{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T10:39:49Z","timestamp":1773657589050,"version":"3.50.1"},"reference-count":41,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[1995,8,1]],"date-time":"1995-08-01T00:00:00Z","timestamp":807235200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[1995,8,1]],"date-time":"1995-08-01T00:00:00Z","timestamp":807235200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[1995,8,1]],"date-time":"1995-08-01T00:00:00Z","timestamp":807235200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Cell Biochem"],"published-print":{"date-parts":[[1995,8]]},"DOI":"10.1007\/bf01076564","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T21:16:32Z","timestamp":1109452592000},"page":"59-69","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase"],"prefix":"10.1007","volume":"149-150","author":[{"given":"Mary D.","family":"Pato","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ewa","family":"Kerc","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephen J.","family":"Lye","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","reference":[{"key":"BF01076564_CR1","first-page":"423","volume-title":"Gastrointestinal Tract","author":"DJ Hartshorne","year":"1987","unstructured":"Hartshorne DJ: Biochemistry of the contractile process in smooth muscle. In: L.R. Johnson (ed.). Gastrointestinal Tract, Second edition, Raven Press, New York 1987, pp 423\u2013482","edition":"Second edition"},{"key":"BF01076564_CR2","first-page":"113","volume-title":"The Enzymes, Vol. XVII","author":"JT Stull","year":"1986","unstructured":"Stull JT, Nunnally MH, Michnoff CH: Calmodulin-dependent protein kinases. In: The Enzymes, Vol. XVII, Academic Press, Inc., Orlando, Florida, 1986, pp 113\u2013166"},{"key":"BF01076564_CR3","doi-asserted-by":"crossref","first-page":"6028","DOI":"10.1021\/bi00343a002","volume":"24","author":"K Takio","year":"1985","unstructured":"Takio K, Blumenthal DK, Edelman AM, Walsh KA, Krebs EG, Titani K: Amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase. Biochemistry 24: 6028\u20136037, 1985","journal-title":"Biochemistry"},{"key":"BF01076564_CR4","doi-asserted-by":"crossref","first-page":"8049","DOI":"10.1021\/bi00372a038","volume":"25","author":"K Takio","year":"1986","unstructured":"Takio K, Blumenthal DK, Walsh KA, Titani K, Krebs EG: Amino acid sequence of rabbit skeletal muscle myosin light chain kinase. Biochemistry 25: 8049\u20138057, 1986","journal-title":"Biochemistry"},{"key":"BF01076564_CR5","doi-asserted-by":"crossref","first-page":"11275","DOI":"10.1016\/S0021-9258(17)39177-9","volume":"260","author":"AM Edelman","year":"1985","unstructured":"Edelman AM, Takio K, Blumenthal DK, Hansen RS, Walsh KA, Titani K, Krebs EG: Characterization of the calmodulin binding and catalytic domains in the skeletal muscle myosin light chain kinase. J Biol Chem 260: 11275\u201311285, 1985","journal-title":"J Biol Chem"},{"key":"BF01076564_CR6","doi-asserted-by":"crossref","first-page":"10510","DOI":"10.1016\/S0021-9258(19)81545-4","volume":"263","author":"CL Rousch","year":"1988","unstructured":"Rousch CL, Kennelly PJ, Glaccum MB, Helfman DM, Scott JD, Krebs EG: Isolation of the cDNA encoding rat skeletal muscle myosin light chain kinase. J Biol Chem 263: 10510\u201310516, 1988","journal-title":"J Biol Chem"},{"key":"BF01076564_CR7","doi-asserted-by":"crossref","first-page":"2284","DOI":"10.1073\/pnas.87.6.2284","volume":"87","author":"NJ Olson","year":"1990","unstructured":"Olson NJ, Pearson RB, Needleman DS, Hurwitz MY, Kemp BE, Means AR: Regulatory and structural motifs of chicken gizzard myosin light chain kinase. Proc Natl Acad Sci USA 87: 2284\u20132288, 1990","journal-title":"Proc Natl Acad Sci USA"},{"key":"BF01076564_CR8","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1083\/jcb.111.3.1107","volume":"111","author":"MD Shoemaker","year":"1990","unstructured":"Shoemaker MD, Lau W, Shattuck RL, Kwiatkowski AP, Matrisian PE, Guerra-Santos L, Wilson E, Lukas TJ, Watterson DM: Use of DNA sequence and mutant analyses and antisense oligodeoxy-nucleotides to examine the molecular basis of nonmuscle myosin light chain kinase autoinhibition, calmodulin recognition, and activity. J Cell Biol 111: 1107\u20131125, 1990","journal-title":"J Cell Biol"},{"key":"BF01076564_CR9","doi-asserted-by":"crossref","first-page":"23936","DOI":"10.1016\/S0021-9258(18)54375-1","volume":"266","author":"PJ Gallagher","year":"1991","unstructured":"Gallagher PJ, Herring BP, Griffin SA, Stull JT: Molecular characterization of a mammalian smooth muscle myosin light chain kinase. J Biol Chem 266: 23936\u201323944, 1991","journal-title":"J Biol Chem"},{"key":"BF01076564_CR10","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1093\/oxfordjournals.jbchem.a123976","volume":"112","author":"H Kobayashi","year":"1992","unstructured":"Kobayashi H, Inoue A, Mikawa T, Kuwayama H, Hotta Y, Masaki T, Ebashi S: Isolation of cDNA for bovine stomach 155 kDa protein exhibiting myosin light chain kinase activity. J Biochem 112: 786\u2013791, 1992","journal-title":"J Biochem"},{"key":"BF01076564_CR11","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/0003-9861(91)90383-T","volume":"287","author":"MD Pato","year":"1991","unstructured":"Pato MD, Lye SJ, Kerc E: Purification and characterization of pregnant sheep myometrium myosin light chain kinase. Arch Bioch Biophy 287: 24\u201332, 1991","journal-title":"Arch Bioch Biophy"},{"key":"BF01076564_CR12","doi-asserted-by":"crossref","first-page":"7501","DOI":"10.1016\/S0021-9258(19)68990-8","volume":"256","author":"RS Adelstein","year":"1981","unstructured":"Adelstein RS, Klee CB: Purification and characterization of smooth muscle myosin light chain kinase. J Biol Chem 256: 7501\u20137509, 1981","journal-title":"J Biol Chem"},{"key":"BF01076564_CR13","doi-asserted-by":"crossref","first-page":"7047","DOI":"10.1016\/S0021-9258(18)32330-5","volume":"258","author":"MD Pato","year":"1983","unstructured":"Pato MD, Adelstein RS: Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. J Biol Chem 258: 7047\u20137054, 1983","journal-title":"J Biol Chem"},{"key":"BF01076564_CR14","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1021\/bi00624a033","volume":"16","author":"CB Klee","year":"1977","unstructured":"Klee CB: Conformational transition accompanying the binding of Ca2+ to the protein activation of 3\u2032,5\u2032-cyclic adenosine monophosphate phosphodiesterase. Biochemistry 16: 1017\u20131024, 1977","journal-title":"Biochemistry"},{"key":"BF01076564_CR15","doi-asserted-by":"crossref","first-page":"8347","DOI":"10.1016\/S0021-9258(17)34295-3","volume":"253","author":"RS Adelstein","year":"1978","unstructured":"Adelstein RS, Conti MA, Hathaway DR, Klee CB: Phosphorylation of smooth muscle myosin light chain kinase by the catalytic subunit of adenosine 3\u2032,5\u2032-monophosphate-dependent protein kinase. J Biol Chem 253: 8347\u20138350, 1978","journal-title":"J Biol Chem"},{"key":"BF01076564_CR16","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0006-291X(76)90276-X","volume":"71","author":"V Kinzel","year":"1976","unstructured":"Kinzel V, Kubler D: Single step purification of the catalytic subunit(s) of cyclic 3\u2032,5\u2032-adenosine monophosphate-dependent protein kinase(s) from rat muscle. Biochem Biophys Res Comm 71: 257\u2013264, 1976","journal-title":"Biochem Biophys Res Comm"},{"key":"BF01076564_CR17","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","volume":"72","author":"MM Bradford","year":"1976","unstructured":"Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal Biochem 72: 248\u2013254, 1976","journal-title":"Anal Biochem"},{"key":"BF01076564_CR18","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","volume":"227","author":"UK Laemmli","year":"1970","unstructured":"Laemmli UK: Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature (Lond.) 227: 680\u2013685, 1970","journal-title":"Nature (Lond.)"},{"key":"BF01076564_CR19","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/0003-2697(75)90743-5","volume":"66","author":"JJ Witt","year":"1975","unstructured":"Witt JJ, Roskoski R Jr: Rapid protein kinase assay using phosphocellulose-paperabsorption. Anal Biochem 66: 253\u2013258, 1975","journal-title":"Anal Biochem"},{"key":"BF01076564_CR20","doi-asserted-by":"crossref","first-page":"8979","DOI":"10.1016\/S0021-9258(17)39445-0","volume":"260","author":"M Nishikawa","year":"1985","unstructured":"Nishikawa M, Shirakawa S, Adelstein RS: Phosphorylation of smooth muscle mosin light chain kinase: comparative study of the phosphorylation sites. J Biol Chem 260: 8979\u20138983, 1985","journal-title":"J Biol Chem"},{"key":"BF01076564_CR21","doi-asserted-by":"crossref","first-page":"3178","DOI":"10.1016\/S0021-9258(19)69586-4","volume":"256","author":"MA