{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,8]],"date-time":"2026-01-08T06:44:22Z","timestamp":1767854662459,"version":"3.49.0"},"reference-count":46,"publisher":"Oxford University Press (OUP)","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2004,2,1]]},"DOI":"10.1095\/biolreprod.103.020024","type":"journal-article","created":{"date-parts":[[2004,10,20]],"date-time":"2004-10-20T18:30:50Z","timestamp":1098297050000},"page":"439-447","source":"Crossref","is-referenced-by-count":42,"title":["Increased Phosphorylation of a Distinct Subcellular Pool of Protein Phosphatase, PP1\u03b32, During Epididymal Sperm Maturation1"],"prefix":"10.1093","volume":"70","author":[{"given":"Zaohua","family":"Huang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Srinivasan","family":"Vijayaraghavan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","reference":[{"key":"key\n\t\t\t\t20170224172328_R1","first-page":"379","article-title":"The mammalian spermatozoon: morphology, biochemistry and physiology.","volume-title":"Marshall\u2019s Physiology of Reproduction","year":"1990"},{"issue":"2","key":"key\n\t\t\t\t20170224172328_R2","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1111\/j.1365-2605.1986.tb00870.x","article-title":"The epididymis and male fertility. A symposium report.","volume":"9","year":"1986","journal-title":"Int J Androl"},{"issue":"11","key":"key\n\t\t\t\t20170224172328_R3","first-page":"2534","article-title":"Initiation of sperm motility in the mammalian epididymis.","volume":"37","year":"1978","journal-title":"Fed Proc"},{"key":"key\n\t\t\t\t20170224172328_R4","first-page":"251","article-title":"The regulation of spermatozoa by calcium and cyclic nucleotides.","volume":"13","year":"1980","journal-title":"Advances In Cyclic Nucleotide Research"},{"key":"key\n\t\t\t\t20170224172328_R5","first-page":"21","article-title":"Studies on the roles of cyclic AMP and calcium in the development of bovine sperm motility.","volume":"15","year":"1983","journal-title":"J Submicrosc Cytol"},{"key":"key\n\t\t\t\t20170224172328_R6","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1095\/biolreprod32.3.489","article-title":"Evidence for a role for cellular alkalinization in the cyclic adenosine 3\u2032,5\u2032-monophosphate-mediated initiation of motility in bovine caput spermatozoa.","volume":"32","year":"1985","journal-title":"Biol Reprod"},{"key":"key\n\t\t\t\t20170224172328_R7","first-page":"499","article-title":"Forskolin stimulates bovine epididymal sperm motility and cyclic AMP levels.","volume":"10","year":"1985","journal-title":"J Cyclic Nucleotide Protein Phosphor Res"},{"key":"key\n\t\t\t\t20170224172328_R8","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1095\/biolreprod34.3.468","article-title":"Regulation of bovine sperm motility and cyclic adenosine 3\u2032,5\u2032-monophosphate by adenosine and its analogues.","volume":"34","year":"1986","journal-title":"Biol Reprod"},{"key":"key\n\t\t\t\t20170224172328_R9","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1095\/biolreprod39.5.1129","article-title":"The interaction of pH and cyclic adenosine 3\u2032,5\u2032-monophosphate on activation of motility in Triton X-100 extracted bull sperm.","volume":"39","year":"1988","journal-title":"Biol Reprod"},{"key":"key\n\t\t\t\t20170224172328_R10","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1002\/mrd.1080250212","article-title":"Changes in the mitochondrial calcium influx and efflux properties are responsible for the decline in sperm calcium during epididymal maturation.","volume":"25","year":"1990","journal-title":"Mol Reprod Dev"},{"issue":"(272)","key":"key\n\t\t\t\t20170224172328_R11","first-page":"4747","article-title":"Protein kinase A-anchoring inhibitor peptides arrest mammalian sperm motility.","volume":"21","year":"1997","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20170224172328_R12","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1093\/humrep\/13.suppl_4.20","article-title":"Role of the ionic environment and internal pH on sperm activity.","volume":"13","year":"1998","journal-title":"Hum Reprod"},{"key":"key\n\t\t\t\t20170224172328_R13","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1095\/biolreprod54.3.709","article-title":"Sperm motility development in the epididymis is associated with decreased glycogen synthase kinase-3 and protein phosphatase 1 activity.","volume":"54","year":"1996","journal-title":"Biol Reprod"},{"key":"key\n\t\t\t\t20170224172328_R14","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1095\/biolreprod54.3.719","article-title":"Primate sperm contain protein phosphatase 1, a biochemical mediator of motility.","volume":"54","year":"1996","journal-title":"Biol