ES2870085T3 - Inhibidores peptídicos permeables a células de la ruta de transducción de señales de JNK para el tratamiento de la cistitis - Google Patents
Inhibidores peptídicos permeables a células de la ruta de transducción de señales de JNK para el tratamiento de la cistitis Download PDFInfo
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- ES2870085T3 ES2870085T3 ES14734003T ES14734003T ES2870085T3 ES 2870085 T3 ES2870085 T3 ES 2870085T3 ES 14734003 T ES14734003 T ES 14734003T ES 14734003 T ES14734003 T ES 14734003T ES 2870085 T3 ES2870085 T3 ES 2870085T3
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| EP2013001896 | 2013-06-27 | ||
| PCT/EP2014/001736 WO2014206563A2 (en) | 2013-06-26 | 2014-06-26 | New use of cell-permeable peptide inhibitors of the jnk signal transduction pathway for the treatment of various diseases |
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| JP5857056B2 (ja) | 2010-10-14 | 2016-02-10 | ザイジェン インフラメーション エルティーディー | 慢性又は非慢性の炎症性眼疾患を治療するためのjnkシグナル伝達経路の細胞透過性ペプチド阻害剤の使用 |
| 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 |
| WO2014206426A1 (en) * | 2013-06-26 | 2014-12-31 | Xigen Inflammation Ltd. | New use for jnk inhibitor molecules for treatment of various diseases |
| US10624948B2 (en) | 2013-06-26 | 2020-04-21 | Xigen Inflammation Ltd. | Use of cell-permeable peptide inhibitors of the JNK signal transduction pathway for the treatment of various diseases |
| 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 |
| EP3936141A3 (en) * | 2015-01-23 | 2022-03-23 | Erasmus University Rotterdam Medical Center | Anti-senescence compounds and uses thereof |
| CN109303782A (zh) * | 2018-10-24 | 2019-02-05 | 厦门大学 | Jnk-in-8在制备干性年龄相关性黄斑变性的神经保护剂中的应用 |
| WO2021046652A1 (en) | 2019-09-12 | 2021-03-18 | The University Of British Columbia | Inhibiting zd17-jnk interaction as a therapy for acute myocardial infarction |
| KR102151133B1 (ko) * | 2019-12-27 | 2020-09-02 | 주식회사 인투앱 | 프로피오니박테리움 아크네스에 특이적으로 결합하는 신규한 항체 및 이의 용도 |
| WO2022009698A1 (ja) * | 2020-07-06 | 2022-01-13 | 学校法人東京薬科大学 | ペプチドおよびそれを含む複合体 |
| KR102273163B1 (ko) * | 2020-09-10 | 2021-07-05 | 주식회사 파이안바이오테크놀로지 | 혈소판 유래 미토콘드리아의 수득 방법 및 이의 용도 |
| CN113633662B (zh) * | 2021-07-02 | 2023-09-26 | 中山大学附属口腔医院 | 线粒体移植在治疗牙周炎中的应用 |
| CN117147251B (zh) * | 2023-08-16 | 2024-04-26 | 四川大学 | 一种人类离体牙髓组织透明化方法 |
Family Cites Families (148)
| 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 |
| US4631211A (en) | 1985-03-25 | 1986-12-23 | Scripps Clinic & Research Foundation | Means for sequential solid phase organic synthesis and methods using the same |
| US4698327A (en) | 1985-04-25 | 1987-10-06 | Eli Lilly And Company | Novel glycopeptide derivatives |
| 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 |
| US5804604A (en) | 1989-12-21 | 1998-09-08 | Biogen, Inc. | Tat-derived transport polypeptides and fusion proteins |
| US6316003B1 (en) | 1989-12-21 | 2001-11-13 | Whitehead Institute For Biomedical Research | Tat-derived transport polypeptides |
| US5747641A (en) | 1989-12-21 | 1998-05-05 | Biogen Inc | Tat-derived transport polypeptide conjugates |
| US5840313A (en) | 1990-09-27 | 1998-11-24 | Syntello Vaccine Development Kb | Peptides for use in vaccination and induction of neutralizing antibodies against human immunodeficiency virus |
