NZ572248A - Antibodies binding to the extracellular domain of the receptor tyrosine kinase alk - Google Patents
Antibodies binding to the extracellular domain of the receptor tyrosine kinase alkInfo
- Publication number
- NZ572248A NZ572248A NZ572248A NZ57224807A NZ572248A NZ 572248 A NZ572248 A NZ 572248A NZ 572248 A NZ572248 A NZ 572248A NZ 57224807 A NZ57224807 A NZ 57224807A NZ 572248 A NZ572248 A NZ 572248A
- Authority
- NZ
- New Zealand
- Prior art keywords
- antibody
- seq
- alk
- sequence
- sequence identity
- Prior art date
Links
- 230000027455 binding Effects 0.000 title claims description 79
- 206010028980 Neoplasm Diseases 0.000 claims abstract description 52
- 101000779641 Homo sapiens ALK tyrosine kinase receptor Proteins 0.000 claims abstract description 36
- 102000051965 human ALK Human genes 0.000 claims abstract description 21
- 238000011282 treatment Methods 0.000 claims abstract description 20
- 102100033793 ALK tyrosine kinase receptor Human genes 0.000 claims description 175
- 210000004027 cell Anatomy 0.000 claims description 55
- 108090000368 Fibroblast growth factor 8 Proteins 0.000 claims description 52
- 239000000427 antigen Substances 0.000 claims description 51
- 108091007433 antigens Proteins 0.000 claims description 51
- 102000036639 antigens Human genes 0.000 claims description 51
- 150000001413 amino acids Chemical class 0.000 claims description 32
- 239000012634 fragment Substances 0.000 claims description 32
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 27
- 208000005017 glioblastoma Diseases 0.000 claims description 25
- 238000000034 method Methods 0.000 claims description 20
- 125000000539 amino acid group Chemical group 0.000 claims description 17
- 239000003814 drug Substances 0.000 claims description 15
- 239000013604 expression vector Substances 0.000 claims description 15
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 13
- 230000001404 mediated effect Effects 0.000 claims description 13
- 230000011664 signaling Effects 0.000 claims description 10
- 206010029260 Neuroblastoma Diseases 0.000 claims description 9
- 239000002246 antineoplastic agent Substances 0.000 claims description 9
- 230000035772 mutation Effects 0.000 claims description 9
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 claims description 8
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 claims description 8
- 206010061902 Pancreatic neoplasm Diseases 0.000 claims description 8
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 claims description 8
- 238000004519 manufacturing process Methods 0.000 claims description 8
- 201000002528 pancreatic cancer Diseases 0.000 claims description 8
- 208000008443 pancreatic carcinoma Diseases 0.000 claims description 8
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 7
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 7
- 239000003053 toxin Substances 0.000 claims description 6
- 230000005764 inhibitory process Effects 0.000 claims description 5
- 201000001441 melanoma Diseases 0.000 claims description 5
- 201000009410 rhabdomyosarcoma Diseases 0.000 claims description 5
- 231100000765 toxin Toxicity 0.000 claims description 5
- 206010006187 Breast cancer Diseases 0.000 claims description 4
- 208000026310 Breast neoplasm Diseases 0.000 claims description 4
- 241000588724 Escherichia coli Species 0.000 claims description 4
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims description 4
- 230000003834 intracellular effect Effects 0.000 claims description 4
- 238000003786 synthesis reaction Methods 0.000 claims description 4
- 206010009944 Colon cancer Diseases 0.000 claims description 3
- 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 claims description 3
- 230000015572 biosynthetic process Effects 0.000 claims description 3
- 201000008275 breast carcinoma Diseases 0.000 claims description 3
- 208000029742 colonic neoplasm Diseases 0.000 claims description 3
- 238000012258 culturing Methods 0.000 claims description 3
- 229960000485 methotrexate Drugs 0.000 claims description 3
- 208000028564 B-cell non-Hodgkin lymphoma Diseases 0.000 claims description 2
- 208000006168 Ewing Sarcoma Diseases 0.000 claims description 2
- 206010060862 Prostate cancer Diseases 0.000 claims description 2
- 208000000236 Prostatic Neoplasms Diseases 0.000 claims description 2
- 201000000582 Retinoblastoma Diseases 0.000 claims description 2
- 208000033781 Thyroid carcinoma Diseases 0.000 claims description 2
- 208000024770 Thyroid neoplasm Diseases 0.000 claims description 2
- 208000000587 small cell lung carcinoma Diseases 0.000 claims description 2
- 201000002510 thyroid cancer Diseases 0.000 claims description 2
- 208000013077 thyroid gland carcinoma Diseases 0.000 claims description 2