Reprod"},{"key":"key\n\t\t\t\t20170224172328_R15","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1002\/j.1939-4640.1999.tb02495.x","article-title":"Motility potential of macaque epididymal sperm: the role of protein phosphatase and glycogen synthase kinase-3 activities.","volume":"20","year":"1999","journal-title":"J Androl"},{"key":"key\n\t\t\t\t20170224172328_R16","first-page":"189","article-title":"Mammalian fertilization.","volume-title":"The Physiology of Reproduction","year":"1994"},{"key":"key\n\t\t\t\t20170224172328_R17","first-page":"29","article-title":"The spermatozoon.","volume-title":"The Physiology of Reproduction","year":"1993"},{"key":"key\n\t\t\t\t20170224172328_R18","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1095\/biolreprod61.1.240","article-title":"Role of tyrosine phosphorylation of flagellar proteins in hamster sperm hyperactivation.","volume":"61","year":"1999","journal-title":"Biol Reprod"},{"key":"key\n\t\t\t\t20170224172328_R19","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1095\/biolreprod61.1.247","article-title":"Hyperactivation of hamster sperm motility by temperature-dependent tyrosine phosphorylation of an 80-kDa protein.","volume":"61","year":"1999","journal-title":"Biol Reprod"},{"key":"key\n\t\t\t\t20170224172328_R20","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/S0015-0282(16)55642-8","article-title":"Calyculin A, protein phosphatase inhibitor, enhances capacitation of human sperm.","volume":"59","year":"1993","journal-title":"Fertil Steril"},{"key":"key\n\t\t\t\t20170224172328_R21","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1095\/biolreprod.102.004093","article-title":"Sperm PP1\u03b32 is regulated by a homologue of the yeast protein phosphatase binding protein sds22.","volume":"67","year":"2002","journal-title":"Biol Reprod"},{"key":"key\n\t\t\t\t20170224172328_R22","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1111\/j.1349-7006.1990.tb02690.x","article-title":"Identification of members of the protein phosphatase 1 gene family in the rat and enhanced expression of protein phosphatase 1\u03b3 gene in rat hepatocellular carcinomas.","volume":"81","year":"1990","journal-title":"Jpn J Cancer Res"},{"key":"key\n\t\t\t\t20170224172328_R23","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/0006-291X(90)91381-2","article-title":"Protein phosphatases possibly involved in rat spermatogenesis.","volume":"171","year":"1990","journal-title":"Biochem Biophys Res Commun"},{"key":"key\n\t\t\t\t20170224172328_R24","doi-asserted-by":"crossref","first-page":"3375","DOI":"10.1523\/JNEUROSCI.15-05-03375.1995","article-title":"Differential expression of protein phosphatase 1 isoforms in mammalian brain.","volume":"15","year":"1995","journal-title":"J Neurosci"},{"key":"key\n\t\t\t\t20170224172328_R25","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1006\/dbio.1998.9100","article-title":"Spermiogenesis is impaired in mice bearing a targeted mutation in the protein phosphatase 1c\u03b3 gene.","volume":"205","year":"1999","journal-title":"Dev Biol"},{"key":"key\n\t\t\t\t20170224172328_R26","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1146\/annurev.bi.58.070189.002321","article-title":"The structure and regulation of protein phosphatases.","volume":"58","year":"1989","journal-title":"Annu Rev Biochem"},{"issue":"Pt 2","key":"key\n\t\t\t\t20170224172328_R27","first-page":"241","article-title":"Protein phosphatase 1-targeted in many directions.","volume":"115","year":"2002","journal-title":"J Cell Sci"},{"key":"key\n\t\t\t\t20170224172328_R28","doi-asserted-by":"crossref","first-page":"R13","DOI":"10.1016\/S1074-5521(00)00069-7","article-title":"Regulation of protein phosphatase-1.","volume":"7","year":"2000","journal-title":"Chem Biol"},{"key":"key\n\t\t\t\t20170224172328_R29","doi-asserted-by":"crossref","first-page":"D961","DOI":"10.2741\/A336","article-title":"Physiologic importance of protein phosphatase inhibitors.","volume":"3","year":"1998","journal-title":"Front Biosci"},{"key":"key\n\t\t\t\t20170224172328_R30","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/0092-8674(90)90463-O","article-title":"Substrates for p34cdc2: in vivo veritas?.","volume":"61","year":"1990","journal-title":"Cell"},{"key":"key\n\t\t\t\t20170224172328_R31","doi-asserted-by":"crossref","first-page":"6408","DOI":"10.1073\/pnas.91.14.6408","article-title":"Phosphorylation and inactivation of protein phosphatase 1 by cyclin-dependent kinases.","volume":"91","year":"1994","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20170224172328_R32","doi-asserted-by":"crossref","first-page":"2168","DOI":"10.1073\/pnas.94.6.2168","article-title":"Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase.","volume":"94","year":"1997","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20170224172328_R33","doi-asserted-by":"crossref","first-page":"29470","DOI":"10.1074\/jbc.274.41.29470","article-title":"Inhibitory