MX2011001880A - Peptidos de epitope inhbb y vacunas que contienen los mismos. - Google Patents
Peptidos de epitope inhbb y vacunas que contienen los mismos.Info
- Publication number
- MX2011001880A MX2011001880A MX2011001880A MX2011001880A MX2011001880A MX 2011001880 A MX2011001880 A MX 2011001880A MX 2011001880 A MX2011001880 A MX 2011001880A MX 2011001880 A MX2011001880 A MX 2011001880A MX 2011001880 A MX2011001880 A MX 2011001880A
- Authority
- MX
- Mexico
- Prior art keywords
- peptide
- peptides
- present
- cells
- cancer
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 317
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 214
- 229960005486 vaccine Drugs 0.000 title claims description 16
- 101150110522 INHBB gene Proteins 0.000 title description 6
- 210000004027 cell Anatomy 0.000 claims abstract description 112
- 206010028980 Neoplasm Diseases 0.000 claims abstract description 101
- 238000000034 method Methods 0.000 claims abstract description 82
- 239000000427 antigen Substances 0.000 claims abstract description 75
- 108091007433 antigens Proteins 0.000 claims abstract description 75
- 102000036639 antigens Human genes 0.000 claims abstract description 75
- 201000011510 cancer Diseases 0.000 claims abstract description 74
- 102000040430 polynucleotide Human genes 0.000 claims abstract description 53
- 108091033319 polynucleotide Proteins 0.000 claims abstract description 53
- 239000002157 polynucleotide Substances 0.000 claims abstract description 53
- 210000001808 exosome Anatomy 0.000 claims abstract description 33
- 230000001939 inductive effect Effects 0.000 claims abstract description 25
- 230000002265 prevention Effects 0.000 claims abstract description 24
- 229920001184 polypeptide Polymers 0.000 claims abstract description 23
- 239000004480 active ingredient Substances 0.000 claims abstract description 21
- 239000008177 pharmaceutical agent Substances 0.000 claims abstract description 20
- 238000011282 treatment Methods 0.000 claims abstract description 17
- 238000011321 prophylaxis Methods 0.000 claims abstract description 13
- 230000002980 postoperative effect Effects 0.000 claims abstract description 7
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 claims description 125
- 210000000612 antigen-presenting cell Anatomy 0.000 claims description 62
- 150000001413 amino acids Chemical group 0.000 claims description 47
- 239000003795 chemical substances by application Substances 0.000 claims description 28
- 210000001744 T-lymphocyte Anatomy 0.000 claims description 22
- 208000002154 non-small cell lung carcinoma Diseases 0.000 claims description 21
- 208000029729 tumor suppressor gene on chromosome 11 Diseases 0.000 claims description 21
- 206010041067 Small cell lung cancer Diseases 0.000 claims description 19
- 208000000587 small cell lung carcinoma Diseases 0.000 claims description 19
- 208000000461 Esophageal Neoplasms Diseases 0.000 claims description 12
- 206010030155 Oesophageal carcinoma Diseases 0.000 claims description 12
- 208000006265 Renal cell carcinoma Diseases 0.000 claims description 12
- 201000004101 esophageal cancer Diseases 0.000 claims description 12
- 206010038389 Renal cancer Diseases 0.000 claims description 11
- 230000028993 immune response Effects 0.000 claims description 11
- 201000010174 renal carcinoma Diseases 0.000 claims description 11
- 206010068771 Soft tissue neoplasm Diseases 0.000 claims description 10
- 208000006990 cholangiocarcinoma Diseases 0.000 claims description 9
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 8
- 125000000539 amino acid group Chemical group 0.000 claims description 8
- 229930182817 methionine Natural products 0.000 claims description 8
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 6
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 5
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 4
- 239000004474 valine Substances 0.000 claims description 4
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 3
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 claims description 2
- 125000001433 C-terminal amino-acid group Chemical group 0.000 claims 1
- 101001054725 Homo sapiens Inhibin beta B chain Proteins 0.000 abstract description 51
- 102100027003 Inhibin beta B chain Human genes 0.000 abstract description 35
- 239000008194 pharmaceutical composition Substances 0.000 abstract description 32
- 230000005809 anti-tumor immunity Effects 0.000 abstract description 4
- 229940023041 peptide vaccine Drugs 0.000 abstract description 2
- 235000001014 amino acid Nutrition 0.000 description 44
- 229940024606 amino acid Drugs 0.000 description 43
- 108090000623 proteins and genes Proteins 0.000 description 29
- 125000003275 alpha amino acid group Chemical group 0.000 description 23
- 239000013598 vector Substances 0.000 description 20
- 150000007523 nucleic acids Chemical class 0.000 description 19
- 239000000203 mixture Substances 0.000 description 18
- 235000018102 proteins Nutrition 0.000 description 18
- 102000004169 proteins and genes Human genes 0.000 description 18
- 210000004443 dendritic cell Anatomy 0.000 description 17
- 102100037850 Interferon gamma Human genes 0.000 description 15
- 108010074328 Interferon-gamma Proteins 0.000 description 15
- 108091008874 T cell receptors Proteins 0.000 description 15
- 238000000338 in vitro Methods 0.000 description 14
- 102000039446 nucleic acids Human genes 0.000 description 14
- 108020004707 nucleic acids Proteins 0.000 description 14
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 13
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 13
- 201000010099 disease Diseases 0.000 description 12
