JP5113523B2 - アミロイド−βに対するナノ抗体及びアルツハイマー病のような神経変性疾患の治療のためのナノ抗体ＴＭを含むポリペプチド - Google Patents
アミロイド−βに対するナノ抗体及びアルツハイマー病のような神経変性疾患の治療のためのナノ抗体ＴＭを含むポリペプチド Download PDFInfo
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
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| US60/718,617 | 2005-09-20 | ||
| PCT/EP2005/011018 WO2006040153A2 (en) | 2004-10-13 | 2005-10-13 | Single domain camelide anti -amyloid beta antibodies and polypeptides comprising the same for the treatment and diagnosis of degenarative neural diseases such as alzheimer's disease |
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| RU2442793C2 (ru) | 2005-11-30 | 2012-02-20 | Эбботт Лэборетриз | АНТИТЕЛА ПРОТИВ ГЛОБУЛОМЕРА Аβ, ИХ АНТИГЕНСВЯЗЫВАЮЩИЕ ЧАСТИ, СООТВЕТСТВУЮЩИЕ ГИБРИДОМЫ, НУКЛЕИНОВЫЕ КИСЛОТЫ, ВЕКТОРЫ, КЛЕТКИ-ХОЗЯЕВА, СПОСОБЫ ПОЛУЧЕНИЯ УКАЗАННЫХ АНТИТЕЛ, КОМПОЗИЦИИ, СОДЕРЖАЩИЕ УКАЗАННЫЕ АНТИТЕЛА, ПРИМЕНЕНИЯ УКАЗАННЫХ АНТИТЕЛ И СПОСОБЫ ИСПОЛЬЗОВАНИЯ УКАЗАННЫХ АНТИТЕЛ |
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| US8455626B2 (en) | 2006-11-30 | 2013-06-04 | Abbott Laboratories | Aβ conformer selective anti-aβ globulomer monoclonal antibodies |
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| EP2142651B1 (en) | 2007-04-27 | 2013-05-22 | Pfenex Inc. | Method for rapidly screening microbial hosts to identify certain strains with improved yield and/or quality in the expression of heterologous proteins |
| US9580719B2 (en) | 2007-04-27 | 2017-02-28 | Pfenex, Inc. | Method for rapidly screening microbial hosts to identify certain strains with improved yield and/or quality in the expression of heterologous proteins |
| US8048420B2 (en) | 2007-06-12 | 2011-11-01 | Ac Immune S.A. | Monoclonal antibody |
| US8613923B2 (en) | 2007-06-12 | 2013-12-24 | Ac Immune S.A. | Monoclonal antibody |
| EP2170389B1 (en) * | 2007-06-12 | 2014-10-29 | AC Immune S.A. | Humanized antibodies to amyloid beta |
| EP2009445A1 (en) * | 2007-06-29 | 2008-12-31 | Institut Pasteur | Use of a camelid single-domain antibody for detecting an oligomeric form of an amyloid beta peptide and its applications |
| EP2008666A1 (en) * | 2007-06-29 | 2008-12-31 | Institut Pasteur | Use of VHH antibodies for the preparation of peptide vectors for delivering a substance of interest and their applications |
| AU2008270274B2 (en) | 2007-07-03 | 2012-06-28 | Ablynx N.V. | Providing improved immunoglobulin sequences by mutating CDR and/or FR positions |
| EP2487190A3 (en) | 2007-07-13 | 2012-11-14 | Bac Ip B.V. | Single-domain antigen-binding proteins that bind mammalian IgG |
| CA2701790A1 (en) * | 2007-10-05 | 2009-04-16 | Ac Immune S.A. | Use of humanized anti-beta-amyloid antibody in ocular diseases |
| RU2482876C2 (ru) * | 2007-10-05 | 2013-05-27 | Дженентек, Инк. | Применение антитела против амилоида-бета при глазных заболеваниях |
| PE20091163A1 (es) | 2007-11-01 | 2009-08-09 | Wyeth Corp | Anticuerpos para gdf8 |
| AU2008328779B2 (en) * | 2007-11-27 | 2014-06-05 | Ablynx N.V. | Amino acid sequences directed against HER2 and polypeptides comprising the same for the treatment of cancers and/or tumors |
| EP2068124A1 (en) | 2007-12-04 | 2009-06-10 | Metris IPR N.V. | Articulated arm measuring machine endowed with multiple measurement disks |
| WO2009109635A2 (en) | 2008-03-05 | 2009-09-11 | Ablynx Nv | Novel antigen binding dimer-complexes, methods of making and uses thereof |
| EP2281005B1 (en) | 2008-04-03 | 2013-11-20 | Vib Vzw | Single domain antibodies capable of modulating bace1 activity |
| US9908943B2 (en) | 2008-04-03 | 2018-03-06 | Vib Vzw | Single domain antibodies capable of modulating BACE activity |
| CA2720763A1 (en) | 2008-04-07 | 2009-10-15 | Ablynx Nv | Amino acid sequences directed against the notch pathways and uses thereof |
| CN102089325A (zh) | 2008-04-17 | 2011-06-08 | 埃博灵克斯股份有限公司 | 能够结合血清白蛋白的肽，以及包含其的化合物、构建体和多肽 |
| JP6034023B2 (ja) | 2008-05-16 | 2016-11-30 | アブリンクス エン．ヴェー． | Ｃｘｃｒ４及び他のｇｐｃｒに指向性を有するアミノ酸配列及びそれを含む化合物 |
| LT2285408T (lt) | 2008-06-05 | 2019-01-25 | Ablynx N.V. | Aminorūgščių sekos, nukreiptos prieš viruso apvalkalo baltymus, ir tokias sekas turintys polipeptidai, skirti virusinių ligų gydymui |
| US8444976B2 (en) | 2008-07-02 | 2013-05-21 | Argen-X B.V. | Antigen binding polypeptides |
| EP2143735A1 (en) * | 2008-07-10 | 2010-01-13 | Institut Pasteur | Variable domains of camelid heavy-chain antibodies directed against glial fibrillary acidic proteins |
| WO2010010119A1 (en) | 2008-07-22 | 2010-01-28 | Ablynx Nv | Amino acid sequences directed against multitarget scavenger receptors and polypeptides |
| WO2010033913A1 (en) * | 2008-09-22 | 2010-03-25 | Icb International, Inc. | Antibodies, analogs and uses thereof |
| US20100136584A1 (en) * | 2008-09-22 | 2010-06-03 | Icb International, Inc. | Methods for using antibodies and analogs thereof |