| WO1992018138A1 (en) | 1991-04-10 | 1992-10-29 | The General Hospital Corporation | Mammalian gap-43 compositions and methods of use |
| US5994108A (en) | 1991-11-05 | 1999-11-30 | Board Of Regents, The University Of Texas System | Mutant TAR virus and transdominant tat mutants as pharmacological agents |
| US5350835A (en) | 1991-11-05 | 1994-09-27 | Board Of Regents, University Of Texas | Cellular nucleic acid binding protein and uses thereof in regulating gene expression and in the treatment of aids |
| EP0632722A4 (en) | 1992-03-20 | 1997-07-30 | Baylor College Medicine | DNA TRANSPORTATION SYSTEM AND INSTRUCTIONS FOR USE. |
| JP4074658B2 (ja) | 1992-04-03 | 2008-04-09 | ザ リージェンツ オブ ザ ユニバーシティ オブ カリフォルニア | 自己構築ポリヌクレオチド送達システム |
| WO1994004562A1 (en) | 1992-08-13 | 1994-03-03 | The General Hospital Corporation | Mammalian gap-43 compositions and methods of use |
| EP0656950B1 (en) * | 1992-08-21 | 1998-11-04 | Biogen, Inc. | Tat-derived transport polypeptides |
| EP0667786B1 (en) | 1992-08-27 | 2004-01-21 | Deakin Research Limited | Retro-, inverso-, and retro-inverso synthetic peptide analogues |
| US5545551A (en) | 1992-08-28 | 1996-08-13 | Mt. Sinai School Of Medicine Of The City University Of New York | Cloning and expression of pur protein |
| EP0693939A1 (de) | 1993-04-14 | 1996-01-31 | Roche Diagnostics GmbH | Nukleinsäure-transferpeptide und deren verwendung zur einschleusung von nukleinsäuren in eukaryontische zellen |
| EP0679716A4 (en) | 1993-11-12 | 1999-06-09 | Kenichi Matsubara | GENE SIGNATURE. |
| US5595756A (en) | 1993-12-22 | 1997-01-21 | Inex Pharmaceuticals Corporation | Liposomal compositions for enhanced retention of bioactive agents |
| US5807746A (en) | 1994-06-13 | 1998-09-15 | Vanderbilt University | Method for importing biologically active molecules into cells |
| EP0767833A1 (en) | 1995-04-25 | 1997-04-16 | Baxter International Inc. | Composition containing collagenase and chymopapain for isolating hepatocytes and pancreatic islet cells |
| CA2227786A1 (en) | 1995-07-28 | 1997-02-13 | Marie Curie Cancer Care | Transport proteins and their uses |
| AU7366896A (en) | 1995-09-21 | 1997-04-09 | Innapharma, Inc. | Peptides and peptidomimetics inhibiting the oncogenic action of p21 ras |
| IE80466B1 (en) | 1995-11-10 | 1998-07-29 | Elan Corp Plc | Peptides which enhance transport across tissues and methods of identifying and using the same |
| US6630351B1 (en) | 1999-06-07 | 2003-10-07 | Mirus Corporation | Compositions and methods for drug delivery using pH sensitive molecules |
| US5877282A (en) | 1996-09-20 | 1999-03-02 | Bristol-Myers Squibb Company | Peptide inhibitors of nuclear protein translocation having nuclear localization sequences and methods of use thereof |
| US6187817B1 (en) | 1996-10-03 | 2001-02-13 | Southern Illinois University School Of Medicine | Therapeutic use of d-methionine to reduce the toxicity of platinum-containing anti-tumor compounds |
| US6361938B1 (en) | 1996-11-08 | 2002-03-26 | Elan Corporation, Plc | Peptides which enhance transport across tissues and methods of identifying and using the same |
| WO1998023781A1 (en) | 1996-11-26 | 1998-06-04 | Johns Hopkins University | Ligand detection system and methods of use thereof |
| US5989814A (en) | 1997-04-01 | 1999-11-23 | Reagents Of The University Of California | Screening methods in eucaryotic cells |