- 230000006870 function Effects 0.000 description 12
- 238000004519 manufacturing process Methods 0.000 description 12
- 230000000694 effects Effects 0.000 description 11
- 238000001727 in vivo Methods 0.000 description 10
- 239000000463 material Substances 0.000 description 10
- 230000004048 modification Effects 0.000 description 10
- 238000012986 modification Methods 0.000 description 10
- 230000003389 potentiating effect Effects 0.000 description 10
- 239000000126 substance Substances 0.000 description 10
- 241000282414 Homo sapiens Species 0.000 description 9
- 239000003814 drug Substances 0.000 description 9
- 230000006698 induction Effects 0.000 description 9
- 230000000638 stimulation Effects 0.000 description 9
- 230000014509 gene expression Effects 0.000 description 8
- 108091005601 modified peptides Proteins 0.000 description 8
- 238000006467 substitution reaction Methods 0.000 description 8
- 108020004705 Codon Proteins 0.000 description 7
- 238000007792 addition Methods 0.000 description 7
- 238000009472 formulation Methods 0.000 description 7
- 210000001519 tissue Anatomy 0.000 description 7
- 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 6
- NWIBSHFKIJFRCO-WUDYKRTCSA-N Mytomycin Chemical compound C1N2C(C(C(C)=C(N)C3=O)=O)=C3[C@@H](COC(N)=O)[C@@]2(OC)[C@@H]2[C@H]1N2 NWIBSHFKIJFRCO-WUDYKRTCSA-N 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 229940079593 drug Drugs 0.000 description 6
- 238000003114 enzyme-linked immunosorbent spot assay Methods 0.000 description 6
- 238000009169 immunotherapy Methods 0.000 description 6
- 230000008569 process Effects 0.000 description 6
- 230000004044 response Effects 0.000 description 6
- 125000006850 spacer group Chemical group 0.000 description 6
- 238000003786 synthesis reaction Methods 0.000 description 6
- 108020004414 DNA Proteins 0.000 description 5
- 239000002671 adjuvant Substances 0.000 description 5
- 210000004369 blood Anatomy 0.000 description 5
- 239000008280 blood Substances 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 230000001900 immune effect Effects 0.000 description 5
- 230000002163 immunogen Effects 0.000 description 5
- 125000003729 nucleotide group Chemical group 0.000 description 5
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 4
- 238000011510 Elispot assay Methods 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 241001465754 Metazoa Species 0.000 description 4
- 241000700605 Viruses Species 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 229910052739 hydrogen Inorganic materials 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 150000002632 lipids Chemical class 0.000 description 4
- 238000002156 mixing Methods 0.000 description 4
- 210000001616 monocyte Anatomy 0.000 description 4
- 238000010647 peptide synthesis reaction Methods 0.000 description 4
- 210000005259 peripheral blood Anatomy 0.000 description 4
- 239000011886 peripheral blood Substances 0.000 description 4
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 4
- 229920000642 polymer Polymers 0.000 description 4
- 230000009467 reduction Effects 0.000 description 4
- 230000004936 stimulating effect Effects 0.000 description 4
- 208000024891 symptom Diseases 0.000 description 4
- 238000013519 translation Methods 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- 102100028972 HLA class I histocompatibility antigen, A alpha chain Human genes 0.000 description 3
- 108010075704 HLA-A Antigens Proteins 0.000 description 3
- 108010002350 Interleukin-2 Proteins 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 235000004279 alanine Nutrition 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 230000003466 anti-cipated effect Effects 0.000 description 3
- 230000004071 biological effect Effects 0.000 description 3
- 238000009566 cancer vaccine Methods 0.000 description 3
- 229940022399 cancer vaccine Drugs 0.000 description 3
- 230000001472 cytotoxic effect Effects 0.000 description 3
- 230000034994 death Effects 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 201000005202 lung cancer Diseases 0.000 description 3
- 208000020816 lung neoplasm Diseases 0.000 description 3
- 229960004857 mitomycin Drugs 0.000 description 3
- 210000002433 mononuclear leukocyte Anatomy 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 239000008196 pharmacological composition Substances 0.000 description 3
- 239000004033 plastic Substances 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 238000002560 therapeutic procedure Methods 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- 108700028369 Alleles Proteins 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 108010088729 HLA-A*02:01 antigen Proteins 0.000 description 2
- 108010004250 Inhibins Proteins 0.000 description 2
- 102000002746 Inhibins Human genes 0.000 description 2
- 108010050904 Interferons Proteins 0.000 description 2
- 102000014150 Interferons Human genes 0.000 description 2
- 108010063738 Interleukins Proteins 0.000 description 2
- 102000015696 Interleukins Human genes 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
- 241000124008 Mammalia Species 0.000 description 2
- 206010027476 Metastases Diseases 0.000 description 2
- 108020004511 Recombinant DNA Proteins 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
- 230000000259 anti-tumor effect Effects 0.000 description 2
- 230000005975 antitumor immune response Effects 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 238000002619 cancer immunotherapy Methods 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 239000003085 diluting agent Substances 0.000 description 2
