{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T04:47:34Z","timestamp":1761540454482},"reference-count":45,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2003,7,1]],"date-time":"2003-07-01T00:00:00Z","timestamp":1057017600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2003,7]]},"DOI":"10.1016\/s0022-2836(03)00713-7","type":"journal-article","created":{"date-parts":[[2003,7,16]],"date-time":"2003-07-16T16:18:16Z","timestamp":1058372296000},"page":"955-966","source":"Crossref","is-referenced-by-count":25,"title":["Phosphorylation of the N-terminal Domain Regulates Subcellular Localization and DNA Binding Properties of the Peptidyl-prolyl cis\/trans Isomerase hPar14"],"prefix":"10.1016","volume":"330","author":[{"given":"Tatiana","family":"Reimer","sequence":"first","affiliation":[]},{"given":"Matthias","family":"Weiwad","sequence":"additional","affiliation":[]},{"given":"Angelika","family":"Schierhorn","sequence":"additional","affiliation":[]},{"given":"Peter-Karl","family":"Ruecknagel","sequence":"additional","affiliation":[]},{"given":"Jens-Ulrich","family":"Rahfeld","sequence":"additional","affiliation":[]},{"given":"Peter","family":"Bayer","sequence":"additional","affiliation":[]},{"given":"Gunter","family":"Fischer","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0022-2836(03)00713-7_BIB1","doi-asserted-by":"crossref","DOI":"10.1007\/s10254-003-0011-3","article-title":"Regulation of peptide bond cis\/trans isomerization by enzyme catalysis and its implication in physiological processes","author":"Fischer","year":"2003","journal-title":"Rev. Physiol. Biochem. Pharmacol."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB2","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/S0014-5793(00)01794-4","article-title":"Evidence that the substrate backbone conformation is critical to phosphorylation by p42 MAP kinase","volume":"478","author":"Weiwad","year":"2000","journal-title":"FEBS Letters"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB3","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"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB4","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1111\/j.1432-1033.1993.tb18189.x","article-title":"Peptidylproline cis-trans-isomerases: immunophilins","volume":"216","author":"Galat","year":"1993","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB5","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/0014-5793(94)00932-5","article-title":"Confirmation of the existence of a third family among peptidyl\u2013prolyl cis\/trans isomerases. Amino acid sequence and recombinant production of parvulin","volume":"352","author":"Rahfeld","year":"1994","journal-title":"FEBS Letters"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB6","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1002\/yea.320050108","article-title":"Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae","volume":"5","author":"Hanes","year":"1989","journal-title":"Yeast"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB7","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1038\/380544a0","article-title":"A human peptidyl\u2013prolyl isomerase essential for regulation of mitosis","volume":"380","author":"Lu","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB8","first-page":"409","article-title":"Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis","volume":"11","author":"Rippmann","year":"2000","journal-title":"Cell. Growth Differ."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB9","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1093\/embo-reports\/kvf118","article-title":"Peptidyl\u2013prolyl isomerases: a new twist to transcription","volume":"3","author":"Shaw","year":"2002","journal-title":"EMBO Rep."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB10","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/S0014-5793(99)00239-2","article-title":"Identification and characterization of a 14kDa human protein as a novel parvulin-like peptidyl prolyl cis\/trans isomerase","volume":"446","author":"Uchida","year":"1999","journal-title":"FEBS Letters"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB11","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1006\/bbrc.1999.0828","article-title":"Identification of eukaryotic parvulin homologues: a new subfamily of peptidylprolyl cis\u2013trans isomerases","volume":"259","author":"Rulten","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB12","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1006\/jmbi.2000.4013","article-title":"NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis\/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein","volume":"301","author":"Sekerina","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB13","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1006\/jmbi.2000.4293","article-title":"Solution structure of the human parvulin-like peptidyl prolyl cis\/trans isomerase, hPar14","volume":"305","author":"Terada","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB14","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/S0022-2836(02)00615-0","article-title":"The N-terminal basic domain of human parvulin hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding","volume":"321","author":"Surmacz","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB15","doi-asserted-by":"crossref","first-page":"23773","DOI":"10.1074\/jbc.M201181200","article-title":"Isolation and proteomic characterization of human Parvulin-associating preribosomal ribonucleoprotein complexes","volume":"277","author":"Fujiyama","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB16","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S1074-5521(02)00310-1","article-title":"Pin1 and Par14 peptidyl prolyl isomerase inhibitors block cell proliferation","volume":"10","author":"Uchida","year":"2003","journal-title":"Chem. Biol."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB17","doi-asserted-by":"crossref","first-page":"2381","DOI":"10.1074\/jbc.C100228200","article-title":"Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function","volume":"277","author":"Lu","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB18","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1096\/fasebj.9.5.7896000","article-title":"Protein kinases. 4. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation","volume":"9","author":"Allende","year":"1995","journal-title":"FASEB J."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB19","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1042\/bj3110705","article-title":"The regulation of protein transport to the nucleus by phosphorylation","volume":"311","author":"Jans","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB20","doi-asserted-by":"crossref","first-page":"14804","DOI":"10.1016\/S0021-9258(17)42674-3","article-title":"Inhibitory effect of 5,6-dichloro-1-beta-d-ribofuranosylbenzimidazole on a protein kinase","volume":"259","author":"Zandomeni","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB21","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/S0167-4838(99)00147-8","article-title":"Kinetic study of the inhibition of CK2 by heparin fragments of different length","volume":"1433","author":"O'Farrell","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB22","doi-asserted-by":"crossref","first-page":"15555","DOI":"10.1016\/S0021-9258(18)98436-X","article-title":"Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases","volume":"266","author":"Kennelly","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB23","first-page":"401","article-title":"Substrate specificity of protein kinase CK2","volume":"40","author":"Meggio","year":"1994","journal-title":"Cell. Mol. Biol. Res."