^ abcMorgan, David L. (2007). The cell cycle: principles of control. London: New Science Press. pp. 30–31. ISBN 978-0-19-920610-0
^“Control of the yeast cell cycle by the Cdc28 protein kinase”. Curr. Opin. Cell Biol.5 (2): 166–179. (April 1993). doi:10.1016/0955-0674(93)90099-C. PMID 8507488.
^ abLee, Melanie; Nurse, Paul (Jun 1987). “Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2”. Nature327 (6117): 31–35. doi:10.1038/327031a0. PMID 3553962.
^“An overview of Cdk1-controlled targets and processes”. Cell Division5 (11): 11. (May 2010). doi:10.1186/1747-1028-5-11. PMC 2876151. PMID 20465793. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2876151/.
^“Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex”. Nature376 (6538): 313–320. (July 1995). doi:10.1038/376313a0. PMID 7630397.
^Brown, Nicholas R.; Korolchuk, Svitlana; Martin, Mathew P.; Stanley, Will A.; Moukhametzianov, Rouslan; Noble, Martin E. M.; Endicott, Jane A. (2015-04-13). “CDK1 structures reveal conserved and unique features of the essential cell cycle CDK”. Nature Communications6: 6769. doi:10.1038/ncomms7769. ISSN 2041-1723. PMC 4413027. PMID 25864384. https://www.ncbi.nlm.nih.gov/pubmed/25864384.
^“Microtubule-targeting drugs induce bcl-2 phosphorylation and association with Pin1”. Neoplasia3 (6): 550–9. (2001). doi:10.1038/sj.neo.7900213. PMC 1506558. PMID 11774038. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1506558/.
^“Microtubule-targeting drugs induce Bcl-2 phosphorylation and association with Pin1”. Neoplasia3 (1): 70–9. (2001). doi:10.1038/sj.neo.7900131. PMC 1505024. PMID 11326318. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1505024/.
^ ab“Cyclin E associates with BAF155 and BRG1, components of the mammalian SWI-SNF complex, and alters the ability of BRG1 to induce growth arrest”. Mol. Cell. Biol.19 (2): 1460–9. (February 1999). doi:10.1128/mcb.19.2.1460. PMC 116074. PMID 9891079. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC116074/.
^“Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2”. Cell58 (5): 833–846. (September 1989). doi:10.1016/0092-8674(89)90936-7. PMID 2570636.
^“Cyclin F regulates the nuclear localization of cyclin B1 through a cyclin-cyclin interaction”. EMBO J.19 (6): 1378–1388. (March 2000). doi:10.1093/emboj/19.6.1378. PMC 305678. PMID 10716937. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC305678/.
^“Formation and activation of a cyclin E-cdk2 complex during the G1 phase of the human cell cycle”. Science257 (5077): 1689–1694. (September 1992). doi:10.1126/science.1388288. PMID 1388288.
^“KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases”. Proc. Natl. Acad. Sci. U.S.A.91 (5): 1731–1735. (March 1994). doi:10.1073/pnas.91.5.1731. PMC 43237. PMID 8127873. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC43237/.
^“Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2”. Cell75 (4): 791–803. (November 1993). doi:10.1016/0092-8674(93)90498-F. PMID 8242750.
^“Cell cycle-dependent phosphorylation of Disabled-2 by cdc2”. Oncogene22 (29): 4524–4530. (July 2003). doi:10.1038/sj.onc.1206767. PMID 12881709.
^“Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport”. Exp. Cell Res.289 (2): 211–221. (October 2003). doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
^“The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase, cdc2”. Blood90 (3): 1047–54. (August 1997). PMID 9242535.
^“Association with Cdc2 and inhibition of Cdc2/Cyclin B1 kinase activity by the p53-regulated protein Gadd45”. Oncogene18 (18): 2892–2900. (May 1999). doi:10.1038/sj.onc.1202667. PMID 10362260.
^“The GADD45 inhibition of Cdc2 kinase correlates with GADD45-mediated growth suppression”. J. Biol. Chem.275 (22): 16602–16608. (June 2000). doi:10.1074/jbc.M000284200. PMID 10747892.
^“Identification of a functional domain in a GADD45-mediated G2/M checkpoint”. J. Biol. Chem.275 (47): 36892–36898. (November 2000). doi:10.1074/jbc.M005319200. PMID 10973963.
^“GADD45b and GADD45g are cdc2/cyclinB1 kinase inhibitors with a role in S and G2/M cell cycle checkpoints induced by genotoxic stress”. J. Cell. Physiol.192 (3): 327–338. (September 2002). doi:10.1002/jcp.10140. PMID 12124778.