| WO2010036856A2 (en) | 2008-09-26 | 2010-04-01 | Wyeth Llc | Compatible display vector systems |
| JP2012503983A (ja) * | 2008-09-26 | 2012-02-16 | ワイス・エルエルシー | 適合性ディスプレイベクター系 |
| CA2738243C (en) | 2008-10-29 | 2020-09-29 | Wyeth Llc | Formulations of single domain antigen binding molecules |
| CN102272154A (zh) | 2008-10-29 | 2011-12-07 | 惠氏有限责任公司 | 单域抗原结合性分子的纯化方法 |
| CA2747644C (en) | 2008-12-19 | 2023-01-24 | Ablynx N.V. | Method for generation of immunoglobulin sequences |
| US9265834B2 (en) | 2009-03-05 | 2016-02-23 | Ablynx N.V. | Stable formulations of polypeptides and uses thereof |
| WO2010100135A1 (en) | 2009-03-05 | 2010-09-10 | Ablynx N.V. | Novel antigen binding dimer-complexes, methods of making/avoiding and uses thereof |
| MX2011010681A (es) | 2009-04-10 | 2012-01-20 | Ablynx Nv | Secuencias mejoradas de aminoacidos dirigidas contra il-6r y polipeptidos que comprenden el mismo para el tratamiento de enfermedades y trastornos relacionados con il-6r. |
| WO2010125187A2 (en) | 2009-04-30 | 2010-11-04 | Ablynx Nv | Method for the production of domain antibodies |
| US9968574B2 (en) * | 2009-05-15 | 2018-05-15 | The University Of Kentucky Research Foundation | Treatment of MCI and Alzheimer's disease |
| AU2010249015A1 (en) * | 2009-05-15 | 2011-11-24 | The University Of Kentucky Research Foundation | Treatment of MCI and Alzheimer's disease |
| PT2438087T (pt) | 2009-06-05 | 2017-08-04 | Ablynx Nv | Construções de nanobody trivalentes de vírus sincicial respiratório humano (hrsv) para a prevenção e/ou tratamento de infeções do trato respiratório |
| HUE051430T2 (hu) * | 2009-07-10 | 2021-03-01 | Ablynx Nv | Eljárás variábilis domének elõállítására |
| NZ598356A (en) * | 2009-07-30 | 2014-06-27 | Pfizer Vaccines Llc | Antigenic tau peptides and uses thereof |
| PL3725330T3 (pl) | 2009-09-03 | 2025-12-08 | Ablynx N.V. | Stabilne formulacje polipeptydów i ich zastosowania |
| UY32917A (es) | 2009-10-02 | 2011-04-29 | Boehringer Ingelheim Int | Moléculas de unión a dll-4 |
| UY32920A (es) | 2009-10-02 | 2011-04-29 | Boehringer Ingelheim Int | Moleculas de unión biespecíficas para la terapia anti-angiogénesis |
| US9644022B2 (en) | 2009-11-30 | 2017-05-09 | Ablynx N.V. | Amino acid sequences directed against human respiratory syncytial virus (HRSV) and polypeptides comprising the same for the prevention and/or treatment of respiratory tract infections |
| EP3309176B1 (en) | 2009-12-14 | 2025-10-01 | Ablynx N.V. | Immunoglobulin single variable domain antibodies against ox40l, constructs and their therapeutic use |
| WO2011083141A2 (en) | 2010-01-08 | 2011-07-14 | Ablynx Nv | Method for generation of immunoglobulin sequences by using lipoprotein particles |
| CA2788993A1 (en) | 2010-02-05 | 2011-08-11 | Ablynx N.V. | Peptides capable of binding to serum albumin and compounds, constructs and polypeptides comprising the same |
| US9120855B2 (en) | 2010-02-10 | 2015-09-01 | Novartis Ag | Biologic compounds directed against death receptor 5 |
| WO2011098518A2 (en) | 2010-02-11 | 2011-08-18 | Ablynx Nv | Delivery of immunoglobulin variable domains and constructs thereof |
| HUE044292T2 (hu) | 2010-02-11 | 2019-10-28 | Ablynx Nv | Eljárások és készítmények aeroszolok elõállítására |
| UY33253A (es) * | 2010-03-03 | 2011-09-30 | Boehringer Ingelheim Int | Polipéptidos de unión a a-beta |
| US8987419B2 (en) | 2010-04-15 | 2015-03-24 | AbbVie Deutschland GmbH & Co. KG | Amyloid-beta binding proteins |
| AU2011254557B2 (en) | 2010-05-20 | 2015-09-03 | Ablynx Nv | Biological materials related to HER3 |
| WO2011161263A1 (en) | 2010-06-25 | 2011-12-29 | Ablynx Nv | Pharmaceutical compositions for cutaneous administration |
| CN108314733A (zh) * | 2010-07-16 | 2018-07-24 | 埃博灵克斯股份有限公司 | 修饰的单结构域抗原结合分子及其应用 |
| CN103179981B (zh) | 2010-07-30 | 2017-02-08 | Ac免疫有限公司 | 安全和功能性的人源化抗β‑淀粉样蛋白抗体 |
| CN103298833B (zh) | 2010-08-14 | 2015-12-16 | Abbvie公司 | β淀粉样蛋白结合蛋白 |
| US20120225081A1 (en) | 2010-09-03 | 2012-09-06 | Boehringer Ingelheim International Gmbh | Vegf-binding molecules |
| DK2632946T3 (en) | 2010-10-29 | 2018-03-12 | Ablynx Nv | PROCEDURE FOR MANUFACTURING VARIABLE IMMUNGLOBULIN SINGLE DOMAINS |
| WO2012062713A1 (en) | 2010-11-08 | 2012-05-18 | Novartis Ag | Cxcr2 binding polypeptides |
| CN103459415B (zh) | 2010-11-26 | 2021-04-09 | 分子组合公司 | 设计的与血清白蛋白结合的重复蛋白 |
| CA2827170A1 (en) | 2011-02-11 | 2012-08-16 | David M. Hilbert | Monovalent and multivalent multispecific complexes and uses thereof |
| AU2012234282B2 (en) | 2011-03-28 | 2015-07-16 | Ablynx Nv | Method for producing solid formulations comprising immunoglobulin single variable domains |
| US9527925B2 (en) | 2011-04-01 | 2016-12-27 | Boehringer Ingelheim International Gmbh | Bispecific binding molecules binding to VEGF and ANG2 |
