サイクリン依存性キナーゼ2 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "サイクリン依存性キナーゼ2" in Japanese language version.

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104nih.gov

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52doi.org

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2ensembl.org

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2wikipedia.org

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2rcsb.org

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doi.org

“Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase”. Nature 353 (6340): 174–7. (September 1991). doi:10.1038/353174a0. PMID 1653904.
“Recent developments in cyclin-dependent kinase biochemical and structural studies”. Biochimica et Biophysica Acta 1804 (3): 511–9. (March 2010). doi:10.1016/j.bbapap.2009.10.002. PMID 19822225.
“Cdk2 knockout mice are viable”. Current Biology 13 (20): 1775–85. (October 2003). doi:10.1016/j.cub.2003.09.024. PMID 14561402.
van den Heuvel, S.; Harlow, E. (1993-12-24). “Distinct roles for cyclin-dependent kinases in cell cycle control”. Science (New York, N.Y.) 262 (5142): 2050–2054. doi:10.1126/science.8266103. ISSN 0036-8075. PMID 8266103.
“Promiscuity rules? The dispensability of cyclin E and Cdk2”. Science's STKE 2004 (224): pe11. (March 2004). doi:10.1126/stke.2242004pe11. PMC 3242733. PMID 15026579.
“Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms”. Oncogene 28 (33): 2925–39. (August 2009). doi:10.1038/onc.2009.170. PMID 19561645.
“Differences in the Conformational Energy Landscape of CDK1 and CDK2 Suggest a Mechanism for Achieving Selective CDK Inhibition”. Cell Chemical Biology 26 (1): 121–130.e5. (November 2018). doi:10.1016/j.chembiol.2018.10.015. PMC 6344228. PMID 30472117.
PDB: 1FIN; “Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex”. Nature 376 (6538): 313–20. (July 1995). doi:10.1038/376313a0. PMID 7630397.
“Cyclin-dependent kinases”. Genome Biology 15 (6): 122. (2014-06-30). doi:10.1186/gb4184. PMC 4097832. PMID 25180339.
PDB: 1W98; “The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles”. The EMBO Journal 24 (3): 452–63. (February 2005). doi:10.1038/sj.emboj.7600554. PMC 548659. PMID 15660127.
“Checking on DNA damage in S phase”. Nature Reviews. Molecular Cell Biology 5 (10): 792–804. (October 2004). doi:10.1038/nrm1493. PMID 15459660.
“Low-Molecular-Weight Cyclin E in Human Cancer: Cellular Consequences and Opportunities for Targeted Therapies”. Cancer Research 78 (19): 5481–5491. (October 2018). doi:10.1158/0008-5472.can-18-1235. PMC 6168358. PMID 30194068.
“RB and cell cycle progression”. Oncogene 25 (38): 5220–7. (August 2006). doi:10.1038/sj.onc.1209615. PMID 16936740.
“Pocket proteins and cell cycle control”. Oncogene 24 (17): 2796–809. (April 2005). doi:10.1038/sj.onc.1208619. PMID 15838516.
“NPAT links cyclin E-Cdk2 to the regulation of replication-dependent histone gene transcription”. Genes & Development 14 (18): 2283–97. (September 2000). doi:10.1101/gad.827700. PMC 316937. PMID 10995386.
“Loss of Cdk2 and cyclin A2 impairs cell proliferation and tumorigenesis”. Cancer Research 74 (14): 3870–9. (July 2014). doi:10.1158/0008-5472.CAN-13-3440. PMC 4102624. PMID 24802190.
“Inhibition of cyclin-dependent kinase 2 protects against doxorubicin-induced cardiomyocyte apoptosis and cardiomyopathy”. The Journal of Biological Chemistry 293 (51): 19672–19685. (October 2018). doi:10.1074/jbc.ra118.004673. PMC 6314117. PMID 30361442.
