NO311366B1 - Isolert nukleinsyremolekyl som koder for gp75, fremgangsmåte for å fremstille en aminosyresekvens fra samme, samt fremgangsmåtefor å fremstille vaksine - Google Patents

Isolert nukleinsyremolekyl som koder for gp75, fremgangsmåte for å fremstille en aminosyresekvens fra samme, samt fremgangsmåtefor å fremstille vaksine Download PDF

Info

Publication number: NO311366B1
Authority: NO; Norway
Prior art keywords: fragment; nucleic acid; melanoma; amino acid; vaccine
Prior art date: 1990-03-22

Application number

NO19923659A

Other languages

English (en)

Norwegian (no)

Other versions

NO923659D0 (no

NO923659L (no

Inventor

Alan N Houghton

Setaluri Vijayasaradhi

Original Assignee

Sloan Kettering Inst Cancer

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1990-03-22

Filing date

1992-09-21

Publication date

2001-11-19

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=23976841&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=NO311366(B1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1992-09-21 Application filed by Sloan Kettering Inst Cancer filed Critical Sloan Kettering Inst Cancer

1992-09-21 Publication of NO923659D0 publication Critical patent/NO923659D0/no

1992-11-06 Publication of NO923659L publication Critical patent/NO923659L/no

2001-11-19 Publication of NO311366B1 publication Critical patent/NO311366B1/no

Links

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Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y110/00—Oxidoreductases acting on diphenols and related substances as donors (1.10)
- C12Y110/03—Oxidoreductases acting on diphenols and related substances as donors (1.10) with an oxygen as acceptor (1.10.3)
- C12Y110/03001—Catechol oxidase (1.10.3.1), i.e. tyrosinase
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- 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
- 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
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0055—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10)
- C12N9/0057—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10) with oxygen as acceptor (1.10.3)
- C12N9/0059—Catechol oxidase (1.10.3.1), i.e. tyrosinase
- 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
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0071—Oxidoreductases (1.) acting on paired donors with incorporation of molecular oxygen (1.14)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y114/00—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14)
- C12Y114/16—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14) with reduced pteridine as one donor, and incorporation of one atom of oxygen (1.14.16)
- C12Y114/16002—Tyrosine 3-monooxygenase (1.14.16.2)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y114/00—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14)
- C12Y114/18—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14) with another compound as one donor, and incorporation of one atom of oxygen (1.14.18)
- C12Y114/18001—Tyrosinase (1.14.18.1)
- 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

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Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
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Life Sciences & Earth Sciences (AREA)
Zoology (AREA)
Genetics & Genomics (AREA)
Engineering & Computer Science (AREA)
Wood Science & Technology (AREA)
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Biochemistry (AREA)
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Molecular Biology (AREA)
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Proteomics, Peptides & Aminoacids (AREA)
Toxicology (AREA)
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Animal Behavior & Ethology (AREA)
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General Chemical & Material Sciences (AREA)
Public Health (AREA)
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Pharmacology & Pharmacy (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)

NO19923659A 1990-03-22 1992-09-21 Isolert nukleinsyremolekyl som koder for gp75, fremgangsmåte for å fremstille en aminosyresekvens fra samme, samt fremgangsmåtefor å fremstille vaksine NO311366B1 (no)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US49743190A	1990-03-22	1990-03-22
PCT/US1991/001942 WO1991014775A1 (en)	1990-03-22	1991-03-22	Gp75 as a tumor vaccine for melanoma

Publications (3)

Publication Number	Publication Date
NO923659D0 NO923659D0 (no)	1992-09-21
NO923659L NO923659L (no)	1992-11-06
NO311366B1 true NO311366B1 (no)	2001-11-19

Family

ID=23976841

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
NO19923659A NO311366B1 (no)	1990-03-22	1992-09-21	Isolert nukleinsyremolekyl som koder for gp75, fremgangsmåte for å fremstille en aminosyresekvens fra samme, samt fremgangsmåtefor å fremstille vaksine

