AU2006204705C1 - ELISA assays using prion-specific peptide reagents - Google Patents
ELISA assays using prion-specific peptide reagents Download PDFInfo
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- AU2006204705C1 AU2006204705C1 AU2006204705A AU2006204705A AU2006204705C1 AU 2006204705 C1 AU2006204705 C1 AU 2006204705C1 AU 2006204705 A AU2006204705 A AU 2006204705A AU 2006204705 A AU2006204705 A AU 2006204705A AU 2006204705 C1 AU2006204705 C1 AU 2006204705C1
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- prion
- peptide
- pathogenic
- seq
- protein
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- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
- G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
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- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
- G01N2800/2814—Dementia; Cognitive disorders
- G01N2800/2828—Prion diseases
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- Peptides Or Proteins (AREA)
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| WO2006076683A2 (en) * | 2005-01-13 | 2006-07-20 | Novartis Vaccines And Diagnostics Inc. | Isolation and detection of pathogenic prions |
| BRPI0615618A2 (pt) | 2005-09-09 | 2011-05-24 | Novartis Ag | reagentes peptóides especìficos para prìon |
| JP2010523977A (ja) * | 2007-04-04 | 2010-07-15 | ノバルティス アーゲー | プリオンアッセイ |
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| WO2010003227A1 (en) * | 2008-07-08 | 2010-01-14 | Amorfix Life Sciences Ltd. | Detection of protein aggregates |
| WO2011057029A1 (en) * | 2009-11-04 | 2011-05-12 | Novartis Ag | Positively charged species as binding reagents in the separation of protein aggregates from monomers |
| GB201015569D0 (en) * | 2010-09-16 | 2010-10-27 | Medical Res Council | Blood assay for prions |
| WO2012099576A1 (en) * | 2011-01-18 | 2012-07-26 | Baxter International Inc. | Measurement of anti-amyloid antibodies in human blood |
| DE102011057019A1 (de) * | 2011-12-23 | 2013-06-27 | Forschungszentrum Jülich GmbH | Standard zur Quantifizierung von pathogenen Aggregaten aus körpereigenen Proteinen |
| CN102879577B (zh) * | 2012-11-01 | 2014-04-09 | 山东龙美生物医学科技有限公司 | 一种检测朊病毒的试剂盒及其制备方法 |
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| WO2024254043A2 (en) * | 2023-06-07 | 2024-12-12 | The Regents Of The University Of California | Nmda-r activating peptides in inflammation and neuronal differentiation |
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| WO2000043791A2 (en) * | 1999-01-25 | 2000-07-27 | Minerva Biotechnologies Corporation | Rapid and sensitive detection of aberrant protein aggregation in neurodegenerative diseases |
| WO2003085086A2 (en) * | 2002-04-09 | 2003-10-16 | The Scripps Research Institute | Motif-grafted hybrid polypeptides and uses thereof |
| WO2004029072A2 (en) * | 2002-09-27 | 2004-04-08 | Caprion Pharmaceuticals Inc. | PrPsc -INTERACTING MOLECULES AND USES THEREOF |
| WO2005016127A2 (en) * | 2003-08-13 | 2005-02-24 | Chiron Corporation | Prion-specific peptide reagents |
Family Cites Families (94)
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|---|---|---|---|---|
| US658619A (en) * | 1900-02-02 | 1900-09-25 | George L Clark | Tire-supporting frame. |
| US4006117A (en) * | 1973-01-24 | 1977-02-01 | Hooker Chemicals & Plastics Corporation | Amine phosphite antioxidants |
| US4244721A (en) * | 1979-01-31 | 1981-01-13 | Pedro Buarque De Macedo | Method of making composite borosilicate glass articles |
| US4666160A (en) * | 1980-07-02 | 1987-05-19 | Hamilton Clarence Q | Apparatus for playing |
| US4569526A (en) * | 1980-07-02 | 1986-02-11 | Gamma-Delta Games, Inc. | Vectorial and Mancala-like games, apparatus and methods |