- 238000010494 dissociation reaction Methods 0.000 description 2
- 230000005593 dissociations Effects 0.000 description 2
- 210000003038 endothelium Anatomy 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 239000008187 granular material Substances 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 239000000893 inhibin Substances 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 229940079322 interferon Drugs 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 210000004698 lymphocyte Anatomy 0.000 description 2
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- 230000009401 metastasis Effects 0.000 description 2
- NRNCYVBFPDDJNE-UHFFFAOYSA-N pemoline Chemical compound O1C(N)=NC(=O)C1C1=CC=CC=C1 NRNCYVBFPDDJNE-UHFFFAOYSA-N 0.000 description 2
- 229910052698 phosphorus Inorganic materials 0.000 description 2
- 229910052700 potassium Inorganic materials 0.000 description 2
- 238000004321 preservation Methods 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 235000019833 protease Nutrition 0.000 description 2
- 230000001177 retroviral effect Effects 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 229910052717 sulfur Inorganic materials 0.000 description 2
- 238000007910 systemic administration Methods 0.000 description 2
- 230000009258 tissue cross reactivity Effects 0.000 description 2
- 239000003053 toxin Substances 0.000 description 2
- 231100000765 toxin Toxicity 0.000 description 2
- 230000009261 transgenic effect Effects 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- LEBVLXFERQHONN-UHFFFAOYSA-N 1-butyl-N-(2,6-dimethylphenyl)piperidine-2-carboxamide Chemical compound CCCCN1CCCCC1C(=O)NC1=C(C)C=CC=C1C LEBVLXFERQHONN-UHFFFAOYSA-N 0.000 description 1
- 108010059616 Activins Proteins 0.000 description 1
- 102000005606 Activins Human genes 0.000 description 1
- 102100027241 Adenylyl cyclase-associated protein 1 Human genes 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 241000193738 Bacillus anthracis Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108010077333 CAP1-6D Proteins 0.000 description 1
- 102100035793 CD83 antigen Human genes 0.000 description 1
- 101100314454 Caenorhabditis elegans tra-1 gene Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical group [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 241001227713 Chiron Species 0.000 description 1
- 102000009016 Cholera Toxin Human genes 0.000 description 1
- 108010049048 Cholera Toxin Proteins 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 208000000666 Fowlpox 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
- 241000282412 Homo Species 0.000 description 1
- 101000946856 Homo sapiens CD83 antigen Proteins 0.000 description 1
- 101000914484 Homo sapiens T-lymphocyte activation antigen CD80 Proteins 0.000 description 1
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 1
- 108010002586 Interleukin-7 Proteins 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 102000043129 MHC class I family Human genes 0.000 description 1
- 108091054437 MHC class I family Proteins 0.000 description 1
- 108700018351 Major Histocompatibility Complex Proteins 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 108010046117 N-palmitoyl-5,6-dipalmitoyl-S-glycerylcysteinyl-seryl-serine Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 241000282577 Pan troglodytes Species 0.000 description 1
- 241001504519 Papio ursinus Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 241000009328 Perro Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 101100221606 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) COS7 gene Proteins 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 241000293871 Salmonella enterica subsp. enterica serovar Typhi Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 108010008038 Synthetic Vaccines Proteins 0.000 description 1
- 102100027222 T-lymphocyte activation antigen CD80 Human genes 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 229910052770 Uranium Inorganic materials 0.000 description 1
- 108070000030 Viral receptors Proteins 0.000 description 1
- 239000006096 absorbing agent Substances 0.000 description 1
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000000488 activin Substances 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 230000000172 allergic effect Effects 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 229940037003 alum Drugs 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 230000001093 anti-cancer Effects 0.000 description 1
- 230000003110 anti-inflammatory 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
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 208000010668 atopic eczema Diseases 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 102000015736 beta 2-Microglobulin Human genes 0.000 description 1
- 108010081355 beta 2-Microglobulin Proteins 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
- 230000033228 biological regulation Effects 0.000 description 1
- 238000001815 biotherapy Methods 0.000 description 1
- 229960003150 bupivacaine Drugs 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- UHBYWPGGCSDKFX-UHFFFAOYSA-N carboxyglutamic acid Chemical compound OC(=O)C(N)CC(C(O)=O)C(O)=O UHBYWPGGCSDKFX-UHFFFAOYSA-N 0.000 description 1
- 150000001732 carboxylic acid derivatives Chemical class 0.000 description 1
- -1 cationic lipid Chemical class 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 230000022534 cell killing Effects 0.000 description 1
- 230000007969 cellular immunity Effects 0.000 description 1
- 238000012822 chemical development Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 230000000973 chemotherapeutic effect Effects 0.000 description 1