Country Status (20)

Country	Link
US (2)	US6168946B1 (cs)
EP (2)	EP0522078B1 (cs)
JP (2)	JP3336006B2 (cs)
AT (1)	ATE187493T1 (cs)
AU (1)	AU660412B2 (cs)
CA (1)	CA2078773C (cs)
CZ (1)	CZ290278B6 (cs)
DE (1)	DE69131829T2 (cs)
DK (1)	DK0522078T3 (cs)
ES (1)	ES2141089T3 (cs)
FI (1)	FI113786B (cs)
GR (1)	GR3032804T3 (cs)
HU (1)	HU218416B (cs)
IE (2)	IE910820A1 (cs)
NO (1)	NO311366B1 (cs)
NZ (1)	NZ237532A (cs)
PL (3)	PL169168B1 (cs)
PT (1)	PT97103B (cs)
SK (1)	SK282873B6 (cs)
WO (1)	WO1991014775A1 (cs)

Families Citing this family (18)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
IE910820A1 (en) *	1990-03-22	1991-09-25	Sloan Kettering Inst Cancer	Gp75 as a tumor vaccine for melanoma
US7041801B1 (en) *	1995-06-07	2006-05-09	Vanderbilt University	Antibodies binding to polypeptides encoded by developmentally-regulated endothelial cell locus-1
US7015312B1 (en)	1996-02-09	2006-03-21	The United States Of America As Represented By The Department Of Health And Human Services	Antibodies to the protein product encoded by ORF3 of the TRP-1 gene and compositions and kits thereof
US5840839A (en) *	1996-02-09	1998-11-24	The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services	Alternative open reading frame DNA of a normal gene and a novel human cancer antigen encoded therein
US7001600B1 (en)	1996-02-09	2006-02-21	The United States Of America As Represented By The Secretary Of Health And Human Services	Identification of TRP-2 as a human tumor antigen recognized by cytotoxic T lymphocytes
US6083703A (en) *	1996-02-09	2000-07-04	The United States Of America As Represented By The Department Of Health And Human Services	Identification of TRP-2 as a human tumor antigen recognized by cytotoxic T lymphocytes
JP2004527449A (ja) *	2000-02-15	2004-09-09	リージェンツオブザユニバーシティオブカリフォルニア	テロメラーゼ逆転写酵素を用いる癌を治療するための万能ワクチンと方法
US6613534B2 (en)	2001-03-20	2003-09-02	Wake Forest University Health Sciences	MAP-2 as a determinant of metastatic potential
US20030113919A1 (en) *	2001-08-17	2003-06-19	Aventis Pasteur, Ltd.	Immunogenic targets for melanoma
US20030157720A1 (en) *	2002-02-06	2003-08-21	Expression Technologies Inc.	Protein standard for estimating size and mass
RU2287575C1 (ru) *	2005-04-22	2006-11-20	Государственное учреждение Российский онкологический научный центр им. Н.Н. Блохина РАМН	КЛЕТОЧНАЯ ЛИНИЯ МЕЛАНОМЫ ЧЕЛОВЕКА mel P, ИСПОЛЬЗУЕМАЯ ДЛЯ ПОЛУЧЕНИЯ ПРОТИВООПУХОЛЕВЫХ ВАКЦИН
RU2287578C1 (ru) *	2005-04-22	2006-11-20	Государственное учреждение Российский онкологический научный центр им. Н.Н. Блохина РАМН	КЛЕТОЧНАЯ ЛИНИЯ МЕЛАНОМЫ ЧЕЛОВЕКА mel Kor, ИСПОЛЬЗУЕМАЯ ДЛЯ ПОЛУЧЕНИЯ ПРОТИВООПУХОЛЕВЫХ ВАКЦИН
RU2287577C1 (ru) *	2005-04-22	2006-11-20	Государственное учреждение Российский онкологический научный центр им. Н.Н. Блохина РАМН	КЛЕТОЧНАЯ ЛИНИЯ МЕЛАНОМЫ ЧЕЛОВЕКА mel IL, ИСПОЛЬЗУЕМАЯ ДЛЯ ПОЛУЧЕНИЯ ПРОТИВООПУХОЛЕВЫХ ВАКЦИН
CA2690627C (en)	2007-06-15	2014-12-02	Genelux Corporation	Microorganisms for imaging and/or treatment of tumors
US7951370B2 (en)	2008-03-12	2011-05-31	Imclone Llc	Anti-TYRP1 antibodies
RU2373280C1 (ru) *	2008-04-24	2009-11-20	Государственное учреждение Российский онкологический научный центр им. Н.Н. Блохина РАМН	КЛЕТОЧНАЯ ЛИНИЯ МЕЛАНОМЫ ЧЕЛОВЕКА mel Gus, ИСПОЛЬЗУЕМАЯ ДЛЯ ПОЛУЧЕНИЯ ПРОТИВООПУХОЛЕВЫХ ВАКЦИН
RU2390556C1 (ru) *	2008-12-26	2010-05-27	Государственное учреждение Российский онкологический научный центр им. Н.Н. Блохина РАМН	КЛЕТОЧНАЯ ЛИНИЯ МЕЛАНОМЫ ЧЕЛОВЕКА mel Z, ИСПОЛЬЗУЕМАЯ ДЛЯ ПОЛУЧЕНИЯ ПРОТИВООПУХОЛЕВЫХ ВАКЦИН
RU2402603C1 (ru) *	2009-02-12	2010-10-27	Государственное учреждение Российский онкологический научный центр им. Н.Н. Блохина РАМН	КЛЕТОЧНАЯ ЛИНИЯ МЕЛАНОМЫ ЧЕЛОВЕКА mel Me, ИСПОЛЬЗУЕМАЯ ДЛЯ ПОЛУЧЕНИЯ ПРОТИВООПУХОЛЕВЫХ ВАКЦИН

