JP5657850B2 - 酸化還元機能性アミノ酸のタンパク質への部位特異的組み入れ - Google Patents

酸化還元機能性アミノ酸のタンパク質への部位特異的組み入れ Download PDF

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Publication number: JP5657850B2
Authority: JP; Japan
Prior art keywords: amino acid; trna; seq; acid sequence; set forth
Prior art date: 2003-10-14
Legal status (The legal status 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 status listed.): Expired - Fee Related

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JP2006535350A

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Japanese (ja)

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JP2007508034A (ja

JP2007508034A5 (2

Inventor

リタル・アルフォンタ

ピーター・ジー．・シュルツ

ツィウェン・ツァング

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ザスクリプスリサーチインスティテュート

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2003-10-14

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2004-10-13

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2015-01-21

2004-10-13 Application filed by ザスクリプスリサーチインスティテュート, ザスクリプスリサーチインスティテュート filed Critical ザスクリプスリサーチインスティテュート

2007-04-05 Publication of JP2007508034A publication Critical patent/JP2007508034A/ja

2007-12-27 Publication of JP2007508034A5 publication Critical patent/JP2007508034A5/ja

2015-01-21 Application granted granted Critical

2015-01-21 Publication of JP5657850B2 publication Critical patent/JP5657850B2/ja

2024-10-13 Anticipated expiration legal-status Critical

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NZVYCXVTEHPMHE-ZSUJOUNUSA-N thymalfasin Chemical compound CC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O NZVYCXVTEHPMHE-ZSUJOUNUSA-N 0.000 description 1
229960004231 thymalfasin Drugs 0.000 description 1
229940113082 thymine Drugs 0.000 description 1
239000005495 thyroid hormone Substances 0.000 description 1
229940036555 thyroid hormone Drugs 0.000 description 1
229960000187 tissue plasminogen activator Drugs 0.000 description 1
238000006257 total synthesis reaction Methods 0.000 description 1
238000002723 toxicity assay Methods 0.000 description 1
230000005026 transcription initiation Effects 0.000 description 1
108091006107 transcriptional repressors Proteins 0.000 description 1
238000012546 transfer Methods 0.000 description 1
230000001131 transforming effect Effects 0.000 description 1
230000009261 transgenic effect Effects 0.000 description 1
230000014621 translational initiation Effects 0.000 description 1
PYHOFAHZHOBVGV-UHFFFAOYSA-N triazane Chemical compound NNN PYHOFAHZHOBVGV-UHFFFAOYSA-N 0.000 description 1
239000001226 triphosphate Substances 0.000 description 1
235000011178 triphosphate Nutrition 0.000 description 1
UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
241001430294 unidentified retrovirus Species 0.000 description 1
229930195735 unsaturated hydrocarbon Natural products 0.000 description 1
229960005356 urokinase Drugs 0.000 description 1
208000007089 vaccinia Diseases 0.000 description 1
239000004474 valine Substances 0.000 description 1
230000002792 vascular Effects 0.000 description 1
239000013603 viral vector Substances 0.000 description 1
235000019154 vitamin C Nutrition 0.000 description 1
239000011718 vitamin C Substances 0.000 description 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
210000005253 yeast cell Anatomy 0.000 description 1
JPZXHKDZASGCLU-LBPRGKRZSA-N β-(2-naphthyl)-alanine Chemical compound C1=CC=CC2=CC(C[C@H](N)C(O)=O)=CC=C21 JPZXHKDZASGCLU-LBPRGKRZSA-N 0.000 description 1

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- 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
- C12N9/93—Ligases (6)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione

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Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
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Wood Science & Technology (AREA)
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Bioinformatics & Cheminformatics (AREA)
Genetics & Genomics (AREA)
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Microbiology (AREA)
Biotechnology (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
General Engineering & Computer Science (AREA)
Medicinal Chemistry (AREA)
Biomedical Technology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Enzymes And Modification Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Peptides Or Proteins (AREA)
Investigating Or Analysing Biological Materials (AREA)

JP2006535350A 2003-10-14 2004-10-13 酸化還元機能性アミノ酸のタンパク質への部位特異的組み入れ Expired - Fee Related JP5657850B2 (ja)

