AU2004292226B2 - Proteome epitope tags and methods of use thereof in protein modification analysis - Google Patents
Proteome epitope tags and methods of use thereof in protein modification analysis Download PDFInfo
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- AU2004292226B2 AU2004292226B2 AU2004292226A AU2004292226A AU2004292226B2 AU 2004292226 B2 AU2004292226 B2 AU 2004292226B2 AU 2004292226 A AU2004292226 A AU 2004292226A AU 2004292226 A AU2004292226 A AU 2004292226A AU 2004292226 B2 AU2004292226 B2 AU 2004292226B2
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Classifications
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/26—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase
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- B—PERFORMING OPERATIONS; TRANSPORTING
- B82—NANOTECHNOLOGY
- B82Y—SPECIFIC USES OR APPLICATIONS OF NANOSTRUCTURES; MEASUREMENT OR ANALYSIS OF NANOSTRUCTURES; MANUFACTURE OR TREATMENT OF NANOSTRUCTURES
- B82Y10/00—Nanotechnology for information processing, storage or transmission, e.g. quantum computing or single electron logic
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/48—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving transferase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/48—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving transferase
- C12Q1/485—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving transferase involving kinase
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- G—PHYSICS
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- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- 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
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
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- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
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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
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6842—Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
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- Cell Biology (AREA)
- Mathematical Physics (AREA)
- Theoretical Computer Science (AREA)
- Medical Informatics (AREA)
- Pharmacology & Pharmacy (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Priority Applications (1)
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| AU2008227063A AU2008227063A1 (en) | 2003-11-13 | 2008-09-25 | Proteome epitome tags and methods of use thereof in protein modification analysis |
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| US10/712,425 US7460960B2 (en) | 2002-05-10 | 2003-11-13 | Proteome epitope tags and methods of use thereof in protein modification analysis |
| US10/712,425 | 2003-11-13 | ||
| PCT/US2004/038283 WO2005050223A2 (en) | 2003-11-13 | 2004-11-15 | Proteome epitope tags and methods of use thereof in protein modification analysis |
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| AU2008227063A Division AU2008227063A1 (en) | 2003-11-13 | 2008-09-25 | Proteome epitome tags and methods of use thereof in protein modification analysis |
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| AU2004292226A1 AU2004292226A1 (en) | 2005-06-02 |
| AU2004292226B2 true AU2004292226B2 (en) | 2008-06-26 |
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| AU2008227063A Abandoned AU2008227063A1 (en) | 2003-11-13 | 2008-09-25 | Proteome epitome tags and methods of use thereof in protein modification analysis |
