CA2481512C - Peptide inhibitors of protein kinase c.gamma. for pain management - Google Patents
Peptide inhibitors of protein kinase c.gamma. for pain management Download PDFInfo
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- CA2481512C CA2481512C CA2481512A CA2481512A CA2481512C CA 2481512 C CA2481512 C CA 2481512C CA 2481512 A CA2481512 A CA 2481512A CA 2481512 A CA2481512 A CA 2481512A CA 2481512 C CA2481512 C CA 2481512C
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US37453002P | 2002-04-22 | 2002-04-22 | |
| US60/374,530 | 2002-04-22 | ||
| PCT/US2003/012542 WO2003089457A2 (en) | 2002-04-22 | 2003-04-22 | Peptide inhibitors of protein kinase c ϝ for pain management |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2481512A1 CA2481512A1 (en) | 2003-10-30 |
| CA2481512C true CA2481512C (en) | 2013-06-18 |
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2481512A Expired - Fee Related CA2481512C (en) | 2002-04-22 | 2003-04-22 | Peptide inhibitors of protein kinase c.gamma. for pain management |
| CA2482598A Expired - Fee Related CA2482598C (en) | 2002-04-22 | 2003-04-22 | Peptide inhibitors of protein kinase c |
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Families Citing this family (50)
| Publication number | Priority date | Publication date | Assignee | Title |
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| US7393835B2 (en) | 2002-04-22 | 2008-07-01 | The Board Of Trustees Of The Leland Stanford Junior University | Peptide inhibitors of protein kinase C |
| US6933275B2 (en) * | 2002-05-01 | 2005-08-23 | The Board Of Trustees Of The Leland Stanford Junior University | Protein kinase C peptides for use in withdrawal |
| WO2004084889A1 (en) * | 2003-03-28 | 2004-10-07 | Pfizer Inc. | Use of protein kinase c inhibitor for suppressing sustained slow postsynaptic excitation (sspe) of enteric neurons |
| AU2003241559A1 (en) * | 2003-05-16 | 2004-12-13 | The Board Of Trustees Of The Leland Stanford Junior University | Protein kinase c peptides for use in withdrawal |
| AU2003264918A1 (en) * | 2003-10-02 | 2005-04-21 | The Board Of Trustees Of The Leland Stanford Junior University | Protein kinase c peptides for use in withdrawal |
| US8133733B2 (en) | 2003-10-24 | 2012-03-13 | Gencia Corporation | Nonviral vectors for delivering polynucleotides to target tissues |
| US20090208478A1 (en) * | 2003-10-24 | 2009-08-20 | Gencia Corporation | Transducible polypeptides for modifying metabolism |
| US20090123468A1 (en) * | 2003-10-24 | 2009-05-14 | Gencia Corporation | Transducible polypeptides for modifying metabolism |
| US8507277B2 (en) * | 2003-10-24 | 2013-08-13 | Gencia Corporation | Nonviral vectors for delivering polynucleotides |
| US8062891B2 (en) | 2003-10-24 | 2011-11-22 | Gencia Corporation | Nonviral vectors for delivering polynucleotides to plants |
| WO2005056752A2 (en) | 2003-10-24 | 2005-06-23 | Gencia Corporation | Methods and compositions for delivering polynucleotides |
| EP1699813A2 (en) * | 2003-12-11 | 2006-09-13 | The Board Of Trustees Of The Leland Stanford Junior University | Isozyme-specific antagonists of protein kinase c |
| US7265092B2 (en) * | 2004-09-30 | 2007-09-04 | Kai Pharmaceuticals, Inc. | Pharmaceutical formulation |
| US20060148700A1 (en) * | 2004-11-10 | 2006-07-06 | Daria Mochly-Rosen | Methods and compositions for reducing injury to a transplanted organ |
| US20060160062A1 (en) * | 2005-01-14 | 2006-07-20 | Young Lindon H | Perfusion and/or preservation solution for organs |
| WO2006108270A1 (en) * | 2005-04-11 | 2006-10-19 | Pharmagap Inc. | Inhibitors of protein kinases and uses thereof |
| US20100041597A1 (en) | 2005-08-05 | 2010-02-18 | Jenny Phipps | Peptides targeted to protein kinase c isoforms and uses thereof |
