EA027160B1 - Модифицированные белки и пептиды - Google Patents
Модифицированные белки и пептиды Download PDFInfo
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- EA027160B1 EA027160B1 EA201490262A EA201490262A EA027160B1 EA 027160 B1 EA027160 B1 EA 027160B1 EA 201490262 A EA201490262 A EA 201490262A EA 201490262 A EA201490262 A EA 201490262A EA 027160 B1 EA027160 B1 EA 027160B1
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- amino acid
- binding
- terminal
- immunoglobulin
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Landscapes
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| US10843420B2 (en) | 2015-12-21 | 2020-11-24 | Hexcel Composites Limited | Relating to electrically conducting materials |
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| MY204220A (en) * | 2018-02-06 | 2024-08-16 | Ablynx Nv | Methods of treating initial episode of ttp with immunoglobulin single variable domains |
| EP3569618A1 (en) | 2018-05-19 | 2019-11-20 | Boehringer Ingelheim International GmbH | Antagonizing cd73 antibody |
| TWI848953B (zh) | 2018-06-09 | 2024-07-21 | 德商百靈佳殷格翰國際股份有限公司 | 針對癌症治療之多特異性結合蛋白 |
| MX2021000239A (es) * | 2018-07-10 | 2021-03-25 | Regeneron Pharma | Modificacion de moleculas de union para minimizar interacciones preexistentes. |
| CN109096394B (zh) * | 2018-09-21 | 2021-11-05 | 成都阿帕克生物科技有限公司 | 一种抗葡萄球菌蛋白a的b亚单位的纳米抗体及核酸分子和应用 |
| FR3088640A1 (fr) | 2018-10-14 | 2020-05-22 | Smart Diagnostix Pharma | Nouveau polypeptide se liant specifiquement a la proteine p16 |
| WO2020089811A1 (en) | 2018-10-31 | 2020-05-07 | Novartis Ag | Dc-sign antibody drug conjugates |
| GB201818460D0 (en) * | 2018-11-13 | 2018-12-26 | Crescendo Biologics Ltd | Single domain antibodies that bind human serum albumin |
| CN120484127A (zh) | 2019-03-05 | 2025-08-15 | 武田药品工业有限公司 | 受约束的条件性活化的结合蛋白 |
| AU2020294980A1 (en) | 2019-06-21 | 2022-02-17 | Sorriso Pharmaceuticals, Inc. | Polypeptides |
| EP3986931A1 (en) | 2019-06-21 | 2022-04-27 | Sorriso Pharmaceuticals, Inc. | Polypeptides |
| TWI878355B (zh) | 2019-10-02 | 2025-04-01 | 德商百靈佳殷格翰國際股份有限公司 | 用於癌症治療之多重專一性結合蛋白 |
| GB201914468D0 (en) | 2019-10-07 | 2019-11-20 | Crescendo Biologics Ltd | Binding Molecules |
| EP4073114A4 (en) * | 2019-12-11 | 2024-04-17 | Cullinan Oncology, Inc. | Anti-serum albumin antibodies |
| IL293725A (en) | 2019-12-11 | 2022-08-01 | Cullinan Oncology Inc | Anti-cd19 antibodies and multispecific binding proteins |
| AR121706A1 (es) * | 2020-04-01 | 2022-06-29 | Hoffmann La Roche | Moléculas de unión a antígeno biespecíficas dirigidas a ox40 y fap |
| CA3191431A1 (en) | 2020-08-17 | 2022-02-24 | Takeda Pharmaceutical Company Limited | Constrained conditionally activated binding proteins |
| CN114075282B (zh) * | 2020-08-20 | 2024-01-02 | 南京融捷康生物科技有限公司 | Il-5的结合分子及其制备方法和应用 |
| JP2023541816A (ja) * | 2020-08-27 | 2023-10-04 | イノージ・セラピューティクス・コーポレイション | 自己免疫性疾患および癌を治療するための方法および組成物 |
| US20230312715A1 (en) | 2020-09-04 | 2023-10-05 | Takeda Pharmaceutical Company Limited | Constrained conditionally activated binding protein constructs with human serum albumin domains |