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| AU2008227063A Abandoned AU2008227063A1 (en) | 2003-11-13 | 2008-09-25 | Proteome epitome tags and methods of use thereof in protein modification analysis |
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| US (2) | US7460960B2 (enExample) |
| EP (1) | EP1683065A2 (enExample) |
| JP (1) | JP2007511837A (enExample) |
| AU (2) | AU2004292226B2 (enExample) |
| CA (1) | CA2545899A1 (enExample) |
| WO (1) | WO2005050223A2 (enExample) |
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| US20030113744A1 (en) * | 2001-05-11 | 2003-06-19 | O' Toole Margot M. | Methods for diagnosing and treating ischemia and reperfusion injury and compositions thereof |
| US7695926B2 (en) | 2001-07-10 | 2010-04-13 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and compositions for detecting receptor-ligand interactions in single cells |
| US7393656B2 (en) * | 2001-07-10 | 2008-07-01 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and compositions for risk stratification |
| EP1415156B1 (en) | 2001-07-10 | 2009-09-02 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and compositions for detecting the activation state of multiple proteins in single cells |
| US7381535B2 (en) | 2002-07-10 | 2008-06-03 | The Board Of Trustees Of The Leland Stanford Junior | Methods and compositions for detecting receptor-ligand interactions in single cells |
| FI118061B (fi) * | 2001-09-24 | 2007-06-15 | Beanor Oy | Menetelmä ja bioanturi analyysiä varten |
| FI115166B (fi) * | 2001-12-31 | 2005-03-15 | Biofons Oy | Diagnostisia menetelmiä |
| WO2004039830A2 (en) | 2002-05-07 | 2004-05-13 | Regents Of The University Of California | Bioactivation of particles |
| US7618788B2 (en) * | 2002-05-10 | 2009-11-17 | Millipore Corporation | Proteome epitope tags and methods of use thereof in protein modification analysis |
| US7460960B2 (en) | 2002-05-10 | 2008-12-02 | Epitome Biosystems, Inc. | Proteome epitope tags and methods of use thereof in protein modification analysis |
| US7632686B2 (en) | 2002-10-03 | 2009-12-15 | Anderson Forschung Group | High sensitivity quantitation of peptides by mass spectrometry |
| US7846748B2 (en) * | 2002-12-02 | 2010-12-07 | The University Of North Carolina At Chapel Hill | Methods of quantitation and identification of peptides and proteins |
| WO2005032453A2 (en) * | 2003-04-28 | 2005-04-14 | Sequoia Pharmaceuticals, Inc. | Antiviral agents for the treatment, control and prevention of infections by coronaviruses |
| US7425700B2 (en) | 2003-05-22 | 2008-09-16 | Stults John T | Systems and methods for discovery and analysis of markers |
| WO2005053649A1 (en) * | 2003-11-05 | 2005-06-16 | The Government Of The United States Of America As Represented By The Secretary Of Health And Human Services | Biofunctionalized quantum dots for biological imaging |
| US7780873B2 (en) * | 2004-02-23 | 2010-08-24 | Texas A&M University System | Bioactive complexes compositions and methods of use thereof |
| US20060154318A1 (en) * | 2004-06-09 | 2006-07-13 | Anderson Norman L | Stable isotope labeled polypeptide standards for protein quantitation |
| WO2006093516A2 (en) | 2004-06-22 | 2006-09-08 | The Regents Of The University Of California | Peptide-coated nanoparticles with graded shell compositions |
