{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T16:17:16Z","timestamp":1762100236689},"reference-count":38,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[1987,3,1]],"date-time":"1987-03-01T00:00:00Z","timestamp":541555200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Mol Cell Biochem"],"published-print":{"date-parts":[[1987,3]]},"DOI":"10.1007\/bf00221915","type":"journal-article","created":{"date-parts":[[2004,9,18]],"date-time":"2004-09-18T07:26:24Z","timestamp":1095492384000},"page":"83-94","source":"Crossref","is-referenced-by-count":7,"title":["Distribution of calmodulin and calmodulin-binding proteins in bovine pituitary: association of myosin light chain kinase with pituitary secretory granule membranes"],"prefix":"10.1007","volume":"74","author":[{"given":"Teresita Yap","family":"Nelson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mary Y.","family":"Lorenson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laurence S.","family":"Jacobs","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"suffix":"III","given":"A. E.","family":"Boyd","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","reference":[{"key":"BF00221915_CR1","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1210\/endo-82-2-225","volume":"82","author":"MH Samli","year":"1968","unstructured":"Samli MH, Geschwind I: Some effects of energy-transfer inhibitors and of Ca2+ free and K+-enhanced media on the release of luteinizing hormone from the rat pituitary gland in vitro. Endocrinology 82:225\u2013231, 1968.","journal-title":"Endocrinology"},{"key":"BF00221915_CR2","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1113\/jphysiol.1970.sp009252","volume":"210","author":"JA Parsons","year":"1970","unstructured":"Parsons JA: Effects of cations on prolactin and growth hormone secretion by rat adenohypophyses in vitro. J Physiol 210:973\u2013987, 1970.","journal-title":"J Physiol"},{"key":"BF00221915_CR3","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1007\/BF02146887","volume":"23","author":"W Vale","year":"1967","unstructured":"Vale W, Burgus R, Guillemin R: Presence of calcium ions as a requisite for the in vitro stimulation of TSH release by hypothalamic TRF. Experientia 23:853\u2013855, 1967.","journal-title":"Experientia"},{"key":"BF00221915_CR4","doi-asserted-by":"crossref","first-page":"6595","DOI":"10.1016\/S0021-9258(18)43611-3","volume":"255","author":"SW Tam","year":"1980","unstructured":"Tam SW, Danies PS: Dopaminergic inhibition of ionophore A23187-stimulated release of prolactin from rat anterior pituitary cells. J Biol Chem 255:6595\u20136599, 1980.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR5","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1210\/endo-103-4-1245","volume":"103","author":"RE Ostlund Jr","year":"1978","unstructured":"Ostlund Jr RE, Leung JT, Hajek SV, Winokur T, Melman M: Acute stimulated hormone release from cultured GH3 pituitary cells. Endocrinology 103:1245\u20131252, 1978.","journal-title":"Endocrinology"},{"key":"BF00221915_CR6","doi-asserted-by":"crossref","first-page":"1522","DOI":"10.1210\/endo-113-4-1522","volume":"113","author":"MC Gershengorn","year":"1983","unstructured":"Gershengorn MC, Thaw C: Calcium influx is not required for TRH to elevate free cytoplasmic calcium in GH3 cells. Endocrinology 113:1522\u20131524, 1983.","journal-title":"Endocrinology"},{"key":"BF00221915_CR7","doi-asserted-by":"crossref","first-page":"5827","DOI":"10.1016\/S0021-9258(18)91089-6","volume":"259","author":"PR Albert","year":"1984","unstructured":"Albert PR, Tashjian Jr AH: Thyrotropin-releasing hormone-induced spike and plateau in cytosolic free Ca2+ concentrations in pituitary cells. J Biol Chem 259:5827\u20135832, 1984.