“Inhibitors of cyclin-dependent kinases as cancer therapeutics”. Pharmacology & Therapeutics 173: 83–105. (May 2017). doi:10.1016/j.pharmthera.2017.02.008. PMC 6141011. PMID 28174091.
“Roscovitine in cancer and other diseases”. Annals of Translational Medicine 3 (10): 135. (June 2015). doi:10.3978/j.issn.2305-5839.2015.03.61. PMC 4486920. PMID 26207228.
“CDK1 structures reveal conserved and unique features of the essential cell cycle CDK”. Nature Communications 6: 6769. (April 2015). doi:10.1038/ncomms7769. PMC 4413027. PMID 25864384.
“Structure-based discovery of the first allosteric inhibitors of cyclin-dependent kinase 2”. Cell Cycle 13 (14): 2296–305. (2014-06-09). doi:10.4161/cc.29295. PMC 4111683. PMID 24911186.
“Targeting Conformational Activation of CDK2 Kinase”. Biotechnology Journal 12 (8): 1600531. (August 2017). doi:10.1002/biot.201600531. PMID 28430399.
“Cleavage of p21Cip1/Waf1 and p27Kip1 mediates apoptosis in endothelial cells through activation of Cdk2: role of a caspase cascade”. Molecular Cell 1 (4): 553–63. (March 1998). doi:10.1016/S1097-2765(00)80055-6. PMID 9660939.
“Constituents of Mediterranean Spices Counteracting Vascular Smooth Muscle Cell Proliferation: Identification and Characterization of Rosmarinic Acid Methyl Ester as a Novel Inhibitor”. Molecular Nutrition & Food Research 62 (7): e1700860. (April 2018). doi:10.1002/mnfr.201700860. PMID 29405576.
“Critical role of CDK2 for melanoma growth linked to its melanocyte-specific transcriptional regulation by MITF”. Cancer Cell 6 (6): 565–76. (December 2004). doi:10.1016/j.ccr.2004.10.014. PMID 15607961.
“Novel MITF targets identified using a two-step DNA microarray strategy”. Pigment Cell & Melanoma Research 21 (6): 665–76. (December 2008). doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
“BRCA1 is phosphorylated at serine 1497 in vivo at a cyclin-dependent kinase 2 phosphorylation site”. Molecular and Cellular Biology 19 (7): 4843–54. (July 1999). doi:10.1128/MCB.19.7.4843. PMC 84283. PMID 10373534.
“BRCA1 proteins are transported to the nucleus in the absence of serum and splice variants BRCA1a, BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases”. Oncogene 15 (2): 143–57. (July 1997). doi:10.1038/sj.onc.1201252. PMID 9244350.
“p12(DOC-1) is a novel cyclin-dependent kinase 2-associated protein”. Molecular and Cellular Biology 20 (17): 6300–7. (September 2000). doi:10.1128/MCB.20.17.6300-6307.2000. PMC 86104. PMID 10938106.
“CRM1/Ran-mediated nuclear export of p27(Kip1) involves a nuclear export signal and links p27 export and proteolysis”. Molecular Biology of the Cell 14 (1): 201–13. (January 2003). doi:10.1091/mbc.E02-06-0319. PMC 140238. PMID 12529437.
“Tuberin binds p27 and negatively regulates its interaction with the SCF component Skp2”. The Journal of Biological Chemistry 279 (47): 48707–15. (November 2004). doi:10.1074/jbc.M405528200. PMID 15355997.
“Bcl-2 expression suppresses mismatch repair activity through inhibition of E2F transcriptional activity”. Nature Cell Biology 7 (2): 137–47. (February 2005). doi:10.1038/ncb1215. PMID 15619620.
“Spy1 interacts with p27Kip1 to allow G1/S progression”. Molecular Biology of the Cell 14 (9): 3664–74. (September 2003). doi:10.1091/mbc.E02-12-0820. PMC 196558. PMID 12972555.
“Rapamycin potentiates transforming growth factor beta-induced growth arrest in nontransformed, oncogene-transformed, and human cancer cells”. Molecular and Cellular Biology 22 (23): 8184–98. (December 2002). doi:10.1128/mcb.22.23.8184-8198.2002. PMC 134072. PMID 12417722.
