Application of mass spectrometry for target identification and characterization
Mass spectrometry‐based methodologies span the vast expanse of drug discovery. Both electrospray ionization (ESI) and matrix‐assisted laser desorption/ionization (MALDI) support proteomics‐based research projects by identifying proteins separated and isolated by polyacrylamide gel electrophoresis. M...
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| Veröffentlicht in: | Medicinal research reviews 1999-07, Vol.19 (4), p.307-319 |
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| container_title | Medicinal research reviews |
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| creator | Loo, Joseph A. DeJohn, Dana E. Du, Ping Stevenson, Tracy I. Ogorzalek Loo, Rachel R. |
| description | Mass spectrometry‐based methodologies span the vast expanse of drug discovery. Both electrospray ionization (ESI) and matrix‐assisted laser desorption/ionization (MALDI) support proteomics‐based research projects by identifying proteins separated and isolated by polyacrylamide gel electrophoresis. MALDI‐MS‐based surface scanning of one‐dimensional isoelectric focusing gels, “virtual 2‐D gel electrophoresis,” represents a potentially high throughput means to map proteins and to determine protein profiles. Mass spectrometry can also be used to directly study the covalent and noncovalent interactions of drug molecules and biomolecule targets. Drug binding examples discussed include the binding of covalent and noncovalent inhibitors to src SH2 domain protein, and the interaction of aminoglycoside antibiotic neomycin and HIV Tat peptide‐TAR RNA. © 1999 John Wiley & Sons, Inc. Med Res Rev, 19, No. 4, 307–319, 1999. |
| doi_str_mv | 10.1002/(SICI)1098-1128(199907)19:4<307::AID-MED4>3.0.CO;2-2 |
| format | Article |
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Res. Rev</addtitle><description>Mass spectrometry‐based methodologies span the vast expanse of drug discovery. Both electrospray ionization (ESI) and matrix‐assisted laser desorption/ionization (MALDI) support proteomics‐based research projects by identifying proteins separated and isolated by polyacrylamide gel electrophoresis. MALDI‐MS‐based surface scanning of one‐dimensional isoelectric focusing gels, “virtual 2‐D gel electrophoresis,” represents a potentially high throughput means to map proteins and to determine protein profiles. Mass spectrometry can also be used to directly study the covalent and noncovalent interactions of drug molecules and biomolecule targets. Drug binding examples discussed include the binding of covalent and noncovalent inhibitors to src SH2 domain protein, and the interaction of aminoglycoside antibiotic neomycin and HIV Tat peptide‐TAR RNA. © 1999 John Wiley & Sons, Inc. Med Res Rev, 19, No. 4, 307–319, 1999.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>drug binding</subject><subject>Drug Design</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects, investigation methods</subject><subject>Macromolecular Substances</subject><subject>mass spectrometry</subject><subject>Mass Spectrometry - methods</subject><subject>Proteins</subject><subject>proteomics</subject><subject>src SH2</subject><subject>Tat-TAR</subject><issn>0198-6325</issn><issn>1098-1128</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkF1v0zAUhiMEYmXwF1AuENouUvwVxy4TUpVuo6LQiw0hcXPkODYY8oWdCsqvJ1nKhgQSV8e2Xj9-_UTRGUZzjBB5cXK1ztenGEmRYEzECZZSouwUywU7oyhbLJbrVfL2fMVe0Tma59uXJCH3otnthfvRDOFhzSlJj6JHIXxBCOMU04fREUZUCkmyWbRddl3ltOpd28StjWsVQhw6o3vf1qb3-9i2Pu6V_2T62JWm6Z39HVdNGevPyivdG-9-3hw-jh5YVQXz5DCPo_cX59f562SzvVzny02iGREsoZnMGDFUUIIVt7QQlGIuETNlYQvOcSqoTLNMlZjZVHHNU6wskynnBcWM0uPo-cTtfPttZ0IPtQvaVJVqTLsLwKUQhBMxBK-noPZtCN5Y6Lyrld8DRjCKBhhFw-gNRm8wiR4GMBhEAwyiYRQNFBDkWyBABuzTw_u7ojblH9DJ7BB4dgiooFVlvWq0C3c5MXxPsLt6311l9n91-0-1fzS72Q_YZMK60Jsft1jlvwLPaJbCh3eXsJJXby42H3Ng9BdA0bMv</recordid><startdate>199907</startdate><enddate>199907</enddate><creator>Loo, Joseph A.