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR8","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1083\/jcb.99.1.83","volume":"99","author":"W Schlegel","year":"1984","unstructured":"Schlegel W, Wollheim CB: Thyrotropin-releasing hormone increases cytosolic free Ca2+ in clonal pituitary cells (GH3 Cells): Direct evidence for the mobilization of cellular calcium. J Cell Biol 99:83\u201387, 1984.","journal-title":"J Cell Biol"},{"key":"BF00221915_CR9","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/0014-5793(81)80954-4","volume":"135","author":"JE Merritt","year":"1981","unstructured":"Merritt JE, Tomlinson S, Brown BL: Phenothiazines inhibit prolactin secretion in vitro. A possible role for calmodulin in stimulus-secretion coupling in the pituitary. FEBS Lett 135:107\u2013110, 1981.","journal-title":"FEBS Lett"},{"key":"BF00221915_CR10","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1210\/endo-112-1-64","volume":"112","author":"G Schettini","year":"1983","unstructured":"Schettini G, Judd AM, MacLeod RM: In vitro studies on basal and stimulated prolactin release by rat anterior pituitary: A possible role for calmodulin. Endocrinology 112:64\u201370, 1983.","journal-title":"Endocrinology"},{"key":"BF00221915_CR11","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1038\/292264a0","volume":"292","author":"PM Conn","year":"1981","unstructured":"Conn PM, Chafouleas J, Rogers D, Means AR: Gonadotropin releasing hormone stimulates calmodulin redistribution in the rat pituitary. Nature 292:264\u2013265, 1981.","journal-title":"Nature"},{"key":"BF00221915_CR12","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1146\/annurev.bi.49.070180.004421","volume":"49","author":"RS Adelstein","year":"1980","unstructured":"Adelstein RS, Eisenberg E: Regulation and kinetics of the actin-myosin-ATP interaction. Ann Rev Biochem 49:921\u2013956, 1980.","journal-title":"Ann Rev Biochem"},{"key":"BF00221915_CR13","doi-asserted-by":"crossref","first-page":"12802","DOI":"10.1016\/S0021-9258(18)42966-3","volume":"256","author":"MY Lorenson","year":"1981","unstructured":"Lorenson MY, Lee Y-C, Jacobs LS: Identification and characterization of an anion sensitive Mg2+-ATPase in pituitary secretory granule membranes. J Biol Chem 256:12802\u201312810, 1981.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR14","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","volume":"193","author":"OH Lowry","year":"1951","unstructured":"Lowry OH, Rosebrough NJ, Farr AL, Randall RJ: Protein measurement with the Folin phenol reagent. J Biol Chem 193:265\u2013275, 1951.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR15","doi-asserted-by":"crossref","first-page":"10262","DOI":"10.1016\/S0021-9258(19)86703-0","volume":"254","author":"JG Chafouleas","year":"1979","unstructured":"Chafouleas JG, Dedman JR, Munjaal RP, Means AR: Calmodulin: Development and application of a sensitive radioimmunoassay. J Biol Chem 254:10262\u201310267, 1979.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR16","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.2337\/diab.32.12.1126","volume":"32","author":"TY Nelson","year":"1983","unstructured":"Nelson TY, Oberwetter JM, Chafouleas JG, Boyd III AE: Calmodulin-binding proteins in a cloned rat insulinoma cell line. Diabetes 32:1126\u20131133, 1983.","journal-title":"Diabetes"},{"key":"BF00221915_CR17","first-page":"277","volume-title":"Methods in Diabetes Research","author":"TY Nelson","year":"1984","unstructured":"Nelson TY, Snabes MC, Boyd III AE: Measurement of actin and identification of actin- and calmodulin-binding proteins in insulin secreting cells. In: Methods in Diabetes Research. Larner J, Pohl S (eds) J Wiley and Sons, New York, 1984, Vol 1, pp 277\u2013285."