- 201000008808 Fibrosarcoma Diseases 0.000 claims 1
- 206010024612 Lipoma Diseases 0.000 claims 1
- 206010024627 liposarcoma Diseases 0.000 claims 1
- 201000011510 cancer Diseases 0.000 abstract description 11
- YSWHPLCDIMUKFE-QWRGUYRKSA-N Glu-Tyr Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 YSWHPLCDIMUKFE-QWRGUYRKSA-N 0.000 abstract 1
- 101710168331 ALK tyrosine kinase receptor Proteins 0.000 description 162
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 59
- 102000005162 pleiotrophin Human genes 0.000 description 51
- 235000001014 amino acid Nutrition 0.000 description 32
- 229940024606 amino acid Drugs 0.000 description 32
- 230000014509 gene expression Effects 0.000 description 29
- 108090000623 proteins and genes Proteins 0.000 description 29
- 101100112922 Candida albicans CDR3 gene Proteins 0.000 description 28
- 150000007523 nucleic acids Chemical class 0.000 description 23
- 125000003275 alpha amino acid group Chemical group 0.000 description 18
- 102000039446 nucleic acids Human genes 0.000 description 18
- 108020004707 nucleic acids Proteins 0.000 description 18
- 102000004169 proteins and genes Human genes 0.000 description 18
- 239000013598 vector Substances 0.000 description 18
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 17
- 235000018102 proteins Nutrition 0.000 description 16
- 239000003446 ligand Substances 0.000 description 15
- 102100035361 Cerebellar degeneration-related protein 2 Human genes 0.000 description 13
- 101000737796 Homo sapiens Cerebellar degeneration-related protein 2 Proteins 0.000 description 13
- 108010025568 Nucleophosmin Proteins 0.000 description 13
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 13
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 13
- 239000011230 binding agent Substances 0.000 description 12
- 238000002474 experimental method Methods 0.000 description 12
- 238000012216 screening Methods 0.000 description 12
- 102100022678 Nucleophosmin Human genes 0.000 description 11
- 230000000694 effects Effects 0.000 description 10
- 239000002773 nucleotide Substances 0.000 description 10
- 125000003729 nucleotide group Chemical group 0.000 description 10
- 208000035475 disorder Diseases 0.000 description 9
- 230000012010 growth Effects 0.000 description 9
- 238000013459 approach Methods 0.000 description 8
- 201000010099 disease Diseases 0.000 description 8
- 239000013612 plasmid Substances 0.000 description 8
- 102000005962 receptors Human genes 0.000 description 8
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 7
- 230000004927 fusion Effects 0.000 description 7
- 108020001507 fusion proteins Proteins 0.000 description 7
- 102000037865 fusion proteins Human genes 0.000 description 7
- 230000003993 interaction Effects 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 108020003175 receptors Proteins 0.000 description 7
- 229960005486 vaccine Drugs 0.000 description 7
- 108091026890 Coding region Proteins 0.000 description 6
- 108060003951 Immunoglobulin Proteins 0.000 description 6
- 102100030335 Midkine Human genes 0.000 description 6
- 108010092801 Midkine Proteins 0.000 description 6
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 6
- 230000004913 activation Effects 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 6
- 102000018358 immunoglobulin Human genes 0.000 description 6
- 108020001756 ligand binding domains Proteins 0.000 description 6
- 238000002703 mutagenesis Methods 0.000 description 6
- 231100000350 mutagenesis Toxicity 0.000 description 6
- 102000027426 receptor tyrosine kinases Human genes 0.000 description 6
- 108091008598 receptor tyrosine kinases Proteins 0.000 description 6
- 102000053642 Catalytic RNA Human genes 0.000 description 5
- 108090000994 Catalytic RNA Proteins 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 5
- 101000956807 Homo sapiens Leukocyte tyrosine kinase receptor Proteins 0.000 description 5
- 102100038420 Leukocyte tyrosine kinase receptor Human genes 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- 101100323015 Mus musculus Alk gene Proteins 0.000 description 5
- 241000699670 Mus sp. Species 0.000 description 5
- 230000009824 affinity maturation Effects 0.000 description 5
- 210000000349 chromosome Anatomy 0.000 description 5
- 230000000875 corresponding effect Effects 0.000 description 5
- 230000006870 function Effects 0.000 description 5
- 108091092562 ribozyme Proteins 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 210000004881 tumor cell Anatomy 0.000 description 5
- 230000004614 tumor growth Effects 0.000 description 5
- 108091035707 Consensus sequence Proteins 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 4
- 108010089610 Nuclear Proteins Proteins 0.000 description 4
