{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,31]],"date-time":"2026-10-31T11:32:57Z","timestamp":1793446377245,"version":"4.5.0"},"reference-count":46,"publisher":"Oxford University Press (OUP)","issue":"1","license":[{"start":{"date-parts":[[2017,10,16]],"date-time":"2017-10-16T00:00:00Z","timestamp":1508112000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000274","name":"British Heart Foundation","doi-asserted-by":"publisher","award":["#PG\/10\/045\/28276"],"award-info":[{"award-number":["#PG\/10\/045\/28276"]}],"id":[{"id":"10.13039\/501100000274","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2018,1,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Aims<\/jats:title>\n                  <jats:p>PKN1 is a stress-responsive protein kinase acting downstream of small GTP-binding proteins of the Rho\/Rac family. The aim was to determine its role in endogenous cardioprotection.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Methods and results<\/jats:title>\n                  <jats:p>Hearts from PKN1 knockout (KO) or wild type (WT) littermate control mice were perfused in Langendorff mode and subjected to global ischaemia and reperfusion (I\/R). Myocardial infarct size was doubled in PKN1 KO hearts compared to WT hearts. PKN1 was basally phosphorylated on the activation loop Thr778 PDK1 target site which was unchanged during I\/R. However, phosphorylation of p42\/p44-MAPK was decreased in KO hearts at baseline and during I\/R. In cultured neonatal rat ventricular cardiomyocytes (NRVM) and NRVM transduced with kinase dead (KD) PKN1 K644R mutant subjected to simulated ischaemia\/reperfusion (sI\/R), PhosTag\u00ae gel analysis showed net dephosphorylation of PKN1 during sI and early R despite Thr778 phosphorylation. siRNA knockdown of PKN1 in NRVM significantly decreased cell survival and increased cell injury by sI\/R which was reversed by WT- or KD-PKN1 expression. Confocal immunofluorescence analysis of PKN1 in NRVM showed increased localization to the sarcoplasmic reticulum (SR) during sI. GC-MS\/MS and immunoblot analysis of PKN1 immunoprecipitates following sI\/R confirmed interaction with CamKII\u03b4. Co-translocation of PKN1 and CamKII\u03b4 to the SR\/membrane fraction during sI correlated with phospholamban (PLB) Thr17 phosphorylation. siRNA knockdown of PKN1 in NRVM resulted in increased basal CamKII\u03b4 activation and increased PLB Thr17 phosphorylation only during sI. In vivo PLB Thr17 phosphorylation, Sarco-Endoplasmic Reticulum Ca2+ ATPase (SERCA2) expression and Junctophilin-2 (Jph2) expression were also basally increased in PKN1 KO hearts. Furthermore, in vivo P-V loop analysis of the beat-to-beat relationship between rate of LV pressure development or relaxation and end diastolic P (EDP) showed mild but significant systolic and diastolic dysfunction with preserved ejection fraction in PKN1 KO hearts.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Conclusion<\/jats:title>\n                  <jats:p>Loss of PKN1 in vivo significantly reduces endogenous cardioprotection and increases myocardial infarct size following I\/R injury. Cardioprotection by PKN1 is associated with reduced CamKII\u03b4-dependent PLB Thr17 phosphorylation at the SR and therefore may stabilize the coupling of SR Ca2+ handling and contractile function, independent of its kinase activity.<\/jats:p>\n               <\/jats:sec>","DOI":"10.1093\/cvr\/cvx206","type":"journal-article","created":{"date-parts":[[2017,10,13]],"date-time":"2017-10-13T15:14:06Z","timestamp":1507907646000},"page":"138-157","source":"Crossref","is-referenced-by-count":18,"title":["Loss of Protein Kinase Novel 1 (PKN1) is associated with mild systolic and\n diastolic contractile dysfunction, increased phospholamban Thr17\n phosphorylation, and exacerbated ischaemia-reperfusion injury"],"prefix":"10.1093","volume":"114","author":[{"given":"Asvi A","family":"Francois","sequence":"first","affiliation":[{"name":"Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King\u2019s College London, St Thomas\u2019s Hospital, Lambeth Palace Road, London, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kofo","family":"Obasanjo-Blackshire","sequence":"additional","affiliation":[{"name":"Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King\u2019s College London, St Thomas\u2019s Hospital, Lambeth Palace Road, London, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James