RU2404192C2 - Иммуноглобулины - Google Patents
Иммуноглобулины Download PDFInfo
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- RU2404192C2 RU2404192C2 RU2007103826/10A RU2007103826A RU2404192C2 RU 2404192 C2 RU2404192 C2 RU 2404192C2 RU 2007103826/10 A RU2007103826/10 A RU 2007103826/10A RU 2007103826 A RU2007103826 A RU 2007103826A RU 2404192 C2 RU2404192 C2 RU 2404192C2
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- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
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- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
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- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
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Families Citing this family (57)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR101073590B1 (ko) * | 2003-07-15 | 2011-10-14 | 메디뮨 리미티드 | Il-13에 대한 인간 항체 분자 |
| GB0407315D0 (en) | 2003-07-15 | 2004-05-05 | Cambridge Antibody Tech | Human antibody molecules |
| PL1711528T3 (pl) * | 2003-12-23 | 2012-11-30 | Genentech Inc | Leczenie nowotworu nowymi przeciwciałami monoklonalnymi anty-IL13 |
| AR049390A1 (es) | 2004-06-09 | 2006-07-26 | Wyeth Corp | Anticuerpos contra la interleuquina-13 humana y usos de los mismos |
| US7501121B2 (en) | 2004-06-17 | 2009-03-10 | Wyeth | IL-13 binding agents |
| MX2007005866A (es) | 2004-11-17 | 2007-11-12 | Amgen Inc | Anticuerpos monoclonales totalmente humanos para il-13. |
| ES2412005T3 (es) | 2005-04-15 | 2013-07-09 | The Government Of The United States Of America, As Represented By The Secretary Of Health And Human Services | Tratamiento y prevención de la enfermedad intestinal inflamatoria que implica IL-13 y células NKT |
| JP2009510046A (ja) | 2005-09-30 | 2009-03-12 | メドイミューン・リミテッド | インターロイキン−13抗体組成物 |
| MY144906A (en) | 2005-10-21 | 2011-11-30 | Novartis Ag | Human antibodies against il13 and therapeutic uses |
| GB0600488D0 (en) * | 2006-01-11 | 2006-02-22 | Glaxo Group Ltd | Immunoglobulins |
| AU2007209202A1 (en) * | 2006-01-24 | 2007-08-02 | Domantis Limited | Ligands that bind IL-4 and/or IL-13 |
| MY161894A (en) | 2006-09-08 | 2017-05-15 | Abbvie Bahamas Ltd | Interleukin-13 binding proteins |
| US7608693B2 (en) | 2006-10-02 | 2009-10-27 | Regeneron Pharmaceuticals, Inc. | High affinity human antibodies to human IL-4 receptor |
| WO2008054606A2 (en) * | 2006-10-02 | 2008-05-08 | Regeneron Pharmaceuticals, Inc. | High affinity human antibodies to human il-4 receptor |
| DE102008053503B4 (de) * | 2008-10-28 | 2011-04-28 | Justus-Liebig-Universität Giessen | Immunologischer Test zum Nachweis von Autoantikörpern gegen testikuläre Antigene |
| GB0904214D0 (en) | 2009-03-11 | 2009-04-22 | Ucb Pharma Sa | Biological products |
| EA201190275A1 (ru) * | 2009-05-28 | 2012-11-30 | Глаксо Груп Лимитед | Белок, связывающий интерлейкин-13 (il-13) |
| PL3037104T3 (pl) | 2009-10-20 | 2020-11-16 | Abbvie Inc. | Izolacja i oczyszczanie przeciwciał anty-il-13 z zastosowaniem chromatografii powinowactwa z białkiem a |