- 108700008625 Reporter Genes Proteins 0.000 description 4
- 230000006907 apoptotic process Effects 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 210000004899 c-terminal region Anatomy 0.000 description 4
- 210000000805 cytoplasm Anatomy 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 230000018109 developmental process Effects 0.000 description 4
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 4
- 238000002744 homologous recombination Methods 0.000 description 4
- 230000006801 homologous recombination Effects 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 230000004083 survival effect Effects 0.000 description 4
- 208000024891 symptom Diseases 0.000 description 4
- 230000008685 targeting Effects 0.000 description 4
- 238000002560 therapeutic procedure Methods 0.000 description 4
- 108700012359 toxins Proteins 0.000 description 4
- 101150023956 ALK gene Proteins 0.000 description 3
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 3
- KLSJWNVTNUYHDU-UHFFFAOYSA-N Amitrole Chemical compound NC1=NC=NN1 KLSJWNVTNUYHDU-UHFFFAOYSA-N 0.000 description 3
- 206010073478 Anaplastic large-cell lymphoma Diseases 0.000 description 3
- 108010001515 Galectin 4 Proteins 0.000 description 3
- 102100039556 Galectin-4 Human genes 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 101000737793 Homo sapiens Cerebellar degeneration-related antigen 1 Proteins 0.000 description 3
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 3
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 3
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 3
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 3
- 208000015914 Non-Hodgkin lymphomas Diseases 0.000 description 3
- 102000007999 Nuclear Proteins Human genes 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 3
- 230000001594 aberrant effect Effects 0.000 description 3
- 230000009830 antibody antigen interaction Effects 0.000 description 3
- 230000003305 autocrine Effects 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 238000004113 cell culture Methods 0.000 description 3
- 210000003169 central nervous system Anatomy 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 238000010494 dissociation reaction Methods 0.000 description 3
- 230000005593 dissociations Effects 0.000 description 3
- 238000009169 immunotherapy Methods 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 229960000310 isoleucine Drugs 0.000 description 3
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 3
- 230000003211 malignant effect Effects 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 230000009826 neoplastic cell growth Effects 0.000 description 3
- 230000001537 neural effect Effects 0.000 description 3
- 210000004498 neuroglial cell Anatomy 0.000 description 3
- 230000026731 phosphorylation Effects 0.000 description 3
- 238000006366 phosphorylation reaction Methods 0.000 description 3
- 238000003908 quality control method Methods 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 238000006467 substitution reaction Methods 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 239000004474 valine Substances 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 2
- 208000005623 Carcinogenesis Diseases 0.000 description 2
- 102100025064 Cellular tumor antigen p53 Human genes 0.000 description 2
- 241000699802 Cricetulus griseus Species 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 208000034951 Genetic Translocation Diseases 0.000 description 2
- 201000010915 Glioblastoma multiforme Diseases 0.000 description 2
- 101150009006 HIS3 gene Proteins 0.000 description 2
- 101000721661 Homo sapiens Cellular tumor antigen p53 Proteins 0.000 description 2
- 101000799194 Homo sapiens Serine/threonine-protein kinase receptor R3 Proteins 0.000 description 2
- 108090000144 Human Proteins Proteins 0.000 description 2
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- 102000000853 LDL receptors Human genes 0.000 description 2
- 108010001831 LDL receptors Proteins 0.000 description 2
- 208000032004 Large-Cell Anaplastic Lymphoma Diseases 0.000 description 2
- NPPQSCRMBWNHMW-UHFFFAOYSA-N Meprobamate Chemical compound NC(=O)OCC(C)(CCC)COC(N)=O NPPQSCRMBWNHMW-UHFFFAOYSA-N 0.000 description 2
- 206010027476 Metastases Diseases 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 108090000143 Mouse Proteins Proteins 0.000 description 2
- 108010025020 Nerve Growth Factor Proteins 0.000 description 2
- 102000007339 Nerve Growth Factor Receptors Human genes 0.000 description 2
- 108010032605 Nerve Growth Factor Receptors Proteins 0.000 description 2
- 102000004207 Neuropilin-1 Human genes 0.000 description 2
- 108090000772 Neuropilin-1 Proteins 0.000 description 2
- -1 PDGF Proteins 0.000 description 2
