CA2690056C - Rage fusion proteins - Google Patents
Rage fusion proteins Download PDFInfo
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- CA2690056C CA2690056C CA2690056A CA2690056A CA2690056C CA 2690056 C CA2690056 C CA 2690056C CA 2690056 A CA2690056 A CA 2690056A CA 2690056 A CA2690056 A CA 2690056A CA 2690056 C CA2690056 C CA 2690056C
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Families Citing this family (31)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| MX2007001559A (es) | 2004-08-03 | 2007-04-10 | Transtech Pharma Inc | Proteinas de fusion de receptor para productos finales glicados avanzados y metodos de uso. |
| KR101580937B1 (ko) | 2007-06-01 | 2015-12-31 | 유니버시티 오브 매릴랜드, 발티모어 | 면역글로불린 불변영역 Ｆｃ 수용체 결합제 |
| BRPI0913047A2 (pt) | 2008-05-23 | 2013-03-05 | Siwa Corp | anticorpo monoclonal humanizado, seu uso, bem como aparelho e mÉtodo in vitro para promover processos regenerativos em uma cultura de tecido ou cultura de cÉlula |
| KR20110139292A (ko) | 2009-04-20 | 2011-12-28 | 화이자 인코포레이티드 | 단백질 글리코실화의 제어 및 그와 관련된 조성물 및 방법 |
| WO2011102845A1 (en) * | 2010-02-18 | 2011-08-25 | Transtech Pharma, Inc. | Rage fusion protein compositions and methods of use |
| DK2598533T3 (en) | 2010-07-28 | 2019-04-23 | Gliknik Inc | Fusion proteins of natural human protein fragments to create in an orderly fashion multimerized immunoglobulin FC compositions |
| ES2725852T3 (es) | 2010-09-27 | 2019-09-27 | Siwa Corp | Eliminación selectiva de células modificadas por AGE para el tratamiento de la aterosclerosis |
| US8721571B2 (en) | 2010-11-22 | 2014-05-13 | Siwa Corporation | Selective removal of cells having accumulated agents |
| JP2015506372A (ja) * | 2012-01-27 | 2015-03-02 | グリックニック インコーポレイテッド | ＩｇＧ２ヒンジドメインを含む融合タンパク質 |
| JP6673200B2 (ja) | 2013-07-05 | 2020-03-25 | エイチ リー モフィット キャンサー センター アンド リサーチ インスティテュート インコーポレイテッド | 骨髄異形成症候群（ｍｄｓ）を治療するための可溶性ｃｄ３３ |
| MA40459A (fr) | 2014-09-19 | 2016-03-24 | Siwa Corp | Anticorps anti-age pour le traitement de l'inflammation et de troubles auto-immuns |
| JP6679096B2 (ja) * | 2014-10-21 | 2020-04-15 | 学校法人 久留米大学 | Ｒａｇｅアプタマーおよびその用途 |
| US9993535B2 (en) | 2014-12-18 | 2018-06-12 | Siwa Corporation | Method and composition for treating sarcopenia |
| US10358502B2 (en) | 2014-12-18 | 2019-07-23 | Siwa Corporation | Product and method for treating sarcopenia |
| FI3325011T6 (fi) | 2015-07-24 | 2023-05-11 | Ihmisen proteiinifragmenttien fuusioproteiineja järjestyksenmukaisesti multimerisoitujen, paremmin komplementtia sitovien immunoglobuliini-fc-koostumusten muodostamiseksi | |
| HUE058854T2 (hu) | 2016-02-19 | 2022-09-28 | Siwa Corp | Módszer és készítmény a rák kezelésére, az áttétes rákos sejtek elpusztítására és a rák áttétképzõdésének megelõzésére a fejlett glikációs végtermékek (AGE) elleni antitest alkalmazásával |
| AU2017250301A1 (en) | 2016-04-15 | 2018-11-15 | Siwa Corporation | Anti-age antibodies for treating neurodegenerative disorders |
| AU2017279538A1 (en) | 2016-06-07 | 2019-01-03 | Gliknik Inc. | Cysteine-optimized stradomers |
| EP3475306A1 (en) | 2016-06-23 | 2019-05-01 | Siwa Corporation | Vaccines for use in treating various diseases and disorders |
| WO2018107079A1 (en) | 2016-12-09 | 2018-06-14 | Gliknik Inc. | Manufacturing optimization of gl-2045, a multimerizing stradomer |
| IL266988B2 (en) | 2016-12-09 | 2024-11-01 | Gliknik Inc | Methods of treating inflammatory disorders with multivalent fc compounds |