| US5880261A (en) | 1997-04-03 | 1999-03-09 | Waeber; Gerard | Transcription factor Islet-Brain 1 (IB1) |
| AU6972798A (en) | 1997-04-18 | 1998-11-13 | University Of Medicine And Dentistry Of New Jersey | Inhibition of hiv-1 replication by a tat rna-binding domain peptide analog |
| US6043083A (en) | 1997-04-28 | 2000-03-28 | Davis; Roger J. | Inhibitors of the JNK signal transduction pathway and methods of use |
| JP4129298B2 (ja) | 1997-05-15 | 2008-08-06 | サイトジェン コーポレーション | 胃腸管(git)輸送受容体に結合するランダムペプチド、及び関連した方法 |
| IL132941A0 (en) | 1997-05-21 | 2001-03-19 | Univ Leland Stanford Junior | Composition and method for enhancing transport across biological membranes |
| FR2767323B1 (fr) | 1997-08-12 | 2001-01-05 | Synt Em | Peptides lineaires derives de peptides antibiotiques, leur preparation et leur utilisation pour vectoriser des substances actives |
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| WO1999016787A1 (en) | 1997-09-26 | 1999-04-08 | Washington University | Cell death agonists |
| US6420031B1 (en) | 1997-11-03 | 2002-07-16 | The Trustees Of Princeton University | Highly transparent non-metallic cathodes |
| AU745579B2 (en) * | 1997-10-20 | 2002-03-21 | F. Hoffmann-La Roche Ag | Bicyclic kinase inhibitors |
| US6270956B1 (en) | 1997-12-11 | 2001-08-07 | The Salk Institute For Biological Studies | Transcriptional coactivator that interacts with Tat protein and regulates its binding to TAR RNA, methods for modulating Tat transactivation, and uses therefor |
| EP0947524A1 (en) | 1998-03-30 | 1999-10-06 | Upither B.V. | Novel peptides for the treatment of autoimmune diseases |
| US6248558B1 (en) | 1998-03-31 | 2001-06-19 | Vanderbilt University | Sequence and method for genetic engineering of proteins with cell membrane translocating activity |
| CA2330458A1 (en) | 1998-04-29 | 1999-11-04 | Georgetown University | Methods of identifying and using hla binding compounds as hla-agonists and antagonists |
| EP1076711A2 (en) | 1998-05-13 | 2001-02-21 | Incyte Pharmaceuticals, Inc. | Human apoptosis associated proteins |
| US6811992B1 (en) | 1998-05-14 | 2004-11-02 | Ya Fang Liu | Method for identifying MLK inhibitors for the treatment of neurological conditions |
| WO1999058561A1 (fr) | 1998-05-14 | 1999-11-18 | Pasteur Merieux Serums & Vaccins | Mimotopes du virus de l'hepatite c |
| US6740524B1 (en) | 1998-06-18 | 2004-05-25 | Dnavec Research, Inc. | Nucleic acid transfer phage |
| AU755564B2 (en) | 1998-06-20 | 2002-12-12 | Washington University | Membrane-permeant peptide complexes for medical imaging, diagnostics, and pharmaceutical therapy |
| US8038984B2 (en) | 1998-06-20 | 2011-10-18 | Washington University | Membrane-permeant peptide complexes for treatment of sepsis |
| US6589503B1 (en) | 1998-06-20 | 2003-07-08 | Washington University | Membrane-permeant peptide complexes for medical imaging, diagnostics, and pharmaceutical therapy |
| EP1107998B1 (en) | 1998-08-28 | 2004-02-04 | Gryphon Sciences | Method for the preparation of polyamide chains of precise length, their conjugates with proteins |
| JP2002525329A (ja) | 1998-09-25 | 2002-08-13 | セフアロン・インコーポレーテツド | 感覚毛細胞及び蝸牛ニューロンへの損傷を予防する/処置するための方法 |
| US20020090696A1 (en) | 1998-12-08 | 2002-07-11 | Miller Carol A. | Treating neurological disorders using human apoptosis inhibiting protein |