| US4507230A (en) * | 1982-05-12 | 1985-03-26 | Research Corporation | Peptide synthesis reagents and method of use |
| US4952496A (en) * | 1984-03-30 | 1990-08-28 | Associated Universities, Inc. | Cloning and expression of the gene for bacteriophage T7 RNA polymerase |
| DE3500180A1 (de) * | 1985-01-04 | 1986-07-10 | Ernst Prof. Dr. 7400 Tübingen Bayer | Pfropfcopolymerisate aus vernetzten polymeren und polyoxyethylen, verfahren zu ihrer herstellung und ihre verwendung |
| US4695053A (en) * | 1986-03-07 | 1987-09-22 | Bally Manufacturing Corporation | Gaming device having player selectable winning combinations |
| US5292814A (en) * | 1987-04-29 | 1994-03-08 | Ernst Bayer | Process for the preparation of monodispersed polymer beads |
| CA2047244C (en) * | 1989-02-24 | 2002-09-17 | Zanetti Maurizio | Genetically engineered immunoglobulins |
| US5306812A (en) * | 1989-09-08 | 1994-04-26 | The Regents Of The University Of California | Immunoglobulin-binding polypeptides |
| US5231167A (en) * | 1989-09-08 | 1993-07-27 | The Regents Of The University Of California | Immunoglobulin-binding polypeptides |
| US6075121A (en) * | 1990-05-15 | 2000-06-13 | Chiron Corporation | Modified peptide and peptide libraries with protease resistance, derivatives thereof and methods of producing and screening such |
| EP0592423B1 (en) * | 1990-08-06 | 2000-11-15 | Chiron Corporation | Methods for the identification of cytokine convertase inhibitors |
| CA2099574A1 (en) * | 1991-01-04 | 1992-07-05 | Noubar B. Afeyan | Sulfonamide bonded hydrophilic coatings |
| US5665539A (en) * | 1991-07-12 | 1997-09-09 | The Regents Of The University Of California | Immuno-polymerase chain reaction system for antigen detection |
| AU675053B2 (en) * | 1991-12-03 | 1997-01-23 | Proteus Molecular Design Limited | Fragments of prion proteins |
| US5424413A (en) * | 1992-01-22 | 1995-06-13 | Gen-Probe Incorporated | Branched nucleic acid probes |
| US5877278A (en) * | 1992-09-24 | 1999-03-02 | Chiron Corporation | Synthesis of N-substituted oligomers |
| US5652138A (en) * | 1992-09-30 | 1997-07-29 | The Scripps Research Institute | Human neutralizing monoclonal antibodies to human immunodeficiency virus |
| US5524888A (en) * | 1994-04-28 | 1996-06-11 | Bally Gaming International, Inc. | Gaming machine having electronic circuit for generating game results with non-uniform probabilities |
| US5565186A (en) * | 1994-05-13 | 1996-10-15 | The Regents Of The University Of California | Method of detecting prions in a sample and transgenic animal used for same |
| US5792901A (en) * | 1994-05-13 | 1998-08-11 | The Regents Of The University Of California | Detecting prions in a sample and prion preparation and transgenic animal used for same |
| US5908969A (en) * | 1994-05-13 | 1999-06-01 | The Regents Of The University Of California | Method of detecting prions in a sample and transgenic animal used for same |
| US6376170B1 (en) * | 1994-10-03 | 2002-04-23 | The Scripps Research Institute | Ligand capture-directed selection of antibody |
| US5639581A (en) * | 1994-10-24 | 1997-06-17 | Fuji Xerox Co., Ltd. | Charge transporting polymer, process for producing the same, and organic electronic device containing the same |
| EP0852011B1 (en) * | 1995-09-14 | 2004-03-31 | The Regents of the University of California | ANTIBODIES SPECIFIC FOR NATIVE PrP?Sc |
| US5750361A (en) * | 1995-11-02 | 1998-05-12 | The Regents Of The University Of California | Formation and use of prion protein (PRP) complexes |
| US5985557A (en) * | 1996-01-24 | 1999-11-16 | Third Wave Technologies, Inc. | Invasive cleavage of nucleic acids |
| US6090606A (en) * | 1996-01-24 | 2000-07-18 | Third Wave Technologies, Inc. | Cleavage agents |