“Abolishment of the interaction between cyclin-dependent kinase 2 and Cdk-associated protein phosphatase by a truncated KAP mutant”. Biochemical and Biophysical Research Communications 305 (2): 311–4. (May 2003). doi:10.1016/s0006-291x(03)00757-5. PMID 12745075.
“KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases”. Proceedings of the National Academy of Sciences of the United States of America 91 (5): 1731–5. (March 1994). doi:10.1073/pnas.91.5.1731. PMC 43237. PMID 8127873.
“The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases”. Cell 75 (4): 805–16. (November 1993). doi:10.1016/0092-8674(93)90499-g. PMID 8242751.
“C/EBPalpha arrests cell proliferation through direct inhibition of Cdk2 and Cdk4”. Molecular Cell 8 (4): 817–28. (October 2001). doi:10.1016/s1097-2765(01)00366-5. PMID 11684017.
“Cyclin A1 directly interacts with B-myb and cyclin A1/cdk2 phosphorylate B-myb at functionally important serine and threonine residues: tissue-specific regulation of B-myb function”. Blood 97 (7): 2091–7. (April 2001). doi:10.1182/blood.v97.7.2091. PMID 11264176.
“The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases”. Nature Cell Biology 1 (7): 438–43. (November 1999). doi:10.1038/15674. PMID 10559988.
“Cyclin E associates with BAF155 and BRG1, components of the mammalian SWI-SNF complex, and alters the ability of BRG1 to induce growth arrest”. Molecular and Cellular Biology 19 (2): 1460–9. (February 1999). doi:10.1128/mcb.19.2.1460. PMC 116074. PMID 9891079.
“Formation and activation of a cyclin E-cdk2 complex during the G1 phase of the human cell cycle”. Science 257 (5077): 1689–94. (September 1992). doi:10.1126/science.1388288. PMID 1388288.
“mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability”. Genes & Development 18 (4): 423–34. (February 2004). doi:10.1101/gad.285504. PMC 359396. PMID 15004009.
“NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry”. The Journal of Biological Chemistry 275 (33): 25411–7. (August 2000). doi:10.1074/jbc.M001676200. PMID 10827081.
“Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation”. Oncogene 22 (28): 4301–13. (July 2003). doi:10.1038/sj.onc.1206606. PMID 12853968.
“Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication”. Molecular Cell 9 (3): 481–91. (March 2002). doi:10.1016/s1097-2765(02)00467-7. PMID 11931757.
“Regulation of cyclin A-Cdk2 by SCF component Skp1 and F-box protein Skp2”. Molecular and Cellular Biology 19 (1): 635–45. (January 1999). doi:10.1128/mcb.19.1.635. PMC 83921. PMID 9858587.
“TOK-1, a novel p21Cip1-binding protein that cooperatively enhances p21-dependent inhibitory activity toward CDK2 kinase”. The Journal of Biological Chemistry 275 (40): 31145–54. (October 2000). doi:10.1074/jbc.M003031200. PMID 10878006.
“Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms”. The Journal of Biological Chemistry 275 (44): 34744–9. (November 2000). doi:10.1074/jbc.M006210200. PMID 10934208.
“Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4”. Molecular and Cellular Biology 22 (7): 2242–54. (April 2002). doi:10.1128/mcb.22.7.2242-2254.2002. PMC 133692. PMID 11884610.
“Identification of a p130 domain mediating interactions with cyclin A/cdk 2 and cyclin E/cdk 2 complexes”. Oncogene 14 (20): 2395–406. (May 1997). doi:10.1038/sj.onc.1201085. PMID 9188854.
“Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation”. Nature Cell Biology 1 (1): 14–9. (May 1999). doi:10.1038/8984. PMID 10559858.