- 102000014160 PTEN Phosphohydrolase Human genes 0.000 description 2
- 108010011536 PTEN Phosphohydrolase Proteins 0.000 description 2
- 102000002727 Protein Tyrosine Phosphatase Human genes 0.000 description 2
- 102000003698 Syndecan-3 Human genes 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 238000007792 addition Methods 0.000 description 2
- 239000000853 adhesive Substances 0.000 description 2
- 230000001070 adhesive effect Effects 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000036952 cancer formation Effects 0.000 description 2
- 231100000504 carcinogenesis Toxicity 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 208000010877 cognitive disease Diseases 0.000 description 2
- 230000005757 colony formation Effects 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 229940127089 cytotoxic agent Drugs 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 239000012636 effector Substances 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 102000047644 human ACVRL1 Human genes 0.000 description 2
- 238000009396 hybridization Methods 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 238000003384 imaging method Methods 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 229940072221 immunoglobulins Drugs 0.000 description 2
- 238000012744 immunostaining Methods 0.000 description 2
- 101150066555 lacZ gene Proteins 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 230000004807 localization Effects 0.000 description 2
- 108091007169 meprins Proteins 0.000 description 2
- 230000009401 metastasis Effects 0.000 description 2
- 210000000653 nervous system Anatomy 0.000 description 2
- 210000003061 neural cell Anatomy 0.000 description 2
- 210000002569 neuron Anatomy 0.000 description 2
- 210000004940 nucleus Anatomy 0.000 description 2
- 210000001672 ovary Anatomy 0.000 description 2
- 230000002018 overexpression Effects 0.000 description 2
- 230000001575 pathological effect Effects 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 230000029279 positive regulation of transcription, DNA-dependent Effects 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 230000009465 prokaryotic expression Effects 0.000 description 2
- 108020000494 protein-tyrosine phosphatase Proteins 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 230000000638 stimulation Effects 0.000 description 2
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 230000005945 translocation Effects 0.000 description 2
- 230000005747 tumor angiogenesis Effects 0.000 description 2
- 238000010396 two-hybrid screening Methods 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 108010002164 tyrosine receptor Proteins 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 1
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 1
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 1
- 229940122531 Anaplastic lymphoma kinase inhibitor Drugs 0.000 description 1
- 102000008102 Ankyrins Human genes 0.000 description 1
- 108010049777 Ankyrins Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 206010003571 Astrocytoma Diseases 0.000 description 1
- 241001112741 Bacillaceae Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 208000003174 Brain Neoplasms Diseases 0.000 description 1
- DLGOEMSEDOSKAD-UHFFFAOYSA-N Carmustine Chemical compound ClCCNC(=O)N(N=O)CCCl DLGOEMSEDOSKAD-UHFFFAOYSA-N 0.000 description 1
- 208000037088 Chromosome Breakage Diseases 0.000 description 1
- 208000028698 Cognitive impairment Diseases 0.000 description 1
- 206010010904 Convulsion Diseases 0.000 description 1
- 102100030497 Cytochrome c Human genes 0.000 description 1
- 108010075031 Cytochromes c Proteins 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 102000052510 DNA-Binding Proteins Human genes 0.000 description 1
- 101710096438 DNA-binding protein Proteins 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 108050002772 E3 ubiquitin-protein ligase Mdm2 Proteins 0.000 description 1
- 102000012199 E3 ubiquitin-protein ligase Mdm2 Human genes 0.000 description 1
- 241000588921 Enterobacteriaceae Species 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 102100037362 Fibronectin Human genes 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- 208000032612 Glial tumor Diseases 0.000 description 1
- 206010018338 Glioma Diseases 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 241000606768 Haemophilus influenzae Species 0.000 description 1
- 206010019233 Headaches Diseases 0.000 description 1
- 101000898034 Homo sapiens Hepatocyte growth factor Proteins 0.000 description 1
- 101000852815 Homo sapiens Insulin receptor Proteins 0.000 description 1
- 101001076408 Homo sapiens Interleukin-6 Proteins 0.000 description 1
- 101000621344 Homo sapiens Protein Wnt-2 Proteins 0.000 description 1
