CKS1B
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. PMID 7791211.
“Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1.”. Cell 84 (6):  863–74. (1996). doi:10.1016/S0092-8674(00)81065-X. PMID 8601310.
“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. PMID 8697818.
“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. PMID 11231585.
“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. PMID 12140288.
“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. PMID 12473461.
“Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.”. Proc. Natl. Acad. Sci. U.S.A. 99 (26):  16899–903. (2003). doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241/.
“Protein-protein interactions involved in the recognition of p27 by E3 ubiquitin ligase.”. Biochem. J. 371 (Pt 3):  957–64. (2003). doi:10.1042/BJ20021722. PMC 1223319. PMID 12529174. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223319/.
“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. PMID 12813041.
“Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase.”. Nature 428 (6979):  190–3. (2004). doi:10.1038/nature02330. PMID 15014502.
“The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”. Genome Res. 14 (10B):  2121–7. (2004). doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928/.
“Role of Cks1 overexpression in oral squamous cell carcinomas: cooperation with Skp2 in promoting p27 degradation.”. Am. J. Pathol. 165 (6):  2147–55. (2005). doi:10.1016/S0002-9440(10)63264-6. PMC 1618711. PMID 15579456. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1618711/.
“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. PMID 15772084.
“The expression of the ubiquitin ligase subunit Cks1 in human breast cancer.”. Breast Cancer Res. 7 (5):  R737–44. (2006). doi:10.1186/bcr1278. PMC 1242136. PMID 16168119. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1242136/.
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.”. Hematology 10 Suppl 1 (4):  117–26. doi:10.1080/10245330512331390140. PMID 16188652.
“Towards a proteome-scale map of the human protein-protein interaction network.”. Nature 437 (7062):  1173–8. (2005). Bibcode: 2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
“Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase.”. Mol. Cell 20 (1):  9–19. (2005). doi:10.1016/j.molcel.2005.09.003. PMID 16209941.
“Mutant B-RAF signaling and cyclin D1 regulate Cks1/S-phase kinase-associated protein 2-mediated degradation of p27Kip1 in human melanoma cells.”. Oncogene 26 (7):  1056–66. (2007). doi:10.1038/sj.onc.1209861. PMID 16924241.
“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. PMID 16979657.