| US20130078247A1 (en) | 2011-04-01 | 2013-03-28 | Boehringer Ingelheim International Gmbh | Bispecific binding molecules binding to dii4 and ang2 |
| UA117218C2 (uk) | 2011-05-05 | 2018-07-10 | Мерк Патент Гмбх | Поліпептид, спрямований проти il-17a, il-17f та/або il17-a/f |
| EP3590950A1 (en) | 2011-05-09 | 2020-01-08 | Ablynx NV | Method for the production of immunoglobulin single varible domains |
| KR102072250B1 (ko) | 2011-05-27 | 2020-03-02 | 아블린쓰 엔.브이. | Ｒａｎｋｌ 결합 펩티드를 이용한 골 재흡수 억제 |
| WO2012175740A1 (en) | 2011-06-23 | 2012-12-27 | Ablynx Nv | Immunoglobulin single variable domains directed against ige |
| US20150158934A1 (en) | 2011-09-09 | 2015-06-11 | Ucl Business Plc | Broadly neutralizing vhh against hiv-1 |
| DK2747782T3 (en) | 2011-09-23 | 2018-04-23 | Ablynx Nv | Long-term inhibition of interleukin-6-mediated signal transmission |
| US10112987B2 (en) * | 2012-01-09 | 2018-10-30 | Icb International, Inc. | Blood-brain barrier permeable peptide compositions comprising a vab domain of a camelid single domain heavy chain antibody against an amyloid-beta peptide |
| US10112988B2 (en) | 2012-01-09 | 2018-10-30 | Icb International, Inc. | Methods of assessing amyloid-beta peptides in the central nervous system by blood-brain barrier permeable peptide compositions comprising a vab domain of a camelid single domain heavy chain antibody against an anti-amyloid-beta peptide |
| EA028183B1 (ru) | 2012-02-27 | 2017-10-31 | Бёрингер Ингельхайм Интернациональ Гмбх | Cx3cr1-связывающие полипептиды |
| USRE49625E1 (en) | 2012-03-29 | 2023-08-29 | Arizona Board Of Regents, A Body Corporate Of The State Of Arizona | Nanoscale process to generate reagents selective for individual protein variants |
| WO2013148166A1 (en) | 2012-03-29 | 2013-10-03 | Arizona Board Of Regents, A Body Corporate Of The State Of Arizona, Acting For And On Behlaf Of Arizona State University | Nanoscale process to generate reagents selective for individual protein variants |
| EA031182B1 (ru) | 2012-03-30 | 2018-11-30 | Бёрингер Ингельхайм Интернациональ Гмбх | Ang2-связывающие молекулы |
| US9328174B2 (en) | 2012-05-09 | 2016-05-03 | Novartis Ag | Chemokine receptor binding polypeptides |
| GB201208370D0 (en) | 2012-05-14 | 2012-06-27 | Ucb Pharma Sa | Antibodies |
| EP2855526B1 (en) | 2012-05-24 | 2018-11-07 | VIB vzw | Anti-macrophage mannose receptor immunoglobulin single variable domains for targeting and in vivo imaging of tumor-associated macrophages |
| WO2014087010A1 (en) | 2012-12-07 | 2014-06-12 | Ablynx N.V. | IMPROVED POLYPEPTIDES DIRECTED AGAINST IgE |
| WO2014096672A1 (fr) | 2012-12-17 | 2014-06-26 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Utilisation d'anticorps monoclonaux pour le traitement de l'inflammation et d'infections bacteriennes |
| US9200068B2 (en) | 2012-12-18 | 2015-12-01 | Regents Of The University Of Minnesota | Compositions and methods related to tauopathy |
| US9593157B2 (en) | 2013-01-30 | 2017-03-14 | Vib Vzw | Chimeric polypeptides comprising G protein-coupled receptors and VHH antibodies |
| CA2900147C (en) | 2013-02-05 | 2023-09-05 | Vib Vzw | Muscarinic acetylcholine receptor binding agents and uses thereof |
| KR20150145225A (ko) | 2013-02-13 | 2015-12-29 | 라보라토이레 프란카이즈 듀 프락티온네먼트 에트 데스 바이오테크놀로지스 | 변경된 글리코실화를 갖는 세툭시맙 및 이의 용도 |
| US10174110B2 (en) | 2013-02-13 | 2019-01-08 | Laboratoire Français Du Fractionnement Et Des Biotechnologies | Highly galactosylated anti-TNF-α antibodies and uses thereof |
| MX2015010428A (es) | 2013-02-13 | 2016-04-13 | Lab Francais Du Fractionnement | Anticuerpos anti-her2 altamente galactosilados y sus usos. |
| CA2902432A1 (en) | 2013-03-12 | 2014-10-09 | Molecular Templates, Inc. | Cytotoxic proteins comprising cell-targeting binding regions and shiga toxin a subunit regions for selective killing of specific cell types |
| CN118028464A (zh) | 2013-03-14 | 2024-05-14 | 儿童医学中心公司 | Cd36鉴定癌症对象以用于治疗的用途 |
| US9617339B2 (en) | 2013-03-15 | 2017-04-11 | Vib Vzw | Method of imaging a cardiovascular disease with an anti-macrophage mannose receptor immunoglobulin single variable domain |
| NL1040254C2 (en) | 2013-05-17 | 2014-11-24 | Ablynx Nv | Stable formulations of immunoglobulin single variable domains and uses thereof. |
| JP6415827B2 (ja) * | 2013-09-08 | 2018-10-31 | 株式会社テクノメデイカ | 紙装置を用いたトランスフェリンファミリータンパク質の検出 |
| KR102665705B1 (ko) | 2013-10-21 | 2024-05-14 | 다케다 파머수티컬 컴패니 리미티드 | 자가면역 질환의 진단 및 치료 |
| EP2873679A1 (en) * | 2013-11-13 | 2015-05-20 | F.Hoffmann-La Roche Ag | Camelid single-domain antibody directed against amyloid bêta and methods for producing conjugates thereof |
| EP2873680A1 (en) * | 2013-11-13 | 2015-05-20 | F.Hoffmann-La Roche Ag | Oligopeptide and methods for producing conjugates thereof |
| EP2899208A1 (en) * | 2014-01-28 | 2015-07-29 | F.Hoffmann-La Roche Ag | Camelid single-domain antibody directed against phosphorylated tau proteins and methods for producing conjugates thereof |