| US5713793A (en) * | 1996-04-05 | 1998-02-03 | Oris, L.L.C. | Sporting event options market trading game |
| DE69724619T2 (de) * | 1996-05-14 | 2004-07-01 | Winnacker, Ernst-Ludwig, Prof. | Chaperone, die prionproteine binden und zwischen den isoformen prpc und prpsc unterscheiden können |
| US5743525A (en) * | 1996-07-01 | 1998-04-28 | Haddad; George N. | Sporting event wagering system |
| JP4320054B2 (ja) * | 1996-08-13 | 2009-08-26 | ノバルティス バクシンズ アンド ダイアグノスティックス,インコーポレーテッド | ポリヌクレオチド送達のための組成物および方法 |
| US6043347A (en) * | 1996-10-10 | 2000-03-28 | Probe International Inc. | Compositions and methods for treating viral infections |
| EP1015013A4 (en) * | 1997-01-10 | 2002-07-24 | Massachusetts Inst Technology | TREATMENTS RELATING TO NEUROTOXICITY IN ALZHEIMER'S DISEASE CAUSED BY beta-AMYLOID PEPTIDES |
| US5891641A (en) * | 1997-02-21 | 1999-04-06 | The Regents Of The University Of California | Assay for disease related conformation of a protein |
| EP0861900A1 (en) * | 1997-02-21 | 1998-09-02 | Erziehungsdirektion Of The Canton Zurich | Immunological detection of prions |
| US6617119B2 (en) * | 1997-02-21 | 2003-09-09 | The Regents Of The University Of California | Assay for specific strains of multiple disease related conformations of a protein |
| US20010001061A1 (en) * | 1997-02-21 | 2001-05-10 | Prusiner Stanley B. | Assay for disease related conformation of a protein |
| US5888136A (en) * | 1997-03-13 | 1999-03-30 | Herbert; Richard A. | Wagering system and method of wagering |
| US7160189B2 (en) * | 1997-04-03 | 2007-01-09 | Walker Jay S | Systems and methods for determining an outcome of a game on a gaming device based on a factor other than a random number |
| US6010404A (en) * | 1997-04-03 | 2000-01-04 | Walker Asset Management Limited Partnership | Method and apparatus for using a player input code to affect a gambling outcome |
| US7005295B1 (en) * | 1997-04-16 | 2006-02-28 | Wyeth | β-amyloid peptide-binding proteins and polynucleotides encoding the same |
| WO1998049187A1 (en) * | 1997-04-28 | 1998-11-05 | Chiron Corporation | Apparatus for synthesis of oligomers, especially peptoids, with reagent recycling |
| US6227972B1 (en) * | 1997-07-01 | 2001-05-08 | Walker Digital, Llc | Method and apparatus for expiration of prepaid slot machine plays |
| EP1015888B1 (de) * | 1997-09-19 | 2002-08-28 | Evotec OAI AG | Verfahren zur messung der assoziation von teilstrukturen pathologischer proteinablagerungen |
| KR100608542B1 (ko) * | 1997-11-19 | 2006-08-09 | 로버트 에이. 사르노 | 컴퓨터 통신망에서 복권 게임을 제공하는 시스템 및 그 방법 |
| US6214565B1 (en) * | 1998-10-09 | 2001-04-10 | The Regents Of The University Of California | Assay for disease related conformation of a protein and isolating same |
| DE69909442T2 (de) * | 1998-02-20 | 2004-04-22 | The Regents Of The University Of California, Oakland | Assay für spezifische stämme von mit mehreren krankheiten zusammenhängenden proteinkonformationen |
| CA2369172A1 (en) * | 1998-04-14 | 1999-10-21 | Sugen, Inc. | Ste20-related protein kinases |
| US6211149B1 (en) * | 1998-08-03 | 2001-04-03 | The United States Of America As Represented By The Department Of Health And Human Services | Inhibitors of formation of protease resistant prion protein |
| US6358150B1 (en) * | 1998-10-29 | 2002-03-19 | Racetech Llc | Methods and apparatus for parimutuel historical gaming |
| GB2348203B (en) * | 1998-11-04 | 2002-06-19 | Imp College Innovations Ltd | Solube beta-forms of prion proteins, methods of preparation and use |
| US6551843B1 (en) * | 1999-01-29 | 2003-04-22 | Immunivest Corporation | Methods for enhancing binding interactions between members of specific binding pairs |
| US6709330B1 (en) * | 1999-08-20 | 2004-03-23 | Ameritrade Holding Corporation | Stock simulation engine for an options trading game |