ensembl.org

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000123374 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000025358 - Ensembl, May 2017

nih.gov

pubmed.ncbi.nlm.nih.gov

“Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase”. Nature 353 (6340): 174–7. (September 1991). doi:10.1038/353174a0. PMID 1653904.
“Recent developments in cyclin-dependent kinase biochemical and structural studies”. Biochimica et Biophysica Acta 1804 (3): 511–9. (March 2010). doi:10.1016/j.bbapap.2009.10.002. PMID 19822225.
“Cdk2 knockout mice are viable”. Current Biology 13 (20): 1775–85. (October 2003). doi:10.1016/j.cub.2003.09.024. PMID 14561402.
van den Heuvel, S.; Harlow, E. (1993-12-24). “Distinct roles for cyclin-dependent kinases in cell cycle control”. Science (New York, N.Y.) 262 (5142): 2050–2054. doi:10.1126/science.8266103. ISSN 0036-8075. PMID 8266103.
“Promiscuity rules? The dispensability of cyclin E and Cdk2”. Science's STKE 2004 (224): pe11. (March 2004). doi:10.1126/stke.2242004pe11. PMC 3242733. PMID 15026579.
“Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms”. Oncogene 28 (33): 2925–39. (August 2009). doi:10.1038/onc.2009.170. PMID 19561645.
“Differences in the Conformational Energy Landscape of CDK1 and CDK2 Suggest a Mechanism for Achieving Selective CDK Inhibition”. Cell Chemical Biology 26 (1): 121–130.e5. (November 2018). doi:10.1016/j.chembiol.2018.10.015. PMC 6344228. PMID 30472117.
PDB: 1FIN; “Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex”. Nature 376 (6538): 313–20. (July 1995). doi:10.1038/376313a0. PMID 7630397.
“Cyclin-dependent kinases”. Genome Biology 15 (6): 122. (2014-06-30). doi:10.1186/gb4184. PMC 4097832. PMID 25180339.
PDB: 1W98; “The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles”. The EMBO Journal 24 (3): 452–63. (February 2005). doi:10.1038/sj.emboj.7600554. PMC 548659. PMID 15660127.
“Checking on DNA damage in S phase”. Nature Reviews. Molecular Cell Biology 5 (10): 792–804. (October 2004). doi:10.1038/nrm1493. PMID 15459660.
“Low-Molecular-Weight Cyclin E in Human Cancer: Cellular Consequences and Opportunities for Targeted Therapies”. Cancer Research 78 (19): 5481–5491. (October 2018). doi:10.1158/0008-5472.can-18-1235. PMC 6168358. PMID 30194068.
“RB and cell cycle progression”. Oncogene 25 (38): 5220–7. (August 2006). doi:10.1038/sj.onc.1209615. PMID 16936740.
“Pocket proteins and cell cycle control”. Oncogene 24 (17): 2796–809. (April 2005). doi:10.1038/sj.onc.1208619. PMID 15838516.
“NPAT links cyclin E-Cdk2 to the regulation of replication-dependent histone gene transcription”. Genes & Development 14 (18): 2283–97. (September 2000). doi:10.1101/gad.827700. PMC 316937. PMID 10995386.
“Loss of Cdk2 and cyclin A2 impairs cell proliferation and tumorigenesis”. Cancer Research 74 (14): 3870–9. (July 2014). doi:10.1158/0008-5472.CAN-13-3440. PMC 4102624. PMID 24802190.
“Inhibition of cyclin-dependent kinase 2 protects against doxorubicin-induced cardiomyocyte apoptosis and cardiomyopathy”. The Journal of Biological Chemistry 293 (51): 19672–19685. (October 2018). doi:10.1074/jbc.ra118.004673. PMC 6314117. PMID 30361442.
“Inhibitors of cyclin-dependent kinases as cancer therapeutics”. Pharmacology & Therapeutics 173: 83–105. (May 2017). doi:10.1016/j.pharmthera.2017.02.008. PMC 6141011. PMID 28174091.
“Roscovitine in cancer and other diseases”. Annals of Translational Medicine 3 (10): 135. (June 2015). doi:10.3978/j.issn.2305-5839.2015.03.61. PMC 4486920. PMID 26207228.
“CDK1 structures reveal conserved and unique features of the essential cell cycle CDK”. Nature Communications 6: 6769. (April 2015). doi:10.1038/ncomms7769. PMC 4413027. PMID 25864384.
“Structure-based discovery of the first allosteric inhibitors of cyclin-dependent kinase 2”. Cell Cycle 13 (14): 2296–305. (2014-06-09). doi:10.4161/cc.29295. PMC 4111683. PMID 24911186.