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB24","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1002\/j.1460-2075.1991.tb07991.x","article-title":"The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen","volume":"10","author":"Rihs","year":"1991","journal-title":"EMBO J."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB25","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1073\/pnas.82.3.737","article-title":"A synthetic peptide substrate specific for casein kinase II","volume":"82","author":"Kuenzel","year":"1985","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB26","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1006\/bbrc.1994.1128","article-title":"Design and synthesis of two new peptide substrates for the specific and sensitive monitoring of casein kinases-1 and -2","volume":"198","author":"Marin","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB27","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/0014-5793(87)80561-6","article-title":"The phosphorylation of nucleoplasmin by casein kinase-2 is resistant to heparin inhibition","volume":"226","author":"Taylor","year":"1987","journal-title":"FEBS Letters"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB28","doi-asserted-by":"crossref","first-page":"7769","DOI":"10.1073\/pnas.90.16.7769","article-title":"The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin","volume":"90","author":"Jin","year":"1993","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB29","doi-asserted-by":"crossref","first-page":"14500","DOI":"10.1073\/pnas.94.26.14500","article-title":"Phosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: regulation of HSP90-binding activity of FKBP52","volume":"94","author":"Miyata","year":"1997","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB30","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/S0378-1119(00)00077-9","article-title":"Phosphorylation of the insect immunophilin FKBP46 by the Spodoptera frugiperda homolog of casein kinase II","volume":"246","author":"Steplewski","year":"2000","journal-title":"Gene"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB31","doi-asserted-by":"crossref","first-page":"8143","DOI":"10.1128\/MCB.21.23.8143-8156.2001","article-title":"Cell density and phosphorylation control the subcellular localization of adenomatous polyposis coli protein","volume":"21","author":"Zhang","year":"2001","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB32","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1042\/0264-6021:3530069","article-title":"Novel properties of the protein kinase CK2-site-regulated nuclear-localization sequence of the interferon-induced nuclear factor IFI 16","volume":"353","author":"Briggs","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB33","doi-asserted-by":"crossref","first-page":"3253","DOI":"10.1002\/j.1460-2075.1990.tb07524.x","article-title":"The p53 tumor suppressor protein is phosphorylated at serine 389 by casein kinase II","volume":"9","author":"Meek","year":"1990","journal-title":"EMBO J."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB34","doi-asserted-by":"crossref","first-page":"22920","DOI":"10.1016\/S0021-9258(18)41614-6","article-title":"DNA topoisomerase II and casein kinase II associate in a molecular complex that is catalytically active","volume":"268","author":"Bojanowski","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB35","doi-asserted-by":"crossref","first-page":"1731","DOI":"10.1126\/science.8259518","article-title":"Association of the APC gene product with beta-catenin","volume":"5140","author":"Rubinfeld","year":"1993","journal-title":"Science"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB36","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1126\/science.281.5382.1509","article-title":"Identification of c-MYC as a target of the APC pathway","volume":"281","author":"He","year":"1998","journal-title":"Science"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB37","doi-asserted-by":"crossref","first-page":"5576","DOI":"10.1128\/MCB.19.8.5576","article-title":"The Wnt\/Wg signal transducer beta-catenin controls fibronectin expression","volume":"19","author":"Gradl","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB38","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1038\/18884","article-title":"Beta-catenin regulates expression of cyclin D1 in colon carcinoma cells","volume":"398","author":"Tetsu","year":"1999","journal-title":"Nature"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB39","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1126\/science.272.5264.1023","article-title":"Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly","volume":"272","author":"Rubinfeld","year":"1996","journal-title":"Science"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB40","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/S0092-8674(00)80829-6","article-title":"PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation","volume":"101","author":"Ohno","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB41","doi-asserted-by":"crossref","first-page":"25893","DOI":"10.1074\/jbc.273.40.25893","article-title":"Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual-specific protein kinases","volume":"273","author":"Becker","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB42","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0092-8674(00)81847-4","article-title":"Association of BRCA1 with Rad51 in mitotic and meiotic cells","volume":"88","author":"Scully","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB43","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/0092-8674(94)90340-9","article-title":"A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein","volume":"76","author":"Dyck","year":"1994","journal-title":"Cell"},{"key":"10.1016\/S0022-2836(03)00713-7_BIB44","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1146\/annurev.cb.09.110193.001405","article-title":"Macromolecular domains within the cell nucleus","volume":"9","author":"Spector","year":"1993","journal-title":"Annu. Rev. Cell Biol."},{"key":"10.1016\/S0022-2836(03)00713-7_BIB45","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1038\/nsb0897-657","article-title":"The solution structure of an HMG-I(Y)\u2013DNA complex defines a new architectural minor groove binding motif","volume":"4","author":"Huth","year":"1997","journal-title":"Nature Struct. Biol."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283603007137?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283603007137?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,8]],"date-time":"2021-06-08T17:13:32Z","timestamp":1623172412000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283603007137"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,7]]},"references-count":45,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2003,7]]}},"alternative-id":["S0022283603007137"],"URL":"https:\/\/doi.org\/10.1016\/s0022-2836(03)00713-7","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2003,7]]}}}