- 101000868152 Homo sapiens Son of sevenless homolog 1 Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 102000003746 Insulin Receptor Human genes 0.000 description 1
- 108010001127 Insulin Receptor Proteins 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 206010064912 Malignant transformation Diseases 0.000 description 1
- 108010006519 Molecular Chaperones Proteins 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 101100490437 Mus musculus Acvrl1 gene Proteins 0.000 description 1
- 101100021974 Mus musculus Ltk gene Proteins 0.000 description 1
- 230000004988 N-glycosylation Effects 0.000 description 1
- 206010028813 Nausea Diseases 0.000 description 1
- 102000007072 Nerve Growth Factors Human genes 0.000 description 1
- 108091005461 Nucleic proteins Chemical group 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 108010067902 Peptide Library Proteins 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 102100022805 Protein Wnt-2 Human genes 0.000 description 1
- 108010026552 Proteome Proteins 0.000 description 1
- 108010090931 Proto-Oncogene Proteins c-bcl-2 Proteins 0.000 description 1
- 102000013535 Proto-Oncogene Proteins c-bcl-2 Human genes 0.000 description 1
- 101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 206010068771 Soft tissue neoplasm Diseases 0.000 description 1
- 102000004584 Somatomedin Receptors Human genes 0.000 description 1
- 108010017622 Somatomedin Receptors Proteins 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 108090000068 Syndecan-3 Proteins 0.000 description 1
- 206010064390 Tumour invasion Diseases 0.000 description 1
- 108091005906 Type I transmembrane proteins Proteins 0.000 description 1
- 101150049278 US20 gene Proteins 0.000 description 1
- 208000007097 Urinary Bladder Neoplasms Diseases 0.000 description 1
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 1
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 1
- 206010047700 Vomiting Diseases 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 229940100198 alkylating agent Drugs 0.000 description 1
- 239000002168 alkylating agent Substances 0.000 description 1
- 230000033115 angiogenesis Effects 0.000 description 1
- 239000002870 angiogenesis inducing agent Substances 0.000 description 1
- 230000002491 angiogenic effect Effects 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000002424 anti-apoptotic effect Effects 0.000 description 1
- 230000001640 apoptogenic effect Effects 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 210000005068 bladder tissue Anatomy 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 230000004641 brain development Effects 0.000 description 1
- 210000000133 brain stem Anatomy 0.000 description 1
- 210000005013 brain tissue Anatomy 0.000 description 1
- 230000005907 cancer growth Effects 0.000 description 1
- 230000009400 cancer invasion Effects 0.000 description 1
- 229960005243 carmustine Drugs 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 210000004720 cerebrum Anatomy 0.000 description 1
- 230000008711 chromosomal rearrangement Effects 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000012411 cloning technique Methods 0.000 description 1
- 230000004186 co-expression Effects 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 230000004154 complement system Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 230000006552 constitutive activation Effects 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 238000009109 curative therapy Methods 0.000 description 1
- 238000011461 current therapy Methods 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
- 230000001086 cytosolic effect Effects 0.000 description 1
- 239000002254 cytotoxic agent Substances 0.000 description 1
- 231100000599 cytotoxic agent Toxicity 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000002074 deregulated effect Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 230000013020 embryo development Effects 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 102000052116 epidermal growth factor receptor activity proteins Human genes 0.000 description 1
- 108700015053 epidermal growth factor receptor activity proteins Proteins 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 108010074605 gamma-Globulins Proteins 0.000 description 1
- 230000004077 genetic alteration Effects 0.000 description 1
- 231100000118 genetic alteration Toxicity 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 229940047650 haemophilus influenzae Drugs 0.000 description 1
- 230000003394 haemopoietic effect Effects 0.000 description 1
- 231100000869 headache Toxicity 0.000 description 1
- 238000011102 hetero oligomerization reaction Methods 0.000 description 1