| WO2011119925A2 (en) * | 2010-03-25 | 2011-09-29 | Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College | Synthetic herpes simplex viruses for treatment of cancers |
| KR101615474B1 (ko) | 2010-12-16 | 2016-04-25 | 제넨테크, 인크. | Th2 억제에 관한 진단 및 치료 |
| HUE064945T2 (hu) | 2012-08-21 | 2024-04-28 | Sanofi Biotechnology | Eljárások asztma kezelésére vagy megelõzésére IL-4R antagonista beadásával |
| TWI679019B (zh) * | 2013-04-29 | 2019-12-11 | 法商賽諾菲公司 | 抗il-4/抗il-13之雙特異性抗體調配物 |
| TWI633891B (zh) | 2013-06-04 | 2018-09-01 | 再生元醫藥公司 | 藉由投與il-4r抑制劑以治療過敏及增強過敏原-特異之免疫療法的方法 |
| TWI682781B (zh) | 2013-07-11 | 2020-01-21 | 美商再生元醫藥公司 | 藉由投與il-4r抑制劑治療嗜酸性食道炎的方法 |
| CN105722532A (zh) | 2013-09-13 | 2016-06-29 | 豪夫迈·罗氏有限公司 | 包含纯化的重组多肽的方法和组合物 |
| BR112016004437A2 (pt) | 2013-09-13 | 2017-10-17 | Genentech Inc | métodos de imunoteste e de seleção de linhagem de células, anticorpos e kit |
| AR098155A1 (es) | 2013-10-23 | 2016-05-04 | Genentech Inc | Métodos para diagnosticar y tratar trastornos eosinofílicos |
| AU2015214103A1 (en) | 2014-02-07 | 2016-07-21 | Abbott Laboratories | Novel assay to detect human periostin |
| JP2017507939A (ja) | 2014-02-21 | 2017-03-23 | ジェネンテック, インコーポレイテッド | 抗il−13/il−17二重特異性抗体及びその使用 |
| RU2704999C2 (ru) | 2014-02-28 | 2019-11-01 | Ридженерон Фармасьютикалз, Инк. | Способ лечения кожной инфекции путем введения антагониста il-4r |
| CN106536754B (zh) | 2014-04-11 | 2021-04-16 | 诺华股份有限公司 | 用il-13拮抗剂选择性治疗哮喘的方法 |
| EP3218412A1 (en) | 2014-11-14 | 2017-09-20 | Sanofi Biotechnology | Methods for treating chronic sinusitis with nasal polyps by administering an il-4r antagonist |
| CN107430117A (zh) | 2015-03-16 | 2017-12-01 | 豪夫迈·罗氏有限公司 | 检测和定量IL‑13的方法和在诊断和治疗Th2相关疾病中的用途 |
| ITUB20155097A1 (it) * | 2015-11-05 | 2017-05-05 | Biouniversa Srl | Anticorpi umanizzati anti-BAG3 |
| WO2017189805A1 (en) | 2016-04-27 | 2017-11-02 | Abbvie Inc. | Methods of treatment of diseases in which il-13 activity is detrimental using anti-il-13 antibodies |
| WO2017198148A1 (zh) * | 2016-05-18 | 2017-11-23 | 上海开拓者生物医药有限公司 | 一种il-13抗体及其制备方法和应用 |
| EP4442323A3 (en) | 2016-09-01 | 2025-01-01 | Regeneron Pharmaceuticals, Inc. | Methods for preventing or treating allergy by administering an il-4r antagonist |
| TWI857389B (zh) | 2016-12-01 | 2024-10-01 | 美商再生元醫藥公司 | 治療發炎症狀的方法 |
| EP3551047A1 (en) | 2016-12-07 | 2019-10-16 | Progenity, Inc. | Gastrointestinal tract detection methods, devices and systems |
| WO2018183932A1 (en) | 2017-03-30 | 2018-10-04 | Progenity Inc. | Treatment of a disease of the gastrointestinal tract with a il-13 inhibitor |
| US11053309B2 (en) | 2017-08-04 | 2021-07-06 | Regeneron Pharmaceuticals, Inc. | Methods for treating active eosinophilic esophagitis |
| MA46269B1 (fr) | 2017-08-18 | 2024-05-31 | Regeneron Pharma | Méthodes de traitement d'une dermatite atopique sévère par administration d'un inhibiteur des il-4r |
| HUE064655T2 (hu) | 2017-10-30 | 2024-04-28 | Sanofi Biotechnology | IL-4R antagonista asztma kezelésére vagy megelõzésére szolgáló eljárásban |
