ZA200500062B - Proteins binding to cross-beta structure comprising amyloid and methods for detection and modulationof the cross-beta structure, its formation and it s associated toxicity. - Google Patents
Proteins binding to cross-beta structure comprising amyloid and methods for detection and modulationof the cross-beta structure, its formation and it s associated toxicity. Download PDFInfo
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- ZA200500062B ZA200500062B ZA200500062A ZA200500062A ZA200500062B ZA 200500062 B ZA200500062 B ZA 200500062B ZA 200500062 A ZA200500062 A ZA 200500062A ZA 200500062 A ZA200500062 A ZA 200500062A ZA 200500062 B ZA200500062 B ZA 200500062B
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EP1820806A1 (fr) * | 2006-02-16 | 2007-08-22 | Crossbeta Biosciences B.V. | Zones d'affinité |
US20070003552A1 (en) * | 2002-07-09 | 2007-01-04 | Gebbink Martijn F B | Cross-beta structure comprising amyloid binding proteins and methods for detection of the cross-beta structure, for modulating cross-beta structures fibril formation and for modulating cross-beta structure-mediated toxicity and method for interfering with blood coagulation |
EP1380290A1 (fr) * | 2002-07-09 | 2004-01-14 | Universitair Medisch Centrum Utrecht | La voie de la structure cross-béta et sa pertinence thérapeutique |
EP1704867A1 (fr) * | 2005-03-18 | 2006-09-27 | Crossbeta Biosciences B.V. | Des Structures cross-Beta sur des microorganismes |
US20090202980A1 (en) * | 2005-03-21 | 2009-08-13 | Crossbeta Biosciences B.V. | Cross-Beta Structure Comprising Amyloid Binding Proteins and Methods for Detection of the Cross-Beta Structure, for Modulating Cross-Beta Structures Fibril Formation and for Modulating Cross-Beta Structure-Mediated Toxicity and Method for Interfering With Blood Coagulation |
BRPI0613525A2 (pt) * | 2005-07-13 | 2011-05-31 | Crossbeta Biosciences Bv | métodos para produzir uma composição imunogênica, para melhorar a imunogenicidade de uma composição, para intensificar a imunogenicidade de uma composição de vacina, e para determinar a quantidade de estruturas beta-cruzadas em uma composição de vacina, usos de estruturas beta-cruzadas, e de uma composição imunogênica, vacina de subunidade, e, composição imunogênica |
US20070015133A1 (en) * | 2005-07-13 | 2007-01-18 | Umc Utrecht Holding B.V. | Method for detecting and/or removing protein and/or peptide comprising a cross-beta structure from an aqueous solution comprising a protein |
US8114832B2 (en) * | 2005-07-13 | 2012-02-14 | Crossbeta Biosciences B.V. | Method for detecting and/or removing a protein comprising a cross-beta structure from a pharmaceutical composition |
CA2615078A1 (fr) * | 2005-07-13 | 2007-01-18 | Crossbeta Biosciences B.V. | Methodes de determination de l'effet d'un traitement sur la teneur d'une proteine a structure croisee-.beta. selection des traitements et leurs utilisations |
ATE554394T1 (de) * | 2005-07-13 | 2012-05-15 | Crossbeta Biosciences Bv | Cross-beta-struktur-bindende verbindungen |
WO2007108675A1 (fr) * | 2006-03-17 | 2007-09-27 | Crossbeta Biosciences B.V. | Procédés de liaison de structures bêta croisées avec des molécules chaperonnes |
GB0710976D0 (en) | 2007-06-07 | 2007-07-18 | Bioalvo | Am Screening method |