- 238000003501 co-culture Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 239000012531 culture fluid Substances 0.000 description 1
- 238000012136 culture method 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
- 230000009089 cytolysis Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 229910003460 diamond Inorganic materials 0.000 description 1
- 239000010432 diamond Substances 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 238000001415 gene therapy Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000011521 glass Substances 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
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- UKAUYVFTDYCKQA-UHFFFAOYSA-N homoserine Chemical compound OC(=O)C(N)CCO UKAUYVFTDYCKQA-UHFFFAOYSA-N 0.000 description 1
- 150000002431 hydrogen Chemical group 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 230000006058 immune tolerance Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 230000002998 immunogenetic effect Effects 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 239000003547 immunosorbent Substances 0.000 description 1
- 230000001024 immunotherapeutic effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000126 in silico method Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 210000001821 langerhans cell Anatomy 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 238000001638 lipofection Methods 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- LSDPWZHWYPCBBB-UHFFFAOYSA-O methylsulfide anion Chemical compound [SH2+]C LSDPWZHWYPCBBB-UHFFFAOYSA-O 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229920005615 natural polymer Polymers 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000011275 oncology therapy Methods 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000003119 painkilling effect Effects 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000002831 pharmacologic agent Substances 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- BZQFBWGGLXLEPQ-REOHCLBHSA-N phosphoserine Chemical compound OC(=O)[C@@H](N)COP(O)(O)=O BZQFBWGGLXLEPQ-REOHCLBHSA-N 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 238000009117 preventive therapy Methods 0.000 description 1
- 238000011324 primary prophylaxis Methods 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 108010031970 prostasin Proteins 0.000 description 1
- 230000010349 pulsation Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 229940124551 recombinant vaccine Drugs 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 150000003462 sulfoxides Chemical class 0.000 description 1
- 125000004434 sulfur atom Chemical group 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- XVQKZSLOGHBCET-INVHGPFASA-N tripalmitoyl-S-glyceryl-cysteinyl-seryl-serine Chemical compound CCCCCCCCCCCCCCCC(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(O)=O)CSCC(OC(=O)CCCCCCCCCCCCCCC)COC(=O)CCCCCCCCCCCCCCC XVQKZSLOGHBCET-INVHGPFASA-N 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K4/00—Peptides having up to 20 amino acids in an undefined or only partially defined sequence; Derivatives thereof
- C07K4/12—Peptides having up to 20 amino acids in an undefined or only partially defined sequence; Derivatives thereof from animals; from humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/70—Carbohydrates; Sugars; Derivatives thereof
- A61K31/7088—Compounds having three or more nucleosides or nucleotides
-
- 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
- A61K39/0005—Vertebrate antigens
- A61K39/0011—Cancer antigens
-
- 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
- A61K39/0005—Vertebrate antigens
- A61K39/0011—Cancer antigens
- A61K39/001102—Receptors, cell surface antigens or cell surface determinants
- A61K39/001122—Ephrin Receptors [Eph]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/10—Cellular immunotherapy characterised by the cell type used
- A61K40/11—T-cells, e.g. tumour infiltrating lymphocytes [TIL] or regulatory T [Treg] cells; Lymphokine-activated killer [LAK] cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K40/00—Cellular immunotherapy
- A61K40/40—Cellular immunotherapy characterised by antigens that are targeted or presented by cells of the immune system
- A61K40/41—Vertebrate antigens
- A61K40/42—Cancer antigens
- A61K40/4202—Receptors, cell surface antigens or cell surface determinants
- A61K40/422—Ephrin Receptors [Eph]
-
- 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
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- 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
- A61K2039/57—Medicinal preparations containing antigens or antibodies characterised by the type of response, e.g. Th1, Th2
- A61K2039/572—Medicinal preparations containing antigens or antibodies characterised by the type of response, e.g. Th1, Th2 cytotoxic response
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2500/00—Screening for compounds of potential therapeutic value
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Epidemiology (AREA)
- Pharmacology & Pharmacy (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Toxicology (AREA)
- Oncology (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Cell Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US8997308P | 2008-08-19 | 2008-08-19 | |
| PCT/JP2009/003894 WO2010021111A1 (en) | 2008-08-19 | 2009-08-14 | Inhbb epitope peptides and vaccines containing the same |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MX2011001880A true MX2011001880A (es) | 2011-03-29 |
Family
ID=41707002