| PE20211304A1 (es) | 2018-02-09 | 2021-07-20 | Genentech Inc | Metodos terapeuticos y diagnosticos para enfermedades inflamatorias mediadas por mastocitos |
| CN112153982A (zh) | 2018-05-13 | 2020-12-29 | 瑞泽恩制药公司 | 用于通过施用il-4r抑制剂治疗特应性皮炎的方法 |
| WO2020092015A1 (en) | 2018-11-02 | 2020-05-07 | University Of Rochester | Therapeutic mitigation of epithelial infection |
| CN116726362A (zh) | 2018-11-19 | 2023-09-12 | 比奥拉治疗股份有限公司 | 用生物治疗剂治疗疾病的方法和装置 |
| CA3120578A1 (en) * | 2018-12-03 | 2020-06-11 | Dermata Therapeutics, Llc | Compositions for the treatment of conditions |
| CA3129963A1 (en) | 2019-03-06 | 2020-09-10 | Regeneron Pharmaceuticals, Inc. | Il-4/il-13 pathway inhibitors for enhanced efficacy in treating cancer |
| MX2021011141A (es) | 2019-03-21 | 2022-01-19 | Regeneron Pharma | Combinacion de inhibidores de la via de il-4/il-13 y ablacion de celulas plasmaticas para el tratamiento de alergia. |
| MX2022000649A (es) | 2019-07-16 | 2022-06-08 | Sanofi Biotechnology | Metodos para tratar o prevenir el asma mediante la administracion de un antagonista de il-4r. |
| EP4010001A1 (en) | 2019-08-05 | 2022-06-15 | Regeneron Pharmaceuticals, Inc. | Methods for treating allergy and enhancing allergen-specific immunotherapy by administering an il-4r antagonist |
| AU2020326713A1 (en) | 2019-08-05 | 2022-02-17 | Regeneron Pharmaceuticals, Inc. | Methods for treating atopic dermatitis by administering an il-4r antagonist |
| CN115666704B (zh) | 2019-12-13 | 2025-09-26 | 比特比德科有限责任公司 | 用于将治疗剂递送至胃肠道的可摄取装置 |
| CN118355034A (zh) | 2021-12-30 | 2024-07-16 | 瑞泽恩制药公司 | 施用il-4/il-13拮抗剂以减弱特应性进程的方法 |
| EP4227321A1 (en) * | 2022-02-10 | 2023-08-16 | AVA Lifescience GmbH | Antibodies targeting the b-cell receptor of chronic lymphocytic leukemia (cll) for use in treatment of cll |
| AR133647A1 (es) | 2023-08-25 | 2025-10-22 | Proteologix Us Inc | Constructos de anticuerpos multiespecíficos anti-il-13 y usos de los mismos |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003080675A2 (en) * | 2002-03-22 | 2003-10-02 | Amrad Operations Pty Ltd | MONOCLONAL ANTIBODY AGAINST INTERLEUKIN-13 RECEPTOR ALPHA 1 (IL-13Rα1) |
| WO2003092610A3 (en) * | 2002-05-01 | 2004-03-25 | Regeneron Pharma | Methods of using cytokine antagonists to treat hiv infection and aids |
Family Cites Families (68)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DD266710A3 (de) | 1983-06-06 | 1989-04-12 | Ve Forschungszentrum Biotechnologie | Verfahren zur biotechnischen Herstellung van alkalischer Phosphatase |
| US5807715A (en) | 1984-08-27 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin |
| US4879231A (en) | 1984-10-30 | 1989-11-07 | Phillips Petroleum Company | Transformation of yeasts of the genus pichia |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| GB8610600D0 (en) | 1986-04-30 | 1986-06-04 | Novo Industri As | Transformation of trichoderma |
| AU600575B2 (en) | 1987-03-18 | 1990-08-16 | Sb2, Inc. | Altered antibodies |
| US6051231A (en) * | 1988-09-01 | 2000-04-18 | Bayer Corporation | Antiviral methods and prepations |
