JP5490343B2 - Jnkシグナル導入経路の細胞透過性ペプチドインヒビター - Google Patents
Jnkシグナル導入経路の細胞透過性ペプチドインヒビター Download PDFInfo
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- JP5490343B2 JP5490343B2 JP2001530472A JP2001530472A JP5490343B2 JP 5490343 B2 JP5490343 B2 JP 5490343B2 JP 2001530472 A JP2001530472 A JP 2001530472A JP 2001530472 A JP2001530472 A JP 2001530472A JP 5490343 B2 JP5490343 B2 JP 5490343B2
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/10—Fusion polypeptide containing a localisation/targetting motif containing a tag for extracellular membrane crossing, e.g. TAT or VP22
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- General Health & Medical Sciences (AREA)
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- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Toxicology (AREA)
- Biochemistry (AREA)
- Dermatology (AREA)
- Molecular Biology (AREA)
- Hematology (AREA)
- Oncology (AREA)
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- Proteomics, Peptides & Aminoacids (AREA)
- Diabetes (AREA)
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- Genetics & Genomics (AREA)
- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
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Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US15877499P | 1999-10-12 | 1999-10-12 | |
| US60/158,774 | 1999-10-12 | ||
| US09/503,954 | 2000-02-14 | ||
| US09/503,954 US6610820B1 (en) | 1999-10-12 | 2000-02-14 | Cell-permeable peptide inhibitors of the JNK signal transduction pathway |
| PCT/IB2000/001538 WO2001027268A2 (en) | 1999-10-12 | 2000-10-12 | Cell-permeable peptide inhibitors of the jnk signal transduction pathway |
Related Child Applications (2)
| Application Number | Title | Priority Date | Filing Date |
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| JP2007227135A Division JP2008024710A (ja) | 1999-10-12 | 2007-08-31 | Jnkシグナル導入経路の細胞透過性ペプチドインヒビター |
| JP2011116398A Division JP2011155990A (ja) | 1999-10-12 | 2011-05-24 | Jnkシグナル導入経路の細胞透過性ペプチドインヒビター |
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| Publication Number | Publication Date |
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| JP2003511071A JP2003511071A (ja) | 2003-03-25 |
| JP2003511071A5 JP2003511071A5 (enExample) | 2007-10-18 |
| JP5490343B2 true JP5490343B2 (ja) | 2014-05-14 |
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| JP2007227135A Pending JP2008024710A (ja) | 1999-10-12 | 2007-08-31 | Jnkシグナル導入経路の細胞透過性ペプチドインヒビター |
| JP2011116398A Withdrawn JP2011155990A (ja) | 1999-10-12 | 2011-05-24 | Jnkシグナル導入経路の細胞透過性ペプチドインヒビター |
| JP2013015111A Withdrawn JP2013081479A (ja) | 1999-10-12 | 2013-01-30 | Jnkシグナル導入経路の細胞透過性ペプチドインヒビター |
| JP2015168555A Withdrawn JP2015221833A (ja) | 1999-10-12 | 2015-08-28 | Jnkシグナル導入経路の細胞透過性ペプチドインヒビター |
Family Applications After (4)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2007227135A Pending JP2008024710A (ja) | 1999-10-12 | 2007-08-31 | Jnkシグナル導入経路の細胞透過性ペプチドインヒビター |
| JP2011116398A Withdrawn JP2011155990A (ja) | 1999-10-12 | 2011-05-24 | Jnkシグナル導入経路の細胞透過性ペプチドインヒビター |
| JP2013015111A Withdrawn JP2013081479A (ja) | 1999-10-12 | 2013-01-30 | Jnkシグナル導入経路の細胞透過性ペプチドインヒビター |
| JP2015168555A Withdrawn JP2015221833A (ja) | 1999-10-12 | 2015-08-28 | Jnkシグナル導入経路の細胞透過性ペプチドインヒビター |
Country Status (12)