| US20220112276A1 (en) * | 2020-10-12 | 2022-04-14 | Janssen Biotech, Inc. | Biosynthetic materials and methods for multidirectional biotransportation |
| CN112225807B (zh) * | 2020-10-30 | 2021-09-07 | 上海洛启生物医药技术有限公司 | 抗il5纳米抗体及其应用 |
| JP2023552865A (ja) | 2020-12-14 | 2023-12-19 | 武田薬品工業株式会社 | 条件付き二重特異性結合タンパク質 |
| CN112341543B (zh) * | 2021-01-11 | 2021-04-23 | 广东赛尔生物科技有限公司 | 包含间充质干细胞外泌体的药物组合物在治疗疾病中的应用 |
| KR20230165798A (ko) | 2021-04-06 | 2023-12-05 | 다케다 야쿠힌 고교 가부시키가이샤 | 제약된 조건부 활성화 결합 단백질을 사용한 치료 방법 |
| US20250026842A1 (en) * | 2021-11-29 | 2025-01-23 | Jiangsu Hengrui Pharmaceuticals Co., Ltd. | Modified protein or polypeptide |
| US20250051826A1 (en) | 2021-12-13 | 2025-02-13 | Heraeus Medical Gmbh | Tests and methods for detecting bacterial infection |
| WO2023147426A2 (en) * | 2022-01-27 | 2023-08-03 | Janssen Biotech, Inc. | Enhanced protein compositions |
| TW202342521A (zh) | 2022-02-23 | 2023-11-01 | 日商武田藥品工業股份有限公司 | 條件性雙特異性結合蛋白 |
| JP2025526384A (ja) | 2022-07-27 | 2025-08-13 | アブリンクス エン．ヴェー． | 新生児型Ｆｃ受容体の特異的エピトープに結合するポリペプチド |
| EP4357778A1 (en) | 2022-10-20 | 2024-04-24 | Heraeus Medical GmbH | Treatment of microbial infections diagnosed using the biomarker d-lactate |
| CN115819599B (zh) * | 2022-11-29 | 2024-01-16 | 江苏耀海生物制药有限公司 | 一种利用重组大肠杆菌分泌表达纳米抗体Cablivi的方法 |
| AU2024207151A1 (en) | 2023-01-09 | 2025-06-19 | Odyssey Therapeutics, Inc. | Anti-tnfr2 antigen-binding proteins and uses thereof |
| TW202448926A (zh) | 2023-02-17 | 2024-12-16 | 比利時商艾伯霖克斯公司 | 結合新生兒fc受體之多肽 |
| TW202444757A (zh) | 2023-03-14 | 2024-11-16 | 美商奧迪希治療公司 | 抗cd25抗原結合蛋白及其用途 |
| WO2024220763A1 (en) * | 2023-04-20 | 2024-10-24 | Xentria, Inc. | Methods for detecting an anti-drug antibody (ada) against an anti-tnf alpha antibody |
| TW202448951A (zh) | 2023-05-17 | 2024-12-16 | 美商奧迪希治療公司 | 經修飾之單域抗體 |
| TW202515917A (zh) | 2023-06-29 | 2025-04-16 | 美商奧迪希治療公司 | 抗trailr2抗原結合蛋白及其用途 |
| AR133188A1 (es) | 2023-07-05 | 2025-09-03 | Ablynx Nv | ANTAGONISTAS DE FcRn MEJORADOS PARA EL TRATAMIENTO DE ENFERMEDADES Y TRASTORNOS RELACIONADOS CON IgG |
| TW202515918A (zh) | 2023-08-30 | 2025-04-16 | 美商艾希利歐發展股份有限公司 | Ｖｈｈ遮蔽之細胞介素及其使用方法 |
| WO2025049948A1 (en) | 2023-08-30 | 2025-03-06 | Xilio Development, Inc. | Masked il-2 cytokines and methods of use thereof |
| AR133903A1 (es) | 2023-09-22 | 2025-11-12 | Ablynx Nv | Agentes de unión de albúmina bi- y multivalentes |
| TW202530265A (zh) | 2023-10-13 | 2025-08-01 | 美商奧迪希治療公司 | 抗cdh17抗原結合蛋白及其用途 |
| WO2025145329A1 (zh) * | 2024-01-03 | 2025-07-10 | 苏州智核生物医药科技有限公司 | 经修饰的免疫球蛋白单一可变结构域 |
| WO2025151752A1 (en) | 2024-01-10 | 2025-07-17 | Xilio Development, Inc. | Masked il-2 cytokines and methods of use thereof |
| WO2025167664A1 (zh) * | 2024-02-07 | 2025-08-14 | 原启生物科技(上海)有限责任公司 | Ror1抗原结合蛋白及其用途 |
| CN120025456B (zh) * | 2024-03-13 | 2025-11-07 | 寻济生物科技（北京）有限公司 | 一种抗vegfa融合构建体及其制备方法和应用 |
| WO2025217240A1 (en) | 2024-04-10 | 2025-10-16 | Odyssey Therapeutics, Inc. | Anti-tnfr2 antigen-binding proteins and uses thereof |
Citations (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2000029004A1 (en) * | 1998-11-18 | 2000-05-25 | Peptor Ltd. | Small functional units of antibody heavy chain variable regions |