EP2058000A1 (fr) * | 2007-11-08 | 2009-05-13 | Crossbeta Biosciences B.V. | Compositions immunogènes capables d'activer des cellules T |
EP2058001A1 (fr) * | 2007-11-08 | 2009-05-13 | Crossbeta Biosciences B.V. | Amélioration de l'immunogénicité des antigènes |
CN104777308B (zh) * | 2008-10-31 | 2017-04-12 | 耶鲁大学 | 先兆子痫检测和治疗的方法和组合物 |
EP2361645B1 (fr) | 2008-12-22 | 2014-10-29 | Fujita Health University | Utilisation d'un support pour l'elimination de proteine amyloïde-beta a partir de fluides extracorporels |
EP2322163A1 (fr) * | 2009-11-03 | 2011-05-18 | Pharnext | Nouvelles approches thérapeutiques pour traiter la maladie d'Alzheimer |
JP5843345B2 (ja) | 2010-07-08 | 2016-01-13 | 旭化成メディカル株式会社 | β−アミロイド除去システム |
DE102011003944A1 (de) | 2011-02-10 | 2012-08-16 | Oxprotect Gmbh | Detektion und Entfernung von missgefalteten Proteinen/Peptiden |
US20130122076A1 (en) * | 2011-11-11 | 2013-05-16 | Mathew Gelfand | Transdermal Patch Having Ultrasound Transducer for Administering Thrombolytic Reagents to Patients Having a Protein Misfolding Disease |
TW202019398A (zh) * | 2018-06-28 | 2020-06-01 | 張翔毓 | 用於治療或預防構形疾病之方法及藥物篩選方法 |
Family Cites Families (125)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS60103964A (ja) * | 1983-11-10 | 1985-06-08 | ユニチカ株式会社 | 抗血栓性材料 |
US5700447A (en) * | 1992-05-21 | 1997-12-23 | The Picowder Institute For Medical Research | Methods and materials for the diagnosis and treatment of conditions such as stroke |
US5869534A (en) * | 1992-05-21 | 1999-02-09 | The Picower Institute For Medical Research | Glycosylation of lipids and lipid-containing particles, and diagnostic and therapeutic methods and materials derived therefrom |
US5733524A (en) * | 1984-03-19 | 1998-03-31 | The Picower Institute For Medical Research | Methods and materials for the diagnosis and treatment of conditions such as stroke |
US5801200A (en) * | 1984-03-19 | 1998-09-01 | The Picower Institute For Medical Research | Methods and materials for the diagnosis and treatment of conditions such as stroke |
US5733933A (en) * | 1984-03-19 | 1998-03-31 | The Picower Institute For Medical Research | Methods and materials for the diagnosis and treatment of conditions such as stroke |
DE3682891D1 (de) * | 1986-02-17 | 1992-01-23 | Stichting Centraal Lab | Gewebeplasminogen-aktivator-mutant, dafuer kodierende rekombinante genetische information und verfahren zur herstellung dieser mutanten, deren verwendung und pharmazeutische zusammensetzungen. |
EP0319144A1 (fr) * | 1987-11-06 | 1989-06-07 | Asahi Kasei Kogyo Kabushiki Kaisha | Absorbant de bêta-2-microglobuline |
JPH01171638A (ja) * | 1987-12-25 | 1989-07-06 | Kanegafuchi Chem Ind Co Ltd | 血清アミロイドa蛋白用吸着体 |
US5216127A (en) * | 1987-11-20 | 1993-06-01 | Kanegafuchi Kagaku Kogyo Kabushiki Kaisha | Adsorbent for serum amyloid protein |
DE3880647T2 (de) * | 1987-11-20 | 1993-11-18 | Kanegafuchi Chemical Ind | Sorbentmittel für Serum-Amyloid-Proteine. |
US5151082A (en) * | 1988-08-05 | 1992-09-29 | Heathdyne, Inc. | Apparatus and method for kidney dialysis using plasma in lieu of blood |
US5679320A (en) * | 1988-12-29 | 1997-10-21 | Bio-Technology General Corp. | Fibrin binding domain polypeptides and uses and methods of producing same |
CA1335361C (fr) * | 1989-05-24 | 1995-04-25 | Andrei Z. Budzynski | Complexes diriges contre les thrombus et formes d'activateurs du plasminogene et de fragments de fibrine |
