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Yawen Bai, Ph.D.

Selected Publications

1)  Hong J, Feng H, Wang F, Ranjan A, Chen J, Jiang J, Ghirlando R, Xiao TS, Wu C, Bai Y.
The Catalytic Subunit of the SWR1 Remodeler Is a Histone Chaperone for the H2A.Z-H2B Dimer.
Mol. Cell. 53: 498-505, 2014.
2)  Kato H, Jiang J, Zhou B, Rozendaal M, Feng H, Ghirlando R, Xiao T, Straight A, Bai Y.
A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C.
Science. 340: 111--3, 2013.
3)  Kato H, Zhou BR, Feng H, Bai Y.
An evolving tail of centromere histone variant CENP-A.
Cell Cycle. 12: 3133-4, 2013.
4)  Hong J, Feng H, Zhou Z, Ghirlando R, Bai Y.
Identification of functionally conserved regions in the structure of the chaperone/CenH3/H4 complex.
J. Mol. Biol. 425: 536-45, 2013.
5)  Zhou BR, Feng H, Kato H, Dai L, Yang Y, Zhou Y, Bai Y.
Structural insights into the histone H1-nucleosome complex.
Proc. Natl. Acad. Sci. U.S.A. 110: 19390-5, 2013.
6)  Zhou BR, Feng H, Ghirlando R, Kato H, Gruschus J, Bai Y.
Histone H4 K16Q mutation, an acetylation mimic, causes structural disorder of its N-terminal basic patch in the nucleosome.
J. Mol. Biol. 421: 30-7, 2012.
7)  Chu X, Wang Y, Gan L, Bai Y, Han W, Wang E, Wang J.
Importance of electrostatic interactions in the association of intrinsically disordered histone chaperone Chz1 and histone H2A.Z-H2B.
PLoS Comput. Biol. 8: e1002608, 2012.
8)  Kato H, van Ingen H, Zhou B, Feng H, Bustin M, Kay LE, Bai Y.
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Proc. Natl. Acad. Sci. U.S.A. 108: 12283-8, 2011.
9)  Bai Y, Zhou Z, Feng H, Zhou B.
Recognition of centromeric histone variant CenH3s by their chaperones-Structurally conserved or not.
Cell Cycle. 10: 3217-3218, 2011.
10)  Zhou Z, Feng H, Zhou B, Ghirlando R, Hu K, Zwolak A, Jenkins LM, Xiao H, Tjandra N, Wu C, Bai Y.
Structural basis for recognition of centromeric histone variant CenH3 by the Scm3 chaperone.
Nature. 472: 234-237, 2011.
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This page was last updated on 4/28/2014.