^“Activation of Src-like p56/p53lyn tyrosine kinase by ionizing radiation”. J. Biol. Chem.269 (32): 20739–43. (August 1994). PMID 8051175.
^“The protein-tyrosine kinase Lck associates with and is phosphorylated by Cdc2”. J. Biol. Chem.271 (44): 27517–27523. (November 1996). doi:10.1074/jbc.271.44.27517. PMID 8910336.
^“The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A”. J. Mol. Biol.300 (3): 503–518. (July 2000). doi:10.1006/jmbi.2000.3830. PMID 10884347.
^“Downregulation of the cdc2/cyclin B protein kinase activity by binding of p53 to p34(cdc2)”. Biochem. Biophys. Res. Commun.283 (2): 507–512. (May 2001). doi:10.1006/bbrc.2001.4792. PMID 11327730.
^“Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells”. Proteomics8 (14): 2885–2896. (July 2008). doi:10.1002/pmic.200700887. PMID 18655026.
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“Cdc25 protein phosphatases in cell proliferation”. Biochim. Biophys. Acta1332 (2): M53–63. (1997). doi:10.1016/S0304-419X(96)00049-2. PMID 9141461.
“Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1”. DNA Cell Biol.23 (4): 193–205. (2004). doi:10.1089/104454904773819789. PMID 15142377. https://zenodo.org/record/1235217.
“Human immunodeficiency virus type-1 accessory protein Vpr: a causative agent of the AIDS-related insulin resistance/lipodystrophy syndrome?”. Ann. N. Y. Acad. Sci.1024: 153–167. (2004). doi:10.1196/annals.1321.013. PMID 15265780. https://zenodo.org/record/1235880.
“Structure and function of HIV-1 auxiliary regulatory protein Vpr: novel clues to drug design”. Curr. Drug Targets Immune Endocr. Metabol. Disord.4 (4): 265–275. (2005). doi:10.2174/1568008043339668. PMID 15578977.
“The Vpr protein from HIV-1: distinct roles along the viral life cycle”. Retrovirology2: 11. (2006). doi:10.1186/1742-4690-2-11. PMC 554975. PMID 15725353. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC554975/.
“Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions”. Cell Res.15 (11–12): 923–934. (2006). doi:10.1038/sj.cr.7290370. PMID 16354571.
“[Biologic availability and "1st pass" effect of drugs]”. Fortschr. Med.95 (28): 1765–6, 1774–80. (1977). PMID 914146.
“Interaction between the cell-cycle-control proteins p34cdc2 and p9CKShs2. Evidence for two cooperative binding domains in p9CKShs2”. Eur. J. Biochem.203 (3): 353–360. (1992). doi:10.1111/j.1432-1033.1992.tb16557.x. PMID 1310466.
“cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication”. EMBO J.11 (6): 2189–99. (1992). doi:10.1002/j.1460-2075.1992.tb05278.x. PMC 556686. PMID 1318195. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC556686/.
“Formation and activation of a cyclin E-cdk2 complex during the G1 phase of the human cell cycle”. Science257 (5077): 1689–1694. (1992). doi:10.1126/science.1388288. PMID 1388288.
“Casein kinase II phosphorylates p34cdc2 kinase in G1 phase of the HeLa cell division cycle”. J. Biol. Chem.267 (28): 20317–25. (1992). PMID 1400350.
“Localization of the rap1GAP catalytic domain and sites of phosphorylation by mutational analysis”. Mol. Cell. Biol.12 (10): 4634–42. (1992). doi:10.1128/MCB.12.10.4634. PMC 360390. PMID 1406653. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC360390/.
“Reversible phosphorylation--dephosphorylation determines the localization of rab4 during the cell cycle”. EMBO J.11 (12): 4379–89. (1992). doi:10.1002/j.1460-2075.1992.tb05538.x. PMC 557012. PMID 1425574. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC557012/.
“A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression”. J. Biol. Chem.266 (35): 23521–4. (1992). PMID 1748630.
“The retinoblastoma protein is phosphorylated on multiple sites by human cdc2”. EMBO J.10 (13): 4279–90. (1992). doi:10.1002/j.1460-2075.1991.tb05006.x. PMC 453181. PMID 1756735. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC453181/.
“Regional assignment of the human cell cycle control gene CDC2 to chromosome 10q21 by in situ hybridization”. Hum. Genet.87 (5): 621–2. (1991). doi:10.1007/BF00209025. PMID 1916766.
“Phosphorylation by cdc2 kinase modulates DNA binding activity of high mobility group I nonhistone chromatin protein”. J. Biol. Chem.266 (30): 19945–52. (1991). PMID 1939057.