Akt phosphorylation on Thr308 but not on Ser473 correlates with Akt protein kinase activity in human non-small cell lung cancer
Background: The activity of the protein kinase Akt is frequently dysregulated in cancer and is an important factor in the growth and survival of tumour cells. Akt activation involves the phosphorylation of two residues: threonine 308 (Thr308) in the activation loop and serine 473 (Ser473) in the C-t...
Gespeichert in:
| Veröffentlicht in: | British journal of cancer 2011-05, Vol.104 (11), p.1755-1761 |
|---|---|
| Hauptverfasser: | , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1761 |
|---|---|
| container_issue | 11 |
| container_start_page | 1755 |
| container_title | British journal of cancer |
| container_volume | 104 |
| creator | Vincent, E E Elder, D J E Thomas, E C Phillips, L Morgan, C Pawade, J Sohail, M May, M T Hetzel, M R Tavaré, J M |
| description | Background:
The activity of the protein kinase Akt is frequently dysregulated in cancer and is an important factor in the growth and survival of tumour cells. Akt activation involves the phosphorylation of two residues: threonine 308 (Thr308) in the activation loop and serine 473 (Ser473) in the C-terminal hydrophobic motif. Phosphorylation of Ser473 has been extensively studied in tumour samples as a correlate for Akt activity, yet the phosphorylation of Thr308 or of downstream Akt substrates is rarely assessed.
Methods:
The phosphorylation status of Thr308 and Ser473 was compared with that of three separate Akt substrates – PRAS40, TSC2 and TBC1D4 – in fresh frozen samples of early-stage human non-small cell lung cancer (NSCLC).
Results:
Akt Thr308 phosphorylation correlated with the phosphorylation of each Akt substrate tested, whereas Akt Ser473 phosphorylation did not correlate with the phosphorylation of any of the substrates examined.
Conclusion:
The phosphorylation of Thr308 is a more reliable biomarker for the protein kinase activity of Akt in tumour samples than Ser473. Any evaluation of the link between Akt phosphorylation or activity in tumour samples and the prediction or prognosis of disease should, therefore, focus on measuring the phosphorylation of Akt on Thr308 and/or at least one downstream Akt substrate, rather than Akt Ser473 phosphorylation alone. |
| doi_str_mv | 10.1038/bjc.2011.132 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3111153</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2356928161</sourcerecordid><originalsourceid>FETCH-LOGICAL-c588t-cc663f9366354ae69eec8d837617d5b5d87942194e3aa9a8e2285903e555634e3</originalsourceid><addsrcrecordid>eNptkctv1DAQxi0EokvhxhlZXLiQxY84cS5IVVUeUiUOlLPl9c5uvE3sxXZa7Yl_vRO2lIew_JBnfv48o4-Ql5wtOZP63WrnloJxvuRSPCILrqSouBbtY7JgjLUV6wQ7Ic9y3uG1Y7p9Sk4EV0zVii_Ij7PrQvd9zLjSYbDFx0BxXvVJMk1XU6EhljnyFVLdSupiSoAcZHrrS09_vk-xgA_02gebgVpX_I0vB4qhfhptQIlQ5dEOA3WA2zCFLXU2OEjPyZONHTK8uD9PybcPF1fnn6rLLx8_n59dVk5pXSrnmkZuOom7qi00HYDTay3bhrdrtVJr3Xa14F0N0trOahBCq45JUEo1EqOn5P1Rdz-tRlg7CCXZweyTH206mGi9-TsTfG-28cZIjkNJFHhzL5Di9wlyMaPPczc2QJyy0Y1ucbIaydf_kLs4pYDdzZDshKhn6O0RcinmnGDzUApnZvbVoK9m9tWgr4i_-rP8B_iXkQhURyBjKmwh_f70v4J3KXytcg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>868392244</pqid></control><display><type>article</type><title>Akt phosphorylation on Thr308 but not on Ser473 correlates with Akt protein kinase activity in human non-small cell lung cancer</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Springer Nature - Complete Springer Journals</source><source>Nature Journals Online</source><source>PubMed Central</source><creator>Vincent, E E ; Elder, D J E ; Thomas, E C ; Phillips, L ; Morgan, C ; Pawade, J ; Sohail, M ; May, M T ; Hetzel, M R ; Tavaré, J M</creator><creatorcontrib>Vincent, E E ; Elder, D J E ; Thomas, E C ; Phillips, L ; Morgan, C ; Pawade, J ; Sohail, M ; May, M T ; Hetzel, M R ; Tavaré, J M</creatorcontrib><description>Background:
The activity of the protein kinase Akt is frequently dysregulated in cancer and is an important factor in the growth and survival of tumour cells. Akt activation involves the phosphorylation of two residues: threonine 308 (Thr308) in the activation loop and serine 473 (Ser473) in the C-terminal hydrophobic motif. Phosphorylation of Ser473 has been extensively studied in tumour samples as a correlate for Akt activity, yet the phosphorylation of Thr308 or of downstream Akt substrates is rarely assessed.
