UNNATURAL LIGANDS FOR ENGINEERED PROTEINS: New Tools for Chemical Genetics
Small molecules that modulate the activity of biological signaling molecules can be powerful probes of signal transduction pathways. Highly specific molecules with high affinity are difficult to identify because of the conserved nature of many protein active sites. A newly developed approach to disc...
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| Veröffentlicht in: | Annual review of biophysics and biomolecular structure 2000-01, Vol.29 (1), p.577-606 |
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| creator | Bishop, Anthony Buzko, Oleksandr Heyeck-Dumas, Stephanie Jung, Ilyoung Kraybill, Brian Liu, Yi Shah, Kavita Ulrich, Scott Witucki, Laurie Yang, Feng Zhang, Chao Shokat, Kevan M |
| description | Small molecules that modulate the activity of biological signaling molecules
can be powerful probes of signal transduction pathways. Highly specific
molecules with high affinity are difficult to identify because of the conserved
nature of many protein active sites. A newly developed approach to discovery of
such small molecules that relies on protein engineering and chemical synthesis
has yielded powerful tools for the study of a wide variety of proteins involved
in signal transduction (G-proteins, protein kinases, 7-transmembrane receptors,
nuclear hormone receptors, and others). Such chemical genetic tools combine the
advantages of traditional genetics and the unparalleled temporal control over
protein function afforded by small molecule inhibitors/activators that act at
diffusion controlled rates with targets. |
| doi_str_mv | 10.1146/annurev.biophys.29.1.577 |
| format | Article |
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can be powerful probes of signal transduction pathways. Highly specific
molecules with high affinity are difficult to identify because of the conserved
nature of many protein active sites. A newly developed approach to discovery of
such small molecules that relies on protein engineering and chemical synthesis
has yielded powerful tools for the study of a wide variety of proteins involved
in signal transduction (G-proteins, protein kinases, 7-transmembrane receptors,
nuclear hormone receptors, and others). Such chemical genetic tools combine the
advantages of traditional genetics and the unparalleled temporal control over
protein function afforded by small molecule inhibitors/activators that act at
diffusion controlled rates with targets.</description><identifier>ISSN: 1056-8700</identifier><identifier>EISSN: 1545-4266</identifier><identifier>DOI: 10.1146/annurev.biophys.29.1.577</identifier><identifier>PMID: 10940260</identifier><identifier>CODEN: ABBSE4</identifier><language>eng</language><publisher>Palo Alto, CA 94303-0139: Annual Reviews</publisher><subject>Alleles ; Amino Acid Sequence ; Animals ; Binding Sites ; Genetic Techniques ; GTP Phosphohydrolases - chemistry ; Humans ; Kinesin - chemistry ; Kinesin - genetics ; Ligands ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Myosins - chemistry ; Myosins - genetics ; nuclear hormone receptors ; orthogonal ligands ; protein design ; Protein Engineering ; Protein Kinases - chemistry ; Proteins - chemical synthesis ; seven-transmembrane receptors ; Signal Transduction</subject><ispartof>Annual review of biophysics and biomolecular structure, 2000-01, Vol.29 (1), p.577-606</ispartof><rights>Copyright © 2000 by Annual Reviews. All rights reserved</rights><rights>Copyright Annual Reviews, Inc. 2000</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a543t-838e1b73ae75cba2a5402d197c453089e144985919b813665fcb9c920094c7053</citedby><cites>FETCH-LOGICAL-a543t-838e1b73ae75cba2a5402d197c453089e144985919b813665fcb9c920094c7053</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.annualreviews.org/content/journals/10.1146/annurev.biophys.29.1.577?crawler=true&mimetype=application/pdf$$EPDF$$P50$$Gannualreviews$$H</linktopdf><linktohtml>$$Uhttps://www.annualreviews.org/content/journals/10.1146/annurev.biophys.29.1.577$$EHTML$$P50$$Gannualreviews$$H</linktohtml><link.rule.ids>70,314,780,784,4182,27924,27925,78254,78255</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10940260$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bishop, Anthony</creatorcontrib><creatorcontrib>Buzko, Oleksandr</creatorcontrib><creatorcontrib>Heyeck-Dumas, Stephanie</creatorcontrib><creatorcontrib>Jung, Ilyoung</creatorcontrib><creatorcontrib>Kraybill, Brian</creatorcontrib><creatorcontrib>Liu, Yi</creatorcontrib><creatorcontrib>Shah, Kavita</creatorcontrib><creatorcontrib>Ulrich, Scott</creatorcontrib><creatorcontrib>Witucki, Laurie</creatorcontrib><creatorcontrib>Yang, Feng</creatorcontrib><creatorcontrib>Zhang, Chao</creatorcontrib><creatorcontrib>Shokat, Kevan M</creatorcontrib><title>UNNATURAL LIGANDS FOR ENGINEERED PROTEINS: New Tools for Chemical Genetics</title><title>Annual review of biophysics and biomolecular structure</title><addtitle>Annu Rev Biophys Biomol Struct</addtitle><description>Small molecules that modulate the activity of biological signaling molecules
can be powerful probes of signal transduction pathways. Highly specific