| WO1990005144A1 (en) | 1988-11-11 | 1990-05-17 | Medical Research Council | Single domain ligands, receptors comprising said ligands, methods for their production, and use of said ligands and receptors |
| FR2646437B1 (fr) | 1989-04-28 | 1991-08-30 | Transgene Sa | Nouvelles sequences d'adn, leur application en tant que sequence codant pour un peptide signal pour la secretion de proteines matures par des levures recombinantes, cassettes d'expression, levures transformees et procede de preparation de proteines correspondant |
| US6291158B1 (en) | 1989-05-16 | 2001-09-18 | Scripps Research Institute | Method for tapping the immunological repertoire |
| EP0402226A1 (en) | 1989-06-06 | 1990-12-12 | Institut National De La Recherche Agronomique | Transformation vectors for yeast yarrowia |
| US6172197B1 (en) | 1991-07-10 | 2001-01-09 | Medical Research Council | Methods for producing members of specific binding pairs |
| BR9206313A (pt) | 1991-07-25 | 1995-04-11 | Idec Pharma Corp | Anticorpos recombinantes para terapia humana. |
| JP3540315B2 (ja) | 1991-09-23 | 2004-07-07 | メディカル リサーチ カウンシル | キメラ抗体の製造−組合せアプローチ |
| GB9122820D0 (en) | 1991-10-28 | 1991-12-11 | Wellcome Found | Stabilised antibodies |
| WO1993008829A1 (en) | 1991-11-04 | 1993-05-13 | The Regents Of The University Of California | Compositions that mediate killing of hiv-infected cells |
| GB9127376D0 (en) | 1991-12-24 | 1992-02-19 | Wellcome Found | Amidino derivatives |
| GB9203459D0 (en) | 1992-02-19 | 1992-04-08 | Scotgen Ltd | Antibodies with germ-line variable regions |
| MX9301943A (es) | 1992-04-02 | 1994-08-31 | Smithkline Beecham Corp | Compuestos. |
| ATE149570T1 (de) | 1992-08-17 | 1997-03-15 | Genentech Inc | Bispezifische immunoadhesine |
| AU6852594A (en) | 1993-06-03 | 1995-01-03 | Therapeutic Antibodies Inc. | Production of antibody fragments |
| US5429746A (en) | 1994-02-22 | 1995-07-04 | Smith Kline Beecham Corporation | Antibody purification |
| EP0957087B1 (en) | 1994-06-15 | 2002-12-04 | The Wellcome Foundation Limited | Intermediates useful in the preparation of enzyme inhibitors |
| US5739277A (en) | 1995-04-14 | 1998-04-14 | Genentech Inc. | Altered polypeptides with increased half-life |
| MY117948A (en) | 1997-01-13 | 2004-08-30 | Glaxo Group Ltd | Nitride oxide synthase inhibitors. |
| DE19723722A1 (de) | 1997-05-30 | 1998-12-10 | Schering Ag | Nichtsteroidale Gestagene |
| AU9281298A (en) | 1997-10-01 | 1999-04-23 | Kyowa Hakko Kogyo Co. Ltd. | Benzodioxole derivatives |
| US6506766B1 (en) | 1998-02-13 | 2003-01-14 | Abbott Laboratories | Glucocortiocoid-selective antinflammatory agents |
| CA2323771A1 (en) | 1998-03-14 | 1999-09-23 | Byk Gulden Lomberg Chemische Fabrik Gmbh | Phthalazinone pde iii/iv inhibitors |
| GB9806530D0 (en) | 1998-03-26 | 1998-05-27 | Glaxo Group Ltd | Inflammatory mediator |
| WO1999055369A1 (en) | 1998-04-28 | 1999-11-04 | Smithkline Beecham Corporation | Monoclonal antibodies with reduced immunogenicity |
