↑“Human cDNAs encoding homologs of the small p34Cdc28/Cdc2-associated protein of Saccharomyces cerevisiae and Schizosaccharomyces pombe”.Genes Dev4(8): 1332–44.(Dec 1990).doi:10.1101/gad.4.8.1332.PMID2227411.
↑“Cks1 regulates cdk1 expression: a novel role during mitotic entry in breast cancer cells”.Cancer Res.67(23): 11393–401.(December 2007).doi:10.1158/0008-5472.CAN-06-4173.PMID18056467.
12“A negatively charged amino acid in Skp2 is required for Skp2-Cks1 interaction and ubiquitination of p27Kip1”.J. Biol. Chem.278(34): 32390–6.(August 2003).doi:10.1074/jbc.M305241200.PMID12813041.
12“Three different binding sites of Cks1 are required for p27-ubiquitin ligation”.J. Biol. Chem.277(44): 42233–40.(November 2002).doi:10.1074/jbc.M205254200.PMID12140288.
↑“The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27”.Nat. Cell Biol.3(3): 321–4.(March 2001).doi:10.1038/35060126.PMID11231585.
↑“Dual-specificity phosphatase 1 ubiquitination in extracellular signal-regulated kinase-mediated control of growth in human hepatocellular carcinoma”.Cancer Res.68(11): 4192–200.(June 2008).doi:10.1158/0008-5472.CAN-07-6157.PMID18519678.
関連文献
“Crystal structure of the human cell cycle protein CksHs1: single domain fold with similarity to kinase N-lobe domain.”.J. Mol. Biol.249(5): 835–42.(1995).doi:10.1006/jmbi.1995.0341.PMID7791211.
“Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1.”.Cell84(6): 863–74.(1996).doi:10.1016/S0092-8674(00)81065-X.PMID8601310.
“Chromosomal mapping of the human genes CKS1 to 8q21 and CKS2 to 9q22.”.Cytogenet. Cell Genet.73(3): 250–4.(1996).doi:10.1159/000134349.PMID8697818.
“The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27.”.Nat. Cell Biol.3(3): 321–4.(2001).doi:10.1038/35060126.PMID11231585.
“Three different binding sites of Cks1 are required for p27-ubiquitin ligation.”.J. Biol. Chem.277(44): 42233–40.(2003).doi:10.1074/jbc.M205254200.PMID12140288.
“Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family.”.J. Mol. Biol.325(1): 189–99.(2003).doi:10.1016/S0022-2836(02)01202-0.PMID12473461.
“A negatively charged amino acid in Skp2 is required for Skp2-Cks1 interaction and ubiquitination of p27Kip1.”.J. Biol. Chem.278(34): 32390–6.(2003).doi:10.1074/jbc.M305241200.PMID12813041.
“Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase.”.Nature428(6979): 190–3.(2004).doi:10.1038/nature02330.PMID15014502.
“Role of conformational heterogeneity in domain swapping and adapter function of the Cks proteins.”.J. Biol. Chem.280(34): 30448–59.(2005).doi:10.1074/jbc.M501450200.PMID15772084.
Shaughnessy J(2006).“Amplification and overexpression of CKS1B at chromosome band 1q21 is associated with reduced levels of p27Kip1 and an aggressive clinical course in multiple myeloma.”.Hematology10 Suppl 1(4): 117–26.doi:10.1080/10245330512331390140.PMID16188652.
“Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase.”.Mol. Cell20(1): 9–19.(2005).doi:10.1016/j.molcel.2005.09.003.PMID16209941.
“Mutant B-RAF signaling and cyclin D1 regulate Cks1/S-phase kinase-associated protein 2-mediated degradation of p27Kip1 in human melanoma cells.”.Oncogene26(7): 1056–66.(2007).doi:10.1038/sj.onc.1209861.PMID16924241.
“Activation of ubiquitin ligase SCF(Skp2) by Cks1: insights from hydrogen exchange mass spectrometry.”.J. Mol. Biol.363(3): 673–86.(2006).doi:10.1016/j.jmb.2006.08.032.PMID16979657.