Charged multivesicular body protein 1b is a protein that in humans is encoded by the CHMP1Bgene.[1][2]
References
↑Reid E, Connell J, Edwards TL, Duley S, Brown SE, Sanderson CM (Dec 2004). "The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B". Hum Mol Genet. 14 (1): 19–38. doi:10.1093/hmg/ddi003. PMID15537668.
Vuoristo JT, Berrettini WH, Ala-Kokko L (2001). "C18orf2, a novel, highly conserved intronless gene within intron 5 of the GNAL gene on chromosome 18p11". Cytogenet. Cell Genet. 93 (1–2): 19–22. doi:10.1159/000056940. PMID11474171.
Stauffer DR, Howard TL, Nyun T, Hollenberg SM (2002). "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression". J. Cell Sci. 114 (Pt 13): 2383–93. PMID11559747.
Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (2002). "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins". J. Cell Sci. 114 (Pt 13): 2395–404. PMID11559748.
Strack B, Calistri A, Craig S, et al. (2003). "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding". Cell. 114 (6): 689–99. doi:10.1016/S0092-8674(03)00653-6. PMID14505569.
Tsang HT, Connell JW, Brown SE, et al. (2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex". Genomics. 88 (3): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID16730941.
Row PE, Liu H, Hayes S, et al. (2007). "The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation". J. Biol. Chem. 282 (42): 30929–37. doi:10.1074/jbc.M704009200. PMID17711858.
