CS91791A3 - Epithelium or epithelium precursors - Google Patents

Epithelium or epithelium precursors Download PDF

Info

Publication number: CS91791A3
Authority: CS; Czechoslovakia
Prior art keywords: epithelin; amino acid; chain; pharmaceutical composition; growth
Prior art date: 1990-04-03

Application number

CS91917A

Other languages

Czech (cs)

English (en)

Inventor

Mohammed Shoyab

Gregory D Plowman

Original Assignee

Bristol Myers Squibb Co

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.)

1990-04-03

Filing date

1991-04-03

Publication date

1992-06-17

1991-04-03 Application filed by Bristol Myers Squibb Co filed Critical Bristol Myers Squibb Co

1992-06-17 Publication of CS91791A3 publication Critical patent/CS91791A3/cs

Links

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Classifications

- 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
- C07K14/475—Growth factors; Growth regulators
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

Landscapes

Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
General Health & Medical Sciences (AREA)
Gastroenterology & Hepatology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
Zoology (AREA)
Genetics & Genomics (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Toxicology (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

CS91917A 1990-04-03 1991-04-03 Epithelium or epithelium precursors CS91791A3 (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US50450890A	1990-04-03	1990-04-03
US07/668,648 US5416192A (en)	1990-04-03	1991-03-13	Epithelins: novel cysteine-rich growth modulating proteins

Publications (1)

Publication Number	Publication Date
CS91791A3 true CS91791A3 (en)	1992-06-17

Family

ID=27054846

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CS91917A CS91791A3 (en)	1990-04-03	1991-04-03	Epithelium or epithelium precursors

Country Status (15)

Country	Link
US (3)	US5416192A (de)
EP (1)	EP0527806B1 (de)
CN (1)	CN1058782A (de)
AT (1)	ATE162549T1 (de)
AU (1)	AU639787B2 (de)
CA (1)	CA2079218A1 (de)
CS (1)	CS91791A3 (de)
DE (1)	DE69128779D1 (de)
GR (1)	GR3026263T3 (de)
HU (1)	HUT63438A (de)
IE (1)	IE911117A1 (de)
IL (1)	IL97758A0 (de)
NZ (1)	NZ237661A (de)
OA (1)	OA09711A (de)
WO (1)	WO1991015510A1 (de)

Families Citing this family (31)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
AU1325792A (en) *	1992-02-03	1993-09-01	Samuel Solomon	Granulins from leukocytes
WO2000075316A1 (en) *	1999-06-02	2000-12-14	Genentech, Inc.	Methods and compositions for inhibiting neoplastic cell growth
WO2000073348A2 (en) *	1999-06-02	2000-12-07	Genentech, Inc.	Methods and compositions for inhibiting neoplastic cell growth
WO2000032778A2 (en) *	1998-12-01	2000-06-08	Genentech, Inc.	Methods and compositions for inhibiting neoplastic cell growth
WO2000053751A1 (en) *	1999-03-08	2000-09-14	Genentech, Inc.	Methods and compositions for inhibiting neoplastic cell growth
US20030215445A1 (en) *	1997-05-23	2003-11-20	Ginette Serrero	Methods and compositions for inhibiting the growth of hematopoietic malignant cells
US6720159B1 (en) *	1997-12-16	2004-04-13	A&G Pharmaceutical, Inc.	88KDA tumorigenic growth factor and antagonists
US20100111928A1 (en) *	1997-05-23	2010-05-06	A & G Pharmaceutical, Inc.	Methods and kits for diagnosis tumorgenicity
US7091047B2 (en)	1997-05-23	2006-08-15	A&G Pharmaceutical, Inc.	Methods and kits for diagnosing tumorigenicity
US6309826B1 (en) *	1997-05-23	2001-10-30	Ginette Serrero	88kDa tumorigenic growth factor and antagonists
US6881548B2 (en) *	1997-05-23	2005-04-19	A&G Pharmaceutical, Inc.	Methods and kits for diagnosing tumorigenicity and determining resistance to the antineoplastic effects of antiestrogen therapy
US8512960B2 (en) *	1997-05-23	2013-08-20	A&G Pharmaceutical, Inc.	88kDa tumorigenic growth factor and antagonists
AU758462B2 (en) *	1998-10-13	2003-03-20	Genentech Inc.	Methods and compositions for inhibiting neoplastic cell growth
EP2075335A3 (de) *	1998-12-22	2009-09-30	Genentech, Inc.	Verfahren und Zusammensetzungen zur Hemmung des neoplastischen Zellenwachstums
ES2327785T3 (es) *	1998-12-22	2009-11-03	Genentech, Inc.	Procedimientos y compuestos para inhibir el crecimiento de celulas neoplasticas.
AU1749800A (en) *	1999-03-12	2000-10-04	Genentech Inc.	Methods and compositions for inhibiting neoplastic cell growth
EP1873244A3 (de) *	1999-06-02	2008-04-02	Genentech, Inc.	Verfahren und Zusammensetzungen zur Hemmung des neoplastischen Zellenwachstums
AU3246100A (en) *	1999-06-02	2000-12-28	Genentech Inc.	Methods and compositions for inhibiting neoplastic cell growth
CA2390685C (en) *	2000-01-06	2008-04-22	Genentech, Inc.	Methods and compositions for inhibiting neoplastic cell growth
EP1268516A4 (de) *	2000-02-28	2004-12-22	Univ California	Verfahren zur detektion und behandlung von neuronalen krebsarten
US6872703B2 (en) *	2000-06-07	2005-03-29	Ajinomoto Co., Inc.	Insulin receptor-related receptor binding protein
AUPR673001A0 (en) *	2001-07-31	2001-08-23	Prince Henry's Institute Of Medical Research	Pregnancy-related enzyme activity
AU2003213606A1 (en) *	2002-03-01	2003-10-13	Exelixis, Inc.	MP53s AS MODIFIERS OF THE p53 PATHWAY AND METHODS OF USE
US7411045B2 (en)	2002-11-19	2008-08-12	A&G Pharmaceutical, Inc.	Autocrine growth factor receptor antibodies and methods
EP1601687B1 (de) *	2003-02-26	2010-10-06	A & G Pharmaceuticals, Inc.	Verfahren zur erhöhung der ausbreitung von b-zellen
US7368428B2 (en) *	2003-06-23	2008-05-06	A&G Pharmaceutical, Inc.	Compositions and methods for restoring sensitivity of tumor cells to antitumor therapy and inducing apoptosis
US20070065887A1 (en) *	2003-07-21	2007-03-22	Kinch Michael S	Diagnosis of pre-cancerous conditions using pcdgf agents
US7674460B2 (en) *	2003-08-01	2010-03-09	A&G Pharmaceutical, Inc.	Compositions and methods for restoring sensitivity to treatment with HER2 antagonists
CN102216470A (zh)	2008-09-05	2011-10-12	A&G药品公司	诊断癌症和确定癌症患者的总体生存和无病生存的方法
US8362218B2 (en) *	2009-04-17	2013-01-29	New York University School Of Medicine	Peptides targeting TNF family receptors and antagonizing TNF action, compositions, methods and uses thereof
US9913399B2 (en)	2015-02-09	2018-03-06	Dell Products, Lp	System and method for wireless rack management controller communication