| Country | Link |
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| US (5) | US6610820B1 (enExample) |
| EP (5) | EP1914310A3 (enExample) |
| JP (5) | JP5490343B2 (enExample) |
| AT (3) | ATE541929T1 (enExample) |
| AU (1) | AU784845B2 (enExample) |
| CA (1) | CA2387184C (enExample) |
| CY (2) | CY1110422T1 (enExample) |
| DE (1) | DE60040564D1 (enExample) |
| DK (3) | DK1811033T3 (enExample) |
| ES (3) | ES2383824T3 (enExample) |
| PT (2) | PT1303600E (enExample) |
| WO (1) | WO2001027268A2 (enExample) |
Families Citing this family (54)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6043083A (en) * | 1997-04-28 | 2000-03-28 | Davis; Roger J. | Inhibitors of the JNK signal transduction pathway and methods of use |
| US20030108539A1 (en) * | 2000-02-14 | 2003-06-12 | Christophe Bonny | Cell-permeable peptide inhibitors of the JNK signal transduction pathway |
| US20040082509A1 (en) * | 1999-10-12 | 2004-04-29 | Christophe Bonny | Cell-permeable peptide inhibitors of the JNK signal transduction pathway |
| US8183339B1 (en) | 1999-10-12 | 2012-05-22 | Xigen S.A. | Cell-permeable peptide inhibitors of the JNK signal transduction pathway |
| US20040220100A1 (en) * | 2000-07-21 | 2004-11-04 | Essentia Biosystems, Inc. | Multi-component biological transport systems |
| DK1301213T3 (en) * | 2000-07-21 | 2017-03-27 | Revance Therapeutics Inc | MULTI-COMPONENT SYSTEMS FOR BIOLOGICAL TRANSPORT |
| EP1385872A4 (en) * | 2001-05-11 | 2004-12-15 | Res Dev Foundation | NF-KAPPA B ACTIVATOR RECEPTOR INHIBITORS AND USES OF SUCH INHIBITORS |
| US7635681B2 (en) | 2002-01-09 | 2009-12-22 | Xigen Sa | Cell-permeable peptide inhibitors of the JNK signal transduction pathway |
| EP3211084B1 (en) * | 2003-05-16 | 2019-03-27 | Acorda Therapeutics, Inc. | Proteoglycan degrading mutants for treatment of cns |
| WO2005072527A2 (en) * | 2004-01-23 | 2005-08-11 | Avi Biopharma, Inc. | Antisense oligomers and methods for inducing immune tolerance and immunosuppression |
| US9211248B2 (en) | 2004-03-03 | 2015-12-15 | Revance Therapeutics, Inc. | Compositions and methods for topical application and transdermal delivery of botulinum toxins |
| HUE025656T2 (en) * | 2004-03-03 | 2016-04-28 | Revance Therapeutics Inc | Topical application and transdermal delivery of botulinum toxins |
| BRPI0508440A (pt) | 2004-03-03 | 2007-07-24 | Revance Therapeutics Inc | composições e métodos para diagnóstico tópico e transporte terapêutico |
| EP1769802A1 (en) * | 2004-06-29 | 2007-04-04 | St. Marianna University School of Medicine | NFκB ACTION INHIBITOR AND ANTIINFLAMMATORY AGENT, AND STEROID ACTION FORTIFIER |
| EP1656951A1 (en) * | 2004-11-12 | 2006-05-17 | Xigen S.A. | Conjugates with enhanced cell uptake activity |
| US20100256041A1 (en) * | 2004-11-12 | 2010-10-07 | Christophe Bonny | Conjugate Molecule Compounds With Enhanced Cell Uptake Activity |
| KR20070110402A (ko) | 2005-03-03 | 2007-11-16 | 레반스 테라퓨틱스 | 보툴리눔 독소의 국소 적용 및 경피 전달을 위한 조성물 및방법 |
| ES2362301T3 (es) | 2005-03-03 | 2011-07-01 | Revance Therapeutics, Inc. | Composiciones y procedimientos para aplicaciones tópicas y liberación transdérmica de un oligopéptido. |
| US20060223807A1 (en) * | 2005-03-29 | 2006-10-05 | University Of Massachusetts Medical School, A Massachusetts Corporation | Therapeutic methods for type I diabetes |