- 102000047882 human INSR Human genes 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 239000002955 immunomodulating agent Substances 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000007917 intracranial administration Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 125000000741 isoleucyl group Chemical group [H]N([H])C(C(C([H])([H])[H])C([H])([H])C([H])([H])[H])C(=O)O* 0.000 description 1
- 229940043355 kinase inhibitor Drugs 0.000 description 1
- 238000011813 knockout mouse model Methods 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 230000001926 lymphatic effect Effects 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 230000036212 malign transformation Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 230000035800 maturation Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 208000018731 motor weakness Diseases 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 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 1
- 230000008693 nausea Effects 0.000 description 1
- 230000007971 neurological deficit Effects 0.000 description 1
- 239000003900 neurotrophic factor Substances 0.000 description 1
- 238000006384 oligomerization reaction Methods 0.000 description 1
- 231100000590 oncogenic Toxicity 0.000 description 1
- 230000002246 oncogenic effect Effects 0.000 description 1
- 230000005305 organ development Effects 0.000 description 1
- 108700009251 p80(NPM-ALK) Proteins 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 239000013610 patient sample Substances 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 230000009984 peri-natal effect Effects 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 230000002688 persistence Effects 0.000 description 1
- 230000002085 persistent effect Effects 0.000 description 1
- 239000003348 petrochemical agent Substances 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 239000003757 phosphotransferase inhibitor Substances 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000000861 pro-apoptotic effect Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000000750 progressive effect Effects 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- GPTFURBXHJWNHR-UHFFFAOYSA-N protopine Chemical compound C1=C2C(=O)CC3=CC=C4OCOC4=C3CN(C)CCC2=CC2=C1OCO2 GPTFURBXHJWNHR-UHFFFAOYSA-N 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 108091008600 receptor tyrosine phosphatases Proteins 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000000278 spinal cord Anatomy 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 238000002626 targeted therapy Methods 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 239000000439 tumor marker Substances 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 230000008673 vomiting Effects 0.000 description 1
- 210000004885 white matter Anatomy 0.000 description 1
- 238000001086 yeast two-hybrid system Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P39/00—General protective or antinoxious agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2896—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against molecules with a "CD"-designation, not provided for elsewhere
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/567—Framework region [FR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/622—Single chain antibody (scFv)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y207/00—Transferases transferring phosphorus-containing groups (2.7)
- C12Y207/10—Protein-tyrosine kinases (2.7.10)
- C12Y207/10001—Receptor protein-tyrosine kinase (2.7.10.1)
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Immunology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Epidemiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Cell Biology (AREA)
- Mycology (AREA)
- Toxicology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US79583106P | 2006-04-28 | 2006-04-28 | |
| PCT/CH2007/000202 WO2007124610A1 (en) | 2006-04-28 | 2007-04-27 | Antibodies binding to the extracellular domain of the receptor tyrosine kinase alk |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NZ572248A true NZ572248A (en) | 2011-08-26 |
Family
ID=38515389
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NZ572248A NZ572248A (en) | 2006-04-28 | 2007-04-27 | Antibodies binding to the extracellular domain of the receptor tyrosine kinase alk |
Country Status (16)
| Country | Link |
|---|---|
| US (3) | US7902340B2 (enExample) |
| EP (2) | EP2604627A1 (enExample) |
| JP (2) | JP5431920B2 (enExample) |
| KR (1) | KR101457228B1 (enExample) |
| CN (1) | CN101443361B (enExample) |
| AU (1) | AU2007246144B2 (enExample) |
| BR (1) | BRPI0710971A2 (enExample) |
| CA (1) | CA2650822C (enExample) |
| DK (1) | DK2013236T3 (enExample) |
| ES (1) | ES2547248T3 (enExample) |