| US10858449B1 (en) | 2017-01-06 | 2020-12-08 | Siwa Corporation | Methods and compositions for treating osteoarthritis |
| US10995151B1 (en) | 2017-01-06 | 2021-05-04 | Siwa Corporation | Methods and compositions for treating disease-related cachexia |
| US10961321B1 (en) | 2017-01-06 | 2021-03-30 | Siwa Corporation | Methods and compositions for treating pain associated with inflammation |
| US10925937B1 (en) | 2017-01-06 | 2021-02-23 | Siwa Corporation | Vaccines for use in treating juvenile disorders associated with inflammation |
| JP6964322B2 (ja) * | 2017-03-13 | 2021-11-10 | 学校法人 久留米大学 | ループス腎炎を処置または予防するための医薬組成物およびループス腎炎のバイオマーカー |
| BR112019021471A2 (pt) | 2017-04-13 | 2020-05-12 | Siwa Corporation | Anticorpo monoclonal humanizado de produto final da glicação avançada |
| US11518801B1 (en) | 2017-12-22 | 2022-12-06 | Siwa Corporation | Methods and compositions for treating diabetes and diabetic complications |
| EP3849578A4 (en) | 2018-09-14 | 2022-06-22 | Bioage Labs, Inc. | Rage fusion proteins with improved stability and ligand binding affinity and uses thereof |
| US11684653B2 (en) * | 2019-03-06 | 2023-06-27 | The Cleveland Clinic Foundation | Compositions and method for reducing virulence of microorganisms |
| CN118043351A (zh) * | 2021-08-31 | 2024-05-14 | 上海医药集团股份有限公司 | 靶向Siglec15的抗原结合蛋白及其用途 |
Family Cites Families (60)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NZ235148A (en) * | 1989-09-05 | 1991-12-23 | Immunex Corp | Tumour necrosis factor receptor protein and dna sequences |
| NZ256293A (en) | 1992-09-15 | 1997-06-24 | Immunex Corp | Method of treating tumour necrosis factor - mediated inflammation by use of tnf antagonist |
| JP3589665B2 (ja) | 1992-10-23 | 2004-11-17 | イミュネックス・コーポレーション | 可溶性オリゴマー蛋白質の調製法 |
| US5656261A (en) * | 1995-01-18 | 1997-08-12 | The Picower Institute For Medical Research | Preventing and reversing advanced glycosylation endproducts |
| EP1327887A3 (en) * | 1995-01-18 | 2008-12-10 | Synvista Therapeutics, Inc. | Use of thiazolium compounds for preventing and reversing the formation of advanced glycosylation end products |
| NO315930B1 (no) * | 1995-01-18 | 2003-11-17 | Picower Inst For Medical Res T | Anvendelse av tiazoliumforbindelser ved fremstilling av farmasöytiske preparater, preparater som inneholder forbindelsene, samt nyetiazoliumforbindelser |
| WO1997026913A1 (en) | 1996-01-26 | 1997-07-31 | The Trustees Of Columbia University In The City Of New York | A POLYPEPTIDE FROM LUNG EXTRACT WHICH BINDS AMYLOID-β PEPTIDE |
| WO1997039121A1 (en) | 1996-04-16 | 1997-10-23 | Schering Aktiengesellschaft | Advanced glycosylation end-product receptor peptides and uses therefor |
| US5864018A (en) * | 1996-04-16 | 1999-01-26 | Schering Aktiengesellschaft | Antibodies to advanced glycosylation end-product receptor polypeptides and uses therefor |
| US5819341A (en) * | 1996-05-24 | 1998-10-13 | Simantob; Constance | Collapsible and convertible combination baby bed and baby carrier system |
| US6790442B1 (en) * | 1996-06-27 | 2004-09-14 | Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo | Genomic DNA encoding a polypeptide capable of inducing the production of interferon-γ |
| US6555651B2 (en) | 1997-10-09 | 2003-04-29 | The Trustees Of Columbia University In The City Of New York | Ligand binding site of rage and uses thereof |