| EP3134730A4 (en) | 2014-04-24 | 2018-01-17 | Immusant Inc. | Methods for diagnosing celiac disease using circulating cytokines/chemokines |
| IL295534B2 (en) | 2014-05-16 | 2025-03-01 | Ablynx Nv | Improved immunoglobulin variable sites |
| US20170088896A1 (en) | 2014-05-16 | 2017-03-30 | Children's Hospital Medical Center d/b/a Cincinnati Children's Hospital, Medical Center | Methods for assessing responsiveness to asthma treatment based on vnn-1 expression and promoter methylation |
| NL2013007B1 (en) | 2014-06-16 | 2016-07-05 | Ablynx Nv | Methods of treating TTP with immunoglobulin single variable domains and uses thereof. |
| NL2013661B1 (en) | 2014-10-21 | 2016-10-05 | Ablynx Nv | KV1.3 Binding immunoglobulins. |
| EP3207048A4 (en) | 2014-10-17 | 2018-05-30 | The Broad Institute, Inc. | Compositions and methods of treating muscular dystrophy |
| EP3230457B1 (en) | 2014-12-09 | 2021-06-30 | New York University | Clostridial neurotoxin fusion proteins, propeptide fusions, their expression, and use |
| EP3233910B1 (en) | 2014-12-19 | 2019-12-11 | Ablynx N.V. | Cysteine linked nanobody dimers |
| CA2975059C (en) | 2015-01-29 | 2023-02-21 | Technophage, Investigacao E Desenvolvimento Em Biotecnologia, Sa | Antibody molecules and peptide delivery systems for use in alzheimer's disease and related disorders |
| JP6929786B2 (ja) | 2015-04-02 | 2021-09-01 | アブリンクス エン．ヴェー． | 強力な抗ｈｉｖ活性を有する二重特異性ｃｘｃｒ４−ｃｄ４ポリペプチド |
| CN119219778A (zh) | 2015-05-13 | 2024-12-31 | 埃博灵克斯股份有限公司 | 基于cd3反应性的t细胞募集多肽 |
| DK3611192T3 (da) | 2015-05-13 | 2025-06-10 | Ablynx Nv | T-celle-rekrutterende polypeptider baseret på tcr-alfa/beta-reaktivitet |
| JOP20200312A1 (ar) | 2015-06-26 | 2017-06-16 | Novartis Ag | الأجسام المضادة للعامل xi وطرق الاستخدام |
| EP3313519B1 (en) | 2015-06-29 | 2023-05-31 | Children's Medical Center Corporation | Jak-stat inhibitors for the treatment of congenital myopathies |
| CN108450004A (zh) | 2015-09-14 | 2018-08-24 | 白血病治疗有限责任公司 | 通过调节RhoH来鉴定新的诊断和治疗 |
| NO2768984T3 (enExample) | 2015-11-12 | 2018-06-09 | ||
| KR102220275B1 (ko) | 2015-11-18 | 2021-02-26 | 머크 샤프 앤드 돔 코포레이션 | Pd1 및/또는 lag3 결합제 |
| MX2018006243A (es) | 2015-11-18 | 2018-11-09 | Merck Sharp & Dohme | Proteinas de union a pd1/ctla4. |
| EA038179B1 (ru) | 2015-11-18 | 2021-07-20 | Мерк Шарп И Доум Корп. | Ctla4-связывающие вещества |
| RU2018122255A (ru) | 2015-11-27 | 2019-12-19 | Аблинкс Нв | Полипептиды, ингибирующие cd40l |
| AR106949A1 (es) | 2015-12-04 | 2018-03-07 | Boehringer Ingelheim Int | Polipéptidos biparatópicos que antagonizan la señalización wnt en células tumorales |
| US20190127447A1 (en) | 2016-05-02 | 2019-05-02 | Ablynx N.V. | Treatment of rsv infection |
| TW201802121A (zh) | 2016-05-25 | 2018-01-16 | 諾華公司 | 抗因子XI/XIa抗體之逆轉結合劑及其用途 |
| WO2018007442A1 (en) | 2016-07-06 | 2018-01-11 | Ablynx N.V. | Treatment of il-6r related diseases |
| WO2018029182A1 (en) | 2016-08-08 | 2018-02-15 | Ablynx N.V. | Il-6r single variable domain antibodies for treatment of il-6r related diseases |
| EP3512880A1 (en) | 2016-09-15 | 2019-07-24 | Ablynx NV | Immunoglobulin single variable domains directed against macrophage migration inhibitory factor |
| CN110177809B (zh) | 2016-11-16 | 2023-11-03 | 埃博灵克斯股份有限公司 | 能够结合CD123和TCRα/β的T细胞募集多肽 |
| WO2018099968A1 (en) | 2016-11-29 | 2018-06-07 | Ablynx N.V. | Treatment of infection by respiratory syncytial virus (rsv) |
| JP7139332B2 (ja) | 2016-12-23 | 2022-09-20 | ノバルティス アーゲー | 第ｘｉ因子抗体および使用方法 |
| JP7186401B2 (ja) | 2017-02-28 | 2022-12-09 | フエー・イー・ベー・フエー・ゼツト・ウエー | タンパク質の経口送達のための手段及び方法 |
| TWI743346B (zh) * | 2017-03-31 | 2021-10-21 | 國立大學法人東京大學 | 諾羅病毒抗體 |
| JP7678244B2 (ja) | 2017-05-11 | 2025-05-16 | ブイアイビー ブイゼットダブリュ | 可変免疫グロブリンドメインのグリコシル化 |
| KR102717656B1 (ko) | 2017-05-31 | 2024-10-14 | 베링거 인겔하임 인터내셔날 게엠베하 | 종양 세포에서 wnt 신호 전달을 길항하는 폴리펩티드 |
| HRP20241562T1 (hr) | 2017-06-02 | 2025-01-31 | Merck Patent Gmbh | Adamts vezujući imunoglobulini |
| BR112019022074A2 (pt) | 2017-06-02 | 2020-05-12 | Boehringer Ingelheim International Gmbh | Terapia de combinação anticâncer |
| JP7249961B2 (ja) | 2017-06-02 | 2023-03-31 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフツング | Ａｄａｍｔｓ５、ｍｍｐ１３およびアグリカンに結合するポリペプチド |
| TW202417517A (zh) | 2017-06-02 | 2024-05-01 | 德商麥克專利有限公司 | 與ｍｍｐ１３結合之免疫球蛋白 |
| AU2018277310B2 (en) | 2017-06-02 | 2024-07-11 | Ablynx Nv | Aggrecan binding immunoglobulins |
| KR102625929B1 (ko) | 2017-07-19 | 2024-01-16 | 브이아이비 브이지더블유 | 혈청 알부민 결합제 |
| WO2019086548A1 (en) | 2017-10-31 | 2019-05-09 | Vib Vzw | Novel antigen-binding chimeric proteins and methods and uses thereof |
| EP3749690A1 (en) | 2018-02-05 | 2020-12-16 | Stichting VU | Inverse agonistic anti-us28 antibodies |
