Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs
Ras and Rho GTPases are prominent participants in malignant transformation. They possess an essential prenyl group (farnesyl or geranylgeranyl) that endows them with membrane-tethering ability and functional specificity. Accumulating evidence suggests that prenyl groups are involved primarily in lip...
Gespeichert in:
| Veröffentlicht in: | Seminars in cancer biology 2004-08, Vol.14 (4), p.253-261 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 261 |
|---|---|
| container_issue | 4 |
| container_start_page | 253 |
| container_title | Seminars in cancer biology |
| container_volume | 14 |
| creator | Kloog, Yoel Cox, Adrienne D |
| description | Ras and Rho GTPases are prominent participants in malignant transformation. They possess an essential prenyl group (farnesyl or geranylgeranyl) that endows them with membrane-tethering ability and functional specificity. Accumulating evidence suggests that prenyl groups are involved primarily in lipid−protein interactions, and recent experiments point to prenyl-binding hydrophobic pockets in proteins regulating Ras and Rho in normal cells and cancer cells. This review presents the evidence for such prenyl-binding domains as significant players in the control of Ras-like GTPases, and the emerging concept of prenyl-binding domains as potential targets for Ras inhibitors and anti-cancer drugs. |
| doi_str_mv | 10.1016/j.semcancer.2004.04.004 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66660897</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1044579X04000215</els_id><sourcerecordid>18018436</sourcerecordid><originalsourceid>FETCH-LOGICAL-c398t-6a362f5c3b2644cafffd21222717acea79ef2586f3d4006fc7c32b112931258d3</originalsourceid><addsrcrecordid>eNqFkFtLwzAYhoMobk7_gvbKu86cmrbejeEJBspQ8C6kOcyMNp1JJuzfm7KhlwtfSAjP-33hAeAGwSmCiN2tp0F3Ujip_RRDSKdDQXoCxgjWLCesgKfDndK8KOvPEbgIYQ0hrCmi52CECoxqhqoxWL557XZt3linrFtlqu-EdeE-2_RRu2hFm0XhVzqGzPQ-W4qQWfdlGxt7HzLhVNrR5vuvZMpvV-ESnBnRBn11OCfg4_Hhff6cL16fXuazRS5JXcWcCcKwKSRpMKNUCmOMwghjXKJSSC3KWhtcVMwQRSFkRpaS4AYhXBOU3hWZgNt9343vv7c6RN7ZIHXbCqf7beAsLVjV5VEQVRBVlLAElntQ-j4Erw3feNsJv-MI8sE7X_M_73zwzoeCNCWvDyO2TafVf-4gOgGzPaCTkR-b4kFanfoo67WMXPX26JBf3pSYfQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18018436</pqid></control><display><type>article</type><title>Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Kloog, Yoel ; Cox, Adrienne D</creator><creatorcontrib>Kloog, Yoel ; Cox, Adrienne D</creatorcontrib><description>Ras and Rho GTPases are prominent participants in malignant transformation. They possess an essential prenyl group (farnesyl or geranylgeranyl) that endows them with membrane-tethering ability and functional specificity. Accumulating evidence suggests that prenyl groups are involved primarily in lipid−protein interactions, and recent experiments point to prenyl-binding hydrophobic pockets in proteins regulating Ras and Rho in normal cells and cancer cells. This review presents the evidence for such prenyl-binding domains as significant players in the control of Ras-like GTPases, and the emerging concept of prenyl-binding domains as potential targets for Ras inhibitors and anti-cancer drugs.</description><identifier>ISSN: 1044-579X</identifier><identifier>EISSN: 1096-3650</identifier><identifier>DOI: 10.1016/j.semcancer.2004.04.004</identifier><identifier>PMID: 15219618</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Animals ; Binding Sites - drug effects ; Farnesyl ; Galectin-1 ; Gene Expression Regulation, Neoplastic - drug effects ; Gene Expression Regulation, Neoplastic - physiology ; Geranylgeranyl ; Humans ; Neoplasms - therapy ; Protein Prenylation ; Ras ; ras Proteins - antagonists & inhibitors ; Rho</subject><ispartof>Seminars in cancer biology, 2004-08, Vol.14 (4), p.253-261</ispartof><rights>2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c398t-6a362f5c3b2644cafffd21222717acea79ef2586f3d4006fc7c32b112931258d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.semcancer.2004.04.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15219618$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kloog, Yoel</creatorcontrib><creatorcontrib>Cox, Adrienne D</creatorcontrib><title>Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs</title><title>Seminars in cancer biology</title><addtitle>Semin Cancer Biol</addtitle><description>Ras and Rho GTPases are prominent participants in malignant transformation. They possess an essential prenyl group (farnesyl or geranylgeranyl) that endows them with membrane-tethering ability and functional specificity. Accumulating evidence suggests that prenyl groups are involved primarily in lipid−protein interactions, and recent experiments point to prenyl-binding hydrophobic pockets in proteins regulating Ras and Rho in normal cells and cancer cells. This review presents the evidence for such prenyl-binding domains as significant players in the control of Ras-like GTPases, and the emerging concept of prenyl-binding domains as potential targets for Ras inhibitors and anti-cancer drugs.