| US20060240227A1 (en) * | 2004-09-23 | 2006-10-26 | Zhijun Zhang | Nanocrystal coated surfaces |
| EP1799626B1 (en) * | 2004-10-12 | 2012-01-18 | Schott AG | Multiplexed protein adsorption assay |
| US20070009923A1 (en) * | 2005-01-24 | 2007-01-11 | Massachusetts Institute Of Technology | Use of bayesian networks for modeling cell signaling systems |
| JP2006248978A (ja) | 2005-03-10 | 2006-09-21 | Mebiopharm Co Ltd | 新規なリポソーム製剤 |
| US20060223194A1 (en) * | 2005-04-01 | 2006-10-05 | Viorica Lopez-Avila | Methods of screening for post-translationally modified proteins |
| US20060223130A1 (en) * | 2005-04-04 | 2006-10-05 | Dan-Hui Yang | Detection of post-translationally modified analytes |
| US9284274B2 (en) | 2005-12-07 | 2016-03-15 | Ramot At Tel-Aviv University Ltd. | Chemical derivatives of jasmonate, pharmaceutical compositions and methods of use thereof |
| CA2632653C (en) * | 2005-12-07 | 2014-11-04 | Ramot At Tel Aviv University Ltd. | Chemical derivatives of jasmonate, pharmaceutical compositions and methods of use thereof in the treatment of cancer |
| US7855057B2 (en) * | 2006-03-23 | 2010-12-21 | Millipore Corporation | Protein splice variant/isoform discrimination and quantitative measurements thereof |
| US20100331200A1 (en) * | 2006-03-31 | 2010-12-30 | Gordon Neal F | Post translational modification pattern analysis |
| GB2474146B (en) * | 2008-04-29 | 2013-04-10 | Nodality Inc | Methods of determining the health status of an individual |
| US20090291458A1 (en) * | 2008-05-22 | 2009-11-26 | Nodality, Inc. | Method for Determining the Status of an Individual |
| US8399206B2 (en) | 2008-07-10 | 2013-03-19 | Nodality, Inc. | Methods for diagnosis, prognosis and methods of treatment |
| WO2010006291A1 (en) | 2008-07-10 | 2010-01-14 | Nodality, Inc. | Methods for diagnosis, prognosis and treatment |
| WO2010045651A1 (en) * | 2008-10-17 | 2010-04-22 | Nodality, Inc. | Methods for analyzing drug response |
| US9284252B2 (en) | 2009-06-09 | 2016-03-15 | Sepal Pharma Ltd. | Use of jasmonate ester derivatives for treating benign hyperproliferative skin disorders |
| KR101061017B1 (ko) * | 2009-10-23 | 2011-08-31 | (주) 수파드엘릭사 | 암세포의 성장 및/또는 전이 억제용 약학 조성물 |
| KR101341640B1 (ko) * | 2010-02-05 | 2013-12-16 | 한국전자통신연구원 | 단백질 미세 구조 분석 방법 및 단백질 미세 구조 분석용 어레이 |
| US9597379B1 (en) | 2010-02-09 | 2017-03-21 | David Gordon Bermudes | Protease inhibitor combination with therapeutic proteins including antibodies |
| US8524220B1 (en) | 2010-02-09 | 2013-09-03 | David Gordon Bermudes | Protease inhibitor: protease sensitivity expression system composition and methods improving the therapeutic activity and specificity of proteins delivered by bacteria |
| US8771669B1 (en) | 2010-02-09 | 2014-07-08 | David Gordon Bermudes | Immunization and/or treatment of parasites and infectious agents by live bacteria |
| WO2012026309A1 (ja) * | 2010-08-23 | 2012-03-01 | 公立大学法人横浜市立大学 | 抗ｐａｄ４抗体医薬の創成 |
| US9068006B2 (en) | 2010-08-25 | 2015-06-30 | President And Fellows Of Harvard College | Glycated CD59 peptides, their preparation, and uses thereof |
| US9383367B1 (en) | 2010-12-07 | 2016-07-05 | Chunli Liu | Methods of detecting conjugation site-specific and hidden epitope/antigen |
| US9417248B2 (en) | 2011-02-10 | 2016-08-16 | President And Fellows Of Harvard College | Surrogates of post-translationally modified proteins and uses thereof |