E","family":"Clark","sequence":"additional","affiliation":[{"name":"Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King\u2019s College London, St Thomas\u2019s Hospital, Lambeth Palace Road, London, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrii","family":"Boguslavskyi","sequence":"additional","affiliation":[{"name":"Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King\u2019s College London, St Thomas\u2019s Hospital, Lambeth Palace Road, London, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark R","family":"Holt","sequence":"additional","affiliation":[{"name":"Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King\u2019s College London, St Thomas\u2019s Hospital, Lambeth Palace Road, London, UK"},{"name":"Randall Division of Cell and Molecular Biophysics, King\u2019s College London, New Hunt\u2019s House, Guy\u2019s Hospital Campus, London, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter J","family":"Parker","sequence":"additional","affiliation":[{"name":"Division of Cancer Studies, School of Cancer and Pharmaceutical Sciences, Faculty of Life Sciences and Medicine, King\u2019s College London, New Hunt\u2019s House, Guy\u2019s Hospital Campus, London, UK"},{"name":"Protein Phosphorylation Laboratory, Francis Crick Institute, Lincoln\u2019s Inn Fields, London, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael S","family":"Marber","sequence":"additional","affiliation":[{"name":"Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King\u2019s College London, St Thomas\u2019s Hospital, Lambeth Palace Road, London, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard J","family":"Heads","sequence":"additional","affiliation":[{"name":"Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King\u2019s College London, St Thomas\u2019s Hospital, Lambeth Palace Road, London, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2017,10,16]]},"reference":[{"key":"2019091808525501000_cvx206-B1","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1177\/1074248413494814","article-title":"Role of protein kinase C in ischemic \u2018conditioning\u2019: from first evidence to\n current perspectives","volume":"18","author":"Simkhovich","year":"2013","journal-title":"J Cardiovasc Pharmacol\n Ther"},{"key":"2019091808525501000_cvx206-B2","first-page":"H1468","article-title":"PKC-dependent activation of p44\/p42 MAPKs during myocardial\n ischemia-reperfusion in conscious rabbits","volume":"276","author":"Ping","year":"1999","journal-title":"Am J\n Physiol"},{"key":"2019091808525501000_cvx206-B3","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1042\/bj3500891","article-title":"Sustained activation of p42\/p44 mitogen-activated protein kinase during\n recovery from simulated ischaemia mediates adaptive cytoprotection in\n cardiomyocytes","volume":"350","author":"Punn","year":"2000","journal-title":"Biochem\n J"},{"key":"2019091808525501000_cvx206-B4","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1006\/bbrc.2000.2522","article-title":"Activation of Akt during simulated ischemia\/reperfusion in cardiac\n myocytes","volume":"270","author":"Mockridge","year":"2000","journal-title":"Biochem Biophys Res\n Commun"},{"key":"2019091808525501000_cvx206-B5","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/j.cardiores.2004.04.011","article-title":"Cross-talk between the survival kinases during early reperfusion: its\n contribution to ischemic preconditioning","volume":"63","author":"Hausenloy","year":"2004","journal-title":"Cardiovasc\n Res"},{"key":"2019091808525501000_cvx206-B6","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/0014-5793(94)01202-4","article-title":"Identification of multiple, novel, protein kinase C-related gene\n products","volume":"356","author":"Palmer","year":"1994","journal-title":"FEBS\n Lett"},{"key":"2019091808525501000_cvx206-B7","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1006\/bbrc.1994.1313","article-title":"A novel protein kinase with leucine zipper-like sequences: its catalytic\n domain is highly homologous to that of protein kinase C","volume":"199","author":"Mukai","year":"1994","journal-title":"Biochem\n Biophys Res\n Commun"},{"key":"2019091808525501000_cvx206-B8","doi-asserted-by":"crossref","first-page":"28772","DOI":"10.1074\/jbc.271.46.28772","article-title":"Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and\n potential effector of Rho protein signaling","volume":"271","author":"Quilliam","year":"1996","journal-title":"J Biol\n