| IL276200B2 (en) | 2018-02-06 | 2025-01-01 | Ablynx Nv | Polypeptide comprising two variable domains of anti-human (vWF) immunoglobulins VON- for use in the treatment of a first episode of von Willebrand Factor (vWF)-related disease |
| WO2019155041A1 (en) | 2018-02-12 | 2019-08-15 | Vib Vzw | Gβγ COMPLEX ANTIBODIES AND USES THEREOF |
| WO2019156566A1 (en) | 2018-02-12 | 2019-08-15 | Umc Utrecht Holding B.V. | Bispecific molecules comprising gamma-delta tcr and t-cell or nk cell binding domain |
| CA3092421A1 (en) | 2018-03-01 | 2019-09-06 | Vrije Universiteit Brussel | Human pd-l1-binding immunoglobulins |
| WO2019226050A2 (en) | 2018-05-24 | 2019-11-28 | Wageningen Universiteit | Novel viral anti-infective reagents |
| EP3636657A1 (en) | 2018-10-08 | 2020-04-15 | Ablynx N.V. | Chromatography-free antibody purification method |
| WO2020080941A1 (en) | 2018-10-16 | 2020-04-23 | Umc Utrecht Holding B.V. | Anti- low-density lipoprotein receptor-related protein 5/6 antibodies |
| WO2020130838A2 (en) | 2018-12-21 | 2020-06-25 | Qvq Holding B.V. | Antibodies for preventing or treating candidiasis |
| GB201901608D0 (en) | 2019-02-06 | 2019-03-27 | Vib Vzw | Vaccine adjuvant conjugates |
| ES2984072T3 (es) | 2019-03-08 | 2024-10-28 | Linxis B V | Moléculas de unión internalizantes que actúan sobre receptores implicados en la proliferación celular o en ladiferenciación celular |
| CN113646048A (zh) | 2019-03-29 | 2021-11-12 | 勃林格殷格翰国际有限公司 | 抗癌组合疗法 |
| EP3947455A1 (en) | 2019-03-29 | 2022-02-09 | Boehringer Ingelheim International GmbH | Anticancer combination therapy |
| EP3946434A1 (en) | 2019-04-02 | 2022-02-09 | Immunetune B.V. | Immune-stimulatory compositions and use thereof |
| EP3963328A1 (en) | 2019-04-29 | 2022-03-09 | Confo Therapeutics N.V. | Chimeric proteins and methods to screen for compounds and ligands binding to gpcrs |
| WO2020221888A1 (en) | 2019-04-30 | 2020-11-05 | Vib Vzw | Cystic fibrosis transmembrane conductance regulator stabilizing agents |
| EP3976650A1 (en) | 2019-05-28 | 2022-04-06 | Vib Vzw | Cancer treatment by targeting plexins in the immune compartment |
| US12472254B2 (en) | 2019-05-28 | 2025-11-18 | Vib Vzw | CD8+ T-cells lacking plexins and their application in cancer treatment |
| WO2021025556A1 (en) | 2019-08-05 | 2021-02-11 | Stichting Vu | Identification and elimination of hcmv-infected cells |
| CN111748571B (zh) * | 2019-10-11 | 2022-05-03 | 浙江禾霖生物科技有限公司 | 一种将枯草芽孢杆菌工程化为生产纳米抗体的多功能稳定平台的方法 |
| US20220380456A1 (en) | 2019-10-21 | 2022-12-01 | Vib Vzw | Nanodisc-specific antigen-binding chimeric proteins |
| WO2021095031A2 (en) | 2019-11-11 | 2021-05-20 | Ibi-Ag Innovative Bio Insecticides Ltd. | Insect control nanobodies and uses thereof |
| CA3158991A1 (en) | 2019-11-27 | 2021-06-03 | Vib Vzw | Positive allosteric modulators of the calcium-sensing receptor |
| GB201918279D0 (en) | 2019-12-12 | 2020-01-29 | Vib Vzw | Glycosylated single chain immunoglobulin domains |
| EP4077372A1 (en) | 2019-12-20 | 2022-10-26 | Vib Vzw | Nanobody exchange chromatography |
| WO2021140205A1 (en) | 2020-01-10 | 2021-07-15 | Confo Therapeutics N.V. | Methods for generating antibodies and antibody fragments and libraries comprising same |
| WO2021156490A2 (en) | 2020-02-06 | 2021-08-12 | Vib Vzw | Corona virus binders |
| US20230087785A1 (en) | 2020-02-25 | 2023-03-23 | Vib Vzw | Leucine-Rich Repeat Kinase 2 Allosteric Modulators |
| JP2023523600A (ja) | 2020-04-22 | 2023-06-06 | マブウェル （シャンハイ） バイオサイエンス カンパニー リミテッド | ヒトプログラム細胞死リガンド１（ｐｄ－ｌ１）を標的とする単一可変ドメイン抗体およびその誘導体 |
| WO2021229104A1 (en) | 2020-05-15 | 2021-11-18 | Université de Liège | Anti-cd38 single-domain antibodies in disease monitoring and treatment |
| WO2022003156A1 (en) | 2020-07-02 | 2022-01-06 | Oncurious Nv | Ccr8 non-blocking binders |
| EP4185612A4 (en) | 2020-07-23 | 2024-12-25 | Othair Prothena Limited | Anti-abeta antibodies |
| WO2022060223A1 (en) | 2020-09-16 | 2022-03-24 | Linxis B.V. | Internalizing binding molecules |
| WO2022063947A1 (en) | 2020-09-24 | 2022-03-31 | Vib Vzw | Combination of p2y6 inhibitors and immune checkpoint inhibitors |
| WO2022063957A1 (en) | 2020-09-24 | 2022-03-31 | Vib Vzw | Biomarker for anti-tumor therapy |
| BR112023005273A2 (pt) | 2020-09-25 | 2023-04-25 | Ablynx Nv | Polipeptídeos compreendendo domínios variáveis únicos de imunoglobulina direcionados a il-13 e ox40l |
| EP4221750A4 (en) * | 2020-09-30 | 2024-11-13 | Merck Sharp & Dohme LLC | BINDING PROTEINS AND ANTIGEN-BINDING FRAGMENTS THEREOF BINDING TO ABETA |
| WO2022098743A1 (en) | 2020-11-03 | 2022-05-12 | Indi Molecular, Inc. | Compositions, imaging, and therapeutic methods targeting folate receptor 1 (folr1) |
| WO2022098745A1 (en) | 2020-11-03 | 2022-05-12 | Indi Molecular, Inc. | Compositions, delivery systems, and methods useful in tumor therapy |
| WO2022117572A2 (en) | 2020-12-02 | 2022-06-09 | Oncurious Nv | An ltbr agonist in combination therapy against cancer |
