BG106655A - Мим...'и-ни п...п'иди за ...пи'оп на аполипопро'...ин в-100, конка'...м...р, '...хни моди"и-ирани п...п'иди и 'ъ''ав на вак'ина - Google Patents

Мим...'и-ни п...п'иди за ...пи'оп на аполипопро'...ин в-100, конка'...м...р, '...хни моди"и-ирани п...п'иди и 'ъ''ав на вак'ина Download PDF

Info

Publication number: BG106655A
Authority: BG; Bulgaria
Prior art keywords: peptide; mimetic; concatemer; apolipoprotein; seq
Prior art date: 2000-09-04

Application number

BG106655A

Other languages

Bulgarian (bg)

English (en)

Inventor

Hyo-Joon Kim

Hae-Jung Joung

Original Assignee

Hyo-Joon Kim

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.)

2000-09-04

Filing date

2002-04-25

Publication date

2004-08-31

2001-09-04 Priority claimed from KR10-2001-0054005A external-priority patent/KR100472841B1/ko

2002-04-25 Application filed by Hyo-Joon Kim filed Critical Hyo-Joon Kim

2004-08-31 Publication of BG106655A publication Critical patent/BG106655A/bg

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
- C07K14/775—Apolipopeptides
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/04—Anorexiants; Antiobesity agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/06—Antihyperlipidemics
- 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
- 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

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Medicinal Chemistry (AREA)
General Health & Medical Sciences (AREA)
General Chemical & Material Sciences (AREA)
Engineering & Computer Science (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Chemical Kinetics & Catalysis (AREA)
Pharmacology & Pharmacy (AREA)
Bioinformatics & Cheminformatics (AREA)
Animal Behavior & Ethology (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Diabetes (AREA)
Genetics & Genomics (AREA)
Hematology (AREA)
Obesity (AREA)
Toxicology (AREA)
Zoology (AREA)
Gastroenterology & Hepatology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Molecular Biology (AREA)
Child & Adolescent Psychology (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)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicinal Preparation (AREA)

BG106655A 2000-09-04 2002-04-25 Мим...'и-ни п...п'иди за ...пи'оп на аполипопро'...ин в-100, конка'...м...р, '...хни моди"и-ирани п...п'иди и 'ъ''ав на вак'ина BG106655A (bg)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
KR20000052055		2000-09-04
PCT/KR2001/001492 WO2002020040A1 (en)	2000-09-04	2001-09-04	Mimetic peptides for epitope of apolipoprotein b-100, concatemer and modified peptides thereof, and the vaccine composition comprising the same
KR10-2001-0054005A KR100472841B1 (ko)	2000-09-04	2001-09-04	아포지단백질 비-100의 에피토프에 대한 모조 펩타이드,그들의 연쇄물 또는 변형체와 이들을 함유하는 백신 조성물

Publications (1)

Publication Number	Publication Date
BG106655A true BG106655A (bg)	2004-08-31

Family

ID=26638363

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Application Number	Title	Priority Date	Filing Date
BG106655A BG106655A (bg)	2000-09-04	2002-04-25	Мим...'и-ни п...п'иди за ...пи'оп на аполипопро'...ин в-100, конка'...м...р, '...хни моди"и-ирани п...п'иди и 'ъ''ав на вак'ина

Country Status (18)

Country	Link
US (1)	US6825318B2 (cs)
EP (1)	EP1315517B1 (cs)
JP (1)	JP2004508029A (cs)
CN (1)	CN1231262C (cs)
AU (1)	AU8628601A (cs)
BG (1)	BG106655A (cs)
BR (1)	BR0107175A (cs)
CA (1)	CA2389739A1 (cs)
CZ (1)	CZ20021571A3 (cs)
EE (1)	EE200200238A (cs)
HU (1)	HUP0203251A2 (cs)
IL (1)	IL149379A0 (cs)
LT (1)	LT4989B (cs)
MX (1)	MXPA02004505A (cs)
NO (1)	NO20022147L (cs)
RU (1)	RU2313536C2 (cs)
SK (1)	SK6312002A3 (cs)
WO (1)	WO2002020040A1 (cs)