| IL (1) | IL194752A0 (enExample) |
| MX (1) | MX2008013705A (enExample) |
| NZ (1) | NZ572248A (enExample) |
| PL (1) | PL2013236T3 (enExample) |
| RU (1) | RU2460540C2 (enExample) |
| WO (1) | WO2007124610A1 (enExample) |
Families Citing this family (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU2007246144B2 (en) * | 2006-04-28 | 2012-12-06 | Delenex Therapeutics Ag | Antibodies binding to the extracellular domain of the Receptor Tyrosine Kinase ALK |
| WO2008131575A2 (en) * | 2007-04-27 | 2008-11-06 | Esbatech Ag | Anti-alk antibodies suitable for treating metastatic cancers or tumors |
| US20110206691A1 (en) * | 2008-02-15 | 2011-08-25 | Mosse Yael P | Methods and Compositions for Treating Neuroblastoma |
| WO2009103061A2 (en) * | 2008-02-15 | 2009-08-20 | The Children's Hospital Of Philadelphia | Methods and compositions for identifying, diagnosing, and treating neuroblastoma |
| MX345395B (es) | 2008-06-25 | 2017-01-30 | Esbatech Alcon Biomed Res Unit | Humanizacion de anticuerpos de conejos usando una estructura de anticuerpos universal. |
| WO2009155723A2 (en) | 2008-06-25 | 2009-12-30 | Esbatech, An Alcon Biomedical Research Unit Llc | STABLE AND SOLUBLE ANTIBODIES INHIBITING TNFα |
| UY33679A (es) | 2010-10-22 | 2012-03-30 | Esbatech | Anticuerpos estables y solubles |
| JP2015527869A (ja) | 2011-08-26 | 2015-09-24 | メリマック ファーマシューティカルズ インコーポレーティッド | タンデムＦｃ二重特異性抗体 |
| WO2013067492A1 (en) | 2011-11-03 | 2013-05-10 | The Trustees Of The University Of Pennsylvania | Isolated b7-h4 specific compositions and methods of use thereof |
| WO2014138449A1 (en) | 2013-03-06 | 2014-09-12 | Merrimack Pharmaceuticals, Inc. | Anti-c-met tandem fc bispecific antibodies |
| CN104861069B (zh) * | 2014-02-21 | 2018-12-18 | 无锡傲锐东源生物科技有限公司 | 针对间变性淋巴瘤激酶的单克隆抗体1a4及其用途 |
| WO2015184231A2 (en) * | 2014-05-30 | 2015-12-03 | Kolltan Pharmaceuticals, Inc. | Regulators of anaplastic lymphoma kinase and uses thereof |
| EP3341021A4 (en) | 2015-08-27 | 2019-03-13 | Celldex Therapeutics, Inc. | ANTI-ALK ANTIBODIES AND METHOD OF USE THEREOF |
| CA2940470C (en) | 2015-09-18 | 2019-08-20 | Signpath Pharma Inc. | Treatment for glioblastoma |
| JP7017015B2 (ja) | 2015-10-13 | 2022-02-08 | エウレカ セラピューティクス インコーポレイテッド | ヒトｃｄ１９に特異的な抗体剤及びその使用 |
| RU2767209C2 (ru) | 2015-10-23 | 2022-03-16 | Еурека Терапьютикс, Инк. | Химерные конструкции антитело/т-клеточный рецептор и их применения |
| WO2017147408A1 (en) * | 2016-02-25 | 2017-08-31 | The Regents Of The University Of California | Methods for the treatment of hematologic cancer |
| IL310182A (en) | 2017-04-26 | 2024-03-01 | Eureka Therapeutics Inc ׂ A Delaware Corp | Structures of chimeric antibody/T-cell receptor and uses thereof |
| EP3749682B1 (en) * | 2018-02-09 | 2025-09-24 | Acceleron Pharma Inc. | Treating heterotopic ossification |
| IT201800009282A1 (it) * | 2018-10-09 | 2020-04-09 | Metis Prec Medicine Sb Srl | Nuovo agente terapeutico per il trattamento di un tumore e/o metastasi |
| CN113960313B (zh) * | 2021-12-22 | 2022-04-12 | 上海思路迪医学检验所有限公司 | 一种外泌体alk融合蛋白磁免疫化学发光检测试剂盒 |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US21505A (en) * | 1858-09-14 | Improvement in bullet-machines | ||
| US5529925A (en) * | 1993-12-03 | 1996-06-25 | St. Jude Children's Research Hospital | Nucleic acid sequences and fusion proteins present in human t(2;5) lymphoma |
| US6696548B2 (en) * | 1993-12-03 | 2004-02-24 | St. Jude Children's Research Hospital | Antibodies for recognition of alk protein tyrosine/kinase receptor |
| CA2229043C (en) | 1995-08-18 | 2016-06-07 | Morphosys Gesellschaft Fur Proteinoptimierung Mbh | Protein/(poly)peptide libraries |
| EP0938506B1 (en) | 1996-07-16 | 2003-11-05 | Plückthun, Andreas, Prof. Dr. | Immunoglobulin superfamily domains and fragments with increased solubility |
| JPH1116250A (ja) * | 1997-06-20 | 1999-01-22 | Pioneer Electron Corp | 情報再生システム |
| DK1242457T3 (da) * | 1999-12-28 | 2004-12-20 | Esbatech Ag | Intracellulære antistoffer [intracellulære antistoffer] med defineret struktur, der er stabil i et reducerende miljö, og anvendelse deraf |
| DE60141518D1 (de) * | 2000-06-14 | 2010-04-22 | Univ Georgetown | Pleiotrophin wachstumfaktor rezeptor alk zur behandlung von proliferativen, gefässer- und neurologischen erkrankungen |
| US7417130B2 (en) | 2000-09-08 | 2008-08-26 | University Of Zurich | Collection of repeat proteins comprising repeat modules |
| CN105175535A (zh) | 2002-05-22 | 2015-12-23 | 艾斯巴技术-诺华有限责任公司 | 在胞内环境中表现出增强的稳定性的免疫球蛋白构架及其鉴定方法 |
| US7888485B2 (en) | 2003-03-26 | 2011-02-15 | Georgetown University | Anti-pleiotrophin antibodies and methods of use thereof |
| AU2005272920B2 (en) | 2004-08-10 | 2011-05-12 | Institute For Multiple Myeloma And Bone Cancer Research | Methods of regulating differentiation and treating of multiple myeloma |