“Targeting Conformational Activation of CDK2 Kinase”. Biotechnology Journal 12 (8): 1600531. (August 2017). doi:10.1002/biot.201600531. PMID 28430399.
“Cleavage of p21Cip1/Waf1 and p27Kip1 mediates apoptosis in endothelial cells through activation of Cdk2: role of a caspase cascade”. Molecular Cell 1 (4): 553–63. (March 1998). doi:10.1016/S1097-2765(00)80055-6. PMID 9660939.
“Constituents of Mediterranean Spices Counteracting Vascular Smooth Muscle Cell Proliferation: Identification and Characterization of Rosmarinic Acid Methyl Ester as a Novel Inhibitor”. Molecular Nutrition & Food Research 62 (7): e1700860. (April 2018). doi:10.1002/mnfr.201700860. PMID 29405576.
“Critical role of CDK2 for melanoma growth linked to its melanocyte-specific transcriptional regulation by MITF”. Cancer Cell 6 (6): 565–76. (December 2004). doi:10.1016/j.ccr.2004.10.014. PMID 15607961.
“Novel MITF targets identified using a two-step DNA microarray strategy”. Pigment Cell & Melanoma Research 21 (6): 665–76. (December 2008). doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
“BRCA1 is a 220-kDa nuclear phosphoprotein that is expressed and phosphorylated in a cell cycle-dependent manner”. Cancer Research 56 (14): 3168–72. (July 1996). PMID 8764100.
“BRCA1 is phosphorylated at serine 1497 in vivo at a cyclin-dependent kinase 2 phosphorylation site”. Molecular and Cellular Biology 19 (7): 4843–54. (July 1999). doi:10.1128/MCB.19.7.4843. PMC 84283. PMID 10373534.
“BRCA1 proteins are transported to the nucleus in the absence of serum and splice variants BRCA1a, BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases”. Oncogene 15 (2): 143–57. (July 1997). doi:10.1038/sj.onc.1201252. PMID 9244350.
“p12(DOC-1) is a novel cyclin-dependent kinase 2-associated protein”. Molecular and Cellular Biology 20 (17): 6300–7. (September 2000). doi:10.1128/MCB.20.17.6300-6307.2000. PMC 86104. PMID 10938106.
“CRM1/Ran-mediated nuclear export of p27(Kip1) involves a nuclear export signal and links p27 export and proteolysis”. Molecular Biology of the Cell 14 (1): 201–13. (January 2003). doi:10.1091/mbc.E02-06-0319. PMC 140238. PMID 12529437.
“Tuberin binds p27 and negatively regulates its interaction with the SCF component Skp2”. The Journal of Biological Chemistry 279 (47): 48707–15. (November 2004). doi:10.1074/jbc.M405528200. PMID 15355997.
“Bcl-2 expression suppresses mismatch repair activity through inhibition of E2F transcriptional activity”. Nature Cell Biology 7 (2): 137–47. (February 2005). doi:10.1038/ncb1215. PMID 15619620.
“Spy1 interacts with p27Kip1 to allow G1/S progression”. Molecular Biology of the Cell 14 (9): 3664–74. (September 2003). doi:10.1091/mbc.E02-12-0820. PMC 196558. PMID 12972555.
“Rapamycin potentiates transforming growth factor beta-induced growth arrest in nontransformed, oncogene-transformed, and human cancer cells”. Molecular and Cellular Biology 22 (23): 8184–98. (December 2002). doi:10.1128/mcb.22.23.8184-8198.2002. PMC 134072. PMID 12417722.
“Abolishment of the interaction between cyclin-dependent kinase 2 and Cdk-associated protein phosphatase by a truncated KAP mutant”. Biochemical and Biophysical Research Communications 305 (2): 311–4. (May 2003). doi:10.1016/s0006-291x(03)00757-5. PMID 12745075.
“KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases”. Proceedings of the National Academy of Sciences of the United States of America 91 (5): 1731–5. (March 1994). doi:10.1073/pnas.91.5.1731. PMC 43237. PMID 8127873.
“The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases”. Cell 75 (4): 805–16. (November 1993). doi:10.1016/0092-8674(93)90499-g. PMID 8242751.
“C/EBPalpha arrests cell proliferation through direct inhibition of Cdk2 and Cdk4”. Molecular Cell 8 (4): 817–28. (October 2001). doi:10.1016/s1097-2765(01)00366-5. PMID 11684017.
“A distinct cyclin A is expressed in germ cells in the mouse”. Development 122 (1): 53–64. (January 1996). PMID 8565853.