US5180615A (en) * | 1989-12-13 | 1993-01-19 | W.R. Grace & Co.-Conn. | Metallized bag for static protection of electronic components |
US5591431A (en) * | 1990-03-09 | 1997-01-07 | G.D. Searle & Co. | Enhancement of clot lysis |
US5753624A (en) * | 1990-04-27 | 1998-05-19 | Milkhaus Laboratory, Inc. | Materials and methods for treatment of plaquing disease |
SE502414C2 (sv) * | 1990-05-28 | 1995-10-16 | Ljungqvist Olle Medical Ab | Användning av glukos för framställning av lösning för preoperativ administrering samt infusionslösning därför |
US5278189A (en) * | 1990-06-04 | 1994-01-11 | Rath Matthias W | Prevention and treatment of occlusive cardiovascular disease with ascorbate and substances that inhibit the binding of lipoprotein (A) |
US5650418A (en) * | 1990-06-04 | 1997-07-22 | Therapy 2000 | Therapeutic lysine salt composition and method of use |
US5230996A (en) * | 1990-06-04 | 1993-07-27 | Therapy 2000 | Use of ascorbate and tranexamic acid solution for organ and blood vessel treatment prior to transplantation |
EP0532706B1 (fr) * | 1990-06-04 | 1995-05-10 | Health Now | REDUCTION D'OCCLUSIONS DE VAISSEAUX CARDIOVASCULAIRES A L'AIDE D'ASCORBATE ET D'INHIBITEURS DE LIAISON DE LA LIPOPROTEINE (a) |
US5780587A (en) * | 1990-08-24 | 1998-07-14 | President And Fellows Of Harvard College | Compounds and methods for inhibiting β-protein filament formation and neurotoxicity |
SE468881B (sv) * | 1991-01-09 | 1993-04-05 | Kabi Pharmacia Ab | Anvaendning av vissa foereningar foer framstaellning av laekemedel foer behandling av endotoxininducerade effekter samt saett att avlaegsna endotoxiner ur diverse loesningar |
US5221628A (en) * | 1991-03-19 | 1993-06-22 | Northwestern University | Binding of aggregated immunoglobulin or immune complexes by serum amyloid P component |
US5276059A (en) * | 1992-07-10 | 1994-01-04 | The United States Of America As Represented By The Department Of Health And Human Services | Inhibition of diseases associated with amyloid formation |
US5491129A (en) * | 1992-07-30 | 1996-02-13 | Yeda Research And Development Co. Ltd. | Synthetic peptides derived from vitronectin and pharmaceutical compositions comprising them |
US5958883A (en) * | 1992-09-23 | 1999-09-28 | Board Of Regents Of The University Of Washington Office Of Technology | Animal models of human amyloidoses |
DE4242736A1 (de) * | 1992-12-17 | 1994-06-23 | Behringwerke Ag | Synthetische Peptide, Antikörper dagegen und ihre Verwendung |
US5955343A (en) * | 1992-12-28 | 1999-09-21 | Massachusetts Institute Of Technology | Stable macroscopic membranes formed by self-assembly of amphiphilic peptides and uses therefor |
EP0683234B2 (fr) * | 1993-01-25 | 2007-06-06 | Takeda Chemical Industries, Ltd. | Anticorps dirige contre le beta-amyloide ou un derive de ce dernier et son utilisation |
US5449663A (en) * | 1993-06-11 | 1995-09-12 | Bicher; Haim I. | Antineoplastic compositions |
JP3680114B2 (ja) * | 1993-09-17 | 2005-08-10 | 敏一 中村 | 脳神経障害治療剤 |
CA2156255C (fr) * | 1993-12-17 | 2008-02-05 | Yasuyuki Kunihiro | Dispositif a semi-conducteur |
US6410598B1 (en) * | 1994-02-03 | 2002-06-25 | Michael P. Vitek | Compositions and methods for advanced glycosylation endproduct-mediated modulation of amyloidosis |
