{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T10:49:59Z","timestamp":1758278999007,"version":"3.44.0"},"reference-count":66,"publisher":"Elsevier BV","issue":"4-5","license":[{"start":{"date-parts":[[1982,10,1]],"date-time":"1982-10-01T00:00:00Z","timestamp":402278400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[1982,10,1]],"date-time":"1982-10-01T00:00:00Z","timestamp":402278400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell Calcium"],"published-print":{"date-parts":[[1982,10]]},"DOI":"10.1016\/0143-4160(82)90018-5","type":"journal-article","created":{"date-parts":[[2004,4,17]],"date-time":"2004-04-17T11:47:08Z","timestamp":1082202428000},"page":"295-309","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":55,"title":["The enzymology of stimulated inositol lipid turnover"],"prefix":"10.1016","volume":"3","author":[{"given":"R.F.","family":"Irvine","sequence":"first","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/0143-4160(82)90018-5_BIB1","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/S0074-7696(08)60272-7","article-title":"Dynamic aspects of phospholipids during protein secretion","volume":"23","author":"Hokin","year":"1968","journal-title":"Int. Rev. Cytol."},{"key":"10.1016\/0143-4160(82)90018-5_BIB2","first-page":"123","article-title":"The stimulation of inositol lipid metabolism that accompanies calcium mobilization in stimulated cells: defined characteristics and unanswered questions","volume":"B296","author":"Michell","year":"1981","journal-title":"Phil. Trans. Roy. Soc. Lond."},{"key":"10.1016\/0143-4160(82)90018-5_BIB3","first-page":"131","article-title":"The intermediary metabolism of thyroid tissue","volume":"Vol. 1","author":"Freinkel","year":"1964"},{"key":"10.1016\/0143-4160(82)90018-5_BIB4","first-page":"301","article-title":"Stimulated phosphatidylinositol turnover, a brief appraisal","volume":"Vol. 2","author":"Irvine","year":"1982"},{"key":"10.1016\/0143-4160(82)90018-5_BIB5","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1042\/bj2040003","article-title":"How is the level of free arachidonic acid controlled in mammalian cells?","volume":"204","author":"Irvine","year":"1982","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB6","doi-asserted-by":"crossref","first-page":"4718","DOI":"10.1016\/S0021-9258(19)41361-6","article-title":"The role of calcium in regulation of cyclic nucleotide content in human umbilical artery","volume":"250","author":"Clyman","year":"1975","journal-title":"J. Biol. Chem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB7","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/0304-4157(75)90017-9","article-title":"Inositol phospholipids in membrane function","volume":"415","author":"Michell","year":"1975","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB8","doi-asserted-by":"crossref","first-page":"5215","DOI":"10.1016\/S0021-9258(19)69389-0","article-title":"The activation of phosphatidyl-inositol-hydrolyzing phospholipase A2 during prostaglandin synthesis in transformed mouse BALB3T3 cells","volume":"256","author":"Hong","year":"1981","journal-title":"J. Biol. Chem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB9","doi-asserted-by":"crossref","first-page":"11463","DOI":"10.1016\/S0021-9258(19)86508-0","article-title":"Specificity of phospholipases in methylcholanthrene-transformed mouse fibroblasts activated by bradykinin, thrombin, serum, and ionophore A23187","volume":"254","author":"Hong","year":"1979","journal-title":"J. Biol. Chem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB10","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1042\/bj2040361","article-title":"Phosphatidylinositol hydrolysing enzymes in blowfly salivary glands","volume":"204","author":"Irvine","year":"1982","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB11","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1042\/bj1820599","article-title":"Hydrolysis of membrane phospholipids by phospholipases of rat liver lysosomes","volume":"182","author":"Richards","year":"1979","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB12","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1016\/S0021-9258(19)86225-7","article-title":"Properties of a phospholipase C isolated from rat liver lysosomes","volume":"254","author":"Matsuzawa","year":"1980","journal-title":"J. Biol. Chem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB13","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1007\/BF02535031","article-title":"Endogenous lipolytic activities during autolysis of highly enriched hepatic lysosomes","volume":"16","author":"Beckman","year":"1981","journal-title":"Lipids"},{"key":"10.1016\/0143-4160(82)90018-5_BIB14","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/0006-3002(59)90499-8","article-title":"Studies on the enzymic hydrolysis of monophosphoinositides by phospholipase preparations from P. notatum and ox pancreas","volume":"33","author":"Dawson","year":"1959","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB15","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1042\/bj0790193","article-title":"Phosphoinositides 3. Enzymic hydrolysis of inositol-containing phospholipids","volume":"79","author":"Kemp","year":"1961","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB16","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.1016\/0024-3205(82)90016-9","article-title":"Phosphatidylinositol specific phospholipase