JP2002505672A - 水溶液中における保護されていないか又はｎ−末端システインで保護されたペプチドの固相での自然化学連結 - Google Patents
水溶液中における保護されていないか又はｎ−末端システインで保護されたペプチドの固相での自然化学連結Info
- Publication number
- JP2002505672A JP2002505672A JP50326799A JP50326799A JP2002505672A JP 2002505672 A JP2002505672 A JP 2002505672A JP 50326799 A JP50326799 A JP 50326799A JP 50326799 A JP50326799 A JP 50326799A JP 2002505672 A JP2002505672 A JP 2002505672A
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- peptide
- solid phase
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- segment
- unprotected
- Prior art date
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- Ceased
Links
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- 230000007423 decrease Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 125000000118 dimethyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 238000000132 electrospray ionisation Methods 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- DWYMPOCYEZONEA-UHFFFAOYSA-L fluoridophosphate Chemical compound [O-]P([O-])(F)=O DWYMPOCYEZONEA-UHFFFAOYSA-L 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 239000011630 iodine Substances 0.000 description 1
- 229910052740 iodine Inorganic materials 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 238000001698 laser desorption ionisation Methods 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- BQPIGGFYSBELGY-UHFFFAOYSA-N mercury(2+) Chemical compound [Hg+2] BQPIGGFYSBELGY-UHFFFAOYSA-N 0.000 description 1
- 125000000250 methylamino group Chemical group [H]N(*)C([H])([H])[H] 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- SBOJXQVPLKSXOG-UHFFFAOYSA-N o-amino-hydroxylamine Chemical compound NON SBOJXQVPLKSXOG-UHFFFAOYSA-N 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 150000002923 oximes Chemical class 0.000 description 1
- 238000010422 painting Methods 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 108010091748 peptide A Proteins 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000003880 polar aprotic solvent Substances 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 229920005990 polystyrene resin Polymers 0.000 description 1
- 239000005373 porous glass Substances 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 238000013341 scale-up Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 238000004611 spectroscopical analysis Methods 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 239000010959 steel Substances 0.000 description 1
- KZNICNPSHKQLFF-UHFFFAOYSA-N succinimide Chemical compound O=C1CCC(=O)N1 KZNICNPSHKQLFF-UHFFFAOYSA-N 0.000 description 1
- 125000000446 sulfanediyl group Chemical group *S* 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 230000009897 systematic effect Effects 0.000 description 1
- FPGGTKZVZWFYPV-UHFFFAOYSA-M tetrabutylammonium fluoride Chemical compound [F-].CCCC[N+](CCCC)(CCCC)CCCC FPGGTKZVZWFYPV-UHFFFAOYSA-M 0.000 description 1
- 238000006257 total synthesis reaction Methods 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/06—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents
- C07K1/08—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents using activating agents
- C07K1/086—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length using protecting groups or activating agents using activating agents containing sulfur
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/02—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length in solution