</description><subject>Animals</subject><subject>Binding Sites - drug effects</subject><subject>Farnesyl</subject><subject>Galectin-1</subject><subject>Gene Expression Regulation, Neoplastic - drug effects</subject><subject>Gene Expression Regulation, Neoplastic - physiology</subject><subject>Geranylgeranyl</subject><subject>Humans</subject><subject>Neoplasms - therapy</subject><subject>Protein Prenylation</subject><subject>Ras</subject><subject>ras Proteins - antagonists & inhibitors</subject><subject>Rho</subject><issn>1044-579X</issn><issn>1096-3650</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkFtLwzAYhoMobk7_gvbKu86cmrbejeEJBspQ8C6kOcyMNp1JJuzfm7KhlwtfSAjP-33hAeAGwSmCiN2tp0F3Ujip_RRDSKdDQXoCxgjWLCesgKfDndK8KOvPEbgIYQ0hrCmi52CECoxqhqoxWL557XZt3linrFtlqu-EdeE-2_RRu2hFm0XhVzqGzPQ-W4qQWfdlGxt7HzLhVNrR5vuvZMpvV-ESnBnRBn11OCfg4_Hhff6cL16fXuazRS5JXcWcCcKwKSRpMKNUCmOMwghjXKJSSC3KWhtcVMwQRSFkRpaS4AYhXBOU3hWZgNt9343vv7c6RN7ZIHXbCqf7beAsLVjV5VEQVRBVlLAElntQ-j4Erw3feNsJv-MI8sE7X_M_73zwzoeCNCWvDyO2TafVf-4gOgGzPaCTkR-b4kFanfoo67WMXPX26JBf3pSYfQ</recordid><startdate>20040801</startdate><enddate>20040801</enddate><creator>Kloog, Yoel</creator><creator>Cox, Adrienne D</creator><general>Elsevier Ltd</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>7TO</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20040801</creationdate><title>Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs</title><author>Kloog, Yoel ; Cox, Adrienne D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c398t-6a362f5c3b2644cafffd21222717acea79ef2586f3d4006fc7c32b112931258d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Binding Sites - drug effects</topic><topic>Farnesyl</topic><topic>Galectin-1</topic><topic>Gene Expression Regulation, Neoplastic - drug effects</topic><topic>Gene Expression Regulation, Neoplastic - physiology</topic><topic>Geranylgeranyl</topic><topic>Humans</topic><topic>Neoplasms - therapy</topic><topic>Protein Prenylation</topic><topic>Ras</topic><topic>ras Proteins - antagonists & inhibitors</topic><topic>Rho</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kloog, Yoel</creatorcontrib><creatorcontrib>Cox, Adrienne D</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Seminars in cancer biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kloog, Yoel</au><au>Cox, Adrienne D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs</atitle><jtitle>Seminars in cancer biology</jtitle><addtitle>Semin Cancer Biol</addtitle><date>2004-08-01</date><risdate>2004</risdate><volume>14</volume><issue>4</issue><spage>253</spage><epage>261</epage><pages>253-261</pages><issn>1044-579X</issn><eissn>1096-3650</eissn><abstract>Ras and Rho GTPases are prominent participants in malignant transformation. They possess an essential prenyl group (farnesyl or geranylgeranyl) that endows them with membrane-tethering ability and functional specificity. Accumulating evidence suggests that prenyl groups are involved primarily in lipid−protein interactions, and recent experiments point to prenyl-binding hydrophobic pockets in proteins regulating Ras and Rho in normal cells and cancer cells. This review presents the evidence for such prenyl-binding domains as significant players in the control of Ras-like GTPases, and the emerging concept of prenyl-binding domains as potential targets for Ras inhibitors and anti-cancer drugs.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>15219618</pmid><doi>10.1016/j.semcancer.2004.04.004</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1044-579X |
| ispartof | Seminars in cancer biology, 2004-08, Vol.14 (4), p.253-261 |
| issn | 1044-579X 1096-3650 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_66660897 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Binding Sites - drug effects Farnesyl Galectin-1 Gene Expression Regulation, Neoplastic - drug effects Gene Expression Regulation, Neoplastic - physiology Geranylgeranyl Humans Neoplasms - therapy Protein Prenylation Ras ras Proteins - antagonists & inhibitors Rho |
| title | Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T14%3A34%3A09IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Prenyl-binding%20domains:%20potential%20targets%20for%20Ras%20inhibitors%20and%20anti-cancer%20drugs&rft.jtitle=Seminars%20in%20cancer%20biology&rft.au=Kloog,%20Yoel&rft.date=2004-08-01&rft.volume=14&rft.issue=4&rft.spage=253&rft.epage=261&rft.pages=253-261&rft.issn=1044-579X&rft.eissn=1096-3650&rft_id=info:doi/10.1016/j.semcancer.2004.04.004&rft_dat=%3Cproquest_cross%3E18018436%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=18018436&rft_id=info:pmid/15219618&rft_els_id=S1044579X04000215&rfr_iscdi=true |