{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T15:48:27Z","timestamp":1770824907182,"version":"3.50.1"},"reference-count":47,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2001,5,1]],"date-time":"2001-05-01T00:00:00Z","timestamp":988675200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":4460,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Cell"],"published-print":{"date-parts":[[2001,5]]},"DOI":"10.1016\/s1097-2765(01)00245-3","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T03:02:01Z","timestamp":1027652521000},"page":"1071-1083","source":"Crossref","is-referenced-by-count":145,"title":["Pin1 Acts Catalytically to Promote a Conformational Change in Cdc25"],"prefix":"10.1016","volume":"7","author":[{"given":"P.Todd","family":"Stukenberg","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marc W","family":"Kirschner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S1097-2765(01)00245-3_BIB1","doi-asserted-by":"crossref","first-page":"2493","DOI":"10.1242\/jcs.112.15.2493","article-title":"A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1","volume":"112","author":"Albert","year":"1999","journal-title":"J. Cell Sci."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB2","doi-asserted-by":"crossref","first-page":"22300","DOI":"10.1074\/jbc.272.35.22300","article-title":"Human Myt1 is a cell cycle-regulated kinase that inhibits Cdc2 but not Cdk2 activity","volume":"272","author":"Booher","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB3","doi-asserted-by":"crossref","first-page":"2195","DOI":"10.1073\/pnas.86.7.2195","article-title":"Proline isomerism leads to multiple folded conformations of calbindin D9k","volume":"86","author":"Chazin","year":"1989","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB4","doi-asserted-by":"crossref","first-page":"3866","DOI":"10.1093\/emboj\/16.13.3866","article-title":"Mechanism of TGFbeta receptor inhibition by FKBP12","volume":"16","author":"Chen","year":"1997","journal-title":"EMBO J."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB5","doi-asserted-by":"crossref","first-page":"7892","DOI":"10.1073\/pnas.92.17.7892","article-title":"14-3-3 proteins associate with cdc25 phosphatases","volume":"92","author":"Conklin","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB6","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1093\/emboj\/17.5.1315","article-title":"The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1","volume":"17","author":"Crenshaw","year":"1998","journal-title":"EMBO J."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB7","doi-asserted-by":"crossref","first-page":"2926","DOI":"10.1073\/pnas.80.10.2926","article-title":"Monoclonal antibodies to mitotic cells","volume":"80","author":"Davis","year":"1983","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB8","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1007\/978-1-4615-5371-7_18","article-title":"Myt1","volume":"3","author":"Fattaey","year":"1997","journal-title":"Prog. Cell Cycle Res."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB9","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1016\/S0092-8674(00)81190-3","article-title":"Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A","volume":"93","author":"Fauman","year":"1998","journal-title":"Cell"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB10","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1006\/bbrc.1999.1736","article-title":"Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest","volume":"265","author":"Fujimori","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB11","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1091\/mbc.4.12.1337","article-title":"Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase","volume":"4","author":"Izumi","year":"1993","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB12","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1091\/mbc.3.8.927","article-title":"Periodic changes in phosphorylation of the Xenopus cdc25 phosphatase regulate its activity","volume":"3","author":"Izumi","year":"1992","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB13","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1016\/0092-8674(94)90542-8","article-title":"Mitosis in transition","volume":"79","author":"King","year":"1994","journal-title":"Cell"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB14","doi-asserted-by":"crossref","first-page":"1652","DOI":"10.1126\/science.274.5293.1652","article-title":"How proteolysis drives the cell cycle","volume":"274","author":"King","year":"1996","journal-title":"Science"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB15","doi-asserted-by":"crossref","first-page":"6127","DOI":"10.1021\/bi00239a007","article-title":"Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay","volume":"30","author":"Kofron","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB16","doi-asserted-by":"crossref","first-page":"4400","DOI":"10.1021\/bi00470a020","article-title":"The rate and structural consequences of proline cis-trans isomerization in calbindin D9k","volume":"29","author":"Kordel","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB17","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1016\/0092-8674(91)90315-P","article-title":"The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system","volume":"64","author":"Kumagai","year":"1991","journal-title":"Cell"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB18","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/0092-8674(92)90540-S","article-title":"Regulation of the cdc25 protein during the cell cycle in Xenopus extracts","volume":"70","author":"Kumagai","year":"1992","journal-title":"Cell"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB19","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.1126\/science.273.5280.1377","article-title":"Purification and molecular cloning pl Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts","volume":"273","author":"Kumagai","year":"1996","journal-title":"Science"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB20","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1016\/S0076-6879(97)83044-3","article-title":"Regulation of Xenopus Cdc25 protein","volume":"283","author":"Kumagai","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB21","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1101\/gad.13.9.1067","article-title":"Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25","volume":"13","author":"Kumagai","year":"1999","journal-title":"Genes Dev."