| WO2022117569A1 (en) | 2020-12-02 | 2022-06-09 | Oncurious Nv | A ccr8 antagonist antibody in combination with a lymphotoxin beta receptor agonist antibody in therapy against cancer |
| KR20230123497A (ko) | 2020-12-18 | 2023-08-23 | 아블린쓰 엔.브이. | IL-6 및 TNF-α를 표적화하는 면역글로불린 단일 가변도메인을 포함하는 폴리펩티드 |
| GB202020502D0 (en) | 2020-12-23 | 2021-02-03 | Vib Vzw | Antibody composistion for treatment of corona virus infection |
| US20240052045A1 (en) | 2020-12-24 | 2024-02-15 | Vib Vzw | Murine cross-reactive human ccr8 binders |
| EP4267618A1 (en) | 2020-12-24 | 2023-11-01 | Vib Vzw | Non-blocking human ccr8 binders |
| EP4267617A1 (en) | 2020-12-24 | 2023-11-01 | Vib Vzw | Human ccr8 binders |
| CN113150140B (zh) * | 2021-01-25 | 2022-11-04 | 山西农业大学 | 一种sox6二价纳米抗体及其应用 |
| AU2022216460A1 (en) | 2021-02-05 | 2023-09-21 | Universiteit Gent | Sarbecovirus binders |
| CN117794566A (zh) | 2021-02-05 | 2024-03-29 | Vib研究所 | 沙贝病毒结合剂 |
| US20240130999A1 (en) | 2021-02-17 | 2024-04-25 | Vib Vzw | Inhibition of SLC4A4 in the Treatment of Cancer |
| EP4294516A1 (en) | 2021-02-19 | 2023-12-27 | Vib Vzw | Cation-independent mannose-6-phosphate receptor binders |
| WO2022199804A1 (en) | 2021-03-24 | 2022-09-29 | Vib Vzw | Nek6 inhibition to treat als and ftd |
| EP4320229A1 (en) | 2021-04-09 | 2024-02-14 | Stichting Radboud Universiteit | Off the shelf proximity biotinylation enzyme |
| US20240261446A1 (en) | 2021-05-17 | 2024-08-08 | Université de Liège | Anti-cd38 single domain antibodies in disease monitoring and treatment |
| WO2022258606A1 (en) | 2021-06-07 | 2022-12-15 | Gadeta B.V. | Delta T-cell or Gamma T-cell receptor chains or parts thereof that mediate an anti-tumour or anti-infective response |
| EP4355778A1 (en) | 2021-06-17 | 2024-04-24 | Boehringer Ingelheim International GmbH | Novel tri-specific binding molecules |
| EP4359421A1 (en) | 2021-06-23 | 2024-05-01 | Vib Vzw | Means and methods for selection of specific binders |
| CN117580865A (zh) | 2021-06-29 | 2024-02-20 | 山东先声生物制药有限公司 | Cd16抗体及其应用 |
| WO2023004293A1 (en) | 2021-07-20 | 2023-01-26 | Lanzatech, Inc. | Recombinant microorganisms and uses therefor |
| WO2023016828A2 (en) | 2021-07-30 | 2023-02-16 | Vib Vzw | Cation-independent mannose-6-phosphate receptor binders for targeted protein degradation |
| JP7727086B2 (ja) | 2021-07-30 | 2025-08-20 | 山▲東▼先声生物制▲薬▼有限公司 | 抗ｐｖｒｉｇ／抗ｔｉｇｉｔ二重特異性抗体及び応用 |
| US20240271186A1 (en) | 2021-08-03 | 2024-08-15 | Wageningen Universiteit | Argonaute-based nucleic acid detection system |
| US20250019460A1 (en) * | 2021-12-01 | 2025-01-16 | Epsilon Molecular Engineering Inc. | Peptide having framework sequence for random region placement and peptide library composed of said peptide |
| WO2023098846A1 (zh) | 2021-12-03 | 2023-06-08 | 江苏先声药业有限公司 | 抗bcma纳米抗体及其应用 |
| TW202342508A (zh) | 2021-12-17 | 2023-11-01 | 比利時商艾伯霖克斯公司 | 包含靶向ＴＣＲαβ、ＣＤ３３和ＣＤ１２３的免疫球蛋白單可變結構域的多肽 |
| WO2023125888A1 (zh) | 2021-12-31 | 2023-07-06 | 山东先声生物制药有限公司 | 一种gprc5d抗体及其应用 |
| EP4463479A1 (en) | 2022-01-12 | 2024-11-20 | Vib Vzw | Human ntcp binders for therapeutic use and liver-specific targeted delivery |
| EP4476250A1 (en) | 2022-02-07 | 2024-12-18 | Vib Vzw | Engineered stabilizing aglycosylated fc-regions |
| WO2023198848A1 (en) | 2022-04-13 | 2023-10-19 | Vib Vzw | An ltbr agonist in combination therapy against cancer |
| US20250313611A1 (en) | 2022-05-18 | 2025-10-09 | Vib Vzw | Sarbecovirus spike s2 subunit binders |
| WO2023227594A1 (en) | 2022-05-24 | 2023-11-30 | Gadeta Bv | Novel deltat-cell receptor chains, gammat-cell receptor chains, or parts thereof |
| IL317463A (en) | 2022-06-06 | 2025-02-01 | Shandong Simcere Biopharmaceutical Co Ltd | Multispecific antibodies targeting BCMA, GPRC5D and T cells and their application |
| WO2023237541A1 (en) | 2022-06-07 | 2023-12-14 | Gadeta B.V. | Delta t-cell or gamma t-cell receptor chains or parts thereof that mediate an anti-tumour or anti-infective response |
| EP4551600A1 (en) | 2022-07-04 | 2025-05-14 | Vib Vzw | Blood-cerebrospinal fluid barrier crossing antibodies |
| AR129879A1 (es) | 2022-07-08 | 2024-10-09 | Novo Nordisk As | Compuestos de isvd altamente potentes capaces de sustituir al fviii(a) |
| WO2024013315A1 (en) | 2022-07-15 | 2024-01-18 | Boehringer Ingelheim International Gmbh | Binding molecules for the treatment of cancer |
| WO2024013402A1 (en) | 2022-07-15 | 2024-01-18 | Gadeta B.V. | Novel soluble gamma t-cell (or soluble delta t-cell) receptor chains (or soluble gammadelta t-cell receptors) or fragments thereof that mediate an anti-tumour or an anti-infective response |
| CN120077065A (zh) | 2022-07-27 | 2025-05-30 | 阿布林克斯有限公司 | 与新生儿Fc受体的特定表位结合的多肽 |
| WO2024068744A1 (en) | 2022-09-27 | 2024-04-04 | Vib Vzw | Antivirals against human parainfluenza virus |