C","volume":"30","author":"Shukla","year":"1982","journal-title":"Life Sciences"},{"key":"10.1016\/0143-4160(82)90018-5_BIB17","series-title":"Form and Function of Phospholipids","first-page":"97","article-title":"Specificity of enzymes involved in the metabolism of phospholipids","author":"Dawson","year":"1973"},{"key":"10.1016\/0143-4160(82)90018-5_BIB18","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/0005-2760(81)90007-2","article-title":"Degradation of phosphatidyl-inositol by soluble enzymes of rat gastric mucosa","volume":"665","author":"Wassef","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB19","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/0005-2760(82)90030-3","article-title":"Phospholipase activities of rat brain cytosol. Occurance of phospholipase C activity with phosphatidylcholine","volume":"711","author":"Edgar","year":"1982","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB20","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1172\/JCI109339","article-title":"Production of diglyceride from phosphatidylinositol in activated human platelets","volume":"63","author":"Rittenhouse-Simmons","year":"1979","journal-title":"J. Clin. Invest."},{"key":"10.1016\/0143-4160(82)90018-5_BIB21","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1042\/bj1780045","article-title":"Relationship between hormonal activation of phosphatidylinositol hydrolysis, fluid secretion, and calcium flux in the blowfly salivary gland","volume":"178","author":"Fain","year":"1979","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB22","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1111\/j.1471-4159.1969.tb10376.x","article-title":"The enzymic hydrolysis of phosphatidylinositol by guinea-pig brain: Subcellular distribution and hydrolysis products","volume":"16","author":"Friedel","year":"1969","journal-title":"J. Neurochem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB23","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1042\/bj1310433","article-title":"A membrane-bound activity catalysing phosphatidylinositol breakdown to 1,2-diacylglycerol, D-myoinositol 1:2 cyclic phosphate, and D-myoinositol 1-phosphate","volume":"131","author":"Lapetina","year":"1973","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB24","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1111\/j.1471-4159.1978.tb06568.x","article-title":"The distribution of calcium-dependent phosphatidylinositol-specific phosphodiesterase in rat brain","volume":"31","author":"Irvine","year":"1978","journal-title":"J. Neurochem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB25","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/0005-2744(80)90232-6","article-title":"Studies on the properties of a soluble phosphatidylinositol-phosphodiesterase of rabbit iris smooth muscle","volume":"614","author":"Abdel-Latif","year":"1980","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB26","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1042\/bj1420591","article-title":"Phosphatidylinositol cleavage catalysed by the soluble fraction from lymphocytes-activity at pH 5.5 and pH 7.0","volume":"142","author":"Allan","year":"1974","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB27","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1042\/bj1420599","article-title":"Phosphatidylinositol cleavage in lymphocytes \u2014 requirement for calcium ions at a low concentration and effects of other cations","volume":"142","author":"Allan","year":"1974","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB28","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1042\/bj2020053","article-title":"The control by Ca2+ of the polyphosphoinositide phosphodiesterase and the Ca2+-pump ATPase in human erythrocytes","volume":"202","author":"Downes","year":"1982","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB29","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1042\/bst0080376","article-title":"The control of phosphatidyl-inositol turnover in cell membranes","volume":"8","author":"Irvine","year":"1980","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/0143-4160(82)90018-5_BIB30","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1111\/j.1432-1033.1979.tb13284.x","article-title":"The calcium-dependent phosphatidylinositol phosphodiesterase of rat brain, mechanisms of suppression and stimulation","volume":"99","author":"Irvine","year":"1979","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB31","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1111\/j.1432-1033.1980.tb04983.x","article-title":"The inhibition and activation of Ca2+-dependent phosphatidylinositol phosphodiesterase by phospholipids and blood plasma","volume":"112","author":"Dawson","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB32","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1042\/bj1930607","article-title":"The hydrolysis of phosphatidylinositol monolayers at an air\/water interface by the calcium-ion-dependent phosphatidylinositol phosphodiesterase of pig brain","volume":"193","author":"Hirasawa","year":"1981","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB33","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1042\/bj2050437","article-title":"Heterogeneity of the calcium-dependent phosphatidylinositol phosphodiesterase in rat brain","volume":"205","author":"Hirasawa","year":"1982","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB34","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/0006-291X(82)91524-8","article-title":"Heterogeneity