| US9023599B2 (en) * | 2011-09-25 | 2015-05-05 | Chang Gung Medical Foundation, Linkou Branch | Method of detecting the presence of pneumococcal neuraminidases in Streptococcus pneumoniae-infected samples |
| US9352020B2 (en) | 2013-03-15 | 2016-05-31 | Mead Johnson Nutrition Company | Reducing proinflammatory response |
| US8889633B2 (en) | 2013-03-15 | 2014-11-18 | Mead Johnson Nutrition Company | Nutritional compositions containing a peptide component with anti-inflammatory properties and uses thereof |
| US9138455B2 (en) | 2013-03-15 | 2015-09-22 | Mead Johnson Nutrition Company | Activating adiponectin by casein hydrolysate |
| US9289461B2 (en) | 2013-03-15 | 2016-03-22 | Mead Johnson Nutrition Company | Reducing the risk of autoimmune disease |
| US9975922B2 (en) | 2013-10-21 | 2018-05-22 | The Research Foundation For The State University Of New York | Peptide inhibitor of HIV reverse transcription |
| CN103698509B (zh) * | 2014-01-08 | 2017-02-08 | 青岛科技大学 | 基于纳米多孔金片电极的电化学免疫传感器对巯基乙酸的检测 |
| US9737592B1 (en) | 2014-02-14 | 2017-08-22 | David Gordon Bermudes | Topical and orally administered protease inhibitors and bacterial vectors for the treatment of disorders and methods of treatment |
| KR101750407B1 (ko) | 2014-11-10 | 2017-06-27 | 한양대학교 산학협력단 | 프로틴 카이네이즈 a 기질 인산화펩타이드에 결합하는 알엔에이 앱타머 |
| WO2016138381A1 (en) * | 2015-02-27 | 2016-09-01 | Regents Of The University Of Minnesota | Detection assays and methods |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| JP6548981B2 (ja) * | 2015-07-14 | 2019-07-24 | 地方独立行政法人東京都立産業技術研究センター | 表面プラズモン共鳴測定装置及びそのチップ |
| US11180535B1 (en) | 2016-12-07 | 2021-11-23 | David Gordon Bermudes | Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria |
| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| US10520514B2 (en) * | 2017-02-01 | 2019-12-31 | Korea Institute Of Science And Technology | Method for monitoring post-translational modification of protein |
| JP7303182B2 (ja) | 2017-04-21 | 2023-07-04 | メリタス エルエルシー | 糖尿病関連用途のための方法及び抗体 |
| EP3404567A1 (en) * | 2017-05-19 | 2018-11-21 | Fujitsu Limited | A system and a method for discovery of predicted site-specific protein phosphorylation candidates |
| CN111201239A (zh) * | 2017-08-04 | 2020-05-26 | 艾博抗公开有限公司 | 用于开发特异于表位翻译后修饰状态的抗体的方法和组合物 |
| CN108776231B (zh) * | 2018-09-06 | 2020-12-29 | 长沙文瀚生物技术有限责任公司 | 一种人尿白蛋白胶乳增强二抗竞争免疫比浊检测试剂盒及其制作和使用方法 |
| EP3640864A1 (en) * | 2018-10-18 | 2020-04-22 | Fujitsu Limited | A computer-implemented method and apparatus for inferring a property of a biomedical entity |
| CN110209770B (zh) * | 2019-06-03 | 2022-04-15 | 北京邮电大学 | 一种基于策略价值网络和树搜索增强的命名实体识别方法 |
| JP7441303B2 (ja) | 2019-08-05 | 2024-02-29 | シアー， インコーポレイテッド | サンプル調製、データ生成、タンパク質コロナ分析のためのシステムおよび方法 |
| US12285437B2 (en) | 2019-10-30 | 2025-04-29 | The Research Foundation For The State University Of New York | Reversing the undesirable pH-profile of doxorubicin via activation of a disubstituted maleamic acid prodrug at tumor acidity |
| CN113899902B (zh) * | 2020-06-22 | 2024-10-29 | 上海科技大学 | 一种酪氨酸磷酸酶底物鉴定方法 |
| CN112305041B (zh) * | 2020-09-15 | 2022-05-27 | 东莞东阳光医疗智能器件研发有限公司 | 多重定量电化学免疫传感器及其构建方法 |
| WO2022066981A1 (en) * | 2020-09-24 | 2022-03-31 | University Of Cincinnati | Solute-phase electrochemical aptamer sensors for improved longevity and sensitivity |
| US11617741B1 (en) | 2021-08-12 | 2023-04-04 | Health Research, Inc. | Method for inhibiting growth of bacteria |