| WO2006003388A2 (en) * | 2004-06-30 | 2006-01-12 | Domantis Limited | Compositions and methods for treating inflammatory disorders |
| WO2006030220A1 (en) * | 2004-09-17 | 2006-03-23 | Domantis Limited | Compositions monovalent for cd40l binding and methods of use |
| WO2006129843A2 (en) * | 2005-05-31 | 2006-12-07 | Canon Kabushiki Kaisha | Bispecific capturing molecule |
| WO2007063308A2 (en) * | 2005-12-01 | 2007-06-07 | Domantis Limited | Noncompetitive domain antibody formats that bind interleukin 1 receptor type 1 |
| WO2007063311A2 (en) * | 2005-12-01 | 2007-06-07 | Domantis Limited | Competitive domain antibody formats that bind interleukin 1 receptor type 1 |
| WO2007085814A1 (en) * | 2006-01-24 | 2007-08-02 | Domantis Limited | Fusion proteins that contain natural junctions |
| WO2008076257A2 (en) * | 2006-12-13 | 2008-06-26 | Schering Corporation | Treating cancer with anti-igflr antibody 19d12 = sch 717454 |
| WO2008149143A2 (en) * | 2007-06-06 | 2008-12-11 | Domantis Limited | Methods for selecting protease resistant polypeptides |
| WO2009068627A2 (en) * | 2007-11-27 | 2009-06-04 | Ablynx N.V. | Amino acid sequences directed against heterodimeric cytokines and/or their receptors and polypeptides comprising the same |
| WO2012042026A1 (en) * | 2010-09-30 | 2012-04-05 | Ablynx Nv | Biological materials related to c-met |
| WO2013024059A2 (en) * | 2011-08-17 | 2013-02-21 | Glaxo Group Limited | Modified proteins and peptides |
Family Cites Families (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR100272077B1 (ko) | 1990-08-29 | 2000-11-15 | 젠팜인터내셔날,인코포레이티드 | 이종 항체를 생산할 수 있는 전이유전자를 가진 인간이외의 동물 |
| EP0656946B2 (en) | 1992-08-21 | 2010-03-31 | Vrije Universiteit Brussel | Immunoglobulins devoid of light chains |
| FR2708622B1 (fr) | 1993-08-02 | 1997-04-18 | Raymond Hamers | Vecteur recombinant contenant une séquence d'un gène de lipoprotéine de structure pour l'expression de séquences de nucléotides. |
| US20050271663A1 (en) * | 2001-06-28 | 2005-12-08 | Domantis Limited | Compositions and methods for treating inflammatory disorders |
| US8420353B2 (en) | 2002-03-22 | 2013-04-16 | Aprogen, Inc. | Humanized antibody and process for preparing same |
| DK1517921T3 (da) | 2002-06-28 | 2006-10-09 | Domantis Ltd | Immunglobulin-enkeltvariable antigen-bindende domæner og dobbeltspecifikke konstruktioner deraf |
| GB0521621D0 (en) | 2005-10-24 | 2005-11-30 | Domantis Ltd | Tumor necrosis factor receptor 1 antagonists for treating respiratory diseases |
| CN101213214B (zh) * | 2005-05-20 | 2014-06-25 | 埃博灵克斯股份有限公司 | 针对冯威勒布兰特因子的单一结构域vhh抗体 |
| DE102005023617A1 (de) * | 2005-05-21 | 2006-11-23 | Aspre Ag | Verfahren zum Mischen von Farben in einem Display |
| JP2007008925A (ja) * | 2005-05-31 | 2007-01-18 | Canon Inc | 標的物質捕捉分子 |
| CA2622968A1 (en) * | 2005-09-23 | 2007-03-29 | Academisch Ziekenhuis Leiden | Vhh for the diagnosis, prevention and treatment of diseases associated with protein aggregates |
| EP2057191A1 (en) | 2006-08-18 | 2009-05-13 | Ablynx N.V. | Amino acid sequences directed against il-6r and polypeptides comprising the same for the treatment of deseases and disorders associated with il-6-mediated signalling |