},{"key":"BF00221915_CR18","doi-asserted-by":"crossref","first-page":"4350","DOI":"10.1073\/pnas.76.9.4350","volume":"76","author":"H Towbin","year":"1979","unstructured":"Towbin H, Staehlin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350\u20134354, 1979.","journal-title":"Proc Natl Acad Sci USA"},{"key":"BF00221915_CR19","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1016\/0092-8674(81)90386-X","volume":"27","author":"V Guerriero","year":"1981","unstructured":"Guerriero V, Rowley DR, Means AR: Production and characterization of an antibody to myosin light chain kinase and intracellular localization of the enzyme. Cell 27:448\u2013458, 1981.","journal-title":"Cell"},{"key":"BF00221915_CR20","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/0003-2697(82)90677-7","volume":"119","author":"R Hawkes","year":"1982","unstructured":"Hawkes R, Niday E, Gordon J: A dot-immunobinding assay for monoclonal and other antibodies. Anal Biochem 119:142\u2013147, 1982.","journal-title":"Anal Biochem"},{"key":"BF00221915_CR21","first-page":"162","volume-title":"Biostatistical analysis","author":"JH Zar","year":"1984","unstructured":"Zar JH: Biostatistical analysis, 2nd ed, Prentice-Hall, Inc, Englewood Cliffs, NJ, 1984, p 162.","edition":"2nd ed"},{"key":"BF00221915_CR22","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1210\/endo-101-5-1621","volume":"101","author":"EG Beale","year":"1977","unstructured":"Beale EG, Dedman JR, Means AR: Isolation and regulation of the protein kinase inhibitor and the calcium-dependent cyclic nucleotide phosphodiesterase regulator in the sertoli cell-enriched testis. Endocrinology 101:1621\u20131634, 1977.","journal-title":"Endocrinology"},{"key":"BF00221915_CR23","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1073\/pnas.78.1.308","volume":"78","author":"CD Linden","year":"1981","unstructured":"Linden CD, Dedman JR, Chafouleas JG, Means AR, Roth TF: Interactions of calmodulin with coated vesicles from brain. Proc Natl Acad Sci USA 78:308\u2013312, 1981.","journal-title":"Proc Natl Acad Sci USA"},{"key":"BF00221915_CR24","doi-asserted-by":"crossref","first-page":"8690","DOI":"10.1016\/S0021-9258(19)86946-6","volume":"254","author":"DJ Grab","year":"1979","unstructured":"Grab DJ, Berzins K, Cohen RS, Siekevitz P: Presence of calmodulin in postsynaptic densities isolated from canine cerebral cortex. J Biol Chem 254:8690\u20138696, 1979.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR25","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/0014-5793(81)80903-9","volume":"131","author":"RB Burgoyne","year":"1981","unstructured":"Burgoyne RB, Giesow MJ: Specific binding of 125I-calmodulin to and protein phosphorylation of adrenal chromaffin granule membranes. FEBS Lett 131:127\u2013131, 1981.","journal-title":"FEBS Lett"},{"key":"BF00221915_CR26","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/0014-5793(82)80518-8","volume":"140","author":"S Grinstein","year":"1982","unstructured":"Grinstein S, Furuya W: Binding of 125I-calmodulin to platelet alpha-granules. FEBS Lett 140:49\u201352, 1982.","journal-title":"FEBS Lett"},{"key":"BF00221915_CR27","doi-asserted-by":"crossref","first-page":"5161","DOI":"10.1016\/S0021-9258(18)89193-1","volume":"260","author":"D Watkins","year":"1985","unstructured":"Watkins D, White BA: Identification and characterization of calmodulin-binding proteins in islet secretory granules. J Biol Chem 260:5161\u20135165, 1985.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR28","doi-asserted-by":"crossref","first-page":"9995","DOI":"10.1016\/S0021-9258(17)44596-0","volume":"258","author":"RR Goewert","year":"1983","unstructured":"Goewert RR, Klaven NB, McDonald JM: Direct effect of insulin on the binding of calmodulin to rat adipocyte plasma membranes. J Biol Chem 258:9995\u20139999, 1983.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR29","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0021-9258(17)43632-5","volume":"259","author":"JE Hooper","year":"1984","unstructured":"Hooper JE, Kelly RB: Calcium-dependent calmodulin binding to cholinergic synaptic vesicles. J Biol Chem 259:141\u2013147, 1984.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR30","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/S0021-9258(17)43633-7","volume":"259","author":"JE Hooper","year":"1984","unstructured":"Hooper JE, Kelly RB: Calmodulin is tightly associated with synaptic vesicles independent of calcium. J Biol Chem 259:148\u2013153, 1984.