phosphorylation of PP1\u03b1 catalytic subunit during the G1\/S transition.","volume":"274","year":"1999","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20170224172328_R34","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1006\/scbi.1995.0028","article-title":"Flicking the switches: phosphorylation of serine\/threonine protein phosphatases.","volume":"6","year":"1995","journal-title":"Semin Cancer Biol"},{"key":"key\n\t\t\t\t20170224172328_R35","doi-asserted-by":"crossref","first-page":"5310","DOI":"10.1002\/j.1460-2075.1994.tb06865.x","article-title":"Phosphorylation of dis2 protein phosphatase at the C-terminal cdc2 consensus and its potential role in cell cycle regulation.","volume":"13","year":"1994","journal-title":"EMBO J"},{"key":"key\n\t\t\t\t20170224172328_R36","doi-asserted-by":"crossref","first-page":"D22","DOI":"10.2741\/A409","article-title":"Protein dephosphorylation and the intracellular control of the cell number.","volume":"4","year":"1999","journal-title":"Front Biosci"},{"key":"key\n\t\t\t\t20170224172328_R37","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1530\/jrf.0.0190423","article-title":"Identification and subcellular localization of the enzymes effecting penetration of the zona pellucida by rabbit spermatozoa.","volume":"19","year":"1969","journal-title":"J Reprod Fertil"},{"key":"key\n\t\t\t\t20170224172328_R38","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.","volume":"72","year":"1976","journal-title":"Anal Biochem"},{"key":"key\n\t\t\t\t20170224172328_R39","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4.","volume":"227","year":"1970","journal-title":"Nature"},{"key":"key\n\t\t\t\t20170224172328_R40","article-title":"Distinct pools of PP1\u03b32 are regulated by sds22, protein 14-3-3 and hsp90 within spermatozoa.","volume-title":"Annual meeting of Experimental Biology, American Society of Molecular Biology and Biochemistry","year":"2003"},{"key":"key\n\t\t\t\t20170224172328_R41","article-title":"Binding to sds22 and inactivation of catalytic activity of the protein phosphatase PP1 gamma 2 occurs during sperm motility in the epididymis.","volume-title":"36th annual meeting, Society for the Study of Reproduction","year":"2003"},{"key":"key\n\t\t\t\t20170224172328_R42","doi-asserted-by":"crossref","first-page":"3007","DOI":"10.1242\/dev.124.15.3007","article-title":"HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes.","volume":"124","year":"1997","journal-title":"Development"},{"key":"key\n\t\t\t\t20170224172328_R43","doi-asserted-by":"crossref","first-page":"2865","DOI":"10.1002\/j.1460-2075.1990.tb07476.x","article-title":"The A- and B-type cyclin associated cdc2 kinases in Xenopus turn on and off at different times in the cell cycle.","volume":"9","year":"1990","journal-title":"EMBO J"},{"key":"key\n\t\t\t\t20170224172328_R44","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/0012-1606(92)90161-9","article-title":"Isolation and characterization of goldfish cdk2, a cognate variant of the cell cycle regulator cdc2.","volume":"152","year":"1992","journal-title":"Dev Biol"},{"key":"key\n\t\t\t\t20170224172328_R45","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1111\/j.1432-1033.1992.tb16810.x","article-title":"M-phase-specific histone H1 kinase in fish oocytes. Purification, components and biochemical properties.","volume":"205","year":"1992","journal-title":"Eur J Biochem"},{"key":"key\n\t\t\t\t20170224172328_R46","doi-asserted-by":"crossref","first-page":"1572","DOI":"10.1095\/biolreprod.103.018739","article-title":"Binding and inactivation of the germ cell-specific protein phosphatase PP1\u03b32 by sds22 during epididymal sperm maturation.","volume":"69","year":"2003","journal-title":"Biol Reprod"}],"container-title":["Biology of Reproduction"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/biolreprod\/article-pdf\/70\/2\/439\/10588573\/biolreprod0439.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,12,19]],"date-time":"2024-12-19T02:32:02Z","timestamp":1734575522000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/biolreprod\/article-lookup\/doi\/10.1095\/biolreprod.103.020024"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,2,1]]},"references-count":46,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2004,2,1]]}},"URL":"https:\/\/doi.org\/10.1095\/biolreprod.103.020024","relation":{},"ISSN":["0006-3363","1529-7268"],"issn-type":[{"value":"0006-3363","type":"print"},{"value":"1529-7268","type":"electronic"}],"subject":[],"published":{"date-parts":[[2004,2,1]]}}}