Chem"},{"key":"2019091808525501000_cvx206-B9","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1042\/bj3320281","article-title":"The extended protein kinase C superfamily","volume":"332","author":"Mellor","year":"1998","journal-title":"Biochem\n J"},{"key":"2019091808525501000_cvx206-B10","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1126\/science.271.5249.648","article-title":"Identification of a putative target for Rho as the serine-threonine kinase\n protein kinase N","volume":"271","author":"Amano","year":"1996","journal-title":"Science"},{"key":"2019091808525501000_cvx206-B11","doi-asserted-by":"crossref","first-page":"2247","DOI":"10.1128\/MCB.17.4.2247","article-title":"The PRK2 kinase is a potential effector target of both Rho and Rac GTPases\n and regulates actin cytoskeletal organization","volume":"17","author":"Vincent","year":"1997","journal-title":"Mol Cell\n Biol"},{"key":"2019091808525501000_cvx206-B12","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1126\/science.271.5249.645","article-title":"Protein kinase N (PKN) and PKN-related protein rhophilin as targets of\n small GTPase Rho","volume":"271","author":"Watanabe","year":"1996","journal-title":"Science"},{"key":"2019091808525501000_cvx206-B13","doi-asserted-by":"crossref","first-page":"2698","DOI":"10.1074\/jbc.273.5.2698","article-title":"Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1\n repeat motif","volume":"273","author":"Flynn","year":"1998","journal-title":"J Biol\n Chem"},{"key":"2019091808525501000_cvx206-B14","doi-asserted-by":"crossref","first-page":"11064","DOI":"10.1074\/jbc.275.15.11064","article-title":"Rho GTPase control of protein kinase C-related protein kinase activation by\n 3-phosphoinositide-dependent protein kinase","volume":"275","author":"Flynn","year":"2000","journal-title":"J Biol\n Chem"},{"key":"2019091808525501000_cvx206-B15","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/S0014-5793(00)02162-1","article-title":"Further evidence that 3-phosphoinositide-dependent protein kinase-1 (PDK1)\n is required for the stability and phosphorylation of protein kinase C (PKC)\n isoforms","volume":"484","author":"Balendran","year":"2000","journal-title":"FEBS\n Lett"},{"key":"2019091808525501000_cvx206-B16","doi-asserted-by":"crossref","first-page":"20806","DOI":"10.1074\/jbc.M000421200","article-title":"A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is\n required for the phosphorylation of protein kinase Czeta (PKCzeta) and PKC-related\n kinase 2 by PDK1","volume":"275","author":"Balendran","year":"2000","journal-title":"J Biol\n Chem"},{"key":"2019091808525501000_cvx206-B17","doi-asserted-by":"crossref","first-page":"32233","DOI":"10.1074\/jbc.271.50.32233","article-title":"Phosphorylation events associated with different states of activation of a\n hepatic cardiolipin\/protease-activated protein kinase. Structural identity to the\n protein kinase N-type protein kinases","volume":"271","author":"Peng","year":"1996","journal-title":"J Biol\n Chem"},{"key":"2019091808525501000_cvx206-B18","doi-asserted-by":"crossref","first-page":"32344","DOI":"10.1074\/jbc.M303532200","article-title":"Hyperosmotic-induced protein kinase N 1 activation in a vesicular\n compartment is dependent upon Rac1 and 3-phosphoinositide-dependent kinase\n 1","volume":"278","author":"Torbett","year":"2003","journal-title":"J Biol\n Chem"},{"key":"2019091808525501000_cvx206-B19","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1096\/fj.04-1876fje","article-title":"Signaling via a novel integral plasma membrane pool of a serine\/threonine\n protein kinase PRK1 in mammalian cells","volume":"18","author":"Zhu","year":"2004","journal-title":"Faseb\n J"},{"key":"2019091808525501000_cvx206-B20","doi-asserted-by":"crossref","first-page":"H191","DOI":"10.1152\/ajpheart.00232.2010","article-title":"Hypotonic swelling-induced activation of PKN1 mediates cell survival in\n cardiac myocytes","volume":"300","author":"Kajimoto","year":"2011","journal-title":"Am J Physiol Heart Circ\n Physiol"},{"key":"2019091808525501000_cvx206-B21","doi-asserted-by":"crossref","first-page":"29449","DOI":"10.1074\/jbc.272.47.29449","article-title":"Specific proteolysis of the kinase protein kinase C-related kinase 2 by\n caspase-3 during apoptosis. Identification by a novel, small pool expression cloning\n strategy","volume":"272","author":"Cryns","year":"1997","journal-title":"J Biol\n Chem"},{"key":"2019091808525501000_cvx206-B22","first-page":"29","article-title":"Induction