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MX2011001880A MX2011001880A (es) | 2008-08-19 | 2009-08-14 | Peptidos de epitope inhbb y vacunas que contienen los mismos. |
Country Status (13)
| Country | Link |
|---|---|
| US (7) | US20110280898A1 (enExample) |
| EP (1) | EP2326718A4 (enExample) |
| JP (1) | JP2012500001A (enExample) |
| KR (1) | KR20110063456A (enExample) |
| CN (1) | CN102186977A (enExample) |
| AU (1) | AU2009283762A1 (enExample) |
| CA (1) | CA2734515A1 (enExample) |
| IL (1) | IL211131A0 (enExample) |
| MX (1) | MX2011001880A (enExample) |
| RU (1) | RU2011110504A (enExample) |
| SG (1) | SG193214A1 (enExample) |
| TW (1) | TW201008574A (enExample) |
| WO (1) | WO2010021111A1 (enExample) |
Families Citing this family (41)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2325305B1 (en) * | 2005-02-25 | 2014-02-12 | Oncotherapy Science, Inc. | Peptide vaccines for lung cancers expressing TTK, URLC10 or KOC1 polypeptides |
| US9732131B2 (en) | 2006-02-27 | 2017-08-15 | Calviri, Inc. | Identification and use of novopeptides for the treatment of cancer |
| US8003098B2 (en) * | 2006-02-28 | 2011-08-23 | Oncotherapy Science, Inc. | Methods for damaging cells using effector functions of anti-EphA4 antibodies |
| US20090169572A1 (en) * | 2006-02-28 | 2009-07-02 | Oncotherapy Science, Inc, | Methods for damaging cells using effector functions of anti-cdh3 antibodies |
| EP2468887A1 (en) * | 2006-12-13 | 2012-06-27 | Oncotherapy Science, Inc. | TTK as tumor marker and therapeutic target for lung cancer |
| EP2185732A1 (en) * | 2007-07-30 | 2010-05-19 | Oncotherapy Science, Inc. | Cancer associated gene ly6k |
| UA100127C2 (ru) * | 2007-08-20 | 2012-11-26 | Онкотерапи Саенс, Инк. | Пептид cdh3 и лекарственное средство, содержащее его |
| JP5593560B2 (ja) | 2008-06-30 | 2014-09-24 | オンコセラピー・サイエンス株式会社 | 放射性同位体標識で標識された抗ｃｄｈ３抗体およびその使用 |
| TWI543767B (zh) | 2008-08-19 | 2016-08-01 | 腫瘤療法 科學股份有限公司 | Ｈｉｇ２與ｕｒｌｃ１０抗原決定位胜肽以及含此胜肽之疫苗 |
| RU2532105C2 (ru) | 2008-10-22 | 2014-10-27 | Онкотерапи Сайенс, Инк. | Эпитопные пептиды rab6kifl/kif20a и содержащие их вакцины |
| TWI500932B (zh) | 2008-12-05 | 2015-09-21 | Oncotherapy Science Inc | Ｗｄｒｐｕｈ抗原決定位胜肽以及含此胜肽之疫苗 |
| TW201102081A (en) | 2009-05-11 | 2011-01-16 | Oncotherapy Science Inc | TTK peptides and vaccines including the same |
| ES2701626T3 (es) | 2009-12-28 | 2019-02-25 | Oncotherapy Science Inc | Anticuerpos anti-CDH3 y sus usos |
| GB201004575D0 (en) | 2010-03-19 | 2010-05-05 | Immatics Biotechnologies Gmbh | Composition of tumor associated peptides and related anti cancer vaccine for the treatment of gastric cancer and other cancers |
| TWI538685B (zh) | 2010-04-02 | 2016-06-21 | 腫瘤療法 科學股份有限公司 | Ｅｃｔ２胜肽及含此胜肽之疫苗 |
| EP2795329A2 (en) * | 2011-12-23 | 2014-10-29 | Medical Research Council | Selective ligands for the angiotensin ii receptors |
| US20150359864A1 (en) * | 2012-03-09 | 2015-12-17 | Oncotherapy Science, Inc. | Pharmaceutical composition containing peptides |
| WO2014010231A1 (en) | 2012-07-10 | 2014-01-16 | Oncotherapy Science, Inc. | Kif20a epitope peptides for th1 cells and vaccines containing the same |
| JP6255594B2 (ja) * | 2012-07-10 | 2018-01-10 | オンコセラピー・サイエンス株式会社 | Ｔｈ１細胞のＬＹ６Ｋエピトープペプチドおよびこれを含有するワクチン |
| EP3640375A3 (en) | 2012-12-11 | 2020-07-29 | Albert Einstein College of Medicine | Methods for high throughput receptor/ligand identification |
| TWI658049B (zh) * | 2013-03-12 | 2019-05-01 | 腫瘤療法 科學股份有限公司 | Ｋｎｔｃ２胜肽及含此胜肽之疫苗 |
| GB201315946D0 (en) * | 2013-09-06 | 2013-10-23 | Immune Targeting Systems Its Ltd | Oncology vaccine |
| RU2016151645A (ru) | 2014-07-01 | 2018-08-03 | Пфайзер Инк. | Биспецифические гетеродимерные диантитела и их применение |
| AU2015300260B2 (en) * | 2014-08-04 | 2020-01-02 | Oncotherapy Science, Inc. | URLC10-derived peptide and vaccine containing same |
| KR102029248B1 (ko) | 2014-09-08 | 2019-10-08 | 국립연구개발법인 고쿠리츠간켄큐센터 | 암세포 특이적 항체, 항암제 및 암 검사 방법 |
| HK1245401A1 (zh) * | 2014-12-03 | 2018-08-24 | Verik Bio, Inc. | 监定、选择和使用高治疗潜力的t细胞表位 |
| GB201604458D0 (en) * | 2016-03-16 | 2016-04-27 | Immatics Biotechnologies Gmbh | Peptides and combination of peptides for use in immunotherapy against cancers |
| US11339201B2 (en) | 2016-05-18 | 2022-05-24 | Albert Einstein College Of Medicine | Variant PD-L1 polypeptides, T-cell modulatory multimeric polypeptides, and methods of use thereof |
| US11505591B2 (en) | 2016-05-18 | 2022-11-22 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| DE102016123893A1 (de) | 2016-12-08 | 2018-06-14 | Immatics Biotechnologies Gmbh | T-Zellrezeptoren mit verbesserter Bindung |
| CA3043630A1 (en) | 2016-12-22 | 2018-06-28 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
| EP3565829A4 (en) | 2017-01-09 | 2021-01-27 | Cue Biopharma, Inc. | T-CELL-MODULATING MULTIMERIC POLYPEPTIDES AND METHOD OF USING THEREOF |
| CN119371510A (zh) * | 2017-03-03 | 2025-01-28 | 特雷斯生物有限公司 | 肽疫苗 |
| CA3054955A1 (en) | 2017-03-15 | 2018-09-20 | Cue Biopharma, Inc. | Methods for modulating an immune response |
| WO2018223092A1 (en) | 2017-06-02 | 2018-12-06 | Arizona Board Of Regents On Behalf Of Arizona State University | A method to create personalized cancer vaccines |
| WO2019055618A1 (en) | 2017-09-15 | 2019-03-21 | Arizona Board Of Regents On Behalf Of Arizona State University | METHODS OF CLASSIFYING RESPONSES TO ANTICANCER IMMUNOTHERAPY |
| EP3737689A4 (en) | 2018-01-09 | 2021-12-01 | Cue Biopharma, Inc. | MULTIMER POLYPEPTIDES T-LYMPHOCYTE MODULATORS AND THEIR METHODS OF USE |
| US11666644B2 (en) | 2018-09-04 | 2023-06-06 | Treos Bio Limited | Peptide vaccines |
| EP4038222A4 (en) | 2019-10-02 | 2023-10-18 | Arizona Board of Regents on behalf of Arizona State University | METHODS AND COMPOSITIONS FOR IDENTIFYING NEOANTIGENS FOR USE IN THE TREATMENT AND PREVENTION OF CANCER |