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US51153203P	2003-10-14	2003-10-14
US60/511,532		2003-10-14
PCT/US2004/034089 WO2005038002A2 (en)	2003-10-14	2004-10-13	Site-specific incorporation of redox active amino acids into proteins

Publications (3)

Publication Number	Publication Date
JP2007508034A JP2007508034A (ja)	2007-04-05
JP2007508034A5 JP2007508034A5 (2)	2007-12-27
JP5657850B2 true JP5657850B2 (ja)	2015-01-21

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JP2006535350A Expired - Fee Related JP5657850B2 (ja)	2003-10-14	2004-10-13	酸化還元機能性アミノ酸のタンパク質への部位特異的組み入れ

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Country	Link
US (5)	US7494796B2 (2)
EP (1)	EP1687401B1 (2)
JP (1)	JP5657850B2 (2)
CN (2)	CN1942579B (2)
AU (1)	AU2004282577B2 (2)
BR (1)	BRPI0415308A (2)
CA (1)	CA2541166A1 (2)
DK (1)	DK1687401T3 (2)
ES (1)	ES2396712T3 (2)
IL (3)	IL174947A (2)
MX (1)	MXPA06004087A (2)
PL (1)	PL1687401T3 (2)
PT (1)	PT1687401E (2)
WO (1)	WO2005038002A2 (2)

Cited By (1)

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US12134725B2 (en)	2019-06-17	2024-11-05	Merck Patent Gmbh	Liquid crystal-based light valve

Families Citing this family (29)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
WO2002085923A2 (en) *	2001-04-19	2002-10-31	The Scripps Research Institute	In vivo incorporation of unnatural amino acids
MXPA05003978A (es) *	2002-10-16	2005-06-22	Scripps Research Inst	Sintesis de glicoproteinas.
JP5642916B2 (ja)	2003-04-17	2014-12-17	ザスクリプスリサーチインスティテュート	真核遺伝コードの拡張
EP2410331B1 (en)	2003-06-18	2015-09-23	The Scripps Research Institute	Aminoacyl-tRNA synthetase for aminoacylation tRNA with unnatural amino acids
EP1649004A4 (en) *	2003-07-07	2008-04-09	Scripps Research Inst	COMPOSITIONS WITH PAIRS OF ORTHOGONAL LYSYL-TRNA AND AMINOACYL-TRNA-SYNTHETASE AND USES THEREOF
JP2008500050A (ja) *	2004-05-25	2008-01-10	ザスクリップスリサーチインスティテュート	結晶構造決定のための重原子含有非天然アミノ酸の部位特異的蛋白質組込み
DE102004031258A1 (de) *	2004-06-29	2006-02-09	Jennissen, Herbert P., Prof. Dr.	Proteinhybride mit polyhydroxyaromatischen Aminosäure-Epitopen
US20080171317A1 (en) *	2004-09-22	2008-07-17	The Scripps Research Institute	Site-Specific Labeling of Proteins for Nmr Studies
CN101048506B (zh)	2004-10-27	2013-06-26	斯克利普斯研究院	体内掺入非天然氨基酸的正交翻译组分
BRPI0617191A2 (pt) *	2005-10-12	2011-07-19	Scripps Research Inst	modificação pós-traducional de polipeptìdeos expressos em fagos
WO2007092475A2 (en) *	2006-02-06	2007-08-16	Franklin And Marshall College	Site-specific incorporation of fluorinated amino acids into proteins
KR20080106430A (ko) *	2006-03-09	2008-12-05	더 스크립스 리서치 인스티튜트	진정 세균 숙주 세포 내에서의 직교형 번역 성분의 발현을 위한 시스템
WO2007109035A2 (en)	2006-03-16	2007-09-27	The Scripps Research Institute	Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine
AU2007267950B2 (en) *	2006-05-23	2012-08-16	The Scripps Research Institute	Genetically encoded fluorescent coumarin amino acids
JP5385143B2 (ja) *	2006-09-21	2014-01-08	ザスクリプスリサーチインスティチュート	真正細菌における選択的に硫酸化された蛋白質の遺伝的にプログラムされた発現
WO2008073184A2 (en)	2006-10-18	2008-06-19	The Scripps Research Institute	Genetic incorporation of unnatural amino acids into proteins in mammalian cells
WO2008137452A1 (en) *	2007-05-04	2008-11-13	Kenergy Royalty Company, Llc	Implantable high efficiency digital stimulation device
US8673591B2 (en)	2007-10-25	2014-03-18	The Scripps Research Institute	Genetic incorporation of 3-aminotyrosine into reductases
WO2009059056A2 (en) *	2007-11-02	2009-05-07	The Scripps Research Institute	A genetically encoded boronate amino acid
JP5513398B2 (ja) *	2007-11-02	2014-06-04	ザスクリプスリサーチインスティチュート	非天然アミノ酸を含有する蛋白質を使用する指向的進化
CN101939410A (zh)	2007-12-11	2011-01-05	斯克利普斯研究院	甲基营养酵母菌巴斯德毕赤酵母中的体内非天然氨基酸表达
EP2249865A4 (en) *	2008-02-08	2012-04-04	Scripps Research Inst	BREAKING IMMUNOLOGICAL TOLERANCE WITH A GENETICALLY ENCODED UNNATURAL AMINO ACID
JP2012511403A (ja) *	2008-12-09	2012-05-24	クックメディカルテクノロジーズエルエルシー	鋲留め器具の制御放出のための装置と方法
US8609383B2 (en)	2008-12-10	2013-12-17	The Scripps Research Institute	Production of carrier-peptide conjugates using chemically reactive unnatural amino acids
US20090197339A1 (en) *	2008-12-10	2009-08-06	The Scripps Research Institute	In vivo unnatural amino acid expression in the methylotrophic yeast pichia pastoris
WO2010089741A1 (en) *	2009-02-04	2010-08-12	Ben-Gurion University Of The Negev Research And Development Authority	Systems and methods for bio-electricity production
JP6574754B2 (ja)	2013-03-19	2019-09-11	ベイジンシェノゲンファーマグループリミテッド	エストロゲン受容体関連疾患を処置するための抗体及び方法
US20150331624A1 (en) *	2014-05-19	2015-11-19	Kabushiki Kaisha Toshiba	Host-controlled flash translation layer snapshot
KR101956042B1 (ko) *	2017-07-13	2019-03-08	서강대학교산학협력단	표적 단백질 내 l-디하이드록시페닐알라닌의 도입 방법

