 2015-09-02 |
| HK1244060A1 (zh) | 2018-07-27 |
| DK2912456T3 (en) | 2017-04-03 |
| CN104718452A (zh) | 2015-06-17 |
| HK1208527A1 (en) | 2016-03-04 |
| RU2015119539A (ru) | 2016-12-20 |
| EP3217174A1 (en) | 2017-09-13 |
| EP2912456B1 (en) | 2017-01-11 |
| JP6302475B2 (ja) | 2018-03-28 |
| JP2015534076A (ja) | 2015-11-26 |
| WO2014064442A1 (en) | 2014-05-01 |
| GB201219024D0 (en) | 2012-12-05 |
| PT2912456T (pt) | 2017-04-19 |
| CN104718452B (zh) | 2017-07-18 |
| US20150241408A1 (en) | 2015-08-27 |
| RU2673086C2 (ru) | 2018-11-22 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Dorca-Arévalo et al. | Binding of ɛ-toxin from Clostridium perfringens in the nervous system | |
| De Beer et al. | Nanobody-based probes for subcellular protein identification and visualization | |
| Atasoy et al. | A genetically specified connectomics approach applied to long-range feeding regulatory circuits | |
| Polgar et al. | The types of neuron which contain protein kinase C gamma in rat spinal cord | |
| FitzGerald et al. | It’s what’s on the inside that counts: Techniques for investigating the uptake and recycling of nanoparticles and proteins in cells | |
| Niescier et al. | MCU interacts with Miro1 to modulate mitochondrial functions in neurons | |
| Matsumoto et al. | Distribution of transient receptor potential vanilloid 1 channel-expressing nerve fibers in mouse rectal and colonic enteric nervous system: relationship to peptidergic and nitrergic neurons | |
| JP2022130378A (ja) | 細胞性ｖａｍｐ切断アッセイ | |
| JP2019532651A5 (hu) | ||
| Marvizón et al. | Enkephalins, dynorphins, and β‐endorphin in the rat dorsal horn: An immunofluorescence colocalization study | |
| PT1869459E (pt) | Ensaios fret à base de corantes lipofílicos para a actividade da toxina de clostrídeo | |
| Pelayo et al. | Endothelin‐converting enzyme‐1 regulates trafficking and signalling of the neurokinin 1 receptor in endosomes of myenteric neurones | |
| Uriarte et al. | Circulating ghrelin crosses the blood-cerebrospinal fluid barrier via growth hormone secretagogue receptor dependent and independent mechanisms | |
| US11360100B2 (en) | Methods and compositions useful in detecting proteins | |
| Geetha et al. | p62 serves as a shuttling factor for TrkA interaction with the proteasome | |
| Hoogstraaten et al. | Tetanus insensitive VAMP2 differentially restores synaptic and dense core vesicle fusion in tetanus neurotoxin treated neurons | |
| Ovespian et al. | Internalization and retrograde axonal trafficking of tetanus toxin in motor neurons and trans-synaptic propagation at central synapses exceed those of its C-terminal-binding fragments | |
| Del Cid-Pellitero et al. | Medial prefrontal cortex receives input from dorsal raphe nucleus neurons targeted by hypocretin1/orexinA-containing axons | |
| Papalampropoulou-Tsiridou et al. | Differential expression of acid–sensing ion channels in mouse primary afferents in naïve and injured conditions | |
| Jain et al. | ERK activated by Histamine H1 receptor is anti-proliferative through spatial restriction in the cytosol | |
| Ghosal et al. | Role of critical elements in botulinum neurotoxin complex in toxin routing across intestinal and bronchial barriers | |
| Pellett et al. | Neuronal targeting, internalization, and biological activity of a recombinant atoxic derivative of botulinum neurotoxin A | |
| Oh et al. | Assessing Als3 peptide-binding cavity and amyloid-forming region contributions to Candida albicans invasion of human oropharyngeal epithelial cells | |
| Schwaller et al. | A polyclonal goat antiserum against the calcium-binding protein calretinin is a versatile tool for various immunochemical techniques | |
| Bauer et al. | Visualizing RNA granule transport and translation in living neurons |