Family Cites Families (16)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
FR2504010B1 (fr) *	1981-04-15	1985-10-25	Sanofi Sa	Medicaments anticancereux contenant la chaine a de la ricine associee a un anticorps antimelanome et procede pour leur preparation
US4808704A (en) *	1981-09-30	1989-02-28	Sloan-Kettering Institute For Cancer Research	Monoclonal antibodies to cell surface antigens of human malignant melanoma
US4806628A (en) *	1982-11-30	1989-02-21	Sloan-Kettering Institute For Cancer Research	Monoclonal antibodies against melanocytes
US4591572A (en) *	1983-04-01	1986-05-27	Sloan-Kettering Institute For Cancer Research	Pigmentation associated, differentiation antigen of human melanoma and autologous antibody
USH819H (en) *	1984-04-30	1990-09-04	The United States Of America As Represented By The Secretary Of Energy	Palladium-109 labeled anti-melanoma monoclonal antibodies
US4851510A (en) *	1984-11-30	1989-07-25	Wadley Technologies, Inc.	Monoclonal antibodies to novel melanoma-associated antigens
US4798790A (en) *	1985-07-18	1989-01-17	Sloan-Kettering Institute	Monoclonal antibody specific for a pigmentation associated antigen
US5262177A (en) *	1986-02-07	1993-11-16	Oncogen	Recombinant viruses encoding the human melanoma-associated antigen
US5141742A (en) *	1986-02-07	1992-08-25	Oncogen	Vaccines against melanoma
US5009995A (en) *	1986-10-27	1991-04-23	Sloan-Kettering Institute For Cancer Research	Monoclonal antibodies to melanoma cells
US5059523A (en) *	1988-05-02	1991-10-22	Sloan-Kettering Institute For Cancer Research	Cell-surface glycoproteins of human sarcomas
US5009495A (en) *	1989-05-26	1991-04-23	Williams Robert D	Hinge for eyeglasses
ES2166352T3 (es)	1989-08-04	2002-04-16	Schering Ag	Dominio externo de c-erbb-2:gp75.
IE910820A1 (en) *	1990-03-22	1991-09-25	Sloan Kettering Inst Cancer	Gp75 as a tumor vaccine for melanoma
US5262117A (en) *	1990-10-12	1993-11-16	Centro Sviluppo Settori Impiego S.R.L.	Process for preparing thermoinsulating and/or structural formed articles and products so obtained
US6180604B1 (en) *	1996-08-21	2001-01-30	Micrologix Biotech Inc.	Compositions and methods for treating infections using analogues of indolicidin