Conti","year":"1981","unstructured":"Conti MA, Adelstein RS: The relationship between calmodulin binding and phosphorylation of smooth muscle myosin kinase by the catalytic subunit of 3\u2032:5\u2032 cAMP-dependent protein kinase. J Biol Chem 256: 3178\u20133181, 1981","journal-title":"J Biol Chem"},{"key":"BF01076564_CR22","doi-asserted-by":"crossref","first-page":"9071","DOI":"10.1016\/S0021-9258(19)76508-9","volume":"263","author":"P de Lanerolle","year":"1988","unstructured":"de Lanerolle P, Nishikawa M: Regulation of embryonic smooth muscle myosin by protein kinase C. J Biol Chem 263: 9071\u20139074, 1988","journal-title":"J Biol Chem"},{"key":"BF01076564_CR23","doi-asserted-by":"crossref","first-page":"5294","DOI":"10.1021\/bi00591a005","volume":"18","author":"JM Chirgwin","year":"1979","unstructured":"Chirgwin JM, Pryzbyla AE, MacDonald RJ, Rutter W: Isolation of biologically active ribonucleicx acid from sources rich in ribonuclease. Biochemistry 18: 5294\u20135299, 1979","journal-title":"Biochemistry"},{"key":"BF01076564_CR24","volume-title":"Molecular Cloning","author":"J Sambrook","year":"1989","unstructured":"Sambrook J, Fritsch EF, Maniatis T: In Molecular Cloning, Second edition, Cold Spring Harbor Laboratory Press, New York, 1989","edition":"Second edition"},{"key":"BF01076564_CR25","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1042\/bj2560283","volume":"256","author":"C Biolojan","year":"1988","unstructured":"Biolojan C, Takai A: Inhibitory effect of marine-sponge toxin, okadaic acid, on protein phosphatases: specificity and kinetics. Biochem J 256: 283\u2013290, 1988","journal-title":"Biochem J"},{"key":"BF01076564_CR26","doi-asserted-by":"crossref","first-page":"4547","DOI":"10.1016\/S0021-9258(18)89101-3","volume":"260","author":"M Ikebe","year":"1985","unstructured":"Ikebe M, Inagaki M, Kanamaru K, Hidaka H: Phosphorylation of smooth muscle myosin light chain kinase by Ca2+-activated, phospholipid-dependent protein kinase. J Biol Chem 260: 4547\u20134550: 1985","journal-title":"J Biol Chem"},{"key":"BF01076564_CR27","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1042\/bj2750679","volume":"275","author":"Y Araki","year":"1991","unstructured":"Araki Y, Ikebe M: Activation of smooth muscle myosin light chain kinase activity by a monoclonal antibody which recognizes the calmodulin-binding region. Biochem J 275: 679\u2013684, 1991","journal-title":"Biochem J"},{"key":"BF01076564_CR28","first-page":"61","volume-title":"Reproductive Biology","author":"JRG Challis","year":"1986","unstructured":"Challis JRG, Lye SJ: Parturition. In: J. Clarke (ed.). Reproductive Biology, Oxford University Press, Oxford, 1986, pp 61\u2013129"},{"key":"BF01076564_CR29","doi-asserted-by":"crossref","first-page":"1458","DOI":"10.1021\/bi00354a041","volume":"25","author":"TJ Lukas","year":"1986","unstructured":"Lukas TJ, Burgess WH, Prendergast FG, Lau W, Watterson DM: Calmodulin binding domains: characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase. Biochemistry 25: 1458\u20131464, 1986","journal-title":"Biochemistry"},{"key":"BF01076564_CR30","doi-asserted-by":"crossref","first-page":"16346","DOI":"10.1016\/S0021-9258(18)66572-X","volume":"261","author":"ME Payne","year":"1986","unstructured":"Payne ME, Elzinga M, Adelstein R: Smooth muscle myosin light chain kinase. Amino acid sequence at the site phosphorylated by adenosine cyclic 3\u2032,5\u2032-phosphate dependent protein kinase whether or not calmodulin is bound. J Biol Chem 261: 16346\u201316350, 1986","journal-title":"J Biol Chem"},{"key":"BF01076564_CR31","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/0003-9861(90)90228-Q","volume":"278","author":"Y Hashimoto","year":"1990","unstructured":"Hashimoto Y, Sordeling TR: phosphorylation of smooth muscle myosin light chain kinase by Ca-2+\/calmodulin-dependent protein kinase-II-comparative study of the phosphorylation sites. Arch Biochem Biophys 278: 41\u201345, 1990","journal-title":"Arch Biochem Biophys"},{"key":"BF01076564_CR32","doi-asserted-by":"crossref","first-page":"16683","DOI":"10.1016\/S0021-9258(17)46275-2","volume":"265","author":"JT Stull","year":"1990","unstructured":"Stull JT, Hsu L-C, Tansey MG, Kamm KE: Myosin light chain kinase phosphorylation in tracheal smooth muscle. J Biol Chem 265: 16683\u201316690, 1990","journal-title":"J Biol