| AU2007246144B2 (en) * | 2006-04-28 | 2012-12-06 | Delenex Therapeutics Ag | Antibodies binding to the extracellular domain of the Receptor Tyrosine Kinase ALK |
-
2007
- 2007-04-27 AU AU2007246144A patent/AU2007246144B2/en not_active Ceased
- 2007-04-27 CA CA2650822A patent/CA2650822C/en not_active Expired - Fee Related
- 2007-04-27 DK DK07720099.6T patent/DK2013236T3/en active
- 2007-04-27 PL PL07720099T patent/PL2013236T3/pl unknown
- 2007-04-27 EP EP13000844.4A patent/EP2604627A1/en not_active Withdrawn
- 2007-04-27 RU RU2008146922/10A patent/RU2460540C2/ru not_active IP Right Cessation
- 2007-04-27 MX MX2008013705A patent/MX2008013705A/es active IP Right Grant
- 2007-04-27 CN CN200780017546.6A patent/CN101443361B/zh not_active Expired - Fee Related
- 2007-04-27 US US11/796,549 patent/US7902340B2/en not_active Expired - Fee Related
- 2007-04-27 ES ES07720099.6T patent/ES2547248T3/es active Active
- 2007-04-27 JP JP2009506889A patent/JP5431920B2/ja not_active Expired - Fee Related
- 2007-04-27 NZ NZ572248A patent/NZ572248A/en not_active IP Right Cessation
- 2007-04-27 EP EP07720099.6A patent/EP2013236B1/en active Active
- 2007-04-27 KR KR1020087026220A patent/KR101457228B1/ko not_active Expired - Fee Related
- 2007-04-27 BR BRPI0710971-7A patent/BRPI0710971A2/pt not_active IP Right Cessation
- 2007-04-27 WO PCT/CH2007/000202 patent/WO2007124610A1/en not_active Ceased
-
2008
- 2008-10-22 IL IL194752A patent/IL194752A0/en active IP Right Grant
-
2011
- 2011-01-31 US US13/017,925 patent/US8945563B2/en not_active Expired - Fee Related
-
2013
- 2013-05-28 JP JP2013112192A patent/JP5911821B2/ja active Active
-
2014
- 2014-12-16 US US14/571,433 patent/US9512411B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| CN101443361A (zh) | 2009-05-27 |
| EP2013236B1 (en) | 2015-06-17 |
| AU2007246144A1 (en) | 2007-11-08 |
| JP5431920B2 (ja) | 2014-03-05 |
| CA2650822C (en) | 2017-03-14 |
| RU2460540C2 (ru) | 2012-09-10 |
| US8945563B2 (en) | 2015-02-03 |
| KR20080113261A (ko) | 2008-12-29 |
| EP2013236A1 (en) | 2009-01-14 |
| US7902340B2 (en) | 2011-03-08 |
| EP2604627A1 (en) | 2013-06-19 |
| IL194752A0 (en) | 2011-08-01 |
| AU2007246144B2 (en) | 2012-12-06 |
| JP2013226144A (ja) | 2013-11-07 |
| MX2008013705A (es) | 2008-11-06 |
| CA2650822A1 (en) | 2007-11-08 |
| WO2007124610A1 (en) | 2007-11-08 |
| JP2009535021A (ja) | 2009-10-01 |
| US20110159008A1 (en) | 2011-06-30 |
| HK1124619A1 (en) | 2009-07-17 |
| US20080118512A1 (en) | 2008-05-22 |
| DK2013236T3 (en) | 2015-09-21 |
| RU2008146922A (ru) | 2010-06-10 |
| CN101443361B (zh) | 2015-08-19 |
| JP5911821B2 (ja) | 2016-04-27 |
| US20150203829A1 (en) | 2015-07-23 |
| KR101457228B1 (ko) | 2014-11-04 |
| US9512411B2 (en) | 2016-12-06 |
| ES2547248T3 (es) | 2015-10-02 |
| PL2013236T3 (pl) | 2015-12-31 |
| BRPI0710971A2 (pt) | 2011-05-31 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US9512411B2 (en) | Nucleic acid encoding antibodies binding to the extracellular domain of the receptor tyrosine kinase ALK | |
| AU2003216748B2 (en) | Novel anti-IGF-IR antibodies and uses thereof | |
| US11359021B2 (en) | PD-L1 antibody, antigen-binding fragment thereof, and pharmaceutical use thereof | |
| US20090070890A1 (en) | Product | |
| CA2776037A1 (en) | Anti-fibroblast activation protein antibodies and methods and uses thereof | |
| WO2009098238A1 (en) | Anti-trka antibodies and derivatives thereof | |
| KR20190077306A (ko) | 항-o2 항체 및 이의 용도 | |
| CN111825766B (zh) | 抗il-4r单域抗体及其应用 | |
| KR20220160670A (ko) | 항 pd-l1 및 pd-l2 항체 및 이의 유도체 및 용도 | |
| WO2008131575A2 (en) | Anti-alk antibodies suitable for treating metastatic cancers or tumors | |
| US20240101663A1 (en) | Method for inhibiting tumour cell growth based on ccdc112 | |
| AU2012244351B2 (en) | Antibodies binding to the extracellular domain of the Receptor Tyrosine Kinase ALK | |
| HK1124619B (en) | Antibodies binding to the extracellular domain of the receptor tyrosine kinase alk | |
| HK40101214A (en) | Method for inhibiting tumour cell growth based on ccdc112 | |
| TW202434643A (zh) | ＴＧＦβ１結合分子、ＧＡＲＰ－ＴＧＦβ１結合分子及其醫藥用途 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| ASS | Change of ownership |
Owner name: ESBATECH AG, CH Free format text: OLD OWNER(S): ADRIAN AUF DER MAUR; PETER LICHTLEN; ALCIDE BARBERIS |
|
| ASS | Change of ownership |
Owner name: DELENEX THERAPEUTICS AG C/- ESBATECH AG, CH Free format text: OLD OWNER(S): ESBATECH AG |
|
| PSEA | Patent sealed | ||
| RENW | Renewal (renewal fees accepted) | ||
| RENW | Renewal (renewal fees accepted) |
Free format text: PATENT RENEWED FOR 3 YEARS UNTIL 27 APR 2017 BY DENNEMEYER SA Effective date: 20140314 |
|
| LAPS | Patent lapsed |