1991
- 1991-03-12 IE IE082091A patent/IE910820A1/en not_active IP Right Cessation
- 1991-03-12 IE IE20000918A patent/IE20000918A1/en not_active IP Right Cessation
- 1991-03-21 SK SK760-91A patent/SK282873B6/sk unknown
- 1991-03-21 CZ CS1991760A patent/CZ290278B6/cs not_active IP Right Cessation
- 1991-03-21 NZ NZ237532A patent/NZ237532A/xx unknown
- 1991-03-21 PT PT97103A patent/PT97103B/pt not_active IP Right Cessation
- 1991-03-22 PL PL91307930A patent/PL169168B1/pl not_active IP Right Cessation
- 1991-03-22 CA CA002078773A patent/CA2078773C/en not_active Expired - Fee Related
- 1991-03-22 DE DE69131829T patent/DE69131829T2/de not_active Revoked
- 1991-03-22 AU AU76906/91A patent/AU660412B2/en not_active Ceased
- 1991-03-22 AT AT91908003T patent/ATE187493T1/de not_active IP Right Cessation
- 1991-03-22 ES ES91908003T patent/ES2141089T3/es not_active Expired - Lifetime
- 1991-03-22 EP EP91908003A patent/EP0522078B1/en not_active Revoked
- 1991-03-22 DK DK91908003T patent/DK0522078T3/da active
- 1991-03-22 PL PL91307929A patent/PL169105B1/pl not_active IP Right Cessation
- 1991-03-22 EP EP99109256A patent/EP0965640A1/en not_active Withdrawn
- 1991-03-22 HU HU9203009A patent/HU218416B/hu unknown
- 1991-03-22 JP JP50783191A patent/JP3336006B2/ja not_active Expired - Fee Related
- 1991-03-22 WO PCT/US1991/001942 patent/WO1991014775A1/en not_active Ceased
- 1991-03-22 PL PL91289550A patent/PL168235B1/pl not_active IP Right Cessation
1992
- 1992-09-21 NO NO19923659A patent/NO311366B1/no unknown
- 1992-09-21 FI FI924222A patent/FI113786B/fi active
1995
- 1995-03-24 US US08/409,794 patent/US6168946B1/en not_active Expired - Lifetime
2000
- 2000-02-29 GR GR20000400507T patent/GR3032804T3/el not_active IP Right Cessation
2001
- 2001-12-25 JP JP2001391870A patent/JP2002241314A/ja active Pending
2004
- 2004-06-25 US US10/877,489 patent/US20050037462A1/en not_active Abandoned