| WO2007025286A2 (en) * | 2005-08-26 | 2007-03-01 | The Board Of Trustees Of The Leland Stanford Junior University | Therapy procedure for drug delivery for trigeminal pain |
| CA2644089A1 (en) * | 2005-09-19 | 2007-03-29 | Kai Pharmaceuticals, Inc. | Protein kinase c peptide modulators of angiogenesis |
| US20100279944A1 (en) * | 2006-03-30 | 2010-11-04 | Ronald Mathison | Suppression and treatment of neuropathic pain |
| WO2007143119A2 (en) * | 2006-06-01 | 2007-12-13 | The Board Of Trustees Of The Leland Stanford Junior University | Method of preventing progression of hypertension-induced heart failure with pkc peptides |
| AU2008206077A1 (en) | 2007-01-19 | 2008-07-24 | Kai Pharmaceuticals, Inc. | Modifications of peptide compositions to increase stability and delivery efficiency |
| US8017583B2 (en) | 2007-01-19 | 2011-09-13 | Kai Pharmaceuticals, Inc. | Methods of use of epsilon inhibitor compounds for the attenuation of pain |
| US20090062208A1 (en) * | 2007-02-06 | 2009-03-05 | Mochly-Rosen Daria D | Methods for maintaining blood-brain barrier integrity in hypertensive subjects using a delta-PKC inhibitor |
| EP2144615A4 (en) * | 2007-04-06 | 2011-02-16 | Kai Pharmaceuticals Inc | METHOD OF USE OF GAMMA INHIBITOR COMPOUNDS FOR PAIN LIFTING |
| WO2008154004A2 (en) * | 2007-06-07 | 2008-12-18 | The Board Of Trustees Of The Leland Stanford Junior University | Inhibition of tumor metastases using protein kinase c (pkc) inhibitors |
| US8975237B2 (en) | 2007-12-21 | 2015-03-10 | Coda Therapeutics, Inc. | Treatment of fibrotic conditions |
| US20090318351A1 (en) * | 2008-03-12 | 2009-12-24 | Kevin Grimes | Method of treating acute st-elevation myocardial infarction with a delta pkc antagonist |
| ES2703571T3 (es) * | 2008-03-27 | 2019-03-11 | Nestec Sa | Métodos para aumentar la absorción de péptidos, peptidomiméticos y otros sustratos de proteína de transporte gastrointestinal |
| WO2010019965A1 (en) * | 2008-08-15 | 2010-02-18 | The Board Of Trustees Of The Leland Stanford Junior University | Compositions and methods for modulating epsilon protein kinase c-mediated cytoprotection |
| EP2398897B1 (en) | 2009-02-20 | 2017-06-28 | Cellular Dynamics International, Inc. | Methods and compositions for the differentiation of stem cells |
| CN102388130B (zh) | 2009-02-27 | 2014-08-27 | 细胞动力国际有限公司 | 多能细胞的分化 |
| AU2010221168A1 (en) * | 2009-03-06 | 2011-10-06 | Angstrom Pharmaceuticals, Inc. | Compositions and methods for modulation of cell migration |
| WO2010111533A2 (en) * | 2009-03-25 | 2010-09-30 | Kai Pharmaceuticals, Inc. | Transdermal delivery of pkc modulatory peptides through microporated skin |
| EP2482837A4 (en) | 2009-09-29 | 2013-05-22 | Joslin Diabetes Center Inc | USE OF PROTEIN KINASE C-DELTA (PKCD) INHIBITORS FOR THE TREATMENT OF DIABETES, ADIPOSITAS AND LIVER VARIATION |
| WO2011109678A1 (en) * | 2010-03-05 | 2011-09-09 | Angstrom Pharmaceuticals, Inc. | Modulation of intracellular signaling |
| US8785648B1 (en) | 2010-08-10 | 2014-07-22 | The Regents Of The University Of California | PKC-epsilon inhibitors |
| WO2013025525A1 (en) | 2011-08-12 | 2013-02-21 | The Board Of Trustees Of The Leland Stanford Junior University | Compositions and methods for specific regulation of pyruvate dehydrogenase kinase |
| US9260696B2 (en) | 2012-04-24 | 2016-02-16 | Dan S. Kaufman | Method for developing natural killer cells from stem cells |
| JP6998657B2 (ja) | 2013-09-18 | 2022-02-04 | エピアクシス セラピューティクス プロプライエタリー リミテッド | 幹細胞調節ｉｉ |
| EP3180003B1 (en) | 2014-07-01 | 2022-01-12 | The Regents of the University of California | Pkc-epsilon inhibitors |
| AU2015309686B2 (en) | 2014-08-25 | 2020-05-14 | Epiaxis Therapeutics Pty Ltd | Compositions for modulating cancer stem cells and uses therefor |
| US11389473B2 (en) | 2015-01-07 | 2022-07-19 | Tonix Pharmaceuticals Holding Corp. | Magnesium-containing oxytocin formulations and methods of use |