of a 55-kDa PKN cleavage product by ischemia\/reperfusion model in\n the rat retina","volume":"41","author":"Sumioka","year":"2000","journal-title":"Invest Ophthalmol Vis\n Sci"},{"key":"2019091808525501000_cvx206-B23","doi-asserted-by":"crossref","first-page":"10195","DOI":"10.1073\/pnas.93.19.10195","article-title":"Translocation of PKN from the cytosol to the nucleus induced by\n stresses","volume":"93","author":"Mukai","year":"1996","journal-title":"Proc Natl Acad Sci\n USA"},{"key":"2019091808525501000_cvx206-B24","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1161\/CIRCRESAHA.110.217554","article-title":"Activation of PKN mediates survival of cardiac myocytes in the heart during\n ischemia\/reperfusion","volume":"107","author":"Takagi","year":"2010","journal-title":"Circ\n Res"},{"key":"2019091808525501000_cvx206-B25","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1016\/j.celrep.2015.12.049","article-title":"Knockout of the PKN family of Rho effector kinases reveals a non-redundant\n role for PKN2 in developmental mesoderm expansion","volume":"14","author":"Quetier","year":"2016","journal-title":"Cell\n Rep"},{"key":"2019091808525501000_cvx206-B26","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.vascn.2008.10.007","article-title":"Measuring left ventricular function in the normal, infarcted and\n CORM-3-preconditioned mouse heart using complex admittance-derived pressure volume\n loops","volume":"59","author":"Clark","year":"2009","journal-title":"J Pharmacol Toxicol\n Methods"},{"key":"2019091808525501000_cvx206-B27","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1007\/BF01457397","article-title":"The role of the sarcoplasmic reticulum in various types of\n cardiomyocytes","volume":"130","author":"Chiesi","year":"1994","journal-title":"Mol Cell\n Biochem"},{"key":"2019091808525501000_cvx206-B28","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1054\/ceca.2001.0249","article-title":"Calcium signaling mechanisms in dedifferentiated cardiac myocytes:\n comparison with neonatal and adult cardiomyocytes","volume":"30","author":"Poindexter","year":"2001","journal-title":"Cell\n Calcium"},{"key":"2019091808525501000_cvx206-B29","doi-asserted-by":"crossref","first-page":"96.","DOI":"10.3389\/fphar.2014.00096","article-title":"CaMKII-dependent responses to ischemia and reperfusion challenges in the\n heart","volume":"5","author":"Bell","year":"2014","journal-title":"Front\n Pharmacol"},{"key":"2019091808525501000_cvx206-B30","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1161\/CIRCRESAHA.109.207423","article-title":"Phospholamban ablation rescues sarcoplasmic reticulum Ca(2+) handling but\n exacerbates cardiac dysfunction in CaMKIIdelta\u00a9 transgenic mice","volume":"106","author":"Zhang","year":"2010","journal-title":"Circ\n Res"},{"key":"2019091808525501000_cvx206-B31","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.yjmcc.2014.06.004","article-title":"CaMKII-dependent phosphorylation of cardiac ryanodine receptors regulates\n cell death in cardiac ischemia\/reperfusion injury","volume":"74","author":"Di Carlo","year":"2014","journal-title":"J Mol Cell\n Cardiol"},{"key":"2019091808525501000_cvx206-B32","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1093\/cvr\/cvv153","article-title":"Late INa increases diastolic SR-Ca2+-leak in atrial myocardium by\n activating PKA and CaMKII","volume":"107","author":"Fischer","year":"2015","journal-title":"Cardiovasc\n Res"},{"key":"2019091808525501000_cvx206-B33","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.ijcard.2011.02.038","article-title":"Ca2+\/calmodulin-dependent protein kinase inhibition suppresses\n post-ischemic arrhythmogenesis and mediates sinus bradycardic recovery in\n reperfusion","volume":"159","author":"Bell","year":"2012","journal-title":"Int J\n Cardiol"},{"key":"2019091808525501000_cvx206-B34","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1038\/nature11444","article-title":"CaMKII determines mitochondrial stress responses in heart","volume":"491","author":"Joiner","year":"2012","journal-title":"Nature"},{"key":"2019091808525501000_cvx206-B35","doi-asserted-by":"crossref","first-page":"H3065","DOI":"10.1152\/ajpheart.00353.2006","article-title":"Calmodulin kinase II inhibition protects against myocardial cell apoptosis\n in vivo","volume":"291","author":"Yang","year":"2006","journal-title":"Am J Physiol Heart Circ\n