Methods:
The phosphorylation status of Thr308 and Ser473 was compared with that of three separate Akt substrates – PRAS40, TSC2 and TBC1D4 – in fresh frozen samples of early-stage human non-small cell lung cancer (NSCLC).
Results:
Akt Thr308 phosphorylation correlated with the phosphorylation of each Akt substrate tested, whereas Akt Ser473 phosphorylation did not correlate with the phosphorylation of any of the substrates examined.
Conclusion:
The phosphorylation of Thr308 is a more reliable biomarker for the protein kinase activity of Akt in tumour samples than Ser473. Any evaluation of the link between Akt phosphorylation or activity in tumour samples and the prediction or prognosis of disease should, therefore, focus on measuring the phosphorylation of Akt on Thr308 and/or at least one downstream Akt substrate, rather than Akt Ser473 phosphorylation alone.</description><identifier>ISSN: 0007-0920</identifier><identifier>EISSN: 1532-1827</identifier><identifier>DOI: 10.1038/bjc.2011.132</identifier><identifier>PMID: 21505451</identifier><identifier>CODEN: BJCAAI</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/67/1059/602 ; 692/53 ; 692/699/67/1612/1350 ; Biomarkers ; Biomarkers, Tumor - analysis ; Biomedical and Life Sciences ; Biomedicine ; Cancer Research ; Carcinoma, Non-Small-Cell Lung - enzymology ; Drug Resistance ; Enzyme Activation ; Epidemiology ; Female ; Humans ; Kinases ; Lung cancer ; Lung Neoplasms - enzymology ; Male ; Medical prognosis ; Medical research ; Middle Aged ; Molecular Diagnostics ; Molecular Medicine ; Oncology ; Phosphorylation ; Protein Kinases - metabolism ; Proteins ; Proto-Oncogene Proteins c-akt - metabolism ; Serine - chemistry ; Threonine - chemistry</subject><ispartof>British journal of cancer, 2011-05, Vol.104 (11), p.1755-1761</ispartof><rights>The Author(s) 2011</rights><rights>Copyright Nature Publishing Group May 24, 2011</rights><rights>Copyright © 2011 Cancer Research UK 2011 Cancer Research UK</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c588t-cc663f9366354ae69eec8d837617d5b5d87942194e3aa9a8e2285903e555634e3</citedby><cites>FETCH-LOGICAL-c588t-cc663f9366354ae69eec8d837617d5b5d87942194e3aa9a8e2285903e555634e3</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/PMC3111153/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3111153/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,41469,42538,51300,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21505451$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vincent, E E</creatorcontrib><creatorcontrib>Elder, D J E</creatorcontrib><creatorcontrib>Thomas, E C</creatorcontrib><creatorcontrib>Phillips, L</creatorcontrib><creatorcontrib>Morgan, C</creatorcontrib><creatorcontrib>Pawade, J</creatorcontrib><creatorcontrib>Sohail, M</creatorcontrib><creatorcontrib>May, M T</creatorcontrib><creatorcontrib>Hetzel, M R</creatorcontrib><creatorcontrib>Tavaré, J M</creatorcontrib><title>Akt phosphorylation on Thr308 but not on Ser473 correlates with Akt protein kinase activity in human non-small cell lung cancer</title><title>British journal of cancer</title><addtitle>Br J Cancer</addtitle><addtitle>Br J Cancer</addtitle><description>Background:
The activity of the protein kinase Akt is frequently dysregulated in cancer and is an important factor in the growth and survival of tumour cells. Akt activation involves the phosphorylation of two residues: threonine 308 (Thr308) in the activation loop and serine 473 (Ser473) in the C-terminal hydrophobic motif. Phosphorylation of Ser473 has been extensively studied in tumour samples as a correlate for Akt activity, yet the phosphorylation of Thr308 or of downstream Akt substrates is rarely assessed.
Methods:
The phosphorylation status of Thr308 and Ser473 was compared with that of three separate Akt substrates – PRAS40, TSC2 and TBC1D4 – in fresh frozen samples of early-stage human non-small cell lung cancer (NSCLC).
Results:
Akt Thr308 phosphorylation correlated with the phosphorylation of each Akt substrate tested, whereas Akt Ser473 phosphorylation did not correlate with the phosphorylation of any of the substrates examined.