| BRPI0811857A2 (pt) | 2007-05-14 | 2014-10-21 | Biogen Idec Inc | Regiões fc (scfc) de cadeia simples, polipeptídeos de aglutinação que as compreendem e métodos relacionados. |
| BRPI0812398A2 (pt) | 2007-06-06 | 2019-09-24 | Domantis Ltd | domínio variável simples de imunoglobulina anti-vegf, antagonista anti-vegf, domínio variável simples de imunoglobulina resistente à protease, uso do antagonista vegf, método para a dispensação oral ou dispensação de um medicamento ao trato gi de um paciente ou ao pulmão ou tecido pulmonar ou olho de um paciente, dispositivo de dispensação pulmonar, formulação oral, ligando específico duplo, ácido nucleico isolado ou recombinante, vetor, célula hospedeira, método para produzir polipeptídeo, composição farmacêutica, polipeptídeo, e, proteína de fusão |
| KR20100018040A (ko) | 2007-06-06 | 2010-02-16 | 도만티스 리미티드 | 프로테아제 내성 폴리펩티드를 선택하는 방법 |
| DE112008003232T5 (de) | 2007-11-30 | 2011-02-24 | Glaxo Group Limited, Greenford | Antigen-Bindungskonstrukte |
| CA2707986A1 (en) | 2007-12-13 | 2009-06-18 | Glaxo Group Limited | Compositions for pulmonary delivery |
| WO2009115614A2 (en) | 2008-03-21 | 2009-09-24 | Ablynx Nv | Von willebrand factor specific binders and methods of use therefor |
| US8020937B2 (en) * | 2008-07-31 | 2011-09-20 | Lear Corporation | Layered technology for energy management of vehicle seating |
| US20110319597A1 (en) * | 2008-08-14 | 2011-12-29 | Caphalon Australia Pty. Ltd. | Variant domain antibodies |
| EP3011953A1 (en) | 2008-10-29 | 2016-04-27 | Ablynx N.V. | Stabilised formulations of single domain antigen binding molecules |
| US10005830B2 (en) | 2009-03-05 | 2018-06-26 | Ablynx N.V. | Antigen binding dimer-complexes, methods of making/avoiding and uses thereof |
| EP2417163B1 (en) * | 2009-04-10 | 2019-02-27 | Ablynx N.V. | Improved amino acid sequences directed against il-6r and polypeptides comprising the same for the treatment of il-6r related diseases and disorders |
| HUE051430T2 (hu) * | 2009-07-10 | 2021-03-01 | Ablynx Nv | Eljárás variábilis domének elõállítására |
| GB201005063D0 (en) * | 2010-03-25 | 2010-05-12 | Ucb Pharma Sa | Biological products |
| MA33930B1 (fr) * | 2009-12-18 | 2013-01-02 | Sanofi Sa | Nouveaux anticorps antagonistes contre gpvi et leurs fragments fab et utilisations de ceux-ci |
| NZ780183A (en) | 2011-06-23 | 2024-12-20 | Ablynx Nv | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobulin single variable domains |
| EP3363813A1 (en) * | 2011-06-23 | 2018-08-22 | Ablynx NV | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobin single variable domains |
| WO2014111550A1 (en) | 2013-01-17 | 2014-07-24 | Glaxosmithkline Intellectual Property Development Limited | Modified anti-serum albumin binding proteins |
-
2012
- 2012-08-13 PE PE2014000214A patent/PE20141522A1/es active IP Right Grant
- 2012-08-13 TW TW101129262A patent/TW201321405A/zh unknown
- 2012-08-13 SG SG10201605891TA patent/SG10201605891TA/en unknown
- 2012-08-13 CA CA2845029A patent/CA2845029A1/en active Pending