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PL379196A1 (pl) *	2003-06-11	2006-07-24	Schering Aktiengesellschaft	Nowe zmodyfikowane cząsteczki koryny posiadające substytut sekwencji aktywacji i ich zastosowanie
KR100639397B1 (ko) *	2004-03-18	2006-10-26	(주)에스제이바이오메드	항비만용 면역원성 하이브리드 폴리펩타이드 및 이를포함하는 항비만 백신 조성물
US20070054298A1 (en) *	2005-08-12	2007-03-08	Kent Kirshenbaum	Methods for enzyme-mediated coupling of oligomers
WO2007075335A2 (en) *	2005-12-16	2007-07-05	The Regents Of The University Of California	Modulation of in utero immune programming
US8961982B2 (en) *	2005-12-16	2015-02-24	The Regents Of The University Of California	Modulation of developmental immune programming and protection against cardiovascular disease, diabetes, infectious diseases, and cancer
RU2418005C2 (ru) *	2006-09-25	2011-05-10	ЭсДжей БАЙОМЕД ИНК.	Иммуногенные гибридные полипептиды против ожирения и композиция вакцин против ожирения, содержащая эти полипептиды
CN103520713B (zh) *	2013-10-16	2015-10-28	西北农林科技大学	一种ApoB100酵母重组疫苗及其制备方法和应用
EP3463416A1 (en)	2016-05-31	2019-04-10	CardioVax, LLC	Methods for diagnosing and treating systemic lupus erythematosus
US10858422B2 (en)	2016-05-31	2020-12-08	Abcentra, Llc	Methods for treating systemic lupus erythematosus with an anti-apolipoprotein B antibody

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DE3215310A1 (de) *	1982-04-23	1983-10-27	Boehringer Mannheim Gmbh, 6800 Mannheim	Verfahren zur bestimmung der low density lipoproteine (ldl) und reagenz zu seiner durchfuehrung
US6309853B1 (en) *	1994-08-17	2001-10-30	The Rockfeller University	Modulators of body weight, corresponding nucleic acids and proteins, and diagnostic and therapeutic uses thereof
CA2283474A1 (en) *	1997-03-04	1998-09-11	Bio-Technology General Corp.	Isolation of tissue specific peptide ligands and their use for targeting pharmaceuticals to organs
AU2801299A (en) *	1998-03-04	1999-09-20	Bio-Technology General Corporation	Isolation of tissue specific peptide ligands and their use for targeting pharmaceuticals to organs
EP1267908B1 (en) *	2000-03-03	2004-05-06	GlaxoSmithKline Biologicals S.A.	Vaccine for the treatment of atherosclerosis

2001
- 2001-09-04 CN CNB018030572A patent/CN1231262C/zh not_active Expired - Fee Related
- 2001-09-04 JP JP2002524523A patent/JP2004508029A/ja active Pending
- 2001-09-04 EP EP01965715A patent/EP1315517B1/en not_active Expired - Lifetime
- 2001-09-04 EE EEP200200238A patent/EE200200238A/xx unknown
- 2001-09-04 HU HU0203251A patent/HUP0203251A2/hu unknown
- 2001-09-04 IL IL14937901A patent/IL149379A0/xx unknown
- 2001-09-04 AU AU86286/01A patent/AU8628601A/en not_active Abandoned
- 2001-09-04 RU RU2003109439/13A patent/RU2313536C2/ru not_active IP Right Cessation
- 2001-09-04 CA CA002389739A patent/CA2389739A1/en not_active Abandoned
- 2001-09-04 CZ CZ20021571A patent/CZ20021571A3/cs unknown
- 2001-09-04 SK SK631-2002A patent/SK6312002A3/sk unknown
- 2001-09-04 BR BR0107175-0A patent/BR0107175A/pt not_active Application Discontinuation
- 2001-09-04 WO PCT/KR2001/001492 patent/WO2002020040A1/en not_active Ceased
- 2001-09-04 MX MXPA02004505A patent/MXPA02004505A/es unknown
2002
- 2002-04-25 BG BG106655A patent/BG106655A/bg unknown
- 2002-04-29 LT LT2002051A patent/LT4989B/lt not_active IP Right Cessation
- 2002-05-03 NO NO20022147A patent/NO20022147L/no not_active Application Discontinuation
2003
- 2003-03-04 US US10/378,707 patent/US6825318B2/en not_active Expired - Lifetime