US5935927A (en) * | 1994-02-03 | 1999-08-10 | The Picower Institute For Medical Research | Compositions and methods for stimulating amyloid removal in amyloidogenic diseases using advanced glycosylation endproducts |
KR0163563B1 (ko) * | 1994-03-23 | 1998-12-01 | 김종인 | 피부질환 치료용 의약조성물 |
US5786324A (en) * | 1994-03-24 | 1998-07-28 | Regents Of The University Of Minnesota | Synthetic peptides with bactericidal activity and endotoxin neutralizing activity for gram negative bacteria and methods for their use |
US5589154A (en) * | 1994-11-22 | 1996-12-31 | Rutgers, The State University Of New Jersey | Methods for the prevention or treatment of vascular hemorrhaging and Alzheimer's disease |
US6136548A (en) * | 1994-11-22 | 2000-10-24 | Rutgers, The State University Of New Jersey | Methods for identifying useful T-PA mutant derivatives for treatment of vascular hemorrhaging |
US5888774A (en) * | 1994-12-19 | 1999-03-30 | Cangene Corporation | Recombinant DNA molecules and expression vectors for erythropoietin |
DE69621607T2 (de) * | 1995-03-14 | 2003-01-02 | Praecis Pharm Inc | VERBINDUNGEN MIT AGGREGATIONS-MODULIERENDEN WIRKUNG AUF DAS AMYLOiD PROTEIN |
US5817626A (en) * | 1995-03-14 | 1998-10-06 | Praecis Pharmaceuticals Incorporated | Modulators of beta-amyloid peptide aggregation |
US5854215A (en) * | 1995-03-14 | 1998-12-29 | Praecis Pharmaceuticals Incorporated | Modulators of β-amyloid peptide aggregation |
US5948763A (en) * | 1995-06-07 | 1999-09-07 | New York University | Peptides and pharmaceutical compositions thereof for treatment of disorders or diseases associated with abnormal protein folding into amyloid or amyloid-like deposits |
US6436969B1 (en) * | 1995-09-12 | 2002-08-20 | Kansas University Medical Center Research Institute Inc. | Dialysis solutions and methods |
AU7253596A (en) * | 1995-10-02 | 1997-04-28 | Mohammad W. Katoot | Biologically-active polymers |
US5985242A (en) * | 1995-10-27 | 1999-11-16 | Praecis Pharmaceuticals, Inc. | Modulators of β-amyloid peptide aggregation comprising D-amino acids |
US6310046B1 (en) * | 1995-11-17 | 2001-10-30 | The United States Of America As Represented By The Secretary Of The Army | Sequestrin of Plasmodium falciparum |
WO1997026919A2 (fr) * | 1996-01-24 | 1997-07-31 | Warner-Lambert Company | Methode d'imagerie de depots amyloides |
US5785187A (en) * | 1996-04-29 | 1998-07-28 | Lipman; Daniel | Mechandising display assembly |
US6034211A (en) * | 1996-06-03 | 2000-03-07 | Kelly; Jeffery W. | β-sheet nucleating peptidomimetics |
AU734183C (en) * | 1996-08-09 | 2001-11-22 | Mannatech, Inc. | Compositions of plant carbohydrates as dietary supplements |
US6929807B1 (en) * | 1996-08-09 | 2005-08-16 | Mannatech, Inc. | Compositions of plant carbohydrates as dietary supplements |
US6689275B1 (en) * | 1996-12-31 | 2004-02-10 | Ajay Gupta | Method and pharmaceutical composition for replacing iron losses in dialysis patients |
US6372473B1 (en) * | 1997-05-28 | 2002-04-16 | Human Genome Sciences, Inc. | Tissue plasminogen activator-like protease |
JP2001509369A (ja) * | 1997-07-08 | 2001-07-24 | ノボファーム バイオテック インコーポレイテッド | ガン細胞を特異的に検出する4b5と命名される抗原結合フラグメント、フラグメントをコードするヌクレオチド、ならびにガンの予防および検出のためのそれらの使用 |
US20020122807A1 (en) * | 1998-07-07 | 2002-09-05 | Dan Michael D. | Antigen binding fragments, designated 4B5, that specifically detect cancer cells, nucleotides encoding the fragments, and use thereof for the prophylaxis and detection of cancers |