Family Cites Families (10)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5879905A (en) *	1996-08-29	1999-03-09	Massachusetts Institute Of Technology	In vivo method of initiating protein synthesis with an amino acid other than methionine
WO2002085923A2 (en)	2001-04-19	2002-10-31	The Scripps Research Institute	In vivo incorporation of unnatural amino acids
MXPA05003978A (es)	2002-10-16	2005-06-22	Scripps Research Inst	Sintesis de glicoproteinas.
JP4444113B2 (ja)	2002-10-16	2010-03-31	ザスクリップスリサーチインスティテュート	ケトアミノ酸の部位特異的蛋白質組込み方法
CA2508939A1 (en)	2002-12-22	2004-07-15	The Scripps Research Institute	Protein arrays
JP5642916B2 (ja)	2003-04-17	2014-12-17	ザスクリプスリサーチインスティテュート	真核遺伝コードの拡張
EP2410331B1 (en)	2003-06-18	2015-09-23	The Scripps Research Institute	Aminoacyl-tRNA synthetase for aminoacylation tRNA with unnatural amino acids
WO2005007624A2 (en)	2003-07-07	2005-01-27	The Scripps Research Institute	Compositions of orthogonal glutamyl-trna and aminoacyl trna synthetase pairs and uses thereof
EP1649004A4 (en)	2003-07-07	2008-04-09	Scripps Research Inst	COMPOSITIONS WITH PAIRS OF ORTHOGONAL LYSYL-TRNA AND AMINOACYL-TRNA-SYNTHETASE AND USES THEREOF
US20060160175A1 (en)	2003-07-07	2006-07-20	The Scripps Research Institute	Compositions of orthogonal leucyl-trna and aminoacyl-trna synthetase pairs and uses thereof