Conclusion:
The phosphorylation of Thr308 is a more reliable biomarker for the protein kinase activity of Akt in tumour samples than Ser473. Any evaluation of the link between Akt phosphorylation or activity in tumour samples and the prediction or prognosis of disease should, therefore, focus on measuring the phosphorylation of Akt on Thr308 and/or at least one downstream Akt substrate, rather than Akt Ser473 phosphorylation alone.</description><subject>631/67/1059/602</subject><subject>692/53</subject><subject>692/699/67/1612/1350</subject><subject>Biomarkers</subject><subject>Biomarkers, Tumor - analysis</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer Research</subject><subject>Carcinoma, Non-Small-Cell Lung - enzymology</subject><subject>Drug Resistance</subject><subject>Enzyme Activation</subject><subject>Epidemiology</subject><subject>Female</subject><subject>Humans</subject><subject>Kinases</subject><subject>Lung cancer</subject><subject>Lung Neoplasms - enzymology</subject><subject>Male</subject><subject>Medical prognosis</subject><subject>Medical research</subject><subject>Middle Aged</subject><subject>Molecular Diagnostics</subject><subject>Molecular Medicine</subject><subject>Oncology</subject><subject>Phosphorylation</subject><subject>Protein Kinases - metabolism</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins c-akt - metabolism</subject><subject>Serine - chemistry</subject><subject>Threonine - chemistry</subject><issn>0007-0920</issn><issn>1532-1827</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><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>eNptkctv1DAQxi0EokvhxhlZXLiQxY84cS5IVVUeUiUOlLPl9c5uvE3sxXZa7Yl_vRO2lIew_JBnfv48o4-Ql5wtOZP63WrnloJxvuRSPCILrqSouBbtY7JgjLUV6wQ7Ic9y3uG1Y7p9Sk4EV0zVii_Ij7PrQvd9zLjSYbDFx0BxXvVJMk1XU6EhljnyFVLdSupiSoAcZHrrS09_vk-xgA_02gebgVpX_I0vB4qhfhptQIlQ5dEOA3WA2zCFLXU2OEjPyZONHTK8uD9PybcPF1fnn6rLLx8_n59dVk5pXSrnmkZuOom7qi00HYDTay3bhrdrtVJr3Xa14F0N0trOahBCq45JUEo1EqOn5P1Rdz-tRlg7CCXZweyTH206mGi9-TsTfG-28cZIjkNJFHhzL5Di9wlyMaPPczc2QJyy0Y1ucbIaydf_kLs4pYDdzZDshKhn6O0RcinmnGDzUApnZvbVoK9m9tWgr4i_-rP8B_iXkQhURyBjKmwh_f70v4J3KXytcg</recordid><startdate>20110524</startdate><enddate>20110524</enddate><creator>Vincent, E E</creator><creator>Elder, D J E</creator><creator>Thomas, E C</creator><creator>Phillips, L</creator><creator>Morgan, C</creator><creator>Pawade, J</creator><creator>Sohail, M</creator><creator>May, M T</creator><creator>Hetzel, M R</creator><creator>Tavaré, J M</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>3V.</scope><scope>7RV</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AN0</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>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110524</creationdate><title>Akt phosphorylation on Thr308 but not on Ser473 correlates with Akt protein kinase activity in human non-small cell lung cancer</title><author>Vincent, E E ; Elder, D J E ; Thomas, E C ; Phillips, L ; Morgan, C ; Pawade, J ; Sohail, M ; May, M T ; Hetzel, M R ; Tavaré, J M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c588t-cc663f9366354ae69eec8d837617d5b5d87942194e3aa9a8e2285903e555634e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>631/67/1059/602</topic><topic>692/53</topic><topic>692/699/67/1612/1350</topic><topic>Biomarkers</topic><topic>Biomarkers, Tumor - analysis</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cancer Research</topic><topic>Carcinoma, Non-Small-Cell Lung - enzymology</topic><topic>Drug Resistance</topic><topic>Enzyme Activation</topic><topic>Epidemiology</topic><topic>Female</topic><topic>Humans</topic><topic>Kinases</topic><topic>Lung cancer</topic><topic>Lung Neoplasms - enzymology</topic><topic>Male</topic><topic>Medical prognosis</topic><topic>Medical research</topic><topic>Middle Aged</topic><topic>Molecular Diagnostics</topic><topic>Molecular Medicine</topic><topic>Oncology</topic><topic>Phosphorylation</topic><topic>Protein Kinases - metabolism</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins c-akt - metabolism</topic><topic>Serine - chemistry</topic><topic>Threonine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vincent, E E</creatorcontrib><creatorcontrib>Elder, D J E</creatorcontrib><creatorcontrib>Thomas, E C</creatorcontrib><creatorcontrib>Phillips, L</creatorcontrib><creatorcontrib>Morgan, C</creatorcontrib><creatorcontrib>Pawade, J</creatorcontrib><creatorcontrib>Sohail, M</creatorcontrib><creatorcontrib>May, M