{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T11:21:30Z","timestamp":1768476090444,"version":"3.49.0"},"reference-count":75,"publisher":"Georg Thieme Verlag KG","issue":"04","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Horm Metab Res"],"published-print":{"date-parts":[[2017,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The cAMP-dependent protein kinase PKA is a well-characterized member of the\n                    serine-threonine protein AGC kinase family and is the effector kinase of cAMP\n                    signaling. As such, PKA is involved in the control of a wide variety of cellular\n                    processes including metabolism, cell growth, gene expression and apoptosis.\n                    cAMP-dependent PKA signaling pathways play important roles during infection and\n                    virulence of various pathogens. Since fluxes in cAMP are involved in multiple\n                    intracellular functions, a variety of different pathological infectious\n                    processes can be affected by PKA signaling pathways. Here, we highlight some\n                    features of cAMP-PKA signaling that are relevant to Plasmodium\n                    falciparum-infection of erythrocytes and present an update on AKAP targeting\n                    of PKA in PGE2 signaling via EP4 in Theileria annulata-infection of\n                    leukocytes and discuss cAMP-PKA signling in Toxoplasma.<\/jats:p>","DOI":"10.1055\/s-0042-118459","type":"journal-article","created":{"date-parts":[[2016,11,11]],"date-time":"2016-11-11T23:57:44Z","timestamp":1478908664000},"page":"296-300","source":"Crossref","is-referenced-by-count":9,"title":["PKA and Apicomplexan Parasite Diseases"],"prefix":"10.1055","volume":"49","author":[{"given":"M.","family":"Haidar","sequence":"additional","affiliation":[{"name":"Cochin Institute, Inserm U1016, CNRS UMR8104, Paris,\n                    France"},{"name":"Laboratoire de Biologie Cellulaire Comparative des Apicomplexes,\n                    Facult\u00e9 de M\u00e9decine, Universit\u00e9 Paris Descartes, Sorbonne Paris Cit\u00e9,\n                    France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Ramdani","sequence":"additional","affiliation":[{"name":"Cochin Institute, Inserm U1016, CNRS UMR8104, Paris,\n                    France"},{"name":"Laboratoire de Biologie Cellulaire Comparative des Apicomplexes,\n                    Facult\u00e9 de M\u00e9decine, Universit\u00e9 Paris Descartes, Sorbonne Paris Cit\u00e9,\n                    France"},{"name":"Departments of Medicine, University of California, San Diego, La Jolla,\n                    California, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E. J.","family":"Kennedy","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical and Biomedical Sciences, College of\n                    Pharmacy, University of Georgia, Athens, Georgia, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Langsley","sequence":"additional","affiliation":[{"name":"Cochin Institute, Inserm U1016, CNRS UMR8104, Paris,\n                    France"},{"name":"Laboratoire de Biologie Cellulaire Comparative des Apicomplexes,\n                    Facult\u00e9 de M\u00e9decine, Universit\u00e9 Paris Descartes, Sorbonne Paris Cit\u00e9,\n                    France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"194","published-online":{"date-parts":[[2016,11,11]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1146\/annurev.ph.56.030194.001321","article-title":"Structure and function of cyclic nucleotide-dependent protein kinases","volume":"56","author":"S H 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