DE19735902A1 (de) * | 1997-08-19 | 1999-02-25 | Imtec Immundiagnostika Gmbh | Selektives Adsorbens für biologische Materialien |
WO1999009999A1 (fr) * | 1997-08-28 | 1999-03-04 | University Of Washington | Compositions de saccharide et methodes de traitement specifiques de la maladie d'alzheimer et d'autres amyloidoses |
ATE555780T1 (de) * | 1997-10-24 | 2012-05-15 | John P Blass | Nahrungsergänzungsmittel für metabolische hirnleistungsstörungen |
WO1999047072A1 (fr) * | 1998-03-18 | 1999-09-23 | Tyndale Plains-Hunter, Ltd. | Polyurethanes de polyether hydrophile contenant de l'acide carboxylique |
JP4037525B2 (ja) | 1998-03-25 | 2008-01-23 | 生化学工業株式会社 | 新規抗菌性ペプチド |
US7041287B2 (en) * | 1998-05-21 | 2006-05-09 | Trustees Of The University Of Pennsylvania | Compositions and methods for selective dissolution of nascent intravascular blood clots |
WO2000009562A1 (fr) | 1998-08-12 | 2000-02-24 | The New York Blood Center, Inc. | Nouveaux fragments scindes du fibrinogene |
JP2002525323A (ja) * | 1998-09-25 | 2002-08-13 | スノル・モレキュラー・コーポレーション | 医薬活性化合物及びその使用方法 |
IN190822B (fr) * | 1998-12-24 | 2003-08-23 | Council Scient Ind Res | |
US6242473B1 (en) * | 1999-01-08 | 2001-06-05 | Maxim Pharmaceuticals, Inc. | Treatment and prevention of reactive oxygen metabolite-mediated cellular damage |
US6161547A (en) * | 1999-01-15 | 2000-12-19 | Coaxia, Inc. | Medical device for flow augmentation in patients with occlusive cerebrovascular disease and methods of use |
WO2000059493A2 (fr) * | 1999-04-06 | 2000-10-12 | Kansas University Medical Center | Solutions de dialyse et methodes de dialyse ameliorees |
EP1179588B9 (fr) * | 1999-04-30 | 2006-07-19 | Akira Matsumoto | Carboxypeptidase b du cerveau humain |
WO2000068263A2 (fr) * | 1999-05-05 | 2000-11-16 | Neurochem, Inc. | Peptides stereoselectifs antifibrillogenese et peptidomimetiques correspondants |
AT500670A1 (de) * | 1999-05-19 | 2006-02-15 | Bio & Bio Licensing Sa | Arzneimittel zur lokalen anwendung |
CA2376693C (fr) * | 1999-06-16 | 2013-09-10 | Boston Biomedical Research Institute | Temoin immunologique de niveaux de .beta.-amyloide in vivo |
GB9917725D0 (en) * | 1999-07-28 | 1999-09-29 | Medical Res Council | Peptides |
AU6766800A (en) * | 1999-08-13 | 2001-03-13 | Trustees Of Columbia University In The City Of New York, The | Methods of inhibiting binding of beta-sheet fibril to rage and consequences thereof |
US20040013647A1 (en) * | 1999-09-03 | 2004-01-22 | Ramot At Tel-Aviv University Ltd. | Methods and compositions for treating a plaque-forming disease |
US20020052311A1 (en) * | 1999-09-03 | 2002-05-02 | Beka Solomon | Methods and compostions for the treatment and/or diagnosis of neurological diseases and disorders |
WO2001019836A1 (fr) * | 1999-09-14 | 2001-03-22 | Meiji Seika Kaisha, Ltd. | Derives d'acides phosphoniques presentant une activite inhibitrice de carboxypeptidase b |
US6399314B1 (en) * | 1999-12-29 | 2002-06-04 | American Cyanamid Company | Methods of detection of amyloidogenic proteins |
DE60116733T2 (de) | 2000-01-20 | 2006-11-02 | Regents Of The University Of Minnesota, Minneapolis | Peptide mit antibakterieller wirkung |
AU3173301A (en) * | 2000-02-11 | 2001-08-20 | European Molecular Biology Laboratory | Methods and compositions for treatment of alzheimer's disease by enhancing plasmin or plasmin-like activity |