- C07K1/023—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length in solution using racemisation inhibiting agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/02—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length in solution
- C07K1/026—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length in solution by fragment condensation in solution
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/04—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length on carriers
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/04—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length on carriers
- C07K1/047—Simultaneous synthesis of different peptide species; Peptide libraries
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Analytical Chemistry (AREA)
- Peptides Or Proteins (AREA)
- Other Investigation Or Analysis Of Materials By Electrical Means (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US4955397P | 1997-06-13 | 1997-06-13 | |
| US60/049,553 | 1997-06-13 | ||
| PCT/US1998/012278 WO1998056807A1 (en) | 1997-06-13 | 1998-06-12 | Solid phase native chemical ligation of unprotected or n-terminal cysteine protected peptides in aqueous solution |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2002505672A true JP2002505672A (ja) | 2002-02-19 |
| JP2002505672A5 JP2002505672A5 (OSRAM) | 2005-12-22 |
Family
ID=21960431
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP50326799A Ceased JP2002505672A (ja) | 1997-06-13 | 1998-06-12 | 水溶液中における保護されていないか又はｎ−末端システインで保護されたペプチドの固相での自然化学連結 |
Country Status (9)
| Country | Link |
|---|---|
| US (4) | US6326468B1 (OSRAM) |
| EP (1) | EP1001968B1 (OSRAM) |
| JP (1) | JP2002505672A (OSRAM) |
| AT (2) | ATE354584T1 (OSRAM) |
| AU (1) | AU745094B2 (OSRAM) |
| CA (1) | CA2292724A1 (OSRAM) |
| DE (2) | DE69828287T2 (OSRAM) |
| ES (2) | ES2282788T3 (OSRAM) |
| WO (1) | WO1998056807A1 (OSRAM) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007046456A1 (ja) * | 2005-10-19 | 2007-04-26 | Chugai Seiyaku Kabushiki Kaisha | 新規水溶性プロドラッグを含有する、膵臓癌、卵巣癌または肝臓癌の予防または治療剤 |
| US7910593B2 (en) | 2004-04-09 | 2011-03-22 | Chugai Seiyaku Kabushiki Kaisha | Water-soluble prodrugs |
| US8022047B2 (en) | 2005-08-22 | 2011-09-20 | Chugai Seiyaku Kabushiki Kaisha | Combination anticancer agents |
| JP2014532075A (ja) * | 2011-10-17 | 2014-12-04 | サントル ナシオナル ドゥ ラ ルシェルシェサイアンティフィク（セエヌエールエス） | タンパク質の合成方法 |
| KR20210098466A (ko) * | 2018-11-30 | 2021-08-10 | 가부시키가이샤 도우사 고가쿠 겐큐쇼 | 펩티드 티오에스테르 및 펩티드의 신규 제조 방법 |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6184344B1 (en) * | 1995-05-04 | 2001-02-06 | The Scripps Research Institute | Synthesis of proteins by native chemical ligation |
| US6849428B1 (en) * | 1997-03-05 | 2005-02-01 | New England Biolabs, Inc. | Intein-mediated protein ligation of expressed proteins |
| EP1001968B1 (en) * | 1997-06-13 | 2004-12-22 | Gryphon Therapeutics, Inc. | Solid phase native chemical ligation of unprotected or n-terminal cysteine protected peptides in aqueous solution |
| WO1999011655A1 (en) * | 1997-09-04 | 1999-03-11 | Gryphon Sciences | Modular protein libraries and methods of preparation |
| AUPP589598A0 (en) | 1998-09-14 | 1998-10-08 | University Of Queensland, The | Novel peptides |
| US7001745B1 (en) * | 1998-09-30 | 2006-02-21 | New England Biolabs, Inc. | Intein mediated peptide ligation |
| AU768118B2 (en) * | 1999-03-11 | 2003-12-04 | Gryphon Sciences | Chemical synthesis and use of soluble membrane protein receptor domains |