| US6394899B1 (en) * | 1999-10-29 | 2002-05-28 | Stephen Tobin Walker | Method of playing a knowledge based wagering game |
| FR2801106B1 (fr) * | 1999-11-12 | 2007-10-05 | Commissariat Energie Atomique | Procede de diagnostic d'une esst provoquee par une souche d'atnc dans un echantillon biologique et son utilisation dans le diagnostic differentiel des differentes souches d'atnc |
| US6235483B1 (en) * | 2000-01-31 | 2001-05-22 | Agilent Technologies, Inc. | Methods and kits for indirect labeling of nucleic acids |
| KR20020081330A (ko) * | 2000-02-16 | 2002-10-26 | 노오쓰웨스턴 유니버시티 | 폴리펩토이드 폐 계면활성제 |
| JP2004513409A (ja) * | 2000-05-01 | 2004-04-30 | シーエフピーエイチ, エル.エル.シー. | イベント結果についてのリアルタイムの双方向賭博 |
| US6511809B2 (en) * | 2000-06-13 | 2003-01-28 | E. I. Du Pont De Nemours And Company | Method for the detection of an analyte by means of a nucleic acid reporter |
| AU6887101A (en) * | 2000-06-20 | 2002-01-02 | Caprion Pharmaceuticals, Inc. | Copolymers and methods of treating prion-related diseases |
| CN1176407C (zh) * | 2000-06-22 | 2004-11-17 | 京瓷株式会社 | 彩色图像形成装置及其方法 |
| US6537548B1 (en) * | 2000-07-27 | 2003-03-25 | The Regents Of The University Of California | Antibodies specific for ungulate PrP |
| US20030092613A1 (en) * | 2000-08-14 | 2003-05-15 | Lee Daniel H. S. | Alpha7 nicotinic receptor peptides as ligands for beta amyloid peptides |
| US20020087447A1 (en) * | 2000-09-19 | 2002-07-04 | Gazebo Inc. | System and method for managing and executing event based investments |
| US6721761B2 (en) * | 2000-12-20 | 2004-04-13 | American Management Systems, Inc. | System for assigning digital identifiers to telephone numbers and IP numbers |
| US20020137114A1 (en) * | 2001-01-19 | 2002-09-26 | Dirk Voelkel | Method of detecting PrP protein and kits therefor |
| US6527270B2 (en) * | 2001-02-13 | 2003-03-04 | Casino Advisory Services, Inc. | Method of effecting multiple wagers on a sports or other event |
| US20020115488A1 (en) * | 2001-02-22 | 2002-08-22 | Nicholas Berry | System and method for conducting an online competition |
| US20050026165A1 (en) * | 2001-05-31 | 2005-02-03 | Cindy Orser | Detection of conformationally altered proteins and prions |
| WO2002097444A2 (en) * | 2001-05-31 | 2002-12-05 | Arete Associates | Misfolded protein sensor method |
| US6869360B2 (en) * | 2001-09-20 | 2005-03-22 | Konami Gaming, Inc. | Gaming apparatus and method including a multiplier feature and bonus features |
| EP1572894B1 (en) * | 2001-11-21 | 2016-04-13 | New York University | Synthetic immunogenic but non-deposit-forming polypeptides and peptides homologous to amyloid beta, prion protein, amylin, alpha synuclein, or polyglutamine repeats for induction of an immune response thereto |
| US7040982B1 (en) * | 2001-11-23 | 2006-05-09 | Igt | Financial trading game |
| US20040052928A1 (en) * | 2002-09-06 | 2004-03-18 | Ehud Gazit | Peptides and methods using same for diagnosing and treating amyloid-associated diseases |
| ES2564293T5 (es) * | 2002-02-28 | 2019-04-04 | Microsens Biophage Ltd | Enlazamiento de formas patológicas de proteínas priónicas |
| US20050119962A1 (en) * | 2002-07-03 | 2005-06-02 | Bowen Christopher K. | Method and system for securitizing contracts valued on an index |
| DE10230141B4 (de) * | 2002-07-04 | 2004-07-15 | Priontype Gmbh | Verfahren und Kit zur Anreicherung und zum Nachweis von veränderten Prion-Proteinen (PrPSc) |
| EP1382971A1 (en) * | 2002-07-17 | 2004-01-21 | Pepscan Systems B.V. | Detection of prion disease |
| WO2004077368A2 (en) * | 2003-02-21 | 2004-09-10 | Walker, Digital, Llc Et Al. | Method and apparatus for setting game parameters |