| AU2012203529B2 (en) * | 2005-09-12 | 2016-01-07 | Xigen Inflammation Ltd. | Cell-Permeable Peptide Inhibitors of the JNK Signal Transduction Pathway |
| US8080517B2 (en) * | 2005-09-12 | 2011-12-20 | Xigen Sa | Cell-permeable peptide inhibitors of the JNK signal transduction pathway |
| WO2007031098A1 (en) * | 2005-09-12 | 2007-03-22 | Xigen S.A. | Cell-permeable peptide inhibitors of the jnk signal transduction pathway |
| US8114581B2 (en) * | 2005-09-15 | 2012-02-14 | The Regents Of The University Of California | Methods and compositions for detecting neoplastic cells |
| WO2007059528A2 (en) * | 2005-11-17 | 2007-05-24 | Revance Therapeutics, Inc. | Compositions and methods of topical application and transdermal delivery of botulinum toxins with reduced non-toxin proteins |
| JPWO2008015841A1 (ja) * | 2006-08-02 | 2009-12-17 | 梅澤 喜夫 | キナーゼ阻害性融合タンパク質と医薬組成物 |
| CA2663545A1 (en) | 2006-09-19 | 2008-03-27 | Phylogica Limited | Neuroprotective peptide inhibitors of ap-1 signaling and uses thereof |
| US20100021502A1 (en) * | 2006-12-28 | 2010-01-28 | Waugh Jacob M | Compositions and Methods of Topical Application and Transdermal Delivery of Botulinum Toxins Stabililzed with Polypeptide Fragments Derived from HIV-TAT |
| WO2008082889A2 (en) * | 2006-12-29 | 2008-07-10 | Revance Therapeutics, Inc. | Compositions and methods of topical application and transdermal delivery of botulinum toxins stabilized with polypeptide fragments derived from hiv-tat |
| NZ598159A (en) * | 2006-12-29 | 2013-08-30 | Revance Therapeutics Inc | Transport molecules using reverse sequence hiv-tat polypeptides |
| WO2008154700A1 (en) * | 2007-06-20 | 2008-12-24 | Phylogica Limited | Compositions and uses thereof for the treatment of acute respiratory distress syndrome (ards) and clinical disorders associated with therewith |
| WO2009143864A1 (en) * | 2008-05-30 | 2009-12-03 | Xigen S.A. | Use of cell-permeable peptide inhibitors of the jnk signal transduction pathway for the treatment of chronic or non-chronic inflammatory digestive diseases |
| WO2009143865A1 (en) * | 2008-05-30 | 2009-12-03 | Xigen S.A. | Use of cell-permeable peptide inhibitors of the jnk signal transduction pathway for the treatment of various diseases |
| WO2010072228A1 (en) | 2008-12-22 | 2010-07-01 | Xigen S.A. | Novel transporter constructs and transporter cargo conjugate molecules |
| EA201171188A1 (ru) | 2009-03-30 | 2012-05-30 | Сантен Фармасьютикал Ко., Лтд. | Профилактическое или терапевтическое средство против болезни сетчатки и способ профилактики или лечения болезни сетчатки с использованием jnk (c-jun-аминоконцевая киназа)-ингибиторного пептида, а также применение указанного пептида |
| US20120077753A1 (en) | 2009-06-25 | 2012-03-29 | Laxman Gangwani | Jnk inhibitors for use in treating spinal muscular atrophy |
| JP5457813B2 (ja) * | 2009-12-16 | 2014-04-02 | ルネサスエレクトロニクス株式会社 | Adpll回路、半導体装置及び携帯情報機器 |
| WO2011160653A1 (en) * | 2010-06-21 | 2011-12-29 | Xigen S.A. | Novel jnk inhibitor molecules |
| AU2010362444B2 (en) | 2010-10-14 | 2015-08-06 | Xigen Inflammation Ltd. | Use of cell-permeable peptide inhibitors of the JNK signal transduction pathway for the treatment of chronic or non-chronic inflammatory eye diseases |