| GB9811599D0 (en) | 1998-05-30 | 1998-07-29 | Glaxo Group Ltd | Nitric oxide synthase inhibitors |
| US6468528B1 (en) * | 1999-02-01 | 2002-10-22 | Amgen Canada Inc. | Materials and methods to inhibit Hodgkin and Reed Sternberg cell growth |
| EP1175422A2 (en) | 1999-05-04 | 2002-01-30 | Ligand Pharmaceuticals Incorporated | Tetracyclic progesterone receptor modulator compounds and methods |
| ES2165768B1 (es) | 1999-07-14 | 2003-04-01 | Almirall Prodesfarma Sa | Nuevos derivados de quinuclidina y composiciones farmaceuticas que los contienen. |
| US6263209B1 (en) | 1999-07-28 | 2001-07-17 | Motorola, Inc. | Method and apparatus in a wireless communication system for creating a learning function |
| CO5180649A1 (es) | 1999-09-01 | 2002-07-30 | Abbott Lab | Antagonistas de los receptores de los glucocorticoides para el tratamiento de la diabetes para el tratamiento de la diabetes |
| CA2423251A1 (en) | 2000-09-29 | 2002-04-04 | Glaxo Group Limited | Morpholin-acetamide derivatives for the treatment of inflammatory diseases |
| GB0031179D0 (en) | 2000-12-21 | 2001-01-31 | Glaxo Group Ltd | Nitric oxide synthase inhibitors |
| US6484903B2 (en) | 2001-01-09 | 2002-11-26 | Riverwood International Corporation | Carton with an improved dispensing feature in combination with a unique handle |
| GB0103630D0 (en) | 2001-02-14 | 2001-03-28 | Glaxo Group Ltd | Chemical compounds |
| GB0105360D0 (en) | 2001-03-03 | 2001-04-18 | Glaxo Group Ltd | Chimaeric immunogens |
| US7144908B2 (en) | 2001-03-08 | 2006-12-05 | Glaxo Group Limited | Agonists of beta-adrenoceptors |
| US7045658B2 (en) | 2001-03-22 | 2006-05-16 | Glaxo Group Limited | Formailide derivatives as beta2-adrenoreceptor agonists |
| BRPI0212455B8 (pt) | 2001-09-14 | 2021-05-25 | Glaxo Group Ltd | composto derivado de fenetanolamina para o tratamento de doenças respiratórias, formulação farmacêutica, combinação, e, uso do mesmo |
| AU2002337496A1 (en) * | 2001-09-20 | 2003-04-28 | Pioneer Corporation | Drive circuit for light emitting elements |
| CA2472746A1 (en) | 2002-01-14 | 2003-07-24 | Boehringer Ingelheim Pharmaceuticals, Inc. | Glucocorticoid mimetics, methods of making them, pharmaceutical formulations containing them and uses thereof |
| EP1467730A4 (en) | 2002-01-22 | 2010-03-10 | Univ California | Non-steroid ligands for the glucocorticoid receptor, compositions and uses thereof |
| GB0204719D0 (en) | 2002-02-28 | 2002-04-17 | Glaxo Group Ltd | Medicinal compounds |
| JP2005521717A (ja) | 2002-03-26 | 2005-07-21 | ベーリンガー インゲルハイム ファーマシューティカルズ インコーポレイテッド | グルココルチコイドミメチックス、その製造方法、その医薬組成物、及び使用 |
| DE60318188T2 (de) | 2002-03-26 | 2008-12-11 | Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield | Glucocorticoid-mimetika, deren herstellung, pharmazeutische zusammensetzungen und verwendung |
| DE10215316C1 (de) | 2002-04-02 | 2003-12-18 | Schering Ag | Chinolin- und Isochinolin-Derivate, ein pharmazeutisches Mittel und ihre Verwendung als Entzündungshemmer |