| US7962400B2 (en) * | 2003-04-02 | 2011-06-14 | Cfph, Llc | System and method for wagering based on the movement of financial markets |
| DK1615992T3 (da) * | 2003-04-04 | 2013-12-09 | Pathogen Removal & Diagnostic Technologies Inc | Prionproteinbindende materialer og fremgangsmåder til anvendelse |
| WO2004092197A2 (en) * | 2003-04-07 | 2004-10-28 | The Regents Of The University Of California | Amyloid-specific peptides and uses thereof |
| US20060035242A1 (en) * | 2004-08-13 | 2006-02-16 | Michelitsch Melissa D | Prion-specific peptide reagents |
| US7311600B2 (en) * | 2003-08-22 | 2007-12-25 | Gameline, Llc | Game based upon fluctuations of an objective environment |
| US7614948B2 (en) * | 2003-09-15 | 2009-11-10 | Igt | Multi-player bingo with slept awards reverting to progressive jackpot pool |
| KR100505713B1 (ko) * | 2003-10-22 | 2005-08-03 | 삼성전자주식회사 | 쉘로우 트렌치 소자 분리막 및 쉘로우 트렌치 소자분리막의 형성 방법 |
| US20060057671A1 (en) * | 2004-09-10 | 2006-03-16 | Orser Cindy S | Immobilized probes and methods of detecting conformationally altered prion proteins |
| US7482172B2 (en) * | 2005-09-19 | 2009-01-27 | Ortho-Clinical Diagnostics, Inc. | Peptides for discrimination of prions |
| US20060105839A1 (en) * | 2004-11-15 | 2006-05-18 | Delta Rangers, Inc. | Casino game based on financial market activity |
| EP1848830A4 (en) * | 2005-01-13 | 2009-05-06 | Novartis Vaccines & Diagnostic | Osplation of pathogenic prions |
-
2006
- 2006-01-13 US US11/795,163 patent/US20090130774A1/en not_active Abandoned
- 2006-01-13 AU AU2006204705A patent/AU2006204705C1/en not_active Ceased
- 2006-01-13 EP EP06718499A patent/EP1848831A4/en not_active Withdrawn
- 2006-01-13 BR BRPI0606529-5A patent/BRPI0606529A2/pt not_active IP Right Cessation
- 2006-01-13 WO PCT/US2006/001437 patent/WO2006076687A2/en not_active Ceased
- 2006-01-13 NZ NZ587255A patent/NZ587255A/en not_active IP Right Cessation
- 2006-01-13 MX MX2007008497A patent/MX2007008497A/es active IP Right Grant
- 2006-01-13 CN CN2006800062251A patent/CN101166976B/zh not_active Expired - Fee Related
- 2006-01-13 NZ NZ560535A patent/NZ560535A/en not_active IP Right Cessation
- 2006-01-13 JP JP2007551450A patent/JP5162250B2/ja not_active Expired - Fee Related
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2009
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-
2012
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Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2000043791A2 (en) * | 1999-01-25 | 2000-07-27 | Minerva Biotechnologies Corporation | Rapid and sensitive detection of aberrant protein aggregation in neurodegenerative diseases |
| WO2003085086A2 (en) * | 2002-04-09 | 2003-10-16 | The Scripps Research Institute | Motif-grafted hybrid polypeptides and uses thereof |
| WO2004029072A2 (en) * | 2002-09-27 | 2004-04-08 | Caprion Pharmaceuticals Inc. | PrPsc -INTERACTING MOLECULES AND USES THEREOF |
| WO2005016127A2 (en) * | 2003-08-13 | 2005-02-24 | Chiron Corporation | Prion-specific peptide reagents |
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| JP2009115815A (ja) | 2009-05-28 |
| CA2594840A1 (en) | 2006-07-20 |
| US20090130774A1 (en) | 2009-05-21 |
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| JP2012181210A (ja) | 2012-09-20 |
| MX2007008497A (es) | 2007-09-14 |
| CN101166976A (zh) | 2008-04-23 |
| WO2006076687A3 (en) | 2007-12-13 |
| WO2006076687A2 (en) | 2006-07-20 |
| EP1848831A4 (en) | 2008-11-05 |
| BRPI0606529A2 (pt) | 2009-06-30 |
| AU2006204705B2 (en) | 2011-12-01 |
| NZ587255A (en) | 2012-03-30 |
| CN101166976B (zh) | 2013-06-12 |
| JP5162250B2 (ja) | 2013-03-13 |
| EP1848831A2 (en) | 2007-10-31 |
| NZ560535A (en) | 2011-01-28 |
| AU2006204705A1 (en) | 2006-07-20 |
| HK1118336A1 (en) | 2009-02-06 |
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