of the calcium-dependent phosphatidylinositol-phosphodiesterase of rat liver and kidney as revealed by column chromatofocusing","volume":"107","author":"Hirasawa","year":"1982","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/0143-4160(82)90018-5_BIB35","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1042\/bj2060675","article-title":"Proteolytic activation can produce a phosphatidylinositol phosphodiesterase highly sensitive to calcium","volume":"206","author":"Hirasawa","year":"1982","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB36","doi-asserted-by":"crossref","first-page":"6769","DOI":"10.1016\/S0021-9258(19)69058-7","article-title":"Purification of phosphatidyl-inositol-specific phospholipase C from rat liver","volume":"256","author":"Takenawa","year":"1981","journal-title":"J. Biol. Chem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB37","doi-asserted-by":"crossref","first-page":"6461","DOI":"10.1016\/S0021-9258(20)65164-X","article-title":"Identification and properties of two distinct phosphatidylinositol-specific phospholipase C enzymes from sheep seminal vesicular glands","volume":"257","author":"Hoffman","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB38","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1042\/bj0910233","article-title":"The hydrolysis of triphosphoinositide by extracts of rat brain","volume":"91","author":"Thompson","year":"1964","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB39","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1042\/bj0910237","article-title":"The triphosphoinositide phosphodiesterase of brain tissue","volume":"91","author":"Thompson","year":"1964","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB40","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1042\/bj0910244","article-title":"The triphosphoinositide phosphomonoesterase of brain tissue","volume":"91","author":"Dawson","year":"1964","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB41","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/0005-2744(78)90265-6","article-title":"Studies on the properties of triphosphoinositide phosphomonoesterase and phosphodiesterase of rabbit iris smooth muscle","volume":"527","author":"Akhtar","year":"1978","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB42","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1042\/bj1980133","article-title":"The polyphosphoinositide phosphodiesterase of erythrocyte membranes","volume":"198","author":"Downes","year":"1981","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB43","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/0005-2760(72)90197-X","article-title":"Soluble and particulate forms of phosphoinositide phosphodiesterase in ox brain","volume":"270","author":"Keough","year":"1972","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB44","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1016\/0005-2744(77)90032-8","article-title":"Purification and properties of polyphosphoinositide phosphomonoesterase from rat brain","volume":"480","author":"Nijar","year":"1977","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB45","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/0005-2744(81)90021-8","article-title":"Human erythrocyte cytosol phosphatidyl-inositol-bisphosphate phosphatase","volume":"661","author":"Roach","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB46","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1042\/bj1500537","article-title":"Phosphomonoesterase hydrolysis of polyphosphoinositides in rat kidney","volume":"150","author":"Cooper","year":"1975","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB47","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1111\/j.1471-4159.1967.tb09512.x","article-title":"Triphosphoinositide phosphomonoesterase activity in nerve cell bodies, neuraglia and subcellular fractions from whole rat brain","volume":"14","author":"Salway","year":"1967","journal-title":"J. Neurochem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB48","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.1111\/j.1471-4159.1969.tb05989.x","article-title":"Metabolism of the phosphoinositides in guinea-pig brain synaptosomes","volume":"16","author":"Harwood","year":"1969","journal-title":"J. Neurochem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB49","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1042\/bj1280579","article-title":"The subcellular distribution of triphosphoinositide phosphomonoesterase in guinea-pig brain","volume":"128","author":"Sheltawy","year":"1972","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB50","doi-asserted-by":"crossref","first-page":"1212","DOI":"10.1126\/science.7268428","article-title":"The Golgi apparatus: two organelles in tandem","volume":"213","author":"Rothman","year":"1981","journal-title":"Science"},{"key":"10.1016\/0143-4160(82)90018-5_BIB51","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/0005-2760(80)90029-6","article-title":"The acylation of lysophosphatidylcholine by subcellular fractions of guinea-pig cerebral cortex","volume":"618","author":"Fisher","year":"1980","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB52","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1042\/bj1010328","article-title":"The phosphatidylinositol kinase of rat