| SK782002A3 (en) | 1999-07-21 | 2003-08-05 | Lexigen Pharm Corp | FC fusion proteins for enhancing the immunogenicity of protein and peptide antigens |
| AU2001284853A1 (en) * | 2000-08-11 | 2002-02-25 | Invitrogen Corporation | Highly homogeneous molecular markers for electrophoresis |
| US20040014082A1 (en) * | 2000-08-11 | 2004-01-22 | Invitrogen Corporation | Highly homogeneous molecular markers for electrophoresis |
| JP2004507557A (ja) * | 2000-09-01 | 2004-03-11 | グリフォン セラピューティクス，インコーポレーテッド | 求核物質に対して安定なチオエステル生成化合物、製造および使用の方法 |
| CA2435394C (en) * | 2001-01-22 | 2018-01-09 | Sangamo Biosciences, Inc. | Modified zinc finger binding proteins |
| DE60216468T2 (de) * | 2001-03-09 | 2007-09-27 | Boston Probes, Inc., Bedford | Kombinationsoligomere betreffende verfahren, kits und zusammensetzungen |
| GB0113657D0 (en) * | 2001-06-05 | 2001-07-25 | Geneprot Inc | Improved native chemical ligation with three or more components |
| EP2042196B1 (en) | 2001-10-10 | 2016-07-13 | ratiopharm GmbH | Remodelling and glycoconjugation of Granulocyte Colony Stimulating Factor (G-CSF) |
| WO2003106615A2 (en) * | 2002-06-10 | 2003-12-24 | Geneprot, Inc. | Post-cleavage sulfur deprotection for convergent protein synthesis by chemical ligation |
| AU2002328824A1 (en) * | 2002-06-29 | 2004-01-19 | Aquanova German Solubilisate Technologies (Agt) Gmbh | Isoflavone concentrate and method for production thereof |
| US7166574B2 (en) * | 2002-08-20 | 2007-01-23 | Biosurface Engineering Technologies, Inc. | Synthetic heparin-binding growth factor analogs |
| US7598224B2 (en) * | 2002-08-20 | 2009-10-06 | Biosurface Engineering Technologies, Inc. | Dual chain synthetic heparin-binding growth factor analogs |
| US8227411B2 (en) | 2002-08-20 | 2012-07-24 | BioSurface Engineering Technologies, Incle | FGF growth factor analogs |
| US7981862B2 (en) | 2003-08-19 | 2011-07-19 | Biosurface Engineering Technologies, Inc. | Composition comprising BMP-2 amplifier/co-activator for enhancement of osteogenesis |
| AU2003300859A1 (en) * | 2002-12-11 | 2004-06-30 | New England Biolabs, Inc. | Carrier-ligand fusions and uses thereof |
| WO2004061094A1 (en) | 2002-12-30 | 2004-07-22 | Gryphon Therapeutics, Inc. | Water-soluble thioester and selenoester compounds and methods for making and using the same |
| NZ542586A (en) | 2003-04-09 | 2009-11-27 | Biogenerix Ag | Method of forming a covalent conjugate between a G-CSF peptide and PEG |
| ES2333598T5 (es) * | 2003-05-06 | 2013-09-04 | Biogen Idec Hemophilia Inc | Proteinas quimericas del factor de coagulacion fc para tratar la hemofilia. |
| US7348004B2 (en) | 2003-05-06 | 2008-03-25 | Syntonix Pharmaceuticals, Inc. | Immunoglobulin chimeric monomer-dimer hybrids |
| TWI353991B (en) | 2003-05-06 | 2011-12-11 | Syntonix Pharmaceuticals Inc | Immunoglobulin chimeric monomer-dimer hybrids |
| WO2004105685A2 (en) * | 2003-05-22 | 2004-12-09 | Gryphon Therapeutics, Inc. | Displaceable linker solid phase chemical ligation |
| US7414028B1 (en) | 2004-02-04 | 2008-08-19 | Biosurface Engineering Technologies, Inc. | Growth factor analogs |
| US7528105B1 (en) | 2004-02-10 | 2009-05-05 | Biosurface Engineering Technologies | Heterodimeric chain synthetic heparin-binding growth factor analogs |
| US20080227696A1 (en) | 2005-02-22 | 2008-09-18 | Biosurface Engineering Technologies, Inc. | Single branch heparin-binding growth factor analogs |