Chem"},{"key":"BF01076564_CR33","doi-asserted-by":"crossref","first-page":"12511","DOI":"10.1016\/S0021-9258(18)42307-1","volume":"267","author":"MG Tansey","year":"1992","unstructured":"Tansey MG, Word RA, Hidaka H, Singer HA, Schworer CM, Kamm KE, Stull JT: Phosphorylation of myosin light chain kinase by the multifunctional calmodulin-dependent protein kinase II in smooth muscle cells. J Biol Chem 267: 12511\u201312516, 1992","journal-title":"J Biol Chem"},{"key":"BF01076564_CR34","doi-asserted-by":"crossref","first-page":"3024","DOI":"10.1016\/S0021-9258(19)50689-5","volume":"267","author":"IC Bagchi","year":"1992","unstructured":"Bagchi IC, Huang Q, Means AR: Identification of amino acids essential for calmodulin binding and activation of smooth muscle myosin light chain kinase. J Biol Chem 267: 3024\u20133029, 1992","journal-title":"J Biol Chem"},{"key":"BF01076564_CR35","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1042\/bj2580313","volume":"258","author":"RJ Colbran","year":"1989","unstructured":"Colbran RJ, Schworer CM, Hashimoto Y, Fong Y-L, Rich DP, Smith MK, Soderling TR: Calcium\/calmodulin dependent protein kinase II. Biochem J 258: 313\u2013325, 1989","journal-title":"Biochem J"},{"key":"BF01076564_CR36","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1113\/jphysiol.1991.sp018661","volume":"439","author":"NL McDaniel","year":"1991","unstructured":"McDaniel NL, Rembold CM, Richard HM, Murphy RA: Cyclic AMP Relaxes Swine Arterial Smooth Muscle Predominantly by Decreasing Cell Ca2+ Concentration. J Physiol 439: 147\u2013160, 1991","journal-title":"J Physiol"},{"key":"BF01076564_CR37","doi-asserted-by":"crossref","first-page":"11839","DOI":"10.1016\/S0021-9258(19)49775-5","volume":"267","author":"D-C Tang","year":"1992","unstructured":"Tang D-C, Stull JT, Kubota Y, Kamm KE: Regulation of the Ca2+ dependence of smooth muscle contraction. J Biol Chem 267: 11839\u201311845, 1992","journal-title":"J Biol Chem"},{"key":"BF01076564_CR38","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1007\/BF01753559","volume":"7","author":"L Dokhac","year":"1986","unstructured":"Dokhac L, D'Albis A, Janmot C, Harbon S: Myosin light chain phosphorylation in intact rat uterine smooth muscle: role of calcium and cyclic AMP. J Muscle Res Cell Motility 7: 259\u2013268, 1986","journal-title":"J Muscle Res Cell Motility"},{"key":"BF01076564_CR39","first-page":"277","volume":"1","author":"AJ Brugger","year":"1975","unstructured":"Brugger AJ: The mechanism of the utero-inhibitory effect of bsympathomimetics. Pharmac Therap 1: 277\u2013296, 1975","journal-title":"Pharmac Therap"},{"key":"BF01076564_CR40","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1016\/0002-9378(75)90459-7","volume":"121","author":"K-E Andersson","year":"1975","unstructured":"Andersson K-E, Bengtsson LPh, Gustafson I, Ingemarsson I: The relaxing effect of terbutaline on the human uterus during term labor. Am J Obstet Gynecol 121: 602\u2013609, 1975","journal-title":"Am J Obstet Gynecol"},{"key":"BF01076564_CR41","doi-asserted-by":"crossref","first-page":"165","DOI":"10.3109\/00016347509156750","volume":"54","author":"K-E Andersson","year":"1975","unstructured":"Andersson K-E, Ingemarsson I, Persson CGA: Effects of terbutaline on human uterine motility at term. Acta Obsete Gynec Scand 54: 165\u2013172, 1975","journal-title":"Acta Obsete Gynec Scand"}],"container-title":["Molecular and Cellular Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/BF01076564.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/BF01076564\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/BF01076564","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/BF01076564.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,4,9]],"date-time":"2025-04-09T01:35:43Z","timestamp":1744162543000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/BF01076564"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,8]]},"references-count":41,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1995,8]]}},"alternative-id":["BF01076564"],"URL":"https:\/\/doi.org\/10.1007\/bf01076564","relation":{},"ISSN":["0300-8177","1573-4919"],"issn-type":[{"value":"0300-8177","type":"print"},{"value":"1573-4919","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,8]]},"assertion":[{"value":"This content has been made available to all.","name":"free","label":"Free to read"}]}}