| WO2013079213A1 (en) * | 2011-11-30 | 2013-06-06 | Xigen Inflammation Ltd. | Use of cell-permeable peptide inhibitors of the jnk signal transduction pathway for the treatment of dry eye syndrome |
| WO2013091670A1 (en) | 2011-12-21 | 2013-06-27 | Xigen S.A. | Novel jnk inhibitor molecules for treatment of various diseases |
| WO2015197097A1 (en) | 2014-06-26 | 2015-12-30 | Xigen Inflammation Ltd. | New use for jnk inhibitor molecules for treatment of various diseases |
| EA201501080A1 (ru) * | 2013-06-26 | 2016-07-29 | Ксижен Инфлемейшн Лтд. | Новое применение обладающих способностью проникать в клетку пептидных ингибиторов пути трансдукции сигнала jnk для лечения различных заболеваний |
| WO2014206427A1 (en) | 2013-06-26 | 2014-12-31 | Xigen Inflammation Ltd. | New use of cell-permeable peptide inhibitors of the jnk signal transduction pathway for the treatment of various diseases |
| WO2015197098A1 (en) | 2014-06-26 | 2015-12-30 | Xigen Inflammation Ltd. | New use of cell-permeable peptide inhibitors of the jnk signal transduction pathway for the treatment of various diseases |
| EP3204031A2 (en) | 2014-10-08 | 2017-08-16 | Xigen Inflammation Ltd. | New use of cell-permeable peptide inhibitors of the jnk signal transduction pathway for the treatment of various diseases |
| ES2985135T3 (es) | 2014-12-18 | 2024-11-04 | Harvard College | Procedimientos para generar células ß derivadas de células madre y usos de las mismas |
| WO2018029336A1 (en) | 2016-08-12 | 2018-02-15 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Methods for determining whether a subject was administered with an activator of the ppar beta/delta pathway. |
| CA3040348A1 (en) | 2016-10-19 | 2018-04-26 | United States Government As Represented By The Department Of Veterans Affairs | Compositions and methods for treating cancer |
| WO2018183762A1 (en) | 2017-03-29 | 2018-10-04 | United States Government As Represented By The Department Of Veterans Affairs | Methods and compositions for treating cancer |
| CN113730548B (zh) * | 2020-05-14 | 2023-06-30 | 山东省科学院生物研究所 | 一种活性十肽在保护听觉毛细胞方面的应用 |
| EP4545552A4 (en) * | 2022-06-22 | 2026-07-22 | Toagosei Co Ltd | Carrier Peptide Fragment and Its Use |
| DE102023203471A1 (de) * | 2023-04-17 | 2024-10-17 | Brose Fahrzeugteile Se & Co. Kommanditgesellschaft, Bamberg | Mitnehmer für einen Seilfensterheber eines Kraftfahrzeugs |
| WO2025262307A2 (en) | 2024-06-21 | 2025-12-26 | Institut Pasteur | Vhh suitable to vectorize molecules intracellularly |
| WO2025262278A1 (en) | 2024-06-21 | 2025-12-26 | Institut Pasteur | A neurovita short interfering peptide suitable for neuroprotection and neuroregeneration and uses thereof |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IT1195304B (it) * | 1981-12-22 | 1988-10-12 | Anic Spa | Metodo per la preparazione di gem-diammino derivati n-monoacilati |
| IT1190389B (it) * | 1985-09-19 | 1988-02-16 | Eniricerche Spa | Esapeptidi ad attivita' ipotensiva |
| US5169933A (en) * | 1988-08-15 | 1992-12-08 | Neorx Corporation | Covalently-linked complexes and methods for enhanced cytotoxicity and imaging |
| IT1227907B (it) * | 1988-12-23 | 1991-05-14 | Eniricerche S P A Milano Sclav | Procedimento per la sintesi di peptidi retro-inversi e nuovi intermediin tale procedimento |
