CENP-F
関連文献

“Mitosin/CENP-F in mitosis, transcriptional control, and differentiation.”. J. Biomed. Sci. 13 (2):  205–13. (2006). doi:10.1007/s11373-005-9057-3. PMID 16456711.
“CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis.”. J. Cell Biol. 130 (3):  507–18. (1995). doi:10.1083/jcb.130.3.507. PMC 2120529. PMID 7542657. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120529/.
“A novel cell-cycle-dependent 350-kDa nuclear protein: C-terminal domain sufficient for nuclear localization.”. Biochem. Biophys. Res. Commun. 212 (1):  220–8. (1995). doi:10.1006/bbrc.1995.1959. PMID 7612011.
“The C terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization.”. J. Biol. Chem. 270 (33):  19545–50. (1995). doi:10.1074/jbc.270.33.19545. PMID 7642639.
“Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression.”. Mol. Cell. Biol. 15 (9):  5017–29. (1995). doi:10.1128/MCB.15.9.5017. PMC 230749. PMID 7651420. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC230749/.
“Identification of a novel cytoplasmic protein that specifically binds to nuclear localization signal motifs.”. J. Biol. Chem. 273 (11):  6183–9. (1998). doi:10.1074/jbc.273.11.6183. PMID 9497340.
“Characterization of the kinetochore binding domain of CENP-E reveals interactions with the kinetochore proteins CENP-F and hBUBR1.”. J. Cell Biol. 143 (1):  49–63. (1998). doi:10.1083/jcb.143.1.49. PMC 2132809. PMID 9763420. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132809/.
Zhu X (1999). “Structural requirements and dynamics of mitosin-kinetochore interaction in M phase.”. Mol. Cell. Biol. 19 (2):  1016–24. doi:10.1128/MCB.19.2.1016. PMC 116032. PMID 9891037. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC116032/.
“Immunohistochemical analysis of the proliferation associated nuclear antigen CENP-F in non-Hodgkin's lymphoma.”. Mod. Pathol. 12 (1):  69–74. (1999). PMID 9950165.
“The cloning and analysis of LEK1 identifies variations in the LEK/centromere protein F/mitosin gene family.”. J. Biol. Chem. 274 (26):  18597–604. (1999). doi:10.1074/jbc.274.26.18597. PMID 10373470.
“Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules.”. J. Biol. Chem. 275 (39):  30451–7. (2000). doi:10.1074/jbc.M003469200. PMID 10852915.
“M phase-specific association of human topoisomerase IIIbeta with chromosomes.”. Biochem. Biophys. Res. Commun. 287 (1):  282–7. (2001). doi:10.1006/bbrc.2001.5580. PMID 11549288.
“Farnesylation of Cenp-F is required for G2/M progression and degradation after mitosis.”. J. Cell Sci. 115 (Pt 17):  3403–14. (2003). doi:10.1242/jcs.115.17.3403. PMID 12154071.
“Synergistic interaction of lovastatin and paclitaxel in human cancer cells.”. Mol. Cancer Ther. 1 (2):  141–9. (2003). PMID 12467231.
“Mitosin, a novel marker of cell proliferation and early recurrence in intracranial meningiomas.”. Histol. Histopathol. 18 (1):  67–74. (2003). PMID 12507285.
“Mitosin/CENP-F is a conserved kinetochore protein subjected to cytoplasmic dynein-mediated poleward transport.”. Cell Res. 13 (4):  275–83. (2004). doi:10.1038/sj.cr.7290172. PMID 12974617.
“FoxM1 is required for execution of the mitotic programme and chromosome stability.”. Nat. Cell Biol. 7 (2):  126–36. (2005). doi:10.1038/ncb1217. PMID 15654331.
“Mitosin/CENP-F as a negative regulator of activating transcription factor-4.”. J. Biol. Chem. 280 (14):  13973–7. (2005). doi:10.1074/jbc.M414310200. PMID 15677469.