| US6656474B1 (en) | 1999-01-15 | 2003-12-02 | Regeneron Pharmaceuticals, Inc. | Methods of using a neurotrophin and its analogues for the treatment of gastrointestinal hypomotility disorders |
| US6673908B1 (en) | 1999-02-22 | 2004-01-06 | Nuvelo, Inc. | Tumor necrosis factor receptor 2 |
| JP2003506071A (ja) | 1999-05-28 | 2003-02-18 | アポプトシス テクノロジー,アイエヌシー. | アポトーシスを制御する化合物および方法ならびにアポトーシスを制御する化合物を製造およびスクリーニングする方法 |
| US7510824B2 (en) | 1999-06-02 | 2009-03-31 | Nono Inc. | Method of screening peptides useful in treating traumatic injury to the brain or spinal cord |
| AU5316900A (en) | 1999-06-03 | 2000-12-28 | Vertex Pharmaceuticals Incorporated | Inhibitors of c-jun n-terminal kinases (jnk) |
| US6669951B2 (en) | 1999-08-24 | 2003-12-30 | Cellgate, Inc. | Compositions and methods for enhancing drug delivery across and into epithelial tissues |
| EP2269654A3 (en) | 1999-08-24 | 2011-04-13 | Cellgate Inc. | Enhancing drug delivery across and into epithelial tissues using oligo arginine moieties |
| US20030104622A1 (en) | 1999-09-01 | 2003-06-05 | Robbins Paul D. | Identification of peptides that facilitate uptake and cytoplasmic and/or nuclear transport of proteins, DNA and viruses |
| EP1210362A2 (en) | 1999-09-01 | 2002-06-05 | University Of Pittsburgh Of The Commonwealth System Of Higher Education | Identification of peptides that facilitate uptake and cytoplasmic and/or nuclear transport of proteins, dna and viruses |
| 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 |
| US6610820B1 (en) | 1999-10-12 | 2003-08-26 | University Of Lausanne | 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 |
| US20010046489A1 (en) | 1999-12-06 | 2001-11-29 | Habener Joel E. | Stem cells of the islets of langerhans and their use in treating diabetes mellitus |
| EP1242118B1 (en) | 1999-12-16 | 2009-11-11 | Biogen Idec MA Inc. | Methods of treating central nervous system ischemic or hemorrhagic injury using anti alpha4 integrin antagonists |
| ATE508138T1 (de) | 2000-06-16 | 2011-05-15 | Serodus As | N- und/oder c-terminal mit kurzen geladenen peptidsequenzen modifizierte peptide |
| US6586403B1 (en) | 2000-07-20 | 2003-07-01 | Salpep Biotechnology, Inc. | Treating allergic reactions and inflammatory responses with tri-and dipeptides |
| US6897231B2 (en) | 2000-07-31 | 2005-05-24 | Signal Pharmaceuticals, Inc. | Indazole derivatives as JNK inhibitors and compositions and methods related thereto |
| EP1345956A2 (en) | 2000-10-13 | 2003-09-24 | University of Lausanne | Intracellular delivery of biological effectors by novel transporter peptide sequences |
| US7033597B2 (en) | 2000-10-13 | 2006-04-25 | Université de Lausanne | Intracellular delivery of biological effectors |
| ES2386505T3 (es) | 2000-10-17 | 2012-08-22 | Diatranz Otsuka Limited | Preparación y xenotrasplante de islotes de cerdo |
| US20030077826A1 (en) | 2001-02-02 | 2003-04-24 | Lena Edelman | Chimeric molecules containing a module able to target specific cells and a module regulating the apoptogenic function of the permeability transition pore complex (PTPC) |
| US7199124B2 (en) | 2001-02-02 | 2007-04-03 | Takeda Pharmaceutical Company Limited | JNK inhibitor |
| US20030091640A1 (en) | 2001-02-08 | 2003-05-15 | Srinivasan Ramanathan | Enhanced oral and transcompartmental delivery of therapeutic or diagnostic agents |
| MXPA03007358A (es) | 2001-02-16 | 2004-12-13 | Cellgate Inc | Transportadores que contienen porciones de arginina separadas. |