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4590003A (en) *	1984-03-23	1986-05-20	Oncogen	Platelet related growth regulator

1991
- 1991-03-13 US US07/668,648 patent/US5416192A/en not_active Expired - Fee Related
- 1991-04-03 CN CN91103067A patent/CN1058782A/zh active Pending
- 1991-04-03 EP EP91908376A patent/EP0527806B1/de not_active Expired - Lifetime
- 1991-04-03 IL IL97758A patent/IL97758A0/xx unknown
- 1991-04-03 CA CA002079218A patent/CA2079218A1/en not_active Abandoned
- 1991-04-03 AT AT91908376T patent/ATE162549T1/de not_active IP Right Cessation
- 1991-04-03 CS CS91917A patent/CS91791A3/cs unknown
- 1991-04-03 NZ NZ237661A patent/NZ237661A/xx unknown
- 1991-04-03 AU AU77447/91A patent/AU639787B2/en not_active Ceased
- 1991-04-03 HU HU923137A patent/HUT63438A/hu unknown
- 1991-04-03 DE DE69128779T patent/DE69128779D1/de not_active Expired - Lifetime
- 1991-04-03 IE IE111791A patent/IE911117A1/en unknown
- 1991-04-03 WO PCT/US1991/002321 patent/WO1991015510A1/en not_active Ceased
1992
- 1992-10-02 OA OA60284A patent/OA09711A/en unknown
1995
- 1995-04-27 US US08/431,333 patent/US5965723A/en not_active Expired - Lifetime
- 1995-04-27 US US08/429,998 patent/US5885961A/en not_active Expired - Lifetime
1998
- 1998-02-27 GR GR980400441T patent/GR3026263T3/el unknown

Also Published As

Publication number	Publication date
CN1058782A (zh)	1992-02-19
CA2079218A1 (en)	1991-10-04
US5885961A (en)	1999-03-23
DE69128779D1 (de)	1998-02-26
GR3026263T3 (en)	1998-05-29
IE911117A1 (en)	1991-10-09
US5416192A (en)	1995-05-16
NZ237661A (en)	1993-07-27
IL97758A0 (en)	1992-06-21
WO1991015510A1 (en)	1991-10-17
OA09711A (en)	1993-08-30
HU9203137D0 (en)	1992-12-28
US5965723A (en)	1999-10-12
HUT63438A (en)	1993-08-30
EP0527806A1 (de)	1993-02-24
AU639787B2 (en)	1993-08-05
ATE162549T1 (de)	1998-02-15
EP0527806B1 (de)	1998-01-21
EP0527806A4 (en)	1993-05-05
AU7744791A (en)	1991-10-30

Publication	Publication Date	Title
CS91791A3 (en)	1992-06-17	Epithelium or epithelium precursors
US5773252A (en)	1998-06-30	Fibroblast growth factor 15
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