“Characterization of a second human cyclin A that is highly expressed in testis and in several leukemic cell lines”. Cancer Research 57 (5): 913–20. (March 1997). PMID 9041194.
“Cyclin A1 directly interacts with B-myb and cyclin A1/cdk2 phosphorylate B-myb at functionally important serine and threonine residues: tissue-specific regulation of B-myb function”. Blood 97 (7): 2091–7. (April 2001). doi:10.1182/blood.v97.7.2091. PMID 11264176.
“The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases”. Nature Cell Biology 1 (7): 438–43. (November 1999). doi:10.1038/15674. PMID 10559988.
“Cyclin E associates with BAF155 and BRG1, components of the mammalian SWI-SNF complex, and alters the ability of BRG1 to induce growth arrest”. Molecular and Cellular Biology 19 (2): 1460–9. (February 1999). doi:10.1128/mcb.19.2.1460. PMC 116074. PMID 9891079.
“P21Waf1/Cip1 dysfunction in neuroblastoma: a novel mechanism of attenuating G0-G1 cell cycle arrest”. Cancer Research 63 (13): 3840–4. (July 2003). PMID 12839982.
“Formation and activation of a cyclin E-cdk2 complex during the G1 phase of the human cell cycle”. Science 257 (5077): 1689–94. (September 1992). doi:10.1126/science.1388288. PMID 1388288.
“mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability”. Genes & Development 18 (4): 423–34. (February 2004). doi:10.1101/gad.285504. PMC 359396. PMID 15004009.
“NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry”. The Journal of Biological Chemistry 275 (33): 25411–7. (August 2000). doi:10.1074/jbc.M001676200. PMID 10827081.
“Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation”. Oncogene 22 (28): 4301–13. (July 2003). doi:10.1038/sj.onc.1206606. PMID 12853968.
“Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication”. Molecular Cell 9 (3): 481–91. (March 2002). doi:10.1016/s1097-2765(02)00467-7. PMID 11931757.
“Regulation of cyclin A-Cdk2 by SCF component Skp1 and F-box protein Skp2”. Molecular and Cellular Biology 19 (1): 635–45. (January 1999). doi:10.1128/mcb.19.1.635. PMC 83921. PMID 9858587.
“TOK-1, a novel p21Cip1-binding protein that cooperatively enhances p21-dependent inhibitory activity toward CDK2 kinase”. The Journal of Biological Chemistry 275 (40): 31145–54. (October 2000). doi:10.1074/jbc.M003031200. PMID 10878006.
“Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms”. The Journal of Biological Chemistry 275 (44): 34744–9. (November 2000). doi:10.1074/jbc.M006210200. PMID 10934208.
“Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4”. Molecular and Cellular Biology 22 (7): 2242–54. (April 2002). doi:10.1128/mcb.22.7.2242-2254.2002. PMC 133692. PMID 11884610.
“Identification of a p130 domain mediating interactions with cyclin A/cdk 2 and cyclin E/cdk 2 complexes”. Oncogene 14 (20): 2395–406. (May 1997). doi:10.1038/sj.onc.1201085. PMID 9188854.
“Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation”. Nature Cell Biology 1 (1): 14–9. (May 1999). doi:10.1038/8984. PMID 10559858.

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

rcsb.org

PDB: 1FIN; “Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex”. Nature 376 (6538): 313–20. (July 1995). doi:10.1038/376313a0. PMID 7630397.
PDB: 1W98; “The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2-independent roles”. The EMBO Journal 24 (3): 452–63. (February 2005). doi:10.1038/sj.emboj.7600554. PMC 548659. PMID 15660127.

wikipedia.org

en.wikipedia.org

GRCh38: Ensembl release 89: ENSG00000123374 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000025358 - Ensembl, May 2017

worldcat.org

search.worldcat.org

van den Heuvel, S.; Harlow, E. (1993-12-24). “Distinct roles for cyclin-dependent kinases in cell cycle control”. Science (New York, N.Y.) 262 (5142): 2050–2054. doi:10.1126/science.8266103. ISSN 0036-8075. PMID 8266103.

worldcat.org

The molecular basis of cancer. Mendelsohn, John, 1936-, Gray, Joe W.,, Howley, Peter M.,, Israel, Mark A.,, Thompson, Craig (Craig B.) (Fourth ed.). Philadelphia, PA. (2015). ISBN 9781455740666. OCLC 870870610