| JP4234999B2 (ja) | 2001-04-06 | 2009-03-04 | トマス ジェファソン ユニバーシティ | 治療標的としてのhiv−1vifタンパク質の多量体形成 |
| DE10117281A1 (de) | 2001-04-06 | 2002-10-24 | Inst Molekulare Biotechnologie | Peptid zur Diagnose und Therapie der Alzheimer-Demenz |
| AU2002322519A1 (en) | 2001-07-17 | 2003-03-03 | Incyte Genomics, Inc. | Proteins associated with cell growth, differentiation, and death |
| AU2002337142B2 (en) | 2001-09-19 | 2007-10-11 | Aventis Pharma S.A. | Indolizines as kinase protein inhibitors |
| US7635681B2 (en) | 2002-01-09 | 2009-12-22 | Xigen Sa | Cell-permeable peptide inhibitors of the JNK signal transduction pathway |
| US7351729B2 (en) | 2002-03-08 | 2008-04-01 | Signal Pharmaceuticals, Llc | JNK inhibitors for use in combination therapy for treating or managing proliferative disorders and cancers |
| US20040034084A1 (en) * | 2002-05-24 | 2004-02-19 | Celgene Corporation | Methods for using JNK inhibitors for treating or preventing disease-related wasting |
| CA2488013A1 (en) * | 2002-05-30 | 2003-12-11 | Celgene Corporation | Methods of using jnk or mkk inhibitors to modulate cell differentiation and to treat myeloproliferative disorders and myelodysplastic syndromes |
| SE0201863D0 (en) | 2002-06-18 | 2002-06-18 | Cepep Ab | Cell penetrating peptides |
| JP2004066595A (ja) | 2002-08-05 | 2004-03-04 | Canon Finetech Inc | 記録装置およびレジストレーション用パターンの記録方法 |
| JP2006502183A (ja) | 2002-09-20 | 2006-01-19 | アルコン,インコーポレイテッド | ドライアイ障害の処置のためのサイトカイン合成インヒビターの使用 |
| EP1408114B1 (de) | 2002-10-11 | 2007-01-03 | Imvision GmbH | Moduläre Antigen-Transporter Moleküle (MAT-Moleküle) zur Modulierung von Immunreaktionen, zugehörige Konstrukte, Verfahren und Verwendungen |
| US20040186052A1 (en) * | 2002-10-24 | 2004-09-23 | Suhasini Iyer | Cytomodulating peptides and methods for treating neurological disorders |
| ZA200503242B (en) * | 2002-10-24 | 2006-10-25 | Celgene Corp | Treatment of pain with JNK inhibitors |
| US20050019366A1 (en) | 2002-12-31 | 2005-01-27 | Zeldis Jerome B. | Drug-coated stents and methods of use therefor |
| US7166692B2 (en) | 2003-03-04 | 2007-01-23 | Canbrex Bio Science Walkersville, Inc. | Intracellular delivery of small molecules, proteins, and nucleic acids |
| JP4787150B2 (ja) | 2003-03-06 | 2011-10-05 | エーザイ・アール・アンド・ディー・マネジメント株式会社 | Jnk阻害剤 |
| CA2523672C (en) | 2003-04-29 | 2012-07-17 | Avi Biopharma, Inc. | Compositions for enhancing transport of molecules into cells |
| US20050048995A1 (en) | 2003-08-25 | 2005-03-03 | Motorola, Inc. | System and method for controlling the operating characteristics of a buffer |
| KR100685345B1 (ko) | 2004-03-27 | 2007-02-22 | 학교법인조선대학교 | 세포사 유도 펩타이드 |
| AU2005230416B2 (en) | 2004-04-08 | 2010-05-13 | Merck Serono Sa | Composition comprising a JNK inhibitor and cyclosporin |
| WO2006021458A2 (en) * | 2004-08-27 | 2006-03-02 | Gpc Biotech Ag | Pyrimidine derivatives |
| US7803824B2 (en) * | 2004-10-29 | 2010-09-28 | Alcon, Inc. | Use of inhibitors of Jun N-terminal kinases to treat glaucoma |
| US20060094753A1 (en) | 2004-10-29 | 2006-05-04 | Alcon, Inc. | Use of inhibitors of Jun N-terminal kinases for the treatment of glaucomatous retinopathy and ocular diseases |
| 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 |
| EP1661912A1 (en) | 2004-11-29 | 2006-05-31 | Xigen S.A. | Fusion protein comprising a BH3-domain of a BH3-only protein |