JP5025871B2 (ja) * | 2000-02-21 | 2012-09-12 | エイチ.リュンドベック エイ/エス | アミロイドの新規なダウン−レギュレート方法 |
CA2400838C (fr) * | 2000-02-21 | 2013-04-23 | Pharmexa A/S | Nouvelle methode de regulation negative d'amyloide |
EP1130031A1 (fr) * | 2000-02-25 | 2001-09-05 | Universitair Medisch Centrum Utrecht | Procédé pour inhiber l'angiogenèse à l'aide des molécules qui augmentent la formation de la plasmine ou qui prolongent son activité |
WO2001070762A2 (fr) * | 2000-03-21 | 2001-09-27 | Research Foundation Of State University Of New York | Adsorption de polyampholytes a des surfaces chargees et analyses associees |
DE10017690A1 (de) * | 2000-04-08 | 2001-10-25 | Simmoteit Robert | Vorrichtung zum Stoffaustausch und Kultivierung von Zellen |
EP2264018B1 (fr) * | 2000-08-24 | 2015-02-11 | University of Pittsburgh - Of the Commonwealth System of Higher Education | Dérivés de thioflavine pour le diagnostic de la maladie d'Alzheimer |
US7270800B2 (en) * | 2000-08-24 | 2007-09-18 | University Of Pittsburgh | Thioflavin derivatives for use in antemortem diagnosis of Alzheimer's disease and in vivo imaging and prevention of amyloid deposition |
EP1186299A1 (fr) * | 2000-09-12 | 2002-03-13 | Universitair Medisch Centrum Utrecht | Diagnostic, prévention et/ou traitement d' athérosclérose, infections et perturbations du système immunitaire |
WO2002028441A2 (fr) * | 2000-10-04 | 2002-04-11 | California Institute Of Technology | Agents d'imagerie par resonance magnetique pour la detection et l'etiquetage in vivo de depots amyloides |
EP1219300B1 (fr) * | 2000-12-28 | 2006-12-06 | BIOMAY Produktions- und Handels- Aktiengesellschaft | Traitement des allergies |
US6808927B2 (en) * | 2001-04-04 | 2004-10-26 | American Diagnostica, Inc. | Method of preparation of stabilized thrombin-activatable fibrinolysis inhibitor (TAFI) and methods of use thereof |
JP4235544B2 (ja) | 2001-05-31 | 2009-03-11 | アドライフ インコーポレーティッド | 欠陥折畳み蛋白質センサー方法 |
US6960465B1 (en) * | 2001-06-27 | 2005-11-01 | Northwestern University | Increased cell resistance to toxic organic substances |
US6737401B2 (en) | 2001-06-28 | 2004-05-18 | Metronic Minimed, Inc. | Methods of evaluating protein formulation stability and surfactant-stabilized insulin formulations derived therefrom |
WO2003006893A2 (fr) * | 2001-07-09 | 2003-01-23 | Elan Pharmaceuticals, Inc. | Procedes inhibant la toxicite amyloide |
JP2003024080A (ja) * | 2001-07-19 | 2003-01-28 | Univ Tokyo | p53依存性アポトーシス誘導タンパク質、およびアポトーシス調節剤のスクリーニング方法 |
GB0202275D0 (en) | 2002-01-31 | 2002-03-20 | Hansa Medica Ab | Peptide |
EP1820806A1 (fr) * | 2006-02-16 | 2007-08-22 | Crossbeta Biosciences B.V. | Zones d'affinité |
CA2477569C (fr) | 2002-02-28 | 2013-09-24 | Microsens Biophage Limited | Liaison selective de formes pathologiques de proteines de prion au moyen de polymeres polyioniques |
EP1507543A4 (fr) * | 2002-05-09 | 2006-07-26 | Cambridgemed Inc | Composition pharmaceutique destinee au traitement de plaies et contenant du plasma ou du serum sanguins |
EP1380290A1 (fr) | 2002-07-09 | 2004-01-14 | Universitair Medisch Centrum Utrecht | La voie de la structure cross-béta et sa pertinence thérapeutique |