Also Published As

Publication number	Publication date
EP1315517B1 (en)	2010-10-20
CA2389739A1 (en)	2002-03-14
SK6312002A3 (en)	2002-09-10
JP2004508029A (ja)	2004-03-18
BR0107175A (pt)	2002-07-02
RU2003109439A (ru)	2004-07-20
LT4989B (lt)	2003-01-27
CN1392798A (zh)	2003-01-22
US6825318B2 (en)	2004-11-30
US20030211997A1 (en)	2003-11-13
MXPA02004505A (es)	2004-09-10
CZ20021571A3 (cs)	2002-09-11
IL149379A0 (en)	2002-11-10
WO2002020040A1 (en)	2002-03-14
EP1315517A1 (en)	2003-06-04
LT2002051A (en)	2002-09-25
NO20022147D0 (no)	2002-05-03
AU8628601A (en)	2002-03-22
HUP0203251A2 (hu)	2003-01-28
NO20022147L (no)	2002-05-03
CN1231262C (zh)	2005-12-14
RU2313536C2 (ru)	2007-12-27
EE200200238A (et)	2003-06-16
EP1315517A4 (en)	2005-02-09

Publication	Publication Date	Title
US6410022B1 (en)	2002-06-25	Modulation of cholesteryl ester transfer protein (CETP) activity
US8114966B2 (en)	2012-02-14	Peptide-based passive immunization therapy for treatment of atherosclerosis
US4521334A (en)	1985-06-04	Synthetic polypeptide fragments
BG106655A (bg)	2004-08-31	Мим...'и-ни п...п'иди за ...пи'оп на аполипопро'...ин в-100, конка'...м...р, '...хни моди"и-ирани п...п'иди и 'ъ''ав на вак'ина
JP2006506450A5 (cs)	2010-02-25
JP3910635B2 (ja)	2007-04-25	Ｈｄｌコレステロールレベルを増大する方法
WO2004030607A2 (en)	2004-04-15	Peptide-based passive immunization therapy for treatment of atherosclerosis
KR100472841B1 (ko)	2005-03-07	아포지단백질 비-100의 에피토프에 대한 모조 펩타이드,그들의 연쇄물 또는 변형체와 이들을 함유하는 백신 조성물
JP2003511061A (ja)	2003-03-25	変更された化学結合体化特性を有するａｂ５毒素ｂサブユニット変異体
AU2007200834B2 (en)	2010-10-14	Mimetic peptides for epitope of apolipoprotein B-100, concatemer and modified peptides thereof, and the vaccine composition comprising the same
US5993820A (en)	1999-11-30	Chimeric LTB vaccines
US5871739A (en)	1999-02-16	Pharmaceutical composition
TRZYNA et al.	1993	Schistosoma mansoni: genetic non‐response to p40, the major protein antigen of the egg, reveals a novel mechanism enhancing IgM production during infection
HK1050857A (en)	2003-07-11	Mimetic peptides for epitope of apolipoprotein b-100, concatemer and modified peptides thereof, and the vaccine composition comprising the same
JP2001520204A (ja)	2001-10-30	コレステリルエステル運搬タンパク質（ｃｅｔｐ）活性を調節するための異種ｃｅｔｐ
MXPA98005626A (es)	1999-05-31	Composiciones de proteolipido de fijacion de calcio, y metodos