| EP1676574A3 (en) | 2004-12-30 | 2006-07-26 | Johnson & Johnson Vision Care, Inc. | Methods for promoting survival of transplanted tissues and cells |
| ZA200706662B (en) * | 2005-01-13 | 2009-04-29 | Signal Pharmaceiticals Llc | Haloaryl substituted Aminopurines, compositions thereof, and methods of treatment therewith |
| US20060223807A1 (en) | 2005-03-29 | 2006-10-05 | University Of Massachusetts Medical School, A Massachusetts Corporation | Therapeutic methods for type I diabetes |
| CA2606110A1 (en) | 2005-04-29 | 2006-12-07 | Celgene Corporation | Solid forms of 1-(5-(1h-1,2,4-triazol-5-yl)(1h-indazol-3-yl))-3-(2-piperidylethoxy)benzene |
| US20070015779A1 (en) | 2005-04-29 | 2007-01-18 | John Griffin | Compositions and treatments for inhibiting kinase and/or hmg-coa reductase |
| US20070003531A1 (en) | 2005-06-30 | 2007-01-04 | University Of Connecticut | Methods for improving immunotherapy by enhancing survival of antigen-specific cytotoxic T lymphocytes |
| WO2007031098A1 (en) | 2005-09-12 | 2007-03-22 | Xigen S.A. | 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 |
| US10045953B2 (en) | 2006-07-06 | 2018-08-14 | Case Western Reserve University | Ceramide composition and method of use |
| EP1884521A1 (en) | 2006-07-31 | 2008-02-06 | Xigen S.A. | Fusion peptide for inhibiting interaction of neuronal NMDA receptor (NMDAR) and NMDAR interacting proteins |
| WO2008094208A2 (en) * | 2006-08-02 | 2008-08-07 | Northwestern University | Protein kinase targeted therapeutics |
| JP5325783B2 (ja) | 2006-09-08 | 2013-10-23 | エフ.ホフマン−ラ ロシュ アーゲー | ベンゾトリアゾールキナーゼモジュレーター |
| EP2074138A4 (en) | 2006-09-19 | 2009-12-30 | Phylogica Ltd | NEUROPROTECTIVE PEPTIDE AP-1 SIGNALING INHIBITORS AND USES THEREOF |
| GB0702259D0 (en) * | 2007-02-06 | 2007-03-14 | Eisai London Res Lab Ltd | 7-azaindole derivatives |
| DK2282779T3 (da) | 2008-04-29 | 2013-05-27 | Pharnext | Nye terapeutiske fremgangsmåder til behandling af alzheimer sygdom og beslægtede lidelser gennem en modulation af cellestress-respons |
| CN105664136A (zh) | 2008-05-07 | 2016-06-15 | 加利福尼亚大学董事会 | 眼表润滑的治疗性补充和富集 |
| 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 |
| 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 |
| US20100183633A1 (en) | 2008-12-04 | 2010-07-22 | University Of Massachusetts | Interleukin 6 and tumor necrosis factor alpha as biomarkers of jnk inhibition |
| WO2010072228A1 (en) | 2008-12-22 | 2010-07-01 | Xigen S.A. | Novel transporter constructs and transporter cargo conjugate molecules |
| EP2381934A2 (en) | 2008-12-23 | 2011-11-02 | Carmel - Haifa University Economic Corp Ltd. | Improving cognitive function |
| US8450363B2 (en) * | 2009-02-06 | 2013-05-28 | Elan Pharmaceuticals, Inc. | Inhibitors of Jun N-terminal kinase |
| JP2010254672A (ja) * | 2009-03-30 | 2010-11-11 | Santen Pharmaceut Co Ltd | JNK(c−Junアミノ末端キナーゼ)阻害ペプチドを有効成分として含有する網膜疾患の予防または治療剤 |
| JP5784604B2 (ja) * | 2009-08-10 | 2015-09-24 | エフ.ホフマン−ラ ロシュ アーゲーF. Hoffmann−La Roche Aktiengesellschaft | Jnk阻害剤 |
| RU2012120783A (ru) | 2009-10-22 | 2013-11-27 | Женентек, Инк. | Модуляция дегенерации аксона |
| US20130190244A1 (en) | 2009-12-31 | 2013-07-25 | Stealth Peptides International, Inc. | Methods for performing a coronary artery bypass graft procedure |
| RU2012155144A (ru) * | 2010-06-04 | 2014-07-20 | Ф. Хоффманн-Ля Рош Аг | Ингибиторы jnk |