| US20250125004A1 (en) * | 2021-08-25 | 2025-04-17 | Ensem Therapeutics, Inc. | Systems and methods for post-translational modification-inspired drug design and screening |
| JP2023121226A (ja) * | 2022-02-21 | 2023-08-31 | 株式会社日立製作所 | 検体の前処理方法及びその応用 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20020137119A1 (en) * | 2001-01-14 | 2002-09-26 | Katz Emil Israel | Peptides representative of polypeptides of interest and antibodies directed thereagainst, and methods, systems and kits for generating and utilizing each |
| AU2003302118A1 (en) * | 2002-05-10 | 2004-06-15 | Epitome Biosystems, Inc. | Unique recognition sequences and methods of use thereof in protein analysis |
Family Cites Families (65)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4478744A (en) * | 1982-01-25 | 1984-10-23 | Sherwood Medical Company | Method of obtaining antibodies |
| US4658022A (en) * | 1985-08-08 | 1987-04-14 | Molecular Diagnostics, Inc. | Binding of antibody reagents to denatured protein analytes |
| US5223441A (en) | 1986-10-09 | 1993-06-29 | Syntex (U.S.A.) Inc. | Receptors for immune complexes |
| DE3773121D1 (de) | 1986-11-10 | 1991-10-24 | Progen Biotechnik Gmbh | Verfahren zum identifizieren gewebstypischer, unloeslicher cytoskelettproteine. |
| DE3815932A1 (de) | 1988-01-26 | 1989-08-03 | Progen Biotechnik Gmbh | Verfahren zur identifizierung des ursprungs einer zellgewebsprobe |
| US4970171A (en) | 1987-11-09 | 1990-11-13 | Miles Inc. | Denaturant reagents for convenient determination of hemoglobin derivatives in blood |
| US5519120A (en) * | 1989-04-07 | 1996-05-21 | Cancerforskningsfondet Af 1989 | Urokinase-type plasminogen activator receptor antibodies |
| US5849531A (en) * | 1989-04-07 | 1998-12-15 | University Of Saskatchewan | Compositions and treatments for pneumonia in animals |
| US6955915B2 (en) | 1989-06-07 | 2005-10-18 | Affymetrix, Inc. | Apparatus comprising polymers |
| US5061790A (en) | 1989-07-10 | 1991-10-29 | Molecular Diagnostics, Inc. | Oxidative denaturation of protein analytes |
| DE4009848A1 (de) * | 1990-03-27 | 1991-10-02 | Boehringer Mannheim Gmbh | Verfahren zum nachweis von phosphoryliertes tyrosin enthaltenden proteinen |
| FR2660757B1 (fr) * | 1990-04-06 | 1994-05-27 | Immunotech Sa | Procede d'identification ou de dosage de proteines et applications. |
| DE4023945A1 (de) | 1990-07-27 | 1992-01-30 | Progen Biotechnik Gmbh | Verfahren zur reinigung von cytokeratin 20 und dessen verwendung zur erzeugung von antikoerpern |
| US5565332A (en) * | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| AU2699192A (en) * | 1991-10-16 | 1993-05-21 | University Of Saskatchewan | Enhanced immunogenicity using leukotoxin chimeras |
| US5723129A (en) * | 1991-10-16 | 1998-03-03 | University Of Saskatchewan | GnRH-leukotoxin chimeras |
| JP4116072B2 (ja) * | 1992-08-27 | 2008-07-09 | バイオクローンズ（プロプライエタリー）リミテッド | 逆向き、鏡像体および逆向き鏡像体合成ペプチド類似物 |
| WO1994008597A1 (en) | 1992-10-14 | 1994-04-28 | The Scripps Research Institute | Methods for the detection of antigen-specific immune complexes |
| US5955317A (en) * | 1993-01-25 | 1999-09-21 | Takeda Chemical Industries, Ltd. | Antibodies to β-amyloids or their derivatives and use thereof |
| JPH07285999A (ja) | 1993-03-30 | 1995-10-31 | Prima Meat Packers Ltd | Ｅｌｉｓａを用いた食品中の乳蛋白質含量の定量分析方法及びその分析用に選別されたモノクローナル抗体及びそのモノクローナル抗体の選別方法 |
| JP3393889B2 (ja) * | 1993-06-11 | 2003-04-07 | 柳川精工株式会社 | 無潤滑軸受の製造方法および無潤滑軸受 |