| MX2018012351A (es) | 2016-04-12 | 2019-02-07 | Trigemina Inc | Formulaciones de oxitocina que contienen magnesio y metodos de uso. |
| WO2018134265A1 (en) | 2017-01-17 | 2018-07-26 | Forrest Michael David | Therapeutic inhibitors of the reverse mode of atp synthase |
| IL271845B2 (en) | 2017-07-13 | 2024-06-01 | Michael David Forrest | Therapeutic modulators of the reverse mode of atp synthase |
| CA3082055A1 (en) | 2017-11-08 | 2019-05-16 | Epiaxis Therapeutics Pty Ltd | Immunogenic compositions and uses therefor |
| US20230003894A1 (en) * | 2019-12-16 | 2023-01-05 | Sony Semiconductor Solutions Corporation | Time-of-flight imaging circuitry, time-of-flight imaging system, time-of-flight imaging method |
| JP7649479B2 (ja) * | 2020-03-31 | 2025-03-21 | 東レ株式会社 | 画像解析装置、画像解析装置の制御方法、画像解析システム、及び、画像解析システムの制御方法 |
| WO2022157548A1 (en) | 2021-01-24 | 2022-07-28 | Forrest Michael David | Inhibitors of atp synthase - cosmetic and therapeutic uses |
Family Cites Families (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4351829A (en) | 1980-09-26 | 1982-09-28 | Farmitalia Carlo Erba Spa | Use of polypeptides as analgesic drugs |
| EP0903408A3 (en) | 1992-08-21 | 2005-11-02 | Biogen, Inc. | Tat-derived transport polypeptide |
| US5776685A (en) * | 1993-07-19 | 1998-07-07 | Joslin Diabetes Center | Protein kinase C assay |
| US5783405A (en) * | 1994-02-01 | 1998-07-21 | Terrapin Technologies, Inc. | Rapid screening method for effectors of signal transduction |
| US5935803A (en) | 1994-02-01 | 1999-08-10 | Terrapin Technologies, Inc. | Methods to identify immunomodulators using cognate interaction of PKC-theta |
| WO1998017299A1 (en) | 1996-10-18 | 1998-04-30 | The Board Of Trustees Of The Leland Stanford Junior University | Isozyme-specific activators of protein kinase c, methods and compositions |
| US6376476B1 (en) * | 1996-12-13 | 2002-04-23 | Zymogenetics Corporation | Isoprenoid pathway inhibitors for stimulating bone growth |
| US6218113B1 (en) | 1998-02-24 | 2001-04-17 | Incyte Genomics, Inc. | Human protein kinase C inhibitor |
| US6376467B1 (en) | 1998-10-09 | 2002-04-23 | The Regents Of The University Of California | Use of inhibitors of protein kinase C epsilon to treat pain |
| DE69934689T2 (de) | 1998-07-06 | 2007-10-25 | The Regents Of The University Of California, Oakland | Verwendung der protein-kinase-c-epsilon-inhibitoren zur behandlung von schmerzen |
| DE69920473T2 (de) * | 1998-07-21 | 2006-02-23 | Cytovia, Inc., San Diego | Neue fluoreszenzfarbstoffe und ihre anwendung in fluoreszenznachweisverfahren ganzer zellen für kaspasen, peptidasen, proteasen und andere enzyme sowie deren verwendung |
| US6395306B1 (en) * | 1998-09-14 | 2002-05-28 | Pan Pacific Pharmaceuticals, Inc. | Bee venom protein and gene encoding same |
| JP2002525382A (ja) * | 1998-09-25 | 2002-08-13 | ザ チルドレンズ メディカル センター コーポレイション | プロテインキナーゼの活性を選択的に調節するショートペプチド |
| GB9905218D0 (en) | 1999-03-09 | 1999-04-28 | Univ Glasgow | Neurodegenerative disorder related gene |
| WO2001044497A2 (en) * | 1999-12-02 | 2001-06-21 | University Of Dundee | Protein kinase regulation |
| CN1300845A (zh) | 1999-12-22 | 2001-06-27 | 上海博德基因开发有限公司 | 一种新的多肽－人二酰基甘油蛋白激酶亚单位9和编码这种多肽的多核苷酸 |
| US6436703B1 (en) | 2000-03-31 | 2002-08-20 | Hyseq, Inc. | Nucleic acids and polypeptides |
| US6496425B1 (en) * | 2000-08-21 | 2002-12-17 | Micron Technology, Inc | Multiple bit line column redundancy |
| WO2002057413A2 (en) * | 2001-01-18 | 2002-07-25 | The Board Of Trustees Of The Leland Stanford Junior University | Peptides for activation and inhibition of delta pkc |
| US7393835B2 (en) | 2002-04-22 | 2008-07-01 | The Board Of Trustees Of The Leland Stanford Junior University | Peptide inhibitors of protein kinase C |
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