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR31","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1038\/295154a0","volume":"295","author":"RA Steinhardt","year":"1982","unstructured":"Steinhardt RA, Alderton JM: Calmodulin confers calcium sensitivity on secretory exocytosis. Nature 295:154\u2013155, 1982.","journal-title":"Nature"},{"key":"BF00221915_CR32","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1083\/jcb.89.3.449","volume":"89","author":"RK Carlin","year":"1981","unstructured":"Carlin RK, Grab DJ, Siekevitz P: Function of calmodulin in postsynaptic densities III calmodulin-binding proteins of the post synaptic density. J Cell Biol 89:449\u2013455, 1981.","journal-title":"J Cell Biol"},{"key":"BF00221915_CR33","doi-asserted-by":"crossref","first-page":"10551","DOI":"10.1016\/S0021-9258(19)70336-6","volume":"255","author":"JR Glenney","year":"1980","unstructured":"Glenney JR, Weber K: Calmodulin-binding proteins of the microfilaments present in isolated brush borders and microvilli of intestinal epithelial cells. J Biol Chem 255:10551\u201310554, 1980.","journal-title":"J Biol Chem"},{"key":"BF00221915_CR34","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1038\/301432a0","volume":"301","author":"MJ Giesow","year":"1983","unstructured":"Giesow MJ, Burgoyne RD: Recruitment of cytosolic proteins to a secretory granule membrane depends on Ca2+-calmodulin. Nature 301:432\u2013435, 1983.","journal-title":"Nature"},{"key":"BF00221915_CR35","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1083\/jcb.99.1.356","volume":"99","author":"RW Rubin","year":"1984","unstructured":"Rubin RW, Lyubkin AK, Pressman BC: Comparison of the protein content of 3 different bovine secretory granule membrane types: A search for exocytosis-specific shared proteins. J Cell Biol 99:356\u2013360, 1984.","journal-title":"J Cell Biol"},{"key":"BF00221915_CR36","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1210\/endo-112-2-766","volume":"112","author":"DT Watkins","year":"1983","unstructured":"Watkins DT, Cooperstein SJ: Role of calcium and calmodulin in the interaction between islet cell secretion granules and plasma membranes. Endocrinology 112:766\u2013768, 1983.","journal-title":"Endocrinology"},{"key":"BF00221915_CR37","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/0014-5793(78)80772-8","volume":"92","author":"P Cohen","year":"1978","unstructured":"Cohen P, Burchell A, Foulkes JG, Cohen PTW, Vanaman TC, Nairn AC: Identification of the Ca2+ -independent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. FEBS Lett 92:287\u2013293, 1978.","journal-title":"FEBS Lett"},{"key":"BF00221915_CR38","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1152\/physrev.1982.62.1.1","volume":"62","author":"AR Means","year":"1982","unstructured":"Means AR, Tash JS, Chafouleas JG: Physiological implications of the presence, distribution, and regulation of calmodulin in eukaryotic cells. Physiological Reviews 62:1\u201339, 1982.","journal-title":"Physiological Reviews"}],"container-title":["Molecular and Cellular Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/BF00221915.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/BF00221915\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/BF00221915","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/BF00221915.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,6,25]],"date-time":"2021-06-25T19:53:43Z","timestamp":1624650823000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/BF00221915"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1987,3]]},"references-count":38,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1987,3]]}},"alternative-id":["BF00221915"],"URL":"https:\/\/doi.org\/10.1007\/bf00221915","relation":{},"ISSN":["0300-8177","1573-4919"],"issn-type":[{"value":"0300-8177","type":"print"},{"value":"1573-4919","type":"electronic"}],"subject":[],"published":{"date-parts":[[1987,3]]}}}