</creator><creator>DeJohn, Dana E.</creator><creator>Du, Ping</creator><creator>Stevenson, Tracy I.</creator><creator>Ogorzalek Loo, Rachel R.</creator><general>John Wiley & Sons, Inc</general><general>Wiley</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199907</creationdate><title>Application of mass spectrometry for target identification and characterization</title><author>Loo, Joseph A. ; DeJohn, Dana E. ; Du, Ping ; Stevenson, Tracy I. ; Ogorzalek Loo, Rachel R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4284-379742e38321a6f3b83316904edbfb6615839577ad14f5a6c651af49566b31433</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>drug binding</topic><topic>Drug Design</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects, investigation methods</topic><topic>Macromolecular Substances</topic><topic>mass spectrometry</topic><topic>Mass Spectrometry - methods</topic><topic>Proteins</topic><topic>proteomics</topic><topic>src SH2</topic><topic>Tat-TAR</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Loo, Joseph A.</creatorcontrib><creatorcontrib>DeJohn, Dana E.</creatorcontrib><creatorcontrib>Du, Ping</creatorcontrib><creatorcontrib>Stevenson, Tracy I.</creatorcontrib><creatorcontrib>Ogorzalek Loo, Rachel R.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Medicinal research reviews</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Loo, Joseph A.</au><au>DeJohn, Dana E.</au><au>Du, Ping</au><au>Stevenson, Tracy I.</au><au>Ogorzalek Loo, Rachel R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Application of mass spectrometry for target identification and characterization</atitle><jtitle>Medicinal research reviews</jtitle><addtitle>Med. Res. Rev</addtitle><date>1999-07</date><risdate>1999</risdate><volume>19</volume><issue>4</issue><spage>307</spage><epage>319</epage><pages>307-319</pages><issn>0198-6325</issn><eissn>1098-1128</eissn><coden>MRREDD</coden><abstract>Mass spectrometry‐based methodologies span the vast expanse of drug discovery. Both electrospray ionization (ESI) and matrix‐assisted laser desorption/ionization (MALDI) support proteomics‐based research projects by identifying proteins separated and isolated by polyacrylamide gel electrophoresis. MALDI‐MS‐based surface scanning of one‐dimensional isoelectric focusing gels, “virtual 2‐D gel electrophoresis,” represents a potentially high throughput means to map proteins and to determine protein profiles. Mass spectrometry can also be used to directly study the covalent and noncovalent interactions of drug molecules and biomolecule targets. Drug binding examples discussed include the binding of covalent and noncovalent inhibitors to src SH2 domain protein, and the interaction of aminoglycoside antibiotic neomycin and HIV Tat peptide‐TAR RNA. © 1999 John Wiley & Sons, Inc. Med Res Rev, 19, No. 4, 307–319, 1999.</abstract><cop>New York</cop><pub>John Wiley & Sons, Inc</pub><pmid>10398927</pmid><doi>10.1002/(SICI)1098-1128(199907)19:4<307::AID-MED4>3.0.CO;2-2</doi><tpages>13</tpages></addata></record> |
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| ispartof | Medicinal research reviews, 1999-07, Vol.19 (4), p.307-319 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences drug binding Drug Design Fundamental and applied biological sciences. Psychology General aspects, investigation methods Macromolecular Substances mass spectrometry Mass Spectrometry - methods Proteins proteomics src SH2 Tat-TAR |
| title | Application of mass spectrometry for target identification and characterization |
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