| US6790443B2 (en) | 1996-11-22 | 2004-09-14 | The Trustees Of Columbia University In The City Of New York | Method for treating symptoms of diabetes |
| US7258857B2 (en) * | 1996-11-22 | 2007-08-21 | The Trustees Of Columbia University In The City Of New York | Rage-related methods for treating inflammation |
| WO1998040071A1 (en) | 1997-03-11 | 1998-09-17 | The General Hospital Corporation | Identification of agents for use in the treatment of alzheimer's disease |
| US7101838B2 (en) | 1997-08-05 | 2006-09-05 | The Trustees Of Columbia University In The City Of New York | Method to prevent accelerated atherosclerosis using (sRAGE) soluble receptor for advanced glycation endproducts |
| US6380165B1 (en) * | 1997-09-19 | 2002-04-30 | The Picower Institute For Medical Research | Immunological advanced glycation endproduct crosslink |
| US6323218B1 (en) | 1998-03-11 | 2001-11-27 | The General Hospital Corporation | Agents for use in the treatment of Alzheimer's disease |
| US20020102604A1 (en) * | 1999-12-08 | 2002-08-01 | Milne Edwards Jean-Baptiste Dumas | Full-length human cDNAs encoding potentially secreted proteins |
| US6465422B1 (en) * | 1998-04-17 | 2002-10-15 | The Trustees Of Columbia University In The City Of New York | Method for inhibiting tumor invasion or spreading in a subject |
| WO2000018970A1 (fr) | 1998-09-29 | 2000-04-06 | Asahi Kasei Kabushiki Kaisha | Procede de commande de liberation de granules |
| US6753150B2 (en) | 1998-10-05 | 2004-06-22 | The Trustees Of Columbia University In The City Of New York | Method for determining whether a compound is capable of inhibiting the interaction of a peptide with rage |
| AU765719B2 (en) * | 1998-10-06 | 2003-09-25 | Trustees Of Columbia University In The City Of New York, The | Extracellular novel rage binding protein (EN-RAGE) and uses thereof |
| US6589944B1 (en) | 1999-04-05 | 2003-07-08 | City Of Hope | Breakers of advanced glycation endproducts |
| US6787566B2 (en) * | 1999-04-05 | 2004-09-07 | City Of Hope | Breakers of advanced glycation endproducts |
| US6605642B2 (en) * | 1999-04-05 | 2003-08-12 | City Of Hope | Inhibitors of formation of advanced glycation endproducts (AGES) |
| FR2797402B1 (fr) * | 1999-07-15 | 2004-03-12 | Biomerieux Stelhys | Utilisation d'un polypeptide pour detecter, prevenir ou traiter un etat pathologique associe a une maladie degenerative, neurologique ou autoimmune |
| JP2003507013A (ja) | 1999-08-13 | 2003-02-25 | ザ・トラスティーズ・オブ・コランビア・ユニバーシティー・イン・ザ・シティー・オブ・ニューヨーク | βシートフィブリルのＲＡＧＥへの結合を阻害する方法及びその結果 |
| EP1219639A4 (en) | 1999-09-08 | 2009-03-25 | Toray Industries | CIPO - Patent |
| WO2001029269A2 (en) | 1999-10-21 | 2001-04-26 | Case Western Reserve University | Gene expression profiling of inflammatory bowel disease |
| CA2400040A1 (en) | 2000-02-25 | 2001-08-30 | Immunex Corporation | Integrin antagonists |
| EP1272843B1 (en) * | 2000-04-14 | 2007-06-20 | Niadyne Corporation | Method for identifying regulators of protein-age formation |
| EP1354037A2 (en) | 2000-04-17 | 2003-10-22 | TransTech Pharma, Inc. | Protein expression system arrays and use in biological screening |
| CA2407630A1 (en) | 2000-05-05 | 2001-11-15 | James J. Osborne | Multi-use and decorative bathing implement |
| AU2001259710A1 (en) | 2000-05-09 | 2001-11-20 | Genetics Institute, Llc | Compositions, kits, and methods for identification, assessment, prevention, and therapy of psoriasis |