| US7671012B2 (en) | 2004-02-10 | 2010-03-02 | Biosurface Engineering Technologies, Inc. | Formulations and methods for delivery of growth factor analogs |
| US20060024347A1 (en) * | 2004-02-10 | 2006-02-02 | Biosurface Engineering Technologies, Inc. | Bioactive peptide coatings |
| DE602005023714D1 (de) | 2004-02-20 | 2010-11-04 | Biosurface Eng Tech Inc | Positiver modulator des knochenmorphogenetisches protein-2 (bmp-2) |
| EP1749022A2 (en) * | 2004-05-24 | 2007-02-07 | Rigel Pharmaceuticals, Inc. | Methods for cyclizing synthetic polymers |
| US7671023B2 (en) | 2005-03-31 | 2010-03-02 | Amylin Pharmaceuticals, Inc. | Amylin agonist for treating depression, anxiety disorder and schizophrenia |
| US7674881B2 (en) * | 2005-10-07 | 2010-03-09 | The University Of Chicago | Convergent synthesis of proteins by kinetically controlled ligation |
| US7820172B1 (en) | 2006-06-01 | 2010-10-26 | Biosurface Engineering Technologies, Inc. | Laminin-derived multi-domain peptides |
| WO2008097536A2 (en) | 2007-02-05 | 2008-08-14 | Amylin Pharmaceuticals, Inc. | Compositions and methods for treating psychiatric diseases and disorders |
| US8404804B2 (en) * | 2007-08-28 | 2013-03-26 | Ipsen Pharma S.A.S. | Methods and intermediates for chemical synthesis of polypeptides and proteins |
| WO2011103409A1 (en) * | 2010-02-18 | 2011-08-25 | Advanced Proteome Therapeutics Inc. | Site-specific modification of proteins through chemical modification enabling protein conjugates, protein dimer formation, and stapled peptides |
| EA201390450A1 (ru) | 2010-09-28 | 2013-07-30 | Амилин Фармасьютикалс, Ллк. | Полипептиды с увеличенной продолжительностью действия |
| JP2014502252A (ja) | 2010-09-28 | 2014-01-30 | アミリン・ファーマシューティカルズ，リミテッド・ライアビリティ・カンパニー | 作用持続時間が増した改変ポリペプチド |
| JP6006309B2 (ja) | 2011-07-08 | 2016-10-12 | アミリン・ファーマシューティカルズ, リミテッド・ライアビリティ・カンパニーAmylin Pharmaceuticals, Llc | 作用持続期間が増大し、免疫原性が減少した操作されたポリペプチド |
| ES2732475T3 (es) | 2011-07-08 | 2019-11-22 | Aegerion Pharmaceuticals Inc | Polipéptidos modificados por ingeniería genética que tienen una duración potenciada de la acción y una inmunogenicidad reducida |
| JP6290187B2 (ja) | 2012-05-11 | 2018-03-07 | クランツ，アレクサンダー | 癌の処置のためのタンパク質の部位特異的標識及び標的送達 |
| JP2015519344A (ja) | 2012-05-21 | 2015-07-09 | マサチューセッツ インスティテュート オブ テクノロジー | 炭疽菌防御抗原ポアを通しての非天然化学実体のトランスロケーション |
| TWI828269B (zh) | 2013-03-15 | 2024-01-01 | 美商百歐維拉提夫治療公司 | 因子ix多肽調配物 |
| US11273176B2 (en) | 2016-03-02 | 2022-03-15 | The Brigham And Women's Hospital, Inc. | Use of PLA2G5-deficient suppressive macrophages in suppression of inflammation |
| JP7067798B2 (ja) * | 2017-03-02 | 2022-05-16 | 株式会社糖鎖工学研究所 | アミノ酸ポリマーの製造方法 |
| WO2020070587A1 (en) | 2018-10-01 | 2020-04-09 | Université De Genève | Methods for producing a plurality of polypeptide variants suitable for biological analysis |
| AU2020361681A1 (en) | 2019-10-10 | 2022-05-05 | 1859, Inc. | Methods and systems for microfluidic screening |
| EP3838913A4 (en) * | 2019-10-23 | 2021-11-03 | MabPlex International Co., Ltd. | OLIGOPEPTIDE LINKER INTERMEDIATE AND MANUFACTURING PROCESS FOR IT |
| WO2022266467A2 (en) | 2021-06-17 | 2022-12-22 | Dana-Farber Cancer Institute, Inc. | Recombinant histone polypeptide and uses thereof |
| WO2024146707A1 (en) | 2023-01-06 | 2024-07-11 | Université De Genève | Variant ligand conjugates for payload delivery |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5064940A (en) * | 1988-05-11 | 1991-11-12 | Protein Technologies, Inc. | Premixed dry reagent containing a protected amino acid and an activating agent for use in solid phase protein synthesis |
