The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members
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| Veröffentlicht in: | Molecular and Cellular Biology 2007-05, Vol.27 (9), p.3542-3555 |
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| container_title | Molecular and Cellular Biology |
| container_volume | 27 |
| creator | Craig, Ashley L. Chrystal, Jennifer A. Fraser, Jennifer A. Sphyris, Nathalie Lin, Yao Harrison, Ben J. Scott, Mary T. Dornreiter, Irena Hupp, Ted R. |
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| doi_str_mv | 10.1128/MCB.01595-06 |
| format | Article |
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</description><identifier>ISSN: 0270-7306</identifier><identifier>ISSN: 1098-5549</identifier><identifier>EISSN: 1098-5549</identifier><identifier>DOI: 10.1128/MCB.01595-06</identifier><identifier>PMID: 17339337</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Amino Acid Motifs ; Apoptosis Regulatory Proteins - metabolism ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Cell Line, Tumor ; Checkpoint Kinase 1 ; Checkpoint Kinase 2 ; Death-Associated Protein Kinases ; DNA - metabolism ; Enzyme Activation ; Gene Deletion ; Humans ; Molecular Sequence Data ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Protein Binding ; Protein Kinases - chemistry ; Protein Kinases - metabolism ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - metabolism ; Proto-Oncogene Proteins c-mdm2 - metabolism ; Sequence Homology, Amino Acid ; Transcriptional Activation ; Tumor Suppressor Protein p53 - chemistry ; Tumor Suppressor Protein p53 - classification ; Tumor Suppressor Protein p53 - metabolism ; Ubiquitin - metabolism</subject><ispartof>Molecular and Cellular Biology, 2007-05, Vol.27 (9), p.3542-3555</ispartof><rights>Copyright © 2007 American Society for Microbiology 2007</rights><rights>Copyright © 2007, American Society for Microbiology 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c553t-f802ff1985d0cef558532d8f99f116c85e723db94f461238e98dae85eaff322e3</citedby><cites>FETCH-LOGICAL-c553t-f802ff1985d0cef558532d8f99f116c85e723db94f461238e98dae85eaff322e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1899961/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1899961/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17339337$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Craig, Ashley L.</creatorcontrib><creatorcontrib>Chrystal, Jennifer A.</creatorcontrib><creatorcontrib>Fraser, Jennifer A.</creatorcontrib><creatorcontrib>Sphyris, Nathalie</creatorcontrib><creatorcontrib>Lin, Yao</creatorcontrib><creatorcontrib>Harrison, Ben J.</creatorcontrib><creatorcontrib>Scott, Mary T.</creatorcontrib><creatorcontrib>Dornreiter, Irena</creatorcontrib><creatorcontrib>Hupp, Ted R.</creatorcontrib><title>The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members</title><title>Molecular and Cellular Biology</title><addtitle>Mol Cell Biol</addtitle><description>Article Usage Stats
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</description><subject>Amino Acid Motifs</subject><subject>Apoptosis Regulatory Proteins - metabolism</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Cell Line, Tumor</subject><subject>Checkpoint Kinase 1</subject><subject>Checkpoint Kinase 2</subject><subject>Death-Associated Protein Kinases</subject><subject>DNA - metabolism</subject><subject>Enzyme Activation</subject><subject>Gene Deletion</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Protein Binding</subject><subject>Protein Kinases - chemistry</subject><subject>Protein Kinases - metabolism</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Proto-Oncogene Proteins c-mdm2 - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Transcriptional Activation</subject><subject>Tumor Suppressor Protein p53 - chemistry</subject><subject>Tumor Suppressor Protein p53 - classification</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><subject>Ubiquitin - metabolism</subject><issn>0270-7306</issn><issn>1098-5549</issn><issn>1098-5549</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtvUzEQhS0EoqGwY43Mpitu8SO-194gtQkFRAOLtGvL8bUTgx-pfS9V_gC_G4dEPBaI1UhnvjkzowPAc4zOMSb89WJ2eY4wE6xB7QMwwUjwhrGpeAgmiHSo6ShqT8CTUr4ghFqB6GNwgjtKBaXdBHy_2Ri4mC8IvF25u9ENLqrBpQiXbh2Vhy7CoRLzTxfNpYu9i2s4T0FVOVm4ZRRepRwKVFXVX_fdpRsMtCnDmfLajWFfQ-pHX0c-VvNi4HLcmmxVcH4HFyasTC5PwSOrfDHPjvUU3F69vZm9b64_v_swu7huNGN0aCxHxFosOOuRNpYxzijpuRXCYtxqzkxHaL8SUzttMaHcCN4rU2VlLSXE0FPw5uC7HVfB9NrEISsvt9kFlXcyKSf_7kS3kev0TWIuhGhxNTg7GuR0N5oyyOCKNt6raNJYZIdovbHu_h-IRctaTvfgqwOocyolG_vrGozkPmFZE5Y_E5aorfiLPz_4DR8jrUB3AFysMQR1n7Lv5aB2PmWbVdSuSPoP65eHyY1bb-5dNlKVIINeSdJJISmbEvoD6R6_Sg</recordid><startdate>20070501</startdate><enddate>20070501</enddate><creator>Craig, Ashley L.</creator><creator>Chrystal, Jennifer A.</creator><creator>Fraser, Jennifer A.</creator><creator>Sphyris, Nathalie</creator><creator>Lin, Yao</creator><creator>Harrison, Ben J.</creator><creator>Scott, Mary T.</creator><creator>Dornreiter, Irena</creator><creator>Hupp, Ted R.</creator><general>American Society for Microbiology</general><general>Taylor & Francis</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>7QP</scope><scope>7TM</scope><scope>7TO</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070501</creationdate><title>The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members</title><author>Craig, Ashley L. ; 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</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>17339337</pmid><doi>10.1128/MCB.01595-06</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0270-7306 |
| ispartof | Molecular and Cellular Biology, 2007-05, Vol.27 (9), p.3542-3555 |
| issn | 0270-7306 1098-5549 1098-5549 |
| language | eng |
| recordid | cdi_pubmed_primary_17339337 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Motifs Apoptosis Regulatory Proteins - metabolism Calcium-Calmodulin-Dependent Protein Kinases - metabolism Cell Line, Tumor Checkpoint Kinase 1 Checkpoint Kinase 2 Death-Associated Protein Kinases DNA - metabolism Enzyme Activation Gene Deletion Humans Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - metabolism Protein Binding Protein Kinases - chemistry Protein Kinases - metabolism Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - metabolism Proto-Oncogene Proteins c-mdm2 - metabolism Sequence Homology, Amino Acid Transcriptional Activation Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - classification Tumor Suppressor Protein p53 - metabolism Ubiquitin - metabolism |
| title | The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members |
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