| US6613801B2 (en) | 2000-05-30 | 2003-09-02 | Transtech Pharma, Inc. | Method for the synthesis of compounds of formula I and their uses thereof |
| US6908741B1 (en) | 2000-05-30 | 2005-06-21 | Transtech Pharma, Inc. | Methods to identify compounds that modulate RAGE |
| US20020052475A1 (en) | 2000-07-20 | 2002-05-02 | Schering Ag | High affinity soluble interleukin-18 receptor |
| ATE547525T1 (de) | 2000-08-08 | 2012-03-15 | Zymogenetics Inc | Lösliche zcyctor 11 cytokinrezeptoren |
| US6825164B1 (en) | 2000-08-14 | 2004-11-30 | The Trustees Of Columbia University In The City Of New York | Method to increase cerebral blood flow in amyloid angiopathy |
| PL366009A1 (en) * | 2000-10-02 | 2005-01-24 | Reddy Us Therapeutics, Inc. | Methods and compositions for the treatment of inflammatory diseases |
| AU2002220593A1 (en) | 2000-10-06 | 2002-04-15 | Novartis Ag | Targeting molecules for adenoviral vectors |
| AU2002213192A1 (en) | 2000-10-13 | 2002-04-22 | The Trustees Of Columbia University In The City Of New York | A method for inhibiting new tissue growth in blood vessels in a patient subjected to blood vessel injury |
| BR0116606A (pt) | 2000-12-29 | 2006-05-09 | Reddy Us Therapeutics Inc | métodos e composições para detecção de compostos que modulam as respostas inflamatórias |
| DE10109466B4 (de) | 2001-02-28 | 2008-01-10 | Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. | Verfahren und Mittel zur Modifikation humaner Angiogenese |
| JP3837494B2 (ja) * | 2001-03-19 | 2006-10-25 | 国立大学法人金沢大学 | 可溶型ｒａｇｅタンパク質 |
| BR0313491A (pt) * | 2002-08-16 | 2007-08-14 | Wyeth Corp | composições e métodos para tratar distúrbios associados ao rage |
| EP1771565B1 (en) | 2004-07-20 | 2012-09-05 | The Feinstein Institute for Medical Research | Rage protein derivatives |
| EP1776459A1 (en) * | 2004-08-03 | 2007-04-25 | Transtech Pharma, Inc. | Rage fusion proteins and methods of use |
| MX2007001559A (es) * | 2004-08-03 | 2007-04-10 | Transtech Pharma Inc | Proteinas de fusion de receptor para productos finales glicados avanzados y metodos de uso. |
| JP2008537874A (ja) * | 2004-09-27 | 2008-10-02 | セントカー・インコーポレーテツド | ｓＲＡＧＥミメティボディ、組成物、方法および使用 |
| WO2006060769A2 (en) * | 2004-12-03 | 2006-06-08 | Xoma Technology Ltd. | Methods and materials for expression of a recombinant protein |
| US20080207499A1 (en) * | 2005-06-29 | 2008-08-28 | Gaetano Barile | Rage-related methods for treating and preventing diabetic retinopathy |
| EP1909834A2 (en) | 2005-07-18 | 2008-04-16 | Critical Therapeutics, Inc. | Use of hmgb1 antagonists for the treatment of inflammatory skin conditions |
| RU2515108C2 (ru) | 2005-08-19 | 2014-05-10 | Эббви Инк | Иммуноглобулин с двойными вариабельными доменами и его применения |
| NZ571692A (en) | 2006-05-05 | 2012-01-12 | Transtech Pharma Inc | Rage fusion proteins, formulations, and methods of use thereof |
| CN105837690A (zh) | 2006-06-12 | 2016-08-10 | 新兴产品开发西雅图有限公司 | 具有效应功能的单链多价结合蛋白 |
| WO2008100470A2 (en) | 2007-02-15 | 2008-08-21 | Transtech Pharma, Inc. | Rage - immunoglobulin fusion proteins |
| WO2008137552A2 (en) | 2007-05-02 | 2008-11-13 | Medimmune, Llc | Anti-rage antibodies and methods of use thereof |
| US20100254983A1 (en) | 2007-06-07 | 2010-10-07 | Ann Marie Schmidt | Uses of rage antagonists for treating obesity and related diseases |
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