US20070003552A1 (en) * | 2002-07-09 | 2007-01-04 | Gebbink Martijn F B | Cross-beta structure comprising amyloid binding proteins and methods for detection of the cross-beta structure, for modulating cross-beta structures fibril formation and for modulating cross-beta structure-mediated toxicity and method for interfering with blood coagulation |
US20050142611A1 (en) * | 2002-09-30 | 2005-06-30 | Auburn University | Method of isolation and self-assembly of small protein particles from blood and other biological materials |
US7470667B2 (en) * | 2002-12-05 | 2008-12-30 | Medgenn (Hong Kong) Ltd | Methods of treating cancer using a modified endostatin protein |
EP1449536A1 (fr) | 2003-02-14 | 2004-08-25 | Prionics AG | Protéines prions comme agents thérapeutiques pour le traitement de maladies associées à AP-1 |
US7172875B2 (en) * | 2003-02-18 | 2007-02-06 | The Ohio State University Research Foundation | Identifying inhibitors of intracellular protein fibrillization |
ES2622522T3 (es) | 2003-08-26 | 2017-07-06 | The Regents Of The University Of Colorado, A Body Corporate | Inhibidores de la actividad proteasa de serina y su uso en métodos y composiciones para el tratamiento de infecciones bacterianas |
AU2004285928B2 (en) | 2003-10-24 | 2012-02-02 | Amgen, Inc. | Process for purifying proteins in a hydrophobic interaction chromatography flow-through fraction |
US20090156471A1 (en) | 2004-07-15 | 2009-06-18 | Ramot At Tel Aviv University Ltd. | Use of anti-amyloid agents for treating and typing pathogen infections |
JP2008531553A (ja) * | 2005-02-25 | 2008-08-14 | メディジーンズ カンパニー リミテッド | 血漿または血清を含むアベリノ角膜ジストロフィー治療用の医薬組成物 |
EP1704867A1 (fr) * | 2005-03-18 | 2006-09-27 | Crossbeta Biosciences B.V. | Des Structures cross-Beta sur des microorganismes |
US20090202980A1 (en) * | 2005-03-21 | 2009-08-13 | Crossbeta Biosciences B.V. | Cross-Beta Structure Comprising Amyloid Binding Proteins and Methods for Detection of the Cross-Beta Structure, for Modulating Cross-Beta Structures Fibril Formation and for Modulating Cross-Beta Structure-Mediated Toxicity and Method for Interfering With Blood Coagulation |
ATE554394T1 (de) * | 2005-07-13 | 2012-05-15 | Crossbeta Biosciences Bv | Cross-beta-struktur-bindende verbindungen |
US20070015133A1 (en) * | 2005-07-13 | 2007-01-18 | Umc Utrecht Holding B.V. | Method for detecting and/or removing protein and/or peptide comprising a cross-beta structure from an aqueous solution comprising a protein |
CA2615078A1 (fr) | 2005-07-13 | 2007-01-18 | Crossbeta Biosciences B.V. | Methodes de determination de l'effet d'un traitement sur la teneur d'une proteine a structure croisee-.beta. selection des traitements et leurs utilisations |
BRPI0613525A2 (pt) * | 2005-07-13 | 2011-05-31 | Crossbeta Biosciences Bv | métodos para produzir uma composição imunogênica, para melhorar a imunogenicidade de uma composição, para intensificar a imunogenicidade de uma composição de vacina, e para determinar a quantidade de estruturas beta-cruzadas em uma composição de vacina, usos de estruturas beta-cruzadas, e de uma composição imunogênica, vacina de subunidade, e, composição imunogênica |
US8114832B2 (en) | 2005-07-13 | 2012-02-14 | Crossbeta Biosciences B.V. | Method for detecting and/or removing a protein comprising a cross-beta structure from a pharmaceutical composition |
