A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain
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| Veröffentlicht in: | Molecular and Cellular Biology 1997-01, Vol.17 (1), p.338-344 |
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| container_end_page | 344 |
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| container_start_page | 338 |
| container_title | Molecular and Cellular Biology |
| container_volume | 17 |
| creator | Klippel, Anke Kavanaugh, W. Michael Pot, David Williams, Lewis T. |
| description | Article Usage Stats
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| doi_str_mv | 10.1128/mcb.17.1.338 |
| 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.17.1.338</identifier><identifier>PMID: 8972214</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Animals ; Blood Proteins - genetics ; COS Cells ; Enzyme Activation ; Inositol Polyphosphate 5-Phosphatases ; Membranes, Artificial ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates - metabolism ; Phosphatidylinositols - metabolism ; Phosphoproteins ; Phosphoric Monoester Hydrolases - metabolism ; Phosphotransferases (Alcohol Group Acceptor) - metabolism ; Point Mutation ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Proto-Oncogene Proteins c-akt ; Sequence Homology, Amino Acid ; Signal Transduction - physiology</subject><ispartof>Molecular and Cellular Biology, 1997-01, Vol.17 (1), p.338-344</ispartof><rights>Copyright © 1997, American Society for Microbiology 1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c548t-e5998204a3dd1f243325c9e7eda137d62d6119481c6e8e6cfbb1c01953c7b3933</citedby><cites>FETCH-LOGICAL-c548t-e5998204a3dd1f243325c9e7eda137d62d6119481c6e8e6cfbb1c01953c7b3933</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/PMC231758/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC231758/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8972214$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Klippel, Anke</creatorcontrib><creatorcontrib>Kavanaugh, W. Michael</creatorcontrib><creatorcontrib>Pot, David</creatorcontrib><creatorcontrib>Williams, Lewis T.</creatorcontrib><title>A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain</title><title>Molecular and Cellular Biology</title><addtitle>Mol Cell Biol</addtitle><description>Article Usage Stats
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</description><subject>Animals</subject><subject>Blood Proteins - genetics</subject><subject>COS Cells</subject><subject>Enzyme Activation</subject><subject>Inositol Polyphosphate 5-Phosphatases</subject><subject>Membranes, Artificial</subject><subject>Phosphatidylinositol 3-Kinases</subject><subject>Phosphatidylinositol Phosphates - metabolism</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Phosphoproteins</subject><subject>Phosphoric Monoester Hydrolases - metabolism</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - metabolism</subject><subject>Point Mutation</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Proto-Oncogene Proteins c-akt</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction - physiology</subject><issn>0270-7306</issn><issn>1098-5549</issn><issn>1098-5549</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkr2P1DAQxS0EOvYOOlokV1Rk8Ucc2wXFsuIA6RAN1JZjOxuzThxs507p-cPJaVcHFIhqpHm_N5rRGwBeYLTFmIg3g2m3mG_xllLxCGwwkqJirJaPwQYRjipOUfMUXOb8HSHUSEQvwIWQnBBcb8DPHcyTM77zBk4p2tkUGDs49TFPvS7eLsGPMfsSA6TV0Y86O2h9cqaEBWpT_K0uLsPSu3t_cX6EZ2p3LGs7xfnQQ18ynIIzx1zSSvRxiCEeFmjjoP34DDzpdMju-blegW_X77_uP1Y3Xz582u9uKsNqUSrHpBQE1ZpaiztSU0qYkY47qzHltiG2wVjWApvGCdeYrm2xQVgyanhLJaVX4O1p7jS3g7PGjSXpoKbkB50WFbVXfyuj79Uh3ipCMWdi9b86-1P8Mbtc1OCzcSHo0cU5Ky44Z7ym_wUxE4QKxFbw9Qk0KeacXPewDEbqPl31ef9OYa6wWtNd8Zd_HvAAn-NcdX7S_djFNOi7mIJVRS8hpi7p0fis6D8mw5Oz94f-bs1X6Tyo9bV-I78AfjfBxA</recordid><startdate>19970101</startdate><enddate>19970101</enddate><creator>Klippel, Anke</creator><creator>Kavanaugh, W. 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| fulltext | fulltext |
| identifier | ISSN: 0270-7306 |
| ispartof | Molecular and Cellular Biology, 1997-01, Vol.17 (1), p.338-344 |
| issn | 0270-7306 1098-5549 1098-5549 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78775743 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals Blood Proteins - genetics COS Cells Enzyme Activation Inositol Polyphosphate 5-Phosphatases Membranes, Artificial Phosphatidylinositol 3-Kinases Phosphatidylinositol Phosphates - metabolism Phosphatidylinositols - metabolism Phosphoproteins Phosphoric Monoester Hydrolases - metabolism Phosphotransferases (Alcohol Group Acceptor) - metabolism Point Mutation Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Proto-Oncogene Proteins c-akt Sequence Homology, Amino Acid Signal Transduction - physiology |
| title | A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain |
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