| EP0767378A1 (de) | 1993-06-22 | 1997-04-09 | BOEHRINGER INGELHEIM INTERNATIONAL GmbH | Verfahren zur Diagnose und Analyse von Magenkarzinomen |
| WO1996005847A1 (en) | 1994-08-22 | 1996-02-29 | The Trustees Of The University Of Pennsylvania | A method of sequencing proteins by epitope ordering and protein restriction mapping |
| EP0812434B1 (en) | 1995-03-01 | 2013-09-18 | President and Fellows of Harvard College | Microcontact printing on surfaces and derivative articles |
| US5961923A (en) * | 1995-04-25 | 1999-10-05 | Irori | Matrices with memories and uses thereof |
| AUPN480095A0 (en) | 1995-08-15 | 1995-09-07 | Commonwealth Scientific And Industrial Research Organisation | Epitope tagging system |
| JP3452111B2 (ja) * | 1995-11-10 | 2003-09-29 | セイコーエプソン株式会社 | インクジェット式記録ヘッド |
| US6420125B1 (en) * | 1996-03-21 | 2002-07-16 | Osteometer Biotech A/S | Assaying fragments of collagen in body fluids |
| US5763158A (en) * | 1997-02-06 | 1998-06-09 | The United States Of America As Represented By The Secretary Of The Army | Detection of multiple antigens or antibodies |
| NZ516848A (en) * | 1997-06-20 | 2004-03-26 | Ciphergen Biosystems Inc | Retentate chromatography apparatus with applications in biology and medicine |
| US5872234A (en) * | 1997-06-27 | 1999-02-16 | Incyte Pharmaceuticals, Inc. | Human extracellular matrix proteins |
| US6253456B1 (en) | 1997-11-17 | 2001-07-03 | Phillip Cooksey | Basketball court layout device and method |
| US6809184B1 (en) * | 1997-12-01 | 2004-10-26 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Antibodies, including FV molecules, and immunoconjugates having high binding affinity for mesothelin and methods for their use |
| DE19802576B4 (de) | 1998-01-23 | 2004-10-28 | Xerion Pharmaceuticals Ag | Verfahren zur gleichzeitigen Identifizierung von Proteinen und ihren Bindungspartnern |
| WO1999039210A1 (en) | 1998-01-29 | 1999-08-05 | Miller, Samuel | High density arrays for proteome analysis and methods and compositions therefor |
| US20020119579A1 (en) * | 1998-07-14 | 2002-08-29 | Peter Wagner | Arrays devices and methods of use thereof |
| US6897073B2 (en) | 1998-07-14 | 2005-05-24 | Zyomyx, Inc. | Non-specific binding resistant protein arrays and methods for making the same |
| US6406921B1 (en) * | 1998-07-14 | 2002-06-18 | Zyomyx, Incorporated | Protein arrays for high-throughput screening |
| US6197599B1 (en) * | 1998-07-30 | 2001-03-06 | Guorong Chin | Method to detect proteins |
| DE60011390T2 (de) | 1999-01-28 | 2004-10-14 | Université De Genève | Verfahren und vorrichtung zur identifikation oder karakterisierung von polypeptiden |
| CA2365431A1 (en) | 1999-03-10 | 2000-09-14 | Hui Ge | Universal protein array system |
| US20020042386A1 (en) * | 2000-01-31 | 2002-04-11 | Rosen Craig A. | Nucleic acids, proteins, and antibodies |
| US20020009740A1 (en) | 2000-04-14 | 2002-01-24 | Rima Kaddurah-Daouk | Methods for drug discovery, disease treatment, and diagnosis using metabolomics |
| US20020110843A1 (en) * | 2000-05-12 | 2002-08-15 | Dumas David P. | Compositions and methods for epitope mapping |
| EP1301632A2 (en) | 2000-07-19 | 2003-04-16 | Pointilliste, Inc. | Nested sorting and high throughput screening |
| GB0022978D0 (en) * | 2000-09-19 | 2000-11-01 | Oxford Glycosciences Uk Ltd | Detection of peptides |
| US7142296B2 (en) * | 2000-10-30 | 2006-11-28 | Sru Biosystems, Inc. | Method and apparatus for detecting biomolecular interactions |