| WO2011160653A1 (en) | 2010-06-21 | 2011-12-29 | Xigen S.A. | Novel jnk inhibitor molecules |
| JP5857056B2 (ja) | 2010-10-14 | 2016-02-10 | ザイジェン インフラメーション エルティーディー | 慢性又は非慢性の炎症性眼疾患を治療するためのjnkシグナル伝達経路の細胞透過性ペプチド阻害剤の使用 |
| PL2902035T3 (pl) | 2010-10-14 | 2019-04-30 | Xigen Inflammation Ltd | Przechodzące przez komórkę peptydowe inhibitory szlaku przekazywania sygnałów przez JNK do zastosowania w leczeniu chorób zapalnych oka |
| US8471027B2 (en) * | 2011-04-06 | 2013-06-25 | Hoffmann-La Roche Inc. | Adamantyl compounds |
| 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 |
| 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 |
| WO2014206426A1 (en) | 2013-06-26 | 2014-12-31 | Xigen Inflammation Ltd. | New use for jnk inhibitor molecules for treatment of various diseases |
| US10624948B2 (en) | 2013-06-26 | 2020-04-21 | Xigen Inflammation Ltd. | Use of cell-permeable peptide inhibitors of the JNK signal transduction pathway for the treatment of various diseases |
| JP2015197193A (ja) | 2014-04-02 | 2015-11-09 | トヨタ自動車株式会社 | 車両用無段変速機の油圧制御装置 |
| EP3160989A2 (en) | 2014-06-26 | 2017-05-03 | Xigen Inflammation Ltd. | New use for jnk inhibitor molecules for treatment of various diseases |
| US20180170983A1 (en) | 2015-06-26 | 2018-06-21 | Xigen Inflammation Ltd. | New Use of Cell-Permeable Peptide Inhibitors of the JNK Signal Transduction Pathway for the Treatment of Mild Cognitive Impairment |
-
2014
- 2014-06-26 US US14/891,067 patent/US10624948B2/en active Active
- 2014-06-26 CA CA2903275A patent/CA2903275A1/en not_active Abandoned
- 2014-06-26 JP JP2016522321A patent/JP2016523274A/ja not_active Withdrawn
- 2014-06-26 KR KR1020157034160A patent/KR20160023669A/ko not_active Withdrawn
- 2014-06-26 CN CN201480030666.XA patent/CN105307670A/zh active Pending
- 2014-06-26 PL PL14734003T patent/PL3013353T3/pl unknown
- 2014-06-26 HK HK16112683.9A patent/HK1224225A1/zh unknown
- 2014-06-26 EP EP14734003.8A patent/EP3013353B1/en active Active
- 2014-06-26 AU AU2014301631A patent/AU2014301631A1/en not_active Abandoned
- 2014-06-26 WO PCT/EP2014/001736 patent/WO2014206563A2/en not_active Ceased
- 2014-06-26 ES ES14734003T patent/ES2870085T3/es active Active
- 2014-06-26 EA EA201501080A patent/EA201501080A1/ru unknown
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2015
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- 2015-06-26 MX MX2016017308A patent/MX2016017308A/es unknown
- 2015-06-26 BR BR112016029413A patent/BR112016029413A2/pt not_active IP Right Cessation
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Also Published As
| Publication number | Publication date |
|---|---|
| US10624948B2 (en) | 2020-04-21 |
| JP2020055866A (ja) | 2020-04-09 |
| JP2016523274A (ja) | 2016-08-08 |
| WO2014206563A2 (en) | 2014-12-31 |
| CA2903275A1 (en) | 2014-12-31 |
| BR112016029413A2 (pt) | 2017-10-17 |
| EP3013353A2 (en) | 2016-05-04 |
| KR20160023669A (ko) | 2016-03-03 |
| PL3013353T3 (pl) | 2021-09-20 |
| HK1224225A1 (zh) | 2017-08-18 |
| AU2014301631A1 (en) | 2015-08-27 |
| WO2014206563A3 (en) | 2015-03-19 |
| JP2017520571A (ja) | 2017-07-27 |
| US20160199444A1 (en) | 2016-07-14 |
| EP3013353B1 (en) | 2021-04-21 |
| MX2016017308A (es) | 2017-05-01 |
| EA201501080A1 (ru) | 2016-07-29 |
| CN105307670A (zh) | 2016-02-03 |
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