| CN116096405A (zh) | 2020-05-12 | 2023-05-09 | Cue生物制药股份有限公司 | 多聚体t细胞调节多肽及其使用方法 |
| JP2023541366A (ja) | 2020-09-09 | 2023-10-02 | キュー バイオファーマ， インコーポレイテッド | １型真性糖尿病（ｔ１ｄ）を治療するためのｍｈｃクラスｉｉ ｔ細胞調節多量体ポリペプチド及びその使用方法 |
Family Cites Families (97)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3322314C2 (de) | 1983-06-21 | 1986-01-02 | Gebhard, Dietrich, 7502 Malsch | Schaltungsanordnung für ein Zugfahrzeug |
| NZ231899A (en) | 1985-10-03 | 1991-07-26 | Genentech Inc | Human or porcine inhibin peptide compositions and dna encoding them |
| US5089396A (en) | 1985-10-03 | 1992-02-18 | Genentech, Inc. | Nucleic acid encoding β chain prodomains of inhibin and method for synthesizing polypeptides using such nucleic acid |
| CA2084180A1 (en) | 1991-12-11 | 1993-06-12 | Paul P. Hung | Expression of specific immunogens using viral antigens |
| JPH09512167A (ja) | 1994-04-15 | 1997-12-09 | アムジエン・インコーポレーテツド | Ｈｅｋ５、ｈｅｋ７、ｈｅｋ８、ｈｅｋ１１、新規なｅｐｈ様受容体タンパク質チロシンキナーゼ |
| WO1998045433A1 (en) | 1997-04-04 | 1998-10-15 | Board Of Regents, The University Of Texas System | Proteins and compositions for modulating mitosis |
| US6800744B1 (en) | 1997-07-02 | 2004-10-05 | Genome Therapeutics Corporation | Nucleic acid and amino acid sequences relating to Streptococcus pneumoniae for diagnostics and therapeutics |
| US5891432A (en) | 1997-07-29 | 1999-04-06 | The Immune Response Corporation | Membrane-bound cytokine compositions comprising GM=CSF and methods of modulating an immune response using same |
| EP1022286A4 (en) | 1997-10-07 | 2003-04-09 | Ono Pharmaceutical Co | POLYPEPTIDES, FOR ENDING CODNA AND THEIR USE |
| US6747137B1 (en) | 1998-02-13 | 2004-06-08 | Genome Therapeutics Corporation | Nucleic acid sequences relating to Candida albicans for diagnostics and therapeutics |
| US6551795B1 (en) | 1998-02-18 | 2003-04-22 | Genome Therapeutics Corporation | Nucleic acid and amino acid sequences relating to pseudomonas aeruginosa for diagnostics and therapeutics |
| US6783961B1 (en) * | 1999-02-26 | 2004-08-31 | Genset S.A. | Expressed sequence tags and encoded human proteins |
| US20070014787A1 (en) | 1998-07-15 | 2007-01-18 | Human Genome Sciences, Inc. | 71 human secreted proteins |
| ATE323719T1 (de) | 1998-07-28 | 2006-05-15 | Greenpeptide Co Ltd | Hla-a2 beschränktes tumorantigen-peptid, das von sart-1 abstammt |
| WO2001064835A2 (en) | 2000-02-28 | 2001-09-07 | Hyseq, Inc. | Novel nucleic acids and polypeptides |
| ATE373715T1 (de) | 1999-08-04 | 2007-10-15 | Adelbert Bacher | Isoprenoid biosynthese |
| WO2001029221A2 (en) | 1999-10-20 | 2001-04-26 | Zymogenetics, Inc. | Proteins and polynucleotides encoding them |
| US6682902B2 (en) | 1999-12-16 | 2004-01-27 | Schering Aktiengesellschaft | DNA encoding a novel RG1 polypeptide |
| US20030013649A1 (en) | 2000-01-31 | 2003-01-16 | Rosen Craig A. | Nucleic acids, proteins, and antibodies |
| CA2400215A1 (en) | 2000-02-23 | 2001-08-30 | Epimmune Inc. | Hla binding peptides and their uses |
| CZ20023567A3 (cs) | 2000-03-29 | 2003-11-12 | Corixa Corporation | Sloučeniny a způsoby pro terapii a diagnostiku karcinomu plic |
| CN1469926A (zh) | 2000-03-29 | 2004-01-21 | 科里克萨有限公司 | 治疗和诊断肺癌的组合物和方法 |
| WO2002008765A2 (en) | 2000-07-26 | 2002-01-31 | Stanford University | Basal cell markers in breast cancer and uses thereof |
| US6830885B1 (en) | 2000-08-18 | 2004-12-14 | Phenogene Therapeutiques Inc. | Nucleic acid molecule, method and kit for selecting a nucleic acid having a desired feature |
| US20090062512A1 (en) | 2000-10-10 | 2009-03-05 | Hildebrand William H | Comparative ligand mapping from MHC class I positive cells |
| US7033832B2 (en) | 2000-10-13 | 2006-04-25 | University Of Medicine And Dentistry Of New Jersey | Endothelial cell—cell cohesion |
| AU2002215345A1 (en) | 2000-10-13 | 2002-04-22 | Eos Biotechnology, Inc. | Methods of diagnosis of prostate cancer, compositions and methods of screening for modulators of prostate cancer |
| US7919467B2 (en) | 2000-12-04 | 2011-04-05 | Immunotope, Inc. | Cytotoxic T-lymphocyte-inducing immunogens for prevention, treatment, and diagnosis of cancer |
| US7214786B2 (en) | 2000-12-14 | 2007-05-08 | Kovalic David K | Nucleic acid molecules and other molecules associated with plants and uses thereof for plant improvement |
| CN100400099C (zh) | 2001-01-04 | 2008-07-09 | 北京迪威华宇生物技术有限公司 | 预防和治疗人前列腺癌的重组蛋白疫苗 |
| WO2002078524A2 (en) | 2001-03-28 | 2002-10-10 | Zycos Inc. | Translational profiling |
| EP1463928A2 (en) | 2001-04-18 | 2004-10-06 | Protein Design Labs | Methods of diagnosis of lung cancer, compositions and methods of screening for modulators of lung cancer |
| AU2002347428A1 (en) | 2001-06-18 | 2003-01-02 | Eos Biotechnology Inc. | Methods of diagnosis of ovarian cancer, compositions and methods of screening for modulators of ovarian cancer |
| US20030124579A1 (en) | 2001-09-05 | 2003-07-03 | Eos Biotechnology, Inc. | Methods of diagnosis of ovarian cancer, compositions and methods of screening for modulators of ovarian cancer |
| US20040142325A1 (en) | 2001-09-14 | 2004-07-22 | Liat Mintz | Methods and systems for annotating biomolecular sequences |
| US20030232350A1 (en) | 2001-11-13 | 2003-12-18 | Eos Biotechnology, Inc. | Methods of diagnosis of cancer, compositions and methods of screening for modulators of cancer |
| US7314974B2 (en) | 2002-02-21 | 2008-01-01 | Monsanto Technology, Llc | Expression of microbial proteins in plants for production of plants with improved properties |
| EP1487857A4 (en) | 2002-03-07 | 2006-08-09 | Ludwig Inst Cancer Res | BLOOD AND LYMPHATIC ENDOTHELIAL CELL GENES |