- 2012-08-13 JP JP2014525418A patent/JP6297976B2/ja active Active
- 2012-08-13 MY MYPI2014700336A patent/MY167125A/en unknown
- 2012-08-13 EP EP17191815.4A patent/EP3339322A3/en active Pending
- 2012-08-13 MX MX2014001883A patent/MX2014001883A/es unknown
- 2012-08-13 US US14/239,196 patent/US10808040B2/en active Active
- 2012-08-13 CN CN201810128962.3A patent/CN108178800B/zh active Active
- 2012-08-13 CN CN201280051150.4A patent/CN103917557B/zh active Active
- 2012-08-13 EP EP15180982.9A patent/EP2987806A3/en active Pending
- 2012-08-13 PH PH1/2014/500380A patent/PH12014500380A1/en unknown
- 2012-08-13 KR KR1020147006909A patent/KR102162413B1/ko active Active
- 2012-08-13 UA UAA201401344A patent/UA118833C2/uk unknown
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- 2012-08-13 EA EA201490262A patent/EA027160B1/ru not_active IP Right Cessation
- 2012-08-13 UY UY0001034254A patent/UY34254A/es not_active Application Discontinuation
- 2012-08-13 AU AU2012296961A patent/AU2012296961B2/en not_active Ceased
- 2012-08-13 KR KR1020197027997A patent/KR102143506B1/ko active Active
- 2012-08-13 EP EP12746095.4A patent/EP2744822B1/en active Active
- 2012-08-13 WO PCT/EP2012/065782 patent/WO2013024059A2/en not_active Ceased
- 2012-08-13 SG SG2014010482A patent/SG2014010482A/en unknown
- 2012-08-13 ES ES12746095T patent/ES2813432T3/es active Active
-
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- 2014-02-11 IL IL230918A patent/IL230918A0/en unknown
- 2014-02-12 CO CO14029997A patent/CO7020851A2/es unknown
- 2014-02-17 DO DO2014000029A patent/DOP2014000029A/es unknown
- 2014-03-06 MA MA36807A patent/MA35428B1/fr unknown
- 2014-06-26 HK HK16102229.1A patent/HK1214281A1/en unknown
-
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- 2016-12-22 AU AU2016277685A patent/AU2016277685B2/en not_active Ceased
-
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- 2018-02-22 JP JP2018029267A patent/JP2018117623A/ja not_active Withdrawn
-
2019
- 2019-03-05 AU AU2019201505A patent/AU2019201505A1/en not_active Abandoned
- 2019-12-09 JP JP2019222041A patent/JP6979446B2/ja active Active
-
2020
- 2020-09-08 US US17/014,441 patent/US20210017293A1/en not_active Abandoned
-
2024
- 2024-09-23 US US18/893,457 patent/US20250136721A1/en active Pending
Patent Citations (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2000029004A1 (en) * | 1998-11-18 | 2000-05-25 | Peptor Ltd. | Small functional units of antibody heavy chain variable regions |
| WO2006003388A2 (en) * | 2004-06-30 | 2006-01-12 | Domantis Limited | Compositions and methods for treating inflammatory disorders |
| WO2006030220A1 (en) * | 2004-09-17 | 2006-03-23 | Domantis Limited | Compositions monovalent for cd40l binding and methods of use |
| WO2006129843A2 (en) * | 2005-05-31 | 2006-12-07 | Canon Kabushiki Kaisha | Bispecific capturing molecule |
| WO2007063308A2 (en) * | 2005-12-01 | 2007-06-07 | Domantis Limited | Noncompetitive domain antibody formats that bind interleukin 1 receptor type 1 |
| WO2007063311A2 (en) * | 2005-12-01 | 2007-06-07 | Domantis Limited | Competitive domain antibody formats that bind interleukin 1 receptor type 1 |