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB22","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1038\/16488","article-title":"Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein","volume":"397","author":"Lopez-Girona","year":"1999","journal-title":"Nature"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB23","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1038\/380544a0","article-title":"A human peptidyl-prolyl isomerase essential for regulation of mitosis","volume":"380","author":"Lu","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB24","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1038\/21650","article-title":"The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein","volume":"399","author":"Lu","year":"1999","journal-title":"Nature"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB25","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1126\/science.283.5406.1325","article-title":"Function of WW domains as phosphoserine- or phosphothreonine-binding modules","volume":"283","author":"Lu","year":"1999","journal-title":"Science"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB26","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1073\/pnas.93.1.447","article-title":"The Drosophila melanogaster dodo (dod) gene, conserved in humans, is functionally interchangeable with the ESS1 cell division gene of Saccharomyces cerevisiae","volume":"93","author":"Maleszka","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB27","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1016\/S0091-679X(08)60298-8","article-title":"Cell cycle extracts","volume":"36","author":"Murray","year":"1991","journal-title":"Methods Cell Biol."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB28","doi-asserted-by":"crossref","first-page":"17977","DOI":"10.1021\/bi9819733","article-title":"Coupling of prolyl peptide bond isomerization and Ca2+ binding in a C- type mannose-binding protein","volume":"37","author":"Ng","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB29","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/S0092-8674(00)81684-0","article-title":"A long twentieth century of the cell cycle and beyond","volume":"100","author":"Nurse","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB30","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1126\/science.277.5331.1501","article-title":"Mitotic and G2 checkpoint control","volume":"277","author":"Peng","year":"1997","journal-title":"Science"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB31","doi-asserted-by":"crossref","first-page":"4262","DOI":"10.1128\/MCB.18.7.4262","article-title":"Activated polo-like kinase Plx1 is required at multiple points during mitosis in Xenopus laevis","volume":"18","author":"Qian","year":"1998","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB32","doi-asserted-by":"crossref","first-page":"8625","DOI":"10.1128\/MCB.19.12.8625","article-title":"Mitotic effects of a constitutively active mutant of the Xenopus polo-like kinase Plx1","volume":"19","author":"Qian","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB33","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1016\/S0092-8674(00)80273-1","article-title":"Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent","volume":"89","author":"Ranganathan","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB34","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1126\/science.277.5331.1497","article-title":"Conservation of the Chk1 checkpoint pathway in mammals","volume":"277","author":"Sanchez","year":"1997","journal-title":"Science"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB35","doi-asserted-by":"crossref","first-page":"5566","DOI":"10.1021\/bi973060z","article-title":"Role of phosphorylation in determining the backbone dynamics of the serine\/threonine-proline motif and Pin1 substrate recognition","volume":"37","author":"Schutkowski","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB36","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1101\/gad.12.5.706","article-title":"The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins","volume":"12","author":"Shen","year":"1998","journal-title":"Genes Dev."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB37","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1016\/0092-8674(90)90504-8","article-title":"Cyclin activation of p34cdc2","volume":"63","author":"Solomon","year":"1990","journal-title":"Cell"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB38","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1091\/mbc.3.1.13","article-title":"Role of phosphorylation in p34cdc2 activation","volume":"3","author":"Solomon","year":"1992","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB39","series-title":"Biochemistry","author":"Stryer","year":"1995"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB40","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1016\/S0960-9822(06)00157-6","article-title":"Systematic identification of mitotic phosphoproteins","volume":"7","author":"Stukenberg","year":"1997","journal-title":"Curr. Biol."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB41","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/0022-2836(92)90976-Q","article-title":"Proline cis-trans isomers in calbindin D9k observed by X-ray crystallography","volume":"223","author":"Svensson","year":"1992","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB42","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1073\/pnas.91.2.714","article-title":"Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2 monoclonal antibody and determination of the phosphorylated epitope","volume":"91","author":"Westendorf","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB43","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/S0076-6879(97)83004-2","article-title":"Purification of recombinant cyclin B1\/cdc2 kinase from Xenopus egg extracts","volume":"283","author":"Wilhelm","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB44","doi-asserted-by":"crossref","first-page":"1644","DOI":"10.1126\/science.287.5458.1644","article-title":"Requirement of the prolyl isomerase Pin1 for the replication checkpoint","volume":"287","author":"Winkler","year":"2000","journal-title":"Science"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB45","doi-asserted-by":"crossref","first-page":"1957","DOI":"10.1126\/science.278.5345.1957","article-title":"Sequence-specific and phosphorylation-dependent proline isomerization","volume":"278","author":"Yaffe","year":"1997","journal-title":"Science"},{"key":"10.1016\/S1097-2765(01)00245-3_BIB46","doi-asserted-by":"crossref","first-page":"2174","DOI":"10.1093\/emboj\/18.8.2174","article-title":"Maintenance of G2 arrest in the Xenopus oocyte","volume":"18","author":"Yang","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/S1097-2765(01)00245-3_BIB47","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/S1097-2765(05)00083-3","article-title":"Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and Tau proteins","volume":"6","author":"Zhou","year":"2000","journal-title":"Mol. Cell"}],"container-title":["Molecular Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1097276501002453?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1097276501002453?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,5,14]],"date-time":"2021-05-14T17:08:13Z","timestamp":1621012093000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1097276501002453"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,5]]},"references-count":47,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2001,5]]}},"alternative-id":["S1097276501002453"],"URL":"https:\/\/doi.org\/10.1016\/s1097-2765(01)00245-3","relation":{},"ISSN":["1097-2765"],"issn-type":[{"value":"1097-2765","type":"print"}],"subject":[],"published":{"date-parts":[[2001,5]]}}}