| US20030194704A1 (en) | 2002-04-03 | 2003-10-16 | Penn Sharron Gaynor | Human genome-derived single exon nucleic acid probes useful for gene expression analysis two |
| US20070015271A1 (en) | 2002-04-04 | 2007-01-18 | Rosen Craig A | Human secreted proteins |
| US20060199179A1 (en) | 2002-06-19 | 2006-09-07 | Oncotherapy Science, Inc. | Method for diagnosis of colorectal tumors |
| JP2005532077A (ja) | 2002-07-10 | 2005-10-27 | オンコセラピー・サイエンス株式会社 | 腸型胃腫瘍の診断法 |
| FI116178B (fi) | 2002-08-22 | 2005-09-30 | Abb Oy | Vaihtosuuntaajan lähtökuristinsovitelma |
| WO2004035732A2 (en) | 2002-08-29 | 2004-04-29 | Five Prime Therapeutics, Inc. | Human polypeptides encoded by polynucleotides and methods of their use |
| DE60321356D1 (de) | 2002-08-30 | 2008-07-10 | Oncotherapy Science Inc | Verfahren zur diagnostik von eierstock endometriose |
| US20050214836A1 (en) | 2002-08-30 | 2005-09-29 | Oncotherapy Science, Inc. | Method of diagnosing ovarian endometriosis |
| US20050259483A1 (en) | 2002-09-30 | 2005-11-24 | Oncotherapy Science, Inc. | Genes and polypeptides relating to prostate cancers |
| US20060024692A1 (en) | 2002-09-30 | 2006-02-02 | Oncotherapy Science, Inc. | Method for diagnosing non-small cell lung cancers |
| JP2006500946A (ja) | 2002-09-30 | 2006-01-12 | オンコセラピー・サイエンス株式会社 | 精巣精上皮腫の診断方法 |
| TW200413725A (en) | 2002-09-30 | 2004-08-01 | Oncotherapy Science Inc | Method for diagnosing non-small cell lung cancers |
| US20050260639A1 (en) | 2002-09-30 | 2005-11-24 | Oncotherapy Science, Inc. | Method for diagnosing pancreatic cancer |
| TW200413539A (en) | 2002-09-30 | 2004-08-01 | Oncotherapy Science Inc | Genes and polypeptides relating to prostate cancers |
| DE60325628D1 (de) | 2002-09-30 | 2009-02-12 | Oncotherapy Science Inc | Gene und polypeptide in verbindung mit menschlichen pankreaskarzinomen |
| US20070224201A1 (en) | 2002-10-02 | 2007-09-27 | Genentech, Inc. | Compositions and methods for the diagnosis and treatment of tumor |
| US20040224408A1 (en) | 2002-12-10 | 2004-11-11 | Jean-Philippe Girard | THAP proteins as nuclear receptors for chemokines and roles in transcriptional regulation, cell proliferation and cell differentiation |
| AU2003297318A1 (en) | 2002-12-20 | 2004-07-22 | Millennium Pharmaceuticals, Inc. | Methods and compositions for treating cancer using 15986, 2188, 20743, 9148, 9151, 9791, 44252, 14184, 42461, 8204, 7970, 25552, 21657, 26492, 2411, 15088, 1905, 28899, 63380, 33935, 10480, 12686, 25501, 17694, 15701, 53062, 49908, 21612, 38949, 6216, 46863, 9235, 2201, 6985, 9883, 12238, 18057, 21617, 39228, 49928, 54476. |
| TWI324608B (en) | 2003-02-28 | 2010-05-11 | Oncotherapy Science Inc | Genes and polypeptides relating to human colorectal cancers |
| US7337154B2 (en) | 2003-05-19 | 2008-02-26 | Raytheon Company | Method for solving the binary minimization problem and a variant thereof |
| EP1651775A2 (en) | 2003-06-18 | 2006-05-03 | Arcturus Bioscience, Inc. | Breast cancer survival and recurrence |
| WO2005019258A2 (en) | 2003-08-11 | 2005-03-03 | Genentech, Inc. | Compositions and methods for the treatment of immune related diseases |
| CN1882698B (zh) | 2003-08-20 | 2011-05-25 | 肿瘤疗法科学股份有限公司 | 低氧可诱导的蛋白2(hig2)作为新的治疗肾细胞癌(rcc)的潜在标靶 |
| CN1898563B (zh) | 2003-09-24 | 2011-11-23 | 肿瘤疗法科学股份有限公司 | 诊断乳腺癌的方法 |
| WO2005091734A2 (en) | 2003-12-08 | 2005-10-06 | Silicon Image, Inc. | Integrated adressin scheme for use in a system having a tree structure |
| EP1730279A2 (en) | 2004-02-27 | 2006-12-13 | Oncotherapy Science, Inc. | Epha4 as therapeutic target of prc and pdaca |
| WO2005090572A2 (en) | 2004-03-24 | 2005-09-29 | Oncotherapy Science, Inc. | Compositions and methods for treating pancreatic cancer |
| KR101234281B1 (ko) | 2004-04-09 | 2013-02-18 | 가부시키가이샤 진케어켄큐쇼 | 염색체 안정화에 관한 유전자를 표적으로 하는 암세포 특이적 아포토시스 유도제 |
| EP1756147A2 (en) | 2004-06-01 | 2007-02-28 | Innogenetics N.V. | Peptides for inducing a ctl and/or htl response to hepatitis c virus |
| US8143228B2 (en) | 2004-07-12 | 2012-03-27 | Medical Research Fund Of Tel Aviv Sourasky Medical Center | Agents capable of downregulating an MSF-A dependent HIF-1α and use thereof in cancer treatment |
| WO2006055371A2 (en) | 2004-11-16 | 2006-05-26 | Alexion Pharmaceuticals, Inc. | Functional screening of antibody libraries |
| CN100381460C (zh) | 2004-11-30 | 2008-04-16 | 北京市肿瘤防治研究所 | Her-2模拟抗原表位及含有该表位的肽 |
| EP2292796A1 (en) | 2005-02-10 | 2011-03-09 | Oncotherapy Science, Inc. | Method of diagnosing bladder cancer |
| US8088976B2 (en) | 2005-02-24 | 2012-01-03 | Monsanto Technology Llc | Methods for genetic control of plant pest infestation and compositions thereof |
| EP1859266A4 (en) | 2005-02-24 | 2010-07-28 | Cemines Inc | COMPOSITIONS AND METHODS FOR CLASSIFYING BIOLOGICAL SAMPLES |
| EP2325305B1 (en) * | 2005-02-25 | 2014-02-12 | Oncotherapy Science, Inc. | Peptide vaccines for lung cancers expressing TTK, URLC10 or KOC1 polypeptides |
| EP1854473A1 (en) | 2005-03-03 | 2007-11-14 | Takeda Pharmaceutical Company Limited | Preventive/therapeutic agent for cancer |
| CN100348614C (zh) | 2005-06-03 | 2007-11-14 | 北京大学 | 一种肝癌－睾丸特异性抗原蛋白质和抗原肽 |
| WO2007009181A1 (en) | 2005-07-20 | 2007-01-25 | Agriculture Victoria Services Pty Ltd | Modification of flavonoid biosynthesis in plants |
| EP2311985A1 (en) | 2005-07-27 | 2011-04-20 | Oncotherapy Science, Inc. | Sirna for treating esophageal cancer |
| EP2305811A1 (en) | 2005-07-27 | 2011-04-06 | Oncotherapy Science, Inc. | Method of diagnosing smal cell lung cancer |
| EP1907580A2 (en) | 2005-07-28 | 2008-04-09 | Oncotherapy Science, Inc. | Method for diagnosing and treating renal cell carcinoma |