| DE10054055A1 (de) * | 2000-10-31 | 2002-05-23 | Nmi Univ Tuebingen | Verfahren zur Analyse von Proteinen |
| WO2002039083A2 (en) * | 2000-11-08 | 2002-05-16 | Science & Technology Corporation @ Unm | Fluorescence and fret based assays for biomolecules on beads |
| GB0103389D0 (en) | 2001-02-12 | 2001-03-28 | Novartis Ag | Organic compounds |
| US20030054408A1 (en) * | 2001-04-20 | 2003-03-20 | Ramamoorthi Ravi | Methods and systems for identifying proteins |
| US20030044862A1 (en) * | 2001-06-22 | 2003-03-06 | The Board Of Trustees Of The Leland Stanford Jr. University | Diagnostic marker for tumor hypoxia and prognosis |
| WO2003001879A2 (en) | 2001-06-26 | 2003-01-09 | Mds Proteomics, Inc. | Methods and systems for identifying kinases, phosphatases and substrates thereof |
| CA2457408A1 (en) * | 2001-07-13 | 2003-01-23 | Pharmacopeia, Inc. | System and method for aqueous solubility prediction |
| US20030143612A1 (en) | 2001-07-18 | 2003-07-31 | Pointilliste, Inc. | Collections of binding proteins and tags and uses thereof for nested sorting and high throughput screening |
| WO2003016904A2 (en) * | 2001-08-13 | 2003-02-27 | Campbell Douglas A | Peptide sequence tags and method of using same |
| US20050153298A1 (en) * | 2001-10-23 | 2005-07-14 | Gembitsky Dmitry S. | Protein micro-arrays and multi-layered affinity interaction detection |
| GB0200595D0 (en) | 2002-01-11 | 2002-02-27 | Oxford Glycosciences Uk Ltd | Quantitation of differential expression |
| US7618788B2 (en) * | 2002-05-10 | 2009-11-17 | Millipore Corporation | Proteome epitope tags and methods of use thereof in protein modification analysis |
| US20060014212A1 (en) * | 2002-05-10 | 2006-01-19 | Epitome Biosystems, Inc. | Proteome epitope tags and methods of use thereof in protein modification analysis |
| US7460960B2 (en) | 2002-05-10 | 2008-12-02 | Epitome Biosystems, Inc. | Proteome epitope tags and methods of use thereof in protein modification analysis |
| US20040229284A1 (en) * | 2003-02-19 | 2004-11-18 | The Regents Of The University Of California | Multiplex analysis of proteins |
| US20050255491A1 (en) | 2003-11-13 | 2005-11-17 | Lee Frank D | Small molecule and peptide arrays and uses thereof |
| US7855057B2 (en) | 2006-03-23 | 2010-12-21 | Millipore Corporation | Protein splice variant/isoform discrimination and quantitative measurements thereof |
| US20100331200A1 (en) | 2006-03-31 | 2010-12-30 | Gordon Neal F | Post translational modification pattern analysis |
-
2003
- 2003-11-13 US US10/712,425 patent/US7460960B2/en not_active Expired - Fee Related
-
2004
- 2004-11-15 JP JP2006539990A patent/JP2007511837A/ja active Pending
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- 2004-11-15 CA CA002545899A patent/CA2545899A1/en not_active Abandoned
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- 2008-09-25 AU AU2008227063A patent/AU2008227063A1/en not_active Abandoned
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20020137119A1 (en) * | 2001-01-14 | 2002-09-26 | Katz Emil Israel | Peptides representative of polypeptides of interest and antibodies directed thereagainst, and methods, systems and kits for generating and utilizing each |
| AU2003302118A1 (en) * | 2002-05-10 | 2004-06-15 | Epitome Biosystems, Inc. | Unique recognition sequences and methods of use thereof in protein analysis |
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