T</creatorcontrib><creatorcontrib>Hetzel, M R</creatorcontrib><creatorcontrib>Tavaré, J M</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Nursing & Allied Health Database</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>British Nursing Database</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>British journal of cancer</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vincent, E E</au><au>Elder, D J E</au><au>Thomas, E C</au><au>Phillips, L</au><au>Morgan, C</au><au>Pawade, J</au><au>Sohail, M</au><au>May, M T</au><au>Hetzel, M R</au><au>Tavaré, J M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Akt phosphorylation on Thr308 but not on Ser473 correlates with Akt protein kinase activity in human non-small cell lung cancer</atitle><jtitle>British journal of cancer</jtitle><stitle>Br J Cancer</stitle><addtitle>Br J Cancer</addtitle><date>2011-05-24</date><risdate>2011</risdate><volume>104</volume><issue>11</issue><spage>1755</spage><epage>1761</epage><pages>1755-1761</pages><issn>0007-0920</issn><eissn>1532-1827</eissn><coden>BJCAAI</coden><abstract>Background:
The activity of the protein kinase Akt is frequently dysregulated in cancer and is an important factor in the growth and survival of tumour cells. Akt activation involves the phosphorylation of two residues: threonine 308 (Thr308) in the activation loop and serine 473 (Ser473) in the C-terminal hydrophobic motif. Phosphorylation of Ser473 has been extensively studied in tumour samples as a correlate for Akt activity, yet the phosphorylation of Thr308 or of downstream Akt substrates is rarely assessed.
Methods:
The phosphorylation status of Thr308 and Ser473 was compared with that of three separate Akt substrates – PRAS40, TSC2 and TBC1D4 – in fresh frozen samples of early-stage human non-small cell lung cancer (NSCLC).
Results:
Akt Thr308 phosphorylation correlated with the phosphorylation of each Akt substrate tested, whereas Akt Ser473 phosphorylation did not correlate with the phosphorylation of any of the substrates examined.
Conclusion:
The phosphorylation of Thr308 is a more reliable biomarker for the protein kinase activity of Akt in tumour samples than Ser473. Any evaluation of the link between Akt phosphorylation or activity in tumour samples and the prediction or prognosis of disease should, therefore, focus on measuring the phosphorylation of Akt on Thr308 and/or at least one downstream Akt substrate, rather than Akt Ser473 phosphorylation alone.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>21505451</pmid><doi>10.1038/bjc.2011.132</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0007-0920 |
| ispartof | British journal of cancer, 2011-05, Vol.104 (11), p.1755-1761 |
| issn | 0007-0920 1532-1827 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3111153 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Springer Nature - Complete Springer Journals; Nature Journals Online; PubMed Central |
| subjects | 631/67/1059/602 692/53 692/699/67/1612/1350 Biomarkers Biomarkers, Tumor - analysis Biomedical and Life Sciences Biomedicine Cancer Research Carcinoma, Non-Small-Cell Lung - enzymology Drug Resistance Enzyme Activation Epidemiology Female Humans Kinases Lung cancer Lung Neoplasms - enzymology Male Medical prognosis Medical research Middle Aged Molecular Diagnostics Molecular Medicine Oncology Phosphorylation Protein Kinases - metabolism Proteins Proto-Oncogene Proteins c-akt - metabolism Serine - chemistry Threonine - chemistry |
| title | Akt phosphorylation on Thr308 but not on Ser473 correlates with Akt protein kinase activity in human non-small cell lung cancer |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T01%3A56%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Akt%20phosphorylation%20on%20Thr308%20but%20not%20on%20Ser473%20correlates%20with%20Akt%20protein%20kinase%20activity%20in%20human%20non-small%20cell%20lung%20cancer&rft.jtitle=British%20journal%20of%20cancer&rft.au=Vincent,%20E%20E&rft.date=2011-05-24&rft.volume=104&rft.issue=11&rft.spage=1755&rft.epage=1761&rft.pages=1755-1761&rft.issn=0007-0920&rft.eissn=1532-1827&rft.coden=BJCAAI&rft_id=info:doi/10.1038/bjc.2011.132&rft_dat=%3Cproquest_pubme%3E2356928161%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=868392244&rft_id=info:pmid/21505451&rfr_iscdi=true |