| WO2007013480A2 (en) | 2005-07-29 | 2007-02-01 | Oncotherapy Science, Inc. | Screening and therapeutic method for nsclc targeting cdca1-kntc2 complex |
| US8030443B2 (en) | 2005-08-09 | 2011-10-04 | Kurume University | Squamous cell carcinoma antigen-derived peptide binding to HLA-A24 molecule |
| DK1806359T3 (da) | 2005-09-05 | 2010-06-14 | Immatics Biotechnologies Gmbh | Tumorassocierede peptider, der bindes promiskuøst til Humant Leukocyt-Antigen (HLA) klasse II molekyler |
| US20090263832A1 (en) | 2005-11-30 | 2009-10-22 | Roberto Polakiewicz | Reagents for the Detection of Protein Phosphorylation in Leukemia Signaling Pathways |
| US20090169572A1 (en) | 2006-02-28 | 2009-07-02 | Oncotherapy Science, Inc, | Methods for damaging cells using effector functions of anti-cdh3 antibodies |
| US8003098B2 (en) | 2006-02-28 | 2011-08-23 | Oncotherapy Science, Inc. | Methods for damaging cells using effector functions of anti-EphA4 antibodies |
| EP2002259B1 (en) | 2006-04-10 | 2012-05-16 | Genentech, Inc. | Disheveled PDZ modulators |
| EP2468887A1 (en) | 2006-12-13 | 2012-06-27 | Oncotherapy Science, Inc. | TTK as tumor marker and therapeutic target for lung cancer |
| WO2008102906A1 (en) | 2007-02-20 | 2008-08-28 | Oncotherapy Science, Inc. | Hspc-hrpc transition genes |
| TWI615403B (zh) * | 2007-02-21 | 2018-02-21 | 腫瘤療法 科學股份有限公司 | 表現腫瘤相關抗原之癌症的胜肽疫苗 |
| US20090081659A1 (en) | 2007-03-07 | 2009-03-26 | Cell Signaling Technology, Inc. | Reagents for the detection of protein phosphorylation in carcinoma signaling pathways |
| EP1983003A3 (en) | 2007-04-19 | 2009-03-11 | Peter Hornbeck | Tyrosine phosphorylation sites and antibodies specific for them |
| EP2185732A1 (en) | 2007-07-30 | 2010-05-19 | Oncotherapy Science, Inc. | Cancer associated gene ly6k |
| UA100127C2 (ru) | 2007-08-20 | 2012-11-26 | Онкотерапи Саенс, Инк. | Пептид cdh3 и лекарственное средство, содержащее его |
| EP2080812A1 (en) | 2008-01-18 | 2009-07-22 | Transmedi SA | Compositions and methods of detecting post-stop peptides |
| TWI543767B (zh) | 2008-08-19 | 2016-08-01 | 腫瘤療法 科學股份有限公司 | Ｈｉｇ２與ｕｒｌｃ１０抗原決定位胜肽以及含此胜肽之疫苗 |
| EP2483690A1 (de) | 2009-09-29 | 2012-08-08 | Protagen AG | Markersequenzen für pankreaskrebserkrankungen, pankreaskarzinom und deren verwendung |
-
2009
- 2009-08-13 TW TW098127225A patent/TW201008574A/zh unknown
- 2009-08-14 AU AU2009283762A patent/AU2009283762A1/en not_active Abandoned
- 2009-08-14 JP JP2011507725A patent/JP2012500001A/ja not_active Ceased
- 2009-08-14 MX MX2011001880A patent/MX2011001880A/es not_active Application Discontinuation
- 2009-08-14 EP EP09808047A patent/EP2326718A4/en not_active Withdrawn
- 2009-08-14 CN CN2009801413475A patent/CN102186977A/zh not_active Withdrawn
- 2009-08-14 KR KR1020117005944A patent/KR20110063456A/ko not_active Withdrawn
- 2009-08-14 RU RU2011110504/10A patent/RU2011110504A/ru not_active Application Discontinuation
- 2009-08-14 US US13/059,617 patent/US20110280898A1/en not_active Abandoned
- 2009-08-14 CA CA2734515A patent/CA2734515A1/en not_active Abandoned
- 2009-08-14 SG SG2013062708A patent/SG193214A1/en unknown
- 2009-08-14 WO PCT/JP2009/003894 patent/WO2010021111A1/en not_active Ceased
- 2009-08-17 US US12/542,638 patent/US8383590B2/en active Active
-
2011
- 2011-02-09 IL IL211131A patent/IL211131A0/en unknown
-
2012
- 2012-05-04 US US13/464,831 patent/US8623829B2/en active Active
-
2013
- 2013-01-17 US US13/744,354 patent/US8759481B2/en not_active Expired - Fee Related
- 2013-11-13 US US14/079,144 patent/US9067973B2/en active Active
-
2014
- 2014-05-09 US US14/274,373 patent/US9284349B2/en active Active
-
2016
- 2016-01-06 US US14/989,741 patent/US20160200764A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| US20140248300A1 (en) | 2014-09-04 |
| US8383590B2 (en) | 2013-02-26 |
| US8759481B2 (en) | 2014-06-24 |
| SG193214A1 (en) | 2013-09-30 |
| KR20110063456A (ko) | 2011-06-10 |
| US20160200764A1 (en) | 2016-07-14 |
| US8623829B2 (en) | 2014-01-07 |
| JP2012500001A (ja) | 2012-01-05 |
| RU2011110504A (ru) | 2012-09-27 |
| CA2734515A1 (en) | 2010-02-25 |
| US20140141027A1 (en) | 2014-05-22 |
| US20120321649A1 (en) | 2012-12-20 |
| US9284349B2 (en) | 2016-03-15 |
| EP2326718A4 (en) | 2012-03-07 |
| IL211131A0 (en) | 2011-04-28 |
| EP2326718A1 (en) | 2011-06-01 |
| WO2010021111A1 (en) | 2010-02-25 |
| US20130189291A1 (en) | 2013-07-25 |
| US20110280898A1 (en) | 2011-11-17 |
| US20100040641A1 (en) | 2010-02-18 |
| AU2009283762A1 (en) | 2010-02-25 |
| TW201008574A (en) | 2010-03-01 |
| CN102186977A (zh) | 2011-09-14 |
| US9067973B2 (en) | 2015-06-30 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US20110280898A1 (en) | Inhbb epitope peptides and vaccines containing the same | |
| US8367799B2 (en) | TEM8 peptides and vaccines comprising the same | |
| US9387238B2 (en) | CDCA1 epitope peptides and vaccines containing the same | |
| US9119800B2 (en) | HIG2 and URLC10 epitope peptide and vaccines containing the same | |
| US9675680B2 (en) | MELK epitope peptides and vaccines containing the same | |
| WO2009150822A1 (en) | Mybl2 epitope peptides and vaccines containing the same | |
| AU2008238739B2 (en) | TEM8 peptides and vaccines comprising the same | |
| HK1155757B (en) | Cdca1 epitope peptides and vaccines containing the same | |
| HK1155757A (en) | Cdca1 epitope peptides and vaccines containing the same | |
| HK1157204B (en) | Hig2 and urlc10 epitope peptide and vaccines containing the same | |
| HK1175197B (en) | Tem8 peptides and vaccines comprising the same |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FA | Abandonment or withdrawal |