| US5670617A (en) | 1989-12-21 | 1997-09-23 | Biogen Inc | Nucleic acid conjugates of tat-derived transport polypeptides |
| US5804604A (en) | 1989-12-21 | 1998-09-08 | Biogen, Inc. | Tat-derived transport polypeptides and fusion proteins |
| EP0903408A3 (en) * | 1992-08-21 | 2005-11-02 | Biogen, Inc. | Tat-derived transport polypeptide |
| US5880261A (en) | 1997-04-03 | 1999-03-09 | Waeber; Gerard | Transcription factor Islet-Brain 1 (IB1) |
| US6043083A (en) * | 1997-04-28 | 2000-03-28 | Davis; Roger J. | Inhibitors of the JNK signal transduction pathway and methods of use |
| EP0897002A3 (en) | 1997-08-14 | 2001-10-04 | Smithkline Beecham Plc | U62317, a protein having a JNK-binding domain |
| JP2002518521A (ja) * | 1998-06-20 | 2002-06-25 | ワシントン・ユニバーシティ | 医用画像解析、診断および治療のための膜透過性ペプチド錯体 |
-
2000
- 2000-02-14 US US09/503,954 patent/US6610820B1/en not_active Expired - Lifetime
- 2000-10-12 ES ES07021046T patent/ES2383824T3/es not_active Expired - Lifetime
- 2000-10-12 EP EP07021048A patent/EP1914310A3/en not_active Withdrawn
- 2000-10-12 EP EP07021046A patent/EP1905830B8/en not_active Expired - Lifetime
- 2000-10-12 AT AT07003426T patent/ATE541929T1/de active
- 2000-10-12 EP EP07003426A patent/EP1811033B1/en not_active Expired - Lifetime
- 2000-10-12 AT AT07021046T patent/ATE548455T1/de active
- 2000-10-12 WO PCT/IB2000/001538 patent/WO2001027268A2/en not_active Ceased
- 2000-10-12 CA CA2387184A patent/CA2387184C/en not_active Expired - Fee Related
- 2000-10-12 PT PT00969730T patent/PT1303600E/pt unknown
- 2000-10-12 JP JP2001530472A patent/JP5490343B2/ja not_active Expired - Lifetime
- 2000-10-12 EP EP07021047.1A patent/EP1895005B1/en not_active Expired - Lifetime
- 2000-10-12 ES ES00969730T patent/ES2313906T3/es not_active Expired - Lifetime
- 2000-10-12 PT PT07003426T patent/PT1811033E/pt unknown
- 2000-10-12 DE DE60040564T patent/DE60040564D1/de not_active Expired - Lifetime
- 2000-10-12 DK DK07003426.9T patent/DK1811033T3/da active
- 2000-10-12 AU AU79382/00A patent/AU784845B2/en not_active Ceased
- 2000-10-12 DK DK00969730T patent/DK1303600T3/da active
- 2000-10-12 AT AT00969730T patent/ATE411388T1/de active
- 2000-10-12 DK DK07021046.3T patent/DK1905830T3/da active
- 2000-10-12 ES ES07003426T patent/ES2381206T3/es not_active Expired - Lifetime
- 2000-10-12 EP EP00969730A patent/EP1303600B1/en not_active Expired - Lifetime
-
2001
- 2001-10-03 US US09/970,515 patent/US6780970B2/en not_active Expired - Lifetime
-
2003
- 2003-01-15 US US10/342,683 patent/US20030220480A1/en not_active Abandoned
-
2004
- 2004-08-23 US US10/924,028 patent/US20050043241A1/en not_active Abandoned
-
2007
- 2007-08-31 JP JP2007227135A patent/JP2008024710A/ja active Pending
-
2008
- 2008-12-16 CY CY20081101452T patent/CY1110422T1/el unknown
-
2010
- 2010-02-16 US US12/706,436 patent/US20100216716A1/en not_active Abandoned
-
2011
- 2011-05-24 JP JP2011116398A patent/JP2011155990A/ja not_active Withdrawn
-
2012
- 2012-03-28 CY CY20121100321T patent/CY1112587T1/el unknown
-
2013
- 2013-01-30 JP JP2013015111A patent/JP2013081479A/ja not_active Withdrawn
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2015
- 2015-08-28 JP JP2015168555A patent/JP2015221833A/ja not_active Withdrawn
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