| WO2024083843A1 (en) | 2022-10-18 | 2024-04-25 | Confo Therapeutics N.V. | Amino acid sequences directed against the melanocortin 4 receptor and polypeptides comprising the same for the treatment of mc4r-related diseases and disorders |
| WO2024084203A1 (en) * | 2022-10-18 | 2024-04-25 | Isogenica Limited | Single domain antibodies binding to albumin |
| EP4628505A1 (en) | 2022-10-28 | 2025-10-08 | Genor Biopharma Co., Ltd. | Novel anti-ctla4 antibody |
| EP4612180A1 (en) | 2022-10-31 | 2025-09-10 | Stichting Amsterdam UMC | Single domain anti-cd169 antibodies |
| EP4615493A1 (en) | 2022-11-08 | 2025-09-17 | Stichting Amsterdam UMC | Activation inducible antigen receptors for adoptive immunotherapy |
| JP2025537809A (ja) | 2022-11-15 | 2025-11-20 | アイメック・ヴェーゼットウェー | 液滴操作のための方法およびシステム |
| AR131388A1 (es) | 2022-12-15 | 2025-03-12 | Univ Aarhus | Activación sintética de receptores transmembrana multiméricos |
| AU2023410327A1 (en) | 2022-12-19 | 2025-06-05 | Umc Utrecht Holding B.V. | Btn2a1 binding peptide |
| US20240415974A1 (en) | 2022-12-23 | 2024-12-19 | Ablynx N.V. | Protein-based conjugation carriers |
| AU2024208858A1 (en) | 2023-01-20 | 2025-06-19 | Boehringer Ingelheim International Gmbh | Il-12 fc fusion proteins |
| WO2024156881A1 (en) | 2023-01-27 | 2024-08-02 | Vib Vzw | CD8b-BINDING POLYPEPTIDES |
| EP4655324A1 (en) | 2023-01-27 | 2025-12-03 | Vib Vzw | Cd163-binding conjugates |
| AR131869A1 (es) | 2023-02-17 | 2025-05-07 | Ablynx Nv | POLIPÉPTIDOS QUE SE UNEN AL RECEPTOR DE Fc NEONATAL |
| WO2024175787A1 (en) | 2023-02-24 | 2024-08-29 | Vrije Universiteit Brussel | Anti-inflammatory pannexin 1 channel inhibitors |
| US20240344078A1 (en) | 2023-03-14 | 2024-10-17 | Aarhus Universitet | Genetically altered nfr5 receptor kinases |
| AU2024243709A1 (en) | 2023-04-03 | 2025-11-06 | Katholieke Universiteit Leuven | Blood-brain barrier crossing antibodies |
| WO2024231348A1 (en) | 2023-05-11 | 2024-11-14 | Vib Vzw | Slc4a4/nbce1 inhibitors |
| WO2024240162A1 (en) | 2023-05-23 | 2024-11-28 | Shanghai Allygen Biologics Co., Ltd. | Pd-l1 and trop-2 targeting conjugates comprising effector molecules and uses thereof |
| WO2024251826A1 (en) | 2023-06-05 | 2024-12-12 | Vib Vzw | Glyco-engineered antibody-drug-conjugates comprising an oxime linker |
| WO2024251981A1 (en) | 2023-06-09 | 2024-12-12 | Umc Utrecht Holding B.V. | Detecting and/or modulating susceptibility to btn2a1 and/or btn3a1 targeting therapeutics |
| WO2024261344A1 (en) | 2023-06-23 | 2024-12-26 | Vib Vzw | Novel binders targeting the multi-drug resistant pathogen acinetobacter baumannii |
| EP4483951A1 (en) | 2023-06-30 | 2025-01-01 | Université de Liège | Single-domain antibody for inhibition of neutrophil elastase activity |
| GB202314424D0 (en) | 2023-09-20 | 2023-11-01 | Cambridge Entpr Ltd | A conjugate |
| WO2025061919A1 (en) | 2023-09-22 | 2025-03-27 | Ablynx Nv | Bi- and multivalent albumin binders |
| WO2025093683A1 (en) | 2023-11-03 | 2025-05-08 | Neuvasq Biotechnologies Sa | Wnt7 signaling agonists |
| WO2025109176A1 (en) | 2023-11-22 | 2025-05-30 | Exevir Bio Bv | Optimized sarbecovirus spike s2 subunit binders and compositions comprising the same |
| WO2025125577A1 (en) | 2023-12-14 | 2025-06-19 | Vib Vzw | Antibodies against influenza b virus |
| WO2025133166A1 (en) | 2023-12-22 | 2025-06-26 | Ablynx Nv | Protein-based carriers for site-specific amine conjugation |
| WO2025133253A2 (en) | 2023-12-22 | 2025-06-26 | Ablynx Nv | Protein-based conjugation carriers for intranuclear delivery |
| WO2025154056A1 (en) | 2024-01-21 | 2025-07-24 | Ibi-Ag Innovative Bio Insecticides Ltd. | Anti-insect cda nanobodies and uses thereof |
| WO2025154058A1 (en) | 2024-01-21 | 2025-07-24 | Ibi-Ag Innovative Bio Insecticides Ltd. | Anti-insect hsp70 nanobodies and uses thereof |
| WO2025181155A1 (en) | 2024-02-26 | 2025-09-04 | Vib Vzw | Human beta-glucocerebrosidase binders and uses thereof |
| WO2025196308A1 (en) | 2024-03-22 | 2025-09-25 | Vib Vzw | Means and methods for displaying fc-containing proteins on cells and selection thereof |
| WO2025210082A1 (en) * | 2024-04-05 | 2025-10-09 | UCB Biopharma SRL | Heavy chain variable domains that bind to free light chains |
| WO2025219231A1 (en) | 2024-04-15 | 2025-10-23 | Vib Vzw | Computer-implemented means and methods for the de novo design of antibodies targeting a specific epitope |
| GB202405566D0 (en) * | 2024-04-19 | 2024-06-05 | 272Bio Ltd | vnh antibodies |
| WO2025229160A1 (en) | 2024-05-01 | 2025-11-06 | Commit Biologics Aps | Engineered proteins that engage complement factor and a protein antigen, methods, and uses thereof |
Family Cites Families (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4559157A (en) * | 1983-04-21 | 1985-12-17 | Creative Products Resource Associates, Ltd. | Cosmetic applicator useful for skin moisturizing |