brain","volume":"101","author":"Kai","year":"1966","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB53","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/0005-2744(69)90107-7","article-title":"The properties and subcellular distribution of phosphatidylinositol kinase in mammalian tissues","volume":"171","author":"Harwood","year":"1969","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB54","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/0003-9861(69)90434-2","article-title":"Phosphatidylinositol kinase in rat kidney cortex II. Subcellular distribution and kinetic properties","volume":"131","author":"Tou","year":"1969","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/0143-4160(82)90018-5_BIB55","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/0005-2736(75)90372-7","article-title":"Localization of enzymes involved in polyphosphoinositide metabolism on the cytoplasmic surface of the human erythrocyte membrane","volume":"382","author":"Garrett","year":"1975","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/0143-4160(82)90018-5_BIB56","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1042\/bj1060791","article-title":"The diphosphoinositide kinase of rat brain","volume":"106","author":"Kai","year":"1968","journal-title":"Biochem. J."},{"key":"10.1016\/0143-4160(82)90018-5_BIB57","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/0003-9861(70)90093-7","article-title":"Biosynthesis of triphosphoinositide in rat kidney cortex","volume":"140","author":"Tou","year":"1970","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/0143-4160(82)90018-5_BIB58","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1111\/j.1471-4159.1981.tb01632.x","article-title":"Rapid incorporation in vivo of intracerebrally injected 32Pi into polyphosphoinositides of three subfractions of rat brain myelin","volume":"36","author":"Desmukh","year":"1981","journal-title":"J. Neurochem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB59","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1111\/j.1471-4159.1969.tb08979.x","article-title":"The biosynthesis of triphosphoinositide by purified myelin of peripheral nerve","volume":"16","author":"Iacobelli","year":"1969","journal-title":"J. Neurochem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB60","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1111\/j.1471-4159.1978.tb12417.x","article-title":"Polyphosphoinositide biosynthesis in three subfractions of rat brain myelin","volume":"30","author":"Desmukh","year":"1978","journal-title":"J. Neurochem."},{"key":"10.1016\/0143-4160(82)90018-5_BIB61","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1038\/286623a0","article-title":"Modulation of brain polyphosphoinositide metabolism by ACTH-sensitive protein phosphorylation","volume":"286","author":"Jolles","year":"1980","journal-title":"Nature (Lond.)"},{"key":"10.1016\/0143-4160(82)90018-5_BIB62","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/0304-4165(72)90275-9","article-title":"Cyclic AMP-dependent diphosphoinositide kinase","volume":"286","author":"Torda","year":"1972","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB63","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1016\/0005-2760(67)90053-7","article-title":"Characteristics of rat liver phosphatidylinositol kinase and its presence in the plasma membrane","volume":"144","author":"Michell","year":"1967","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB64","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/0005-2736(80)90574-X","article-title":"Intracellular phospholipases A","volume":"604","author":"Van den Bosch","year":"1980","journal-title":"Biochem. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB65","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/0005-2736(82)90346-7","article-title":"Origins of the latency phase during the action of phospholipase A2 on unmodified phosphatidylcholine vesicles","volume":"688","author":"Apitz-Castro","year":"1982","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/0143-4160(82)90018-5_BIB66","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/0005-2760(68)90150-1","article-title":"The structure of enzymically produced diphosphoinositide and triphosphoinositide","volume":"164","author":"Prottey","year":"1968","journal-title":"Biochim. Biophys. Acta."}],"container-title":["Cell Calcium"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:0143416082900185?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:0143416082900185?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,9]],"date-time":"2025-09-09T19:32:17Z","timestamp":1757446337000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/0143416082900185"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1982,10]]},"references-count":66,"journal-issue":{"issue":"4-5","published-print":{"date-parts":[[1982,10]]}},"alternative-id":["0143416082900185"],"URL":"https:\/\/doi.org\/10.1016\/0143-4160(82)90018-5","relation":{},"ISSN":["0143-4160"],"issn-type":[{"type":"print","value":"0143-4160"}],"subject":[],"published":{"date-parts":[[1982,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The enzymology of stimulated inositol lipid turnover","name":"articletitle","label":"Article Title"},{"value":"Cell Calcium","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/0143-4160(82)90018-5","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"converted-article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 1982 Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}