| AU2003223497A1 (en) * | 2002-04-05 | 2003-10-27 | Centocor, Inc. | Asthma-related anti-il-13 immunoglobulin derived proteins, compositions, methods and uses |
| WO2003086294A2 (en) | 2002-04-11 | 2003-10-23 | Merck & Co., Inc. | 1h-benzo[f]indazol-5-yl derivatives as selective glucocorticoid receptor modulators |
| US7186864B2 (en) | 2002-05-29 | 2007-03-06 | Boehringer Ingelheim Pharmaceuticals, Inc. | Glucocorticoid mimetics, methods of making them, pharmaceutical compositions, and uses thereof |
| US7074806B2 (en) | 2002-06-06 | 2006-07-11 | Boehringer Ingelheim Pharmaceuticals, Inc. | Glucocorticoid mimetics, methods of making them, pharmaceutical compositions, and uses thereof |
| EP1521733B1 (en) | 2002-07-08 | 2014-08-20 | Pfizer Products Inc. | Modulators of the glucocorticoid receptor |
| EP1575502B1 (en) | 2002-07-18 | 2010-01-20 | Bristol-Myers Squibb Company | Compositions and methods involving nuclear hormone receptor site ii |
| JP2006508042A (ja) | 2002-07-18 | 2006-03-09 | ブリストル−マイヤーズ スクイブ カンパニー | グルココルチコイド受容体の修飾物質および方法 |
| GB0216648D0 (en) | 2002-07-18 | 2002-08-28 | Lonza Biologics Plc | Method of expressing recombinant protein in CHO cells |
| CN101745112A (zh) * | 2002-07-19 | 2010-06-23 | 艾博特生物技术有限公司 | TNFα相关疾病的治疗 |
| WO2004018429A2 (en) | 2002-08-21 | 2004-03-04 | Boehringer Ingelheim Pharmaceuticals, Inc. | Substituted hihydroquinolines as glucocorticoid mimetics, methods of making them, pharmaceutical compositions, and uses thereof |
| US20060089375A1 (en) | 2002-09-16 | 2006-04-27 | Allen David G | Pyrazolo[3,4-b] pyridine compounds, and their use as phosphodiesterase inhibitors |
| CA2499150A1 (en) | 2002-09-20 | 2004-04-01 | Merck & Co., Inc. | Octahydro-2-h-naphtho[1,2-f] indole-4-carboxamide derivatives as selective glucocorticoid receptor modulators |
| GB0407315D0 (en) * | 2003-07-15 | 2004-05-05 | Cambridge Antibody Tech | Human antibody molecules |
| US7790405B2 (en) * | 2004-04-26 | 2010-09-07 | Centocor, Inc. | Solution phase biopanning method using engineered decoy proteins |
| AR049390A1 (es) * | 2004-06-09 | 2006-07-26 | Wyeth Corp | Anticuerpos contra la interleuquina-13 humana y usos de los mismos |
| US7501121B2 (en) * | 2004-06-17 | 2009-03-10 | Wyeth | IL-13 binding agents |
-
2005
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- 2010-08-24 US US12/862,235 patent/US20110243928A1/en not_active Abandoned
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003080675A2 (en) * | 2002-03-22 | 2003-10-02 | Amrad Operations Pty Ltd | MONOCLONAL ANTIBODY AGAINST INTERLEUKIN-13 RECEPTOR ALPHA 1 (IL-13Rα1) |
| WO2003092610A3 (en) * | 2002-05-01 | 2004-03-25 | Regeneron Pharma | Methods of using cytokine antagonists to treat hiv infection and aids |
Non-Patent Citations (2)
| Title |
|---|
| PUNNONEN J. ET AL. The relative contribution of IL-4 and IL-13 to human IgE synthesis induced by activated CD4+ or CD8+ T cells. J Allergy Clin Immunol. 1997 Dec; 100(6 Pt 1): 792-801. * |
| РОЙТ А. и др. Иммунология. - М.: Мир, 2000, с.168-193. * |
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