| LU84979A1 (fr) * | 1983-08-30 | 1985-04-24 | Oreal | Composition cosmetique ou pharmaceutique sous forme aqueuse ou anhydre dont la phase grasse contient un polyether oligomere et polyethers oligomeres nouveaux |
| EP0279582A3 (en) * | 1987-02-17 | 1989-10-18 | Pharming B.V. | Dna sequences to target proteins to the mammary gland for efficient secretion |
| US4820508A (en) * | 1987-06-23 | 1989-04-11 | Neutrogena Corporation | Skin protective composition |
| US4992478A (en) * | 1988-04-04 | 1991-02-12 | Warner-Lambert Company | Antiinflammatory skin moisturizing composition and method of preparing same |
| US4938949A (en) * | 1988-09-12 | 1990-07-03 | University Of New York | Treatment of damaged bone marrow and dosage units therefor |
| US5530101A (en) * | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5703055A (en) * | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| US5399346A (en) * | 1989-06-14 | 1995-03-21 | The United States Of America As Represented By The Department Of Health And Human Services | Gene therapy |
| US5977307A (en) * | 1989-09-07 | 1999-11-02 | Alkermes, Inc. | Transferrin receptor specific ligand-neuropharmaceutical agent fusion proteins |
| US5633076A (en) * | 1989-12-01 | 1997-05-27 | Pharming Bv | Method of producing a transgenic bovine or transgenic bovine embryo |
| WO1994004679A1 (en) * | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
| ES2109362T3 (es) * | 1991-06-21 | 1998-01-16 | Univ Cincinnati | Unas proteinas administrables oralmente y metodo para hacerlas. |
| US5441870A (en) * | 1992-04-15 | 1995-08-15 | Athena Neurosciences, Inc. | Methods for monitoring cellular processing of β-amyloid precursor protein |
| WO1994002610A1 (en) * | 1992-07-17 | 1994-02-03 | Dana-Farber Cancer Institute | Method of intracellular binding of target molecules |
| DE69330523D1 (de) * | 1992-08-21 | 2001-09-06 | Vrije Universiteit Brussel Bru | Immunoglobuline ohne leichte ketten |
| US5750349A (en) * | 1993-01-25 | 1998-05-12 | Takeda Chemical Industries Ltd. | Antibodies to β-amyloids or their derivatives and use thereof |
| US5827690A (en) * | 1993-12-20 | 1998-10-27 | Genzyme Transgenics Corporatiion | Transgenic production of antibodies in milk |
| WO1996022307A1 (en) * | 1995-01-19 | 1996-07-25 | The Research Foundation Of State University Of New York | Genes encoding an insect calcium channel |
| EP0739981A1 (en) * | 1995-04-25 | 1996-10-30 | Vrije Universiteit Brussel | Variable fragments of immunoglobulins - use for therapeutic or veterinary purposes |
| US5693492A (en) * | 1995-05-05 | 1997-12-02 | Merck & Co., Inc. | DNA encoding glutamate gated chloride channels |
| US6221645B1 (en) * | 1995-06-07 | 2001-04-24 | Elan Pharmaceuticals, Inc. | β-secretase antibody |
| IL115465A0 (en) * | 1995-09-29 | 1995-12-31 | Yeda Res & Dev | Assay for the diagnosis of dementia |
| US8173127B2 (en) * | 1997-04-09 | 2012-05-08 | Intellect Neurosciences, Inc. | Specific antibodies to amyloid beta peptide, pharmaceutical compositions and methods of use thereof |
| US6743427B1 (en) * | 1997-12-02 | 2004-06-01 | Neuralab Limited | Prevention and treatment of amyloidogenic disease |
| US6761888B1 (en) * | 2000-05-26 | 2004-07-13 | Neuralab Limited | Passive immunization treatment of Alzheimer's disease |
| NO314086B1 (no) * | 1998-05-08 | 2003-01-27 | Gemvax As | Peptider og farmasöytiske sammensetninger inneholdende disse, nukleinsyresekvenser som koder for slike peptider, plasmider og virusvektoreromfattende slike DNA-sekvenser samt anvendelse av disse for fremstilling avfarmasöytiske preparater til |
| NZ534876A (en) * | 1999-02-10 | 2006-02-24 | Elan Pharm Inc | Human beta-secretase enzyme, inhibitors and their compositions and uses |
| CA2441903C (en) * | 2000-05-26 | 2012-07-31 | National Research Council Of Canada | Single-domain brain-targeting antibody fragments derived from llama antibodies |
| FR2846667B1 (fr) * | 2002-11-06 | 2004-12-31 | Pasteur Institut | Fragments variables d'anticorps de camelides a chaine unique diriges contre le peptide beta-amyloide 1-42 et leurs applications pour le diagnostic et le traitement des maladies neuroagregatives |
| JP2006519763A (ja) * | 2002-11-08 | 2006-08-31 | アブリンクス エン．ヴェー． | 治療用ポリペプチドの投与法およびそのためのポリペプチド |
| AU2003286002B2 (en) * | 2002-11-08 | 2011-06-16 | Ablynx N.V. | Single domain antibodies directed against tumour necrosis factor-alpha and uses therefor |
| US20100323905A1 (en) * | 2005-09-23 | 2010-12-23 | Academisch Ziekenhuis Leiden | Vhh for the Diagnosis, Prevention and Treatment of Diseases Associated with Protein Aggregates |
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| WO2006040153A3 (en) | 2007-04-19 |
| KR20070084170A (ko) | 2007-08-24 |
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