Also Published As

Publication number	Publication date
DE69131829D1 (de)	2000-01-13
JP3336006B2 (ja)	2002-10-21
PT97103A (pt)	1991-12-31
PL289550A1 (en)	1992-07-27
SK282873B6 (sk)	2003-01-09
FI113786B (fi)	2004-06-15
NZ237532A (en)	1993-03-26
NO923659D0 (no)	1992-09-21
HK1014732A1 (en)	1999-09-30
US20050037462A1 (en)	2005-02-17
PL169105B1 (pl)	1996-06-28
GR3032804T3 (en)	2000-06-30
JPH06501837A (ja)	1994-03-03
EP0522078A1 (en)	1993-01-13
PT97103B (pt)	1999-02-26
ES2141089T3 (es)	2000-03-16
HU218416B (hu)	2000-08-28
DE69131829T2 (de)	2000-06-15
US6168946B1 (en)	2001-01-02
PL169168B1 (pl)	1996-06-28
CS76091A3 (en)	1992-02-19
AU7690691A (en)	1991-10-21
NO923659L (no)	1992-11-06
FI924222A0 (fi)	1992-09-21
IE20000918A1 (en)	2001-05-30
PL168235B1 (pl)	1996-01-31
AU660412B2 (en)	1995-06-29
JP2002241314A (ja)	2002-08-28
EP0522078A4 (en)	1993-05-26
FI924222L (fi)	1992-09-21
CA2078773C (en)	2001-07-03
HUT62934A (en)	1993-06-28
EP0965640A1 (en)	1999-12-22
WO1991014775A1 (en)	1991-10-03
ATE187493T1 (de)	1999-12-15
CZ290278B6 (cs)	2002-07-17
IE910820A1 (en)	1991-09-25
DK0522078T3 (da)	2000-06-13
EP0522078B1 (en)	1999-12-08
CA2078773A1 (en)	1991-09-23

Publication	Publication Date	Title
EP0522078B1 (en)	1999-12-08	Gp75 as a tumor vaccine for melanoma
Jimenez et al.	1989	Specific identification of an authentic clone for mammalian tyrosinase
Vijayasaradhi et al.	1990	The melanoma antigen gp75 is the human homologue of the mouse b (brown) locus gene product.
US5141742A (en)	1992-08-25	Vaccines against melanoma
Vijayasaradhi et al.	1991	Purification of an autoantigenic 75‐kDa human melanosomal glycoprotein
JP4019040B2 (ja)	2007-12-05	抗原提示の調節
CA2182889C (en)	2008-12-23	Peptides recognized by melanoma-specific cytotoxic lymphocytes, and uses therefor
Cohen-Solal et al.	2003	Identification and characterization of mouse Rab32 by mRNA and protein expression analysis
Nussbaum et al.	1985	Site-specific antibodies to rat myelin proteolipids directed against the C-terminal hexapeptide
JP4315257B2 (ja)	2009-08-19	新規コンドロイチン硫酸プロテオグリカン、そのコア蛋白質、それをコードするｄｎａおよびそれに対する抗体
Bouchard et al.	1994	Production and characterization of antibodies against human tyrosinase
HK1025790A (en)	2000-11-24	Gp75 as a tumor vaccine for melanoma
HK1014732B (en)	2000-08-18	Gp75 as a tumor vaccine for melanoma
JPH0751065A (ja)	1995-02-28	糖タンパク質３９遺伝子
JPH09194502A (ja)	1997-07-29	新規コンドロイチン硫酸プロテオグリカン、そのコア蛋白質、それをコードするｄｎａおよびそれに対する抗体
Amar-Costesec et al.	1994	Identification and characterization of the tumor-specific P1A gene product
Kahn-Perles et al.	1989	Cytotoxic T lymphocyte recognition of secreted HLA class I molecules.
EP1369478A1 (en)	2003-12-10	Novel scavenger receptor class a protein
Verdier et al.	2005	Identification of a new, testis-specific sperm antigen localized on the principal piece of the spermatozoa tail in the fox (Vulpes vulpes)
KR20060114326A (ko)	2006-11-06	티로시나아제 돌연변이 및 이의 사용 방법
Jaanson et al.	2003	Identification of the immunodominant regions of the melanoma antigen tyrosinase by anti-tyrosinase monoclonal antibodies
WO1991014698A1 (en)	1991-10-03	Marine tyrosinase gene
Walker	1998	Characterization of adenylate cyclase toxin plus macrophage and thymic peptides by mass spectrometry
JPH11222499A (ja)	1999-08-17	プロテアソーム抑制蛋白質およびそれをコードするポリヌクレオチド
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