molecules with high affinity are difficult to identify because of the conserved
nature of many protein active sites. A newly developed approach to discovery of
such small molecules that relies on protein engineering and chemical synthesis
has yielded powerful tools for the study of a wide variety of proteins involved
in signal transduction (G-proteins, protein kinases, 7-transmembrane receptors,
nuclear hormone receptors, and others). Such chemical genetic tools combine the
advantages of traditional genetics and the unparalleled temporal control over
protein function afforded by small molecule inhibitors/activators that act at
diffusion controlled rates with targets.</description><subject>Alleles</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Genetic Techniques</subject><subject>GTP Phosphohydrolases - chemistry</subject><subject>Humans</subject><subject>Kinesin - chemistry</subject><subject>Kinesin - genetics</subject><subject>Ligands</subject><subject>Models, Biological</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Myosins - chemistry</subject><subject>Myosins - genetics</subject><subject>nuclear hormone receptors</subject><subject>orthogonal ligands</subject><subject>protein design</subject><subject>Protein Engineering</subject><subject>Protein Kinases - chemistry</subject><subject>Proteins - chemical synthesis</subject><subject>seven-transmembrane receptors</subject><subject>Signal Transduction</subject><issn>1056-8700</issn><issn>1545-4266</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqVkV1r2zAUhkXZaLu0f2GIXezO7pFkSdZgFyF105TglHxcC1mRqYtjZ5a9rv9-KslFKXSjVzqI532PxIMQJhATkogr0zRD537HRdXuH559TFVMYi7lCTonPOFRQoX4FGbgIkolwBn64v0jAAgK8hSdEVAJUAHn6G6T5-P1Zjme4_lsOs6vV_hmscRZPp3lWbbMrvH9crHOZvnqB87dE163be1x2XZ48uB2lTU1nrrG9ZX1F-hzaWrvLo_nCG1usvXkNpovprPJeB4ZnrA-SlnqSCGZcZLbwtBwC3RLlLQJZ5AqR5JEpVwRVaSECcFLWyirKIQ3WwmcjdD3Q---a38Nzvd6V3nr6to0rh28lkRyUAD_BYmUVDCqAvjtDfjYDl0TPqEppUQC4zRA6QGyXet950q976qd6Z41Af1iRR-t6KMVTZUmOlgJ0a_H_qHYue2r4EFDAH4egJcKU4eSyj35jyz4Z_69nN5vS93_6dlff020mA</recordid><startdate>20000101</startdate><enddate>20000101</enddate><creator>Bishop, Anthony</creator><creator>Buzko, Oleksandr</creator><creator>Heyeck-Dumas, Stephanie</creator><creator>Jung, Ilyoung</creator><creator>Kraybill, Brian</creator><creator>Liu, Yi</creator><creator>Shah, Kavita</creator><creator>Ulrich, Scott</creator><creator>Witucki, Laurie</creator><creator>Yang, Feng</creator><creator>Zhang, Chao</creator><creator>Shokat, Kevan M</creator><general>Annual Reviews</general><general>Annual Reviews, Inc</general><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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20000101</creationdate><title>UNNATURAL LIGANDS FOR ENGINEERED PROTEINS: New Tools for Chemical Genetics</title><author>Bishop, Anthony ; Buzko, Oleksandr ; Heyeck-Dumas, Stephanie ; Jung, Ilyoung ; Kraybill, Brian ; Liu, Yi ; Shah, Kavita ; Ulrich, Scott ; Witucki, Laurie ; Yang, Feng ; Zhang, Chao ; Shokat, Kevan M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a543t-838e1b73ae75cba2a5402d197c453089e144985919b813665fcb9c920094c7053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Alleles</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Genetic Techniques</topic><topic>GTP Phosphohydrolases - 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can be powerful probes of signal transduction pathways. Highly specific
molecules with high affinity are difficult to identify because of the conserved
nature of many protein active sites. A newly developed approach to discovery of
such small molecules that relies on protein engineering and chemical synthesis
has yielded powerful tools for the study of a wide variety of proteins involved
in signal transduction (G-proteins, protein kinases, 7-transmembrane receptors,
nuclear hormone receptors, and others). Such chemical genetic tools combine the
advantages of traditional genetics and the unparalleled temporal control over
protein function afforded by small molecule inhibitors/activators that act at
diffusion controlled rates with targets.</abstract><cop>Palo Alto, CA 94303-0139</cop><cop>4139 El Camino Way, P.O. Box 10139</cop><cop>USA</cop><pub>Annual Reviews</pub><pmid>10940260</pmid><doi>10.1146/annurev.biophys.29.1.577</doi><tpages>30</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1056-8700 |
| ispartof | Annual review of biophysics and biomolecular structure, 2000-01, Vol.29 (1), p.577-606 |
| issn | 1056-8700 1545-4266 |
| language | eng |
| recordid | cdi_proquest_journals_222170352 |
| source | Annual Reviews; MEDLINE |
| subjects | Alleles Amino Acid Sequence Animals Binding Sites Genetic Techniques GTP Phosphohydrolases - chemistry Humans Kinesin - chemistry Kinesin - genetics Ligands Models, Biological Models, Molecular Molecular Sequence Data Myosins - chemistry Myosins - genetics nuclear hormone receptors orthogonal ligands protein design Protein Engineering Protein Kinases - chemistry Proteins - chemical synthesis seven-transmembrane receptors Signal Transduction |
| title | UNNATURAL LIGANDS FOR ENGINEERED PROTEINS: New Tools for Chemical Genetics |
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