2004
- 2004-10-13 PT PT47952767T patent/PT1687401E/pt unknown
- 2004-10-13 ES ES04795276T patent/ES2396712T3/es not_active Expired - Lifetime
- 2004-10-13 PL PL04795276T patent/PL1687401T3/pl unknown
- 2004-10-13 US US10/965,218 patent/US7494796B2/en not_active Expired - Lifetime
- 2004-10-13 MX MXPA06004087A patent/MXPA06004087A/es active IP Right Grant
- 2004-10-13 BR BRPI0415308-1A patent/BRPI0415308A/pt not_active IP Right Cessation
- 2004-10-13 CN CN2004800301376A patent/CN1942579B/zh not_active Expired - Fee Related
- 2004-10-13 AU AU2004282577A patent/AU2004282577B2/en not_active Ceased
- 2004-10-13 EP EP04795276A patent/EP1687401B1/en not_active Expired - Lifetime
- 2004-10-13 CN CN200910004743A patent/CN101532046A/zh active Pending
- 2004-10-13 US US10/575,991 patent/US8008041B2/en not_active Expired - Lifetime
- 2004-10-13 WO PCT/US2004/034089 patent/WO2005038002A2/en not_active Ceased
- 2004-10-13 CA CA002541166A patent/CA2541166A1/en not_active Abandoned
- 2004-10-13 JP JP2006535350A patent/JP5657850B2/ja not_active Expired - Fee Related
- 2004-10-13 DK DK04795276.7T patent/DK1687401T3/da active
2006
- 2006-04-11 IL IL174947A patent/IL174947A/en not_active IP Right Cessation
2008
- 2008-12-17 US US12/317,034 patent/US7811801B2/en not_active Expired - Lifetime
2009
- 2009-10-22 IL IL201705A patent/IL201705A0/en unknown
2010
- 2010-07-08 IL IL206889A patent/IL206889A0/en unknown
- 2010-08-20 US US12/806,751 patent/US8114654B2/en not_active Expired - Lifetime
2012
- 2012-01-05 US US13/344,436 patent/US9783798B2/en not_active Expired - Fee Related

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US12134725B2 (en)	2019-06-17	2024-11-05	Merck Patent Gmbh	Liquid crystal-based light valve

Also Published As

Publication number	Publication date
DK1687401T3 (da)	2013-02-04
ES2396712T3 (es)	2013-02-25
US20120100570A1 (en)	2012-04-26
AU2004282577B2 (en)	2009-10-29
PL1687401T3 (pl)	2013-04-30
BRPI0415308A (pt)	2006-12-05
IL174947A0 (en)	2006-08-20
CN101532046A (zh)	2009-09-16
US9783798B2 (en)	2017-10-10
CA2541166A1 (en)	2005-04-28
CN1942579A (zh)	2007-04-04
US8114654B2 (en)	2012-02-14
WO2005038002A2 (en)	2005-04-28
EP1687401B1 (en)	2012-11-21
US20050227318A1 (en)	2005-10-13
CN1942579B (zh)	2013-06-26
IL201705A0 (en)	2011-08-01
JP2007508034A (ja)	2007-04-05
US20090298124A1 (en)	2009-12-03
US20070009990A1 (en)	2007-01-11
IL206889A0 (en)	2010-12-30
WO2005038002A3 (en)	2006-11-23
EP1687401A2 (en)	2006-08-09
AU2004282577A1 (en)	2005-04-28
IL174947A (en)	2011-11-30
US7494796B2 (en)	2009-02-24
US8008041B2 (en)	2011-08-30
EP1687401A4 (en)	2007-08-01
PT1687401E (pt)	2013-02-26
US7811801B2 (en)	2010-10-12
US20110008782A1 (en)	2011-01-13
MXPA06004087A (es)	2006-06-27

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Publication	Publication Date	Title
JP5657850B2 (ja)	2015-01-21	酸化還元機能性アミノ酸のタンパク質への部位特異的組み入れ
JP5192150B2 (ja)	2013-05-08	直交リシルｔＲＮＡとアミノアシルｔＲＮＡシンテターゼの対の組成物及びその使用
EP1994165B1 (en)	2014-11-05	Genetically programmed expression of proteins containing the unnatural amino acid phenylselenocysteine
US7960141B2 (en)	2011-06-14	Systems for the expression of orthogonal translation components in eubacterial host cells
US7824893B2 (en)	2010-11-02	In vivo incorporation of alkynyl amino acids into proteins in eubacteria
KR20090094812A (ko)	2009-09-08	포유동물 세포에서 비천연 아미노산의 단백질 내로의 유전적 도입

JP5657850B2 - 酸化還元機能性アミノ酸のタンパク質への部位特異的組み入れ - Google Patents

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