| US5101059A (en) * | 1989-12-05 | 1992-03-31 | Research Corporation Technologies, Inc. | Amino acid protecting groups |
| PT832096E (pt) | 1995-05-04 | 2002-01-30 | Scripps Research Inst | Sintese de proteinas atraves de ligacao quimica nativa |
| JP4358307B2 (ja) * | 1996-12-24 | 2009-11-04 | ザ スクリップス リサーチ インスティテュート | 一般的化学結合 |
| EP1001968B1 (en) * | 1997-06-13 | 2004-12-22 | Gryphon Therapeutics, Inc. | Solid phase native chemical ligation of unprotected or n-terminal cysteine protected peptides in aqueous solution |
| US6329468B1 (en) * | 2000-01-21 | 2001-12-11 | Bostik Findley, Inc. | Hot melt adhesive based on semicrystalline flexible polyolefins |
-
1998
- 1998-06-12 EP EP98929035A patent/EP1001968B1/en not_active Expired - Lifetime
- 1998-06-12 ES ES04029270T patent/ES2282788T3/es not_active Expired - Lifetime
- 1998-06-12 DE DE69828287T patent/DE69828287T2/de not_active Expired - Fee Related
- 1998-06-12 CA CA002292724A patent/CA2292724A1/en not_active Abandoned
- 1998-06-12 AT AT04029270T patent/ATE354584T1/de not_active IP Right Cessation
- 1998-06-12 ES ES98929035T patent/ES2235336T3/es not_active Expired - Lifetime
- 1998-06-12 WO PCT/US1998/012278 patent/WO1998056807A1/en not_active Ceased
- 1998-06-12 DE DE69837170T patent/DE69837170T2/de not_active Expired - Fee Related
- 1998-06-12 US US09/097,094 patent/US6326468B1/en not_active Expired - Fee Related
- 1998-06-12 JP JP50326799A patent/JP2002505672A/ja not_active Ceased
- 1998-06-12 AT AT98929035T patent/ATE285415T1/de not_active IP Right Cessation
- 1998-06-12 AU AU80695/98A patent/AU745094B2/en not_active Ceased
-
2001
- 2001-11-15 US US09/987,675 patent/US7030217B2/en not_active Expired - Fee Related
- 2001-11-15 US US09/987,655 patent/US7094871B2/en not_active Expired - Fee Related
-
2005
- 2005-05-03 US US11/119,831 patent/US20050209440A1/en not_active Abandoned
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7910593B2 (en) | 2004-04-09 | 2011-03-22 | Chugai Seiyaku Kabushiki Kaisha | Water-soluble prodrugs |
| US8022047B2 (en) | 2005-08-22 | 2011-09-20 | Chugai Seiyaku Kabushiki Kaisha | Combination anticancer agents |
| WO2007046456A1 (ja) * | 2005-10-19 | 2007-04-26 | Chugai Seiyaku Kabushiki Kaisha | 新規水溶性プロドラッグを含有する、膵臓癌、卵巣癌または肝臓癌の予防または治療剤 |
| JP2014532075A (ja) * | 2011-10-17 | 2014-12-04 | サントル ナシオナル ドゥ ラ ルシェルシェサイアンティフィク（セエヌエールエス） | タンパク質の合成方法 |
| KR20210098466A (ko) * | 2018-11-30 | 2021-08-10 | 가부시키가이샤 도우사 고가쿠 겐큐쇼 | 펩티드 티오에스테르 및 펩티드의 신규 제조 방법 |
| KR102769851B1 (ko) * | 2018-11-30 | 2025-02-20 | 가부시키가이샤 도우사 고가쿠 겐큐쇼 | 펩티드 티오에스테르 및 펩티드의 신규 제조 방법 |
Also Published As
| Publication number | Publication date |
|---|---|
| DE69837170T2 (de) | 2007-11-22 |
| US20050209440A1 (en) | 2005-09-22 |
| ES2235336T3 (es) | 2005-07-01 |
| ES2282788T3 (es) | 2007-10-16 |
| DE69828287T2 (de) | 2005-12-15 |
| EP1001968B1 (en) | 2004-12-22 |
| WO1998056807A1 (en) | 1998-12-17 |
| EP1001968A1 (en) | 2000-05-24 |
| DE69837170D1 (de) | 2007-04-05 |
| ATE285415T1 (de) | 2005-01-15 |
| US7030217B2 (en) | 2006-04-18 |
| US20020132975A1 (en) | 2002-09-19 |
| US7094871B2 (en) | 2006-08-22 |
| ATE354584T1 (de) | 2007-03-15 |
| US6326468B1 (en) | 2001-12-04 |
| US20020169282A1 (en) | 2002-11-14 |
| AU8069598A (en) | 1998-12-30 |
| AU745094B2 (en) | 2002-03-14 |
| DE69828287D1 (de) | 2005-01-27 |
| CA2292724A1 (en) | 1998-12-17 |
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