US20090136587A1 (en) | 2005-08-11 | 2009-05-28 | Medigenes Co., Ltd | Pharmaceutical composition for the treatment of nerve damage comprising blood plasma or serum |
US8543424B2 (en) * | 2005-12-30 | 2013-09-24 | Darryl Mark Hunsaker | Vehicle insurance status display system |
WO2007108675A1 (fr) | 2006-03-17 | 2007-09-27 | Crossbeta Biosciences B.V. | Procédés de liaison de structures bêta croisées avec des molécules chaperonnes |
PL2029173T3 (pl) * | 2006-06-26 | 2017-04-28 | Macrogenics, Inc. | Przeciwciała swoiste dla FC RIIB i sposoby ich zastosowania |
EP2058000A1 (fr) * | 2007-11-08 | 2009-05-13 | Crossbeta Biosciences B.V. | Compositions immunogènes capables d'activer des cellules T |
EP2058001A1 (fr) * | 2007-11-08 | 2009-05-13 | Crossbeta Biosciences B.V. | Amélioration de l'immunogénicité des antigènes |
-
2002
- 2002-07-09 EP EP02077797A patent/EP1380290A1/fr not_active Withdrawn
-
2003
- 2003-07-08 EP EP08153132A patent/EP1978362A3/fr not_active Withdrawn
- 2003-07-08 EP EP10185187A patent/EP2322154A3/fr not_active Withdrawn
- 2003-07-08 AU AU2003251233A patent/AU2003251233B2/en not_active Ceased
- 2003-07-08 DK DK03762927T patent/DK1536778T3/da active
- 2003-07-08 AT AT03762927T patent/ATE417605T1/de active
- 2003-07-08 EP EP11153594A patent/EP2341348A1/fr not_active Withdrawn
- 2003-07-08 NZ NZ537495A patent/NZ537495A/en not_active IP Right Cessation
- 2003-07-08 JP JP2004519368A patent/JP2005537254A/ja active Pending
- 2003-07-08 NZ NZ561168A patent/NZ561168A/en not_active IP Right Cessation
- 2003-07-08 DE DE60325381T patent/DE60325381D1/de not_active Expired - Lifetime
- 2003-07-08 EP EP03762927A patent/EP1536778B1/fr not_active Expired - Lifetime
- 2003-07-08 ES ES03762927T patent/ES2319982T3/es not_active Expired - Lifetime
- 2003-07-08 PT PT03762927T patent/PT1536778E/pt unknown
- 2003-07-08 CA CA002492010A patent/CA2492010A1/fr not_active Abandoned
- 2003-07-08 WO PCT/NL2003/000501 patent/WO2004004698A2/fr active Application Filing
-
2005
- 2005-01-04 ZA ZA200500062A patent/ZA200500062B/en unknown
- 2005-01-10 US US11/033,105 patent/US20060045853A1/en not_active Abandoned
-
2007
- 2007-10-31 US US11/982,161 patent/US8158585B2/en not_active Expired - Fee Related
-
2010
- 2010-01-29 AU AU2010200343A patent/AU2010200343A1/en not_active Abandoned
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2012
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Also Published As
Publication number | Publication date |
---|---|
PT1536778E (pt) | 2009-03-24 |
EP2322154A2 (fr) | 2011-05-18 |
AU2003251233B2 (en) | 2009-10-29 |
DE60325381D1 (de) | 2009-01-29 |
US20080241165A1 (en) | 2008-10-02 |
NZ537495A (en) | 2009-04-30 |
US20060045853A1 (en) | 2006-03-02 |
AU2003251233A1 (en) | 2004-01-23 |
EP2341348A1 (fr) | 2011-07-06 |
ATE417605T1 (de) | 2009-01-15 |
EP1978362A2 (fr) | 2008-10-08 |
EP1380290A1 (fr) | 2004-01-14 |
DK1536778T3 (da) | 2009-04-14 |
EP1978362A3 (fr) | 2009-02-11 |
WO2004004698A2 (fr) | 2004-01-15 |
CA2492010A1 (fr) | 2004-01-15 |
EP2322154A3 (fr) | 2011-10-05 |
US20120189615A1 (en) | 2012-07-26 |
EP1536778A2 (fr) | 2005-06-08 |
NZ561168A (en) | 2009-06-26 |
EP1536778B1 (fr) | 2008-12-17 |
US8158585B2 (en) | 2012-04-17 |
ES2319982T3 (es) | 2009-05-18 |
WO2004004698A3 (fr) | 2004-06-10 |
AU2010200343A1 (en) | 2010-02-18 |
JP2005537254A (ja) | 2005-12-08 |
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