Physiol"},{"key":"2019091808525501000_cvx206-B36","doi-asserted-by":"crossref","first-page":"2478","DOI":"10.1111\/j.1582-4934.2010.01249.x","article-title":"Interplay between Ca2+ cycling and mitochondrial permeability transition\n pores promotes reperfusion-induced injury of cardiac myocytes","volume":"15","author":"Abdallah","year":"2011","journal-title":"J\n Cell Mol\n Med"},{"key":"2019091808525501000_cvx206-B37","doi-asserted-by":"crossref","first-page":"15271","DOI":"10.1073\/pnas.1521051112","article-title":"Intensity matters: Ryanodine receptor regulation during\n exercise","volume":"112","author":"Kohl","year":"2015","journal-title":"Proc Natl Acad Sci\n USA"},{"key":"2019091808525501000_cvx206-B38","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1113\/jphysiol.2012.243279","article-title":"Ca2+-dependent proteolysis of junctophilin-1 and junctophilin-2 in skeletal\n and cardiac muscle","volume":"591","author":"Murphy","year":"2013","journal-title":"J\n Physiol"},{"key":"2019091808525501000_cvx206-B39","doi-asserted-by":"crossref","first-page":"17946","DOI":"10.1074\/jbc.M115.652396","article-title":"Molecular determinants of calpain-dependent cleavage of junctophilin-2\n protein in cardiomyocytes","volume":"290","author":"Guo","year":"2015","journal-title":"J Biol\n Chem"},{"key":"2019091808525501000_cvx206-B40","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1023\/B:MCBI.0000041854.72511.14","article-title":"Phosphorylation of phospholamban in ischemia-reperfusion injury: functional\n role of Thr17 residue","volume":"263","author":"Mattiazzi","year":"2004","journal-title":"Mol Cell\n Biochem"},{"key":"2019091808525501000_cvx206-B41","doi-asserted-by":"crossref","first-page":"13187.","DOI":"10.1038\/ncomms13187","article-title":"Disulfide-activated protein kinase G Ialpha regulates cardiac diastolic\n relaxation and fine-tunes the Frank-Starling response","volume":"7","author":"Scotcher","year":"2016","journal-title":"Nat\n Comms"},{"key":"2019091808525501000_cvx206-B42","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1093\/cvr\/cvu163","article-title":"Delayed phospholamban phosphorylation in post-conditioned heart favours\n Ca2+ normalization and contributes to protection","volume":"103","author":"Inserte","year":"2014","journal-title":"Cardiovasc\n Res"},{"key":"2019091808525501000_cvx206-B43","doi-asserted-by":"crossref","first-page":"e9350.","DOI":"10.1371\/journal.pone.0009350","article-title":"PI3Kgamma protects from myocardial ischemia and reperfusion injury through\n a kinase-independent pathway","volume":"5","author":"Haubner","year":"2010","journal-title":"PLoS\n One"},{"key":"2019091808525501000_cvx206-B44","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1093\/cvr\/cvu024","article-title":"B-RAF and its novel negative regulator reticulocalbin 1 (RCN1) modulates\n cardiomyocyte hypertrophy","volume":"102","author":"Kramann","year":"2014","journal-title":"Cardiovasc\n Res"},{"key":"2019091808525501000_cvx206-B45","doi-asserted-by":"crossref","first-page":"7925","DOI":"10.1074\/jbc.M110.185645","article-title":"A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling complex\n involved in alpha1-adrenergic receptor-induced p38 activation","volume":"286","author":"Cariolato","year":"2011","journal-title":"J\n Biol\n Chem"},{"key":"2019091808525501000_cvx206-B46","doi-asserted-by":"crossref","first-page":"2903","DOI":"10.1128\/MCB.00031-13","article-title":"A-kinase anchoring protein Lbc coordinates a p38 activating signaling\n complex controlling compensatory cardiac hypertrophy","volume":"33","author":"Perez Lopez","year":"2013","journal-title":"Mol Cell\n Biol"}],"container-title":["Cardiovascular Research"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/cardiovascres\/article-pdf\/114\/1\/138\/30033730\/cvx206.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,9,18]],"date-time":"2019-09-18T08:53:18Z","timestamp":1568796798000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/cardiovascres\/article\/114\/1\/138\/4554420"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,10,16]]},"references-count":46,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2017,10,16]]},"published-print":{"date-parts":[[2018,1,1]]}},"URL":"https:\/\/doi.org\/10.1093\/cvr\/cvx206","relation":{},"ISSN":["0008-6363","1755-3245"],"issn-type":[{"value":"0008-6363","type":"print"},{"value":"1755-3245","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2018,1,1]]},"published":{"date-parts":[[2017,10,16]]}}}