| WO2007085814A1 (en) * | 2006-01-24 | 2007-08-02 | Domantis Limited | Fusion proteins that contain natural junctions |
| WO2008076257A2 (en) * | 2006-12-13 | 2008-06-26 | Schering Corporation | Treating cancer with anti-igflr antibody 19d12 = sch 717454 |
| WO2008149143A2 (en) * | 2007-06-06 | 2008-12-11 | Domantis Limited | Methods for selecting protease resistant polypeptides |
| WO2009068627A2 (en) * | 2007-11-27 | 2009-06-04 | Ablynx N.V. | Amino acid sequences directed against heterodimeric cytokines and/or their receptors and polypeptides comprising the same |
| WO2012042026A1 (en) * | 2010-09-30 | 2012-04-05 | Ablynx Nv | Biological materials related to c-met |
| WO2013024059A2 (en) * | 2011-08-17 | 2013-02-21 | Glaxo Group Limited | Modified proteins and peptides |
Non-Patent Citations (8)
| Title |
|---|
| EDWARD G ROUTLEDGE: "Reshaping antibodies for therapy - 5. Prospects for producing non-immunogenic monoclonal antibodies", 1 January 1996 (1996-01-01), XP055040855, [retrieved on 20121012] * |
| FIONA A HARDING: "Eur J Immunol. 1983 Jul;13(7):533-40.", MABS, vol. 2, no. 3, 1 June 2010 (2010-06-01), pages 256 - 265, XP055040346 * |
| HOLT, L.J. HERRING, C. JESPERS, L.S. WOOLVEN, B.P. TOMLINSON, I.M.: "Domain antibodies: proteins for therapy", TRENDS IN BIOTECHNOLOGY., ELSEVIER PUBLICATIONS, CAMBRIDGE., GB, vol. 21, no. 11, 1 November 2003 (2003-11-01), GB, pages 484 - 490, XP004467495, ISSN: 0167-7799, DOI: 10.1016/j.tibtech.2003.08.007 * |
| KUEPPER MICHAEL B; HUHN MICHAEL; SPIEGEL HOLGER; MA JULIAN KC; BARTH STEFAN; FISCHER RAINER; FINNERN RICARDA: "Generation of human antibody fragments against Streptococcus mutans using a phage display chain shuffling approach", BMC BIOTECHNOLOGY, BIOMED CENTRAL LTD. LONDON, GB, vol. 5, no. 1, 25 January 2005 (2005-01-25), GB, pages 4, XP021005985, ISSN: 1472-6750, DOI: 10.1186/1472-6750-5-4 * |
| PETER DURAND SKOTTRUP; PAUL LEONARD; JAKUB ZBIGNIEW KACZMAREK; FLORIAN VEILLARD; JAN JOHANNES ENGHILD; RICHARD OKENNEDY; ANETA SRO: "Diagnostic evaluation of a nanobody with picomolar affinity toward the protease RgpB from", ANALYTICAL BIOCHEMISTRY, ELSEVIER, AMSTERDAM, NL, vol. 415, no. 2, 11 April 2011 (2011-04-11), AMSTERDAM, NL, pages 158 - 167, XP028378085, ISSN: 0003-2697, DOI: 10.1016/j.ab.2011.04.015 * |
| WARD E. S., ET AL.: "BINDING ACTIVITIES OF A REOPERTOIRE OF SINGLE IMMUNOGLOBULIN VARIABLE DOMAINS SECRETED FROM ESCHERICHIA COLI.", NATURE, MACMILLAN JOURNALS LTD., ETC, vol. 341., no. 6242., 12 October 1989 (1989-10-12), pages 544 - 546., XP000086104, ISSN: 0028-0836, DOI: 10.1038/341544a0 * |
| WO 2007/063308 A2 * |
| Z ESHHAR: "Monoclonal anti-VH antibodies recognize a common VH determinant expressed on immunoglobulin heavy chains from various species.", EUR J IMMUNOL., vol. 13, no. 7, 1 July 1983 (1983-07-01), pages 533 - 540, XP055040345, DOI: 10.1002/eji.1830130704 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US10843420B2 (en) | 2015-12-21 | 2020-11-24 | Hexcel Composites Limited | Relating to electrically conducting materials |
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