Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Yunhe Bao"'
Autor:
Prabodh Kapoor, Xuetong Shen, Alexsandra Espejo, Lin Yang, Guang Peng, Yunhe Bao, Mark T. Bedford, Jing Xiao
Publikováno v:
Molecular Cell. 58:863-869
ATP-dependent chromatin remodeling complexes such as INO80 have been implicated in checkpoint regulation in response to DNA damage. However, how chromatin remodeling complexes regulate DNA damage checkpoints remain unclear. Here, we identified a mech
Autor:
Judith A. Boyle, Laurie S. Minamide, Richard C. Davis, James R. Bamburg, Judith A. Coppinger, Yunhe Bao, Timothy Y. Huang, Gary M. Bokoch, John R. Yates, Sankar Maiti
Publikováno v:
Journal of Biological Chemistry. 285:5450-5460
Cofilin-actin bundles (rods), which form in axons and dendrites of stressed neurons, lead to synaptic dysfunction and may mediate cognitive deficits in dementias. Rods form abundantly in the cytoplasm of non-neuronal cells in response to many treatme
Autor:
Tammy S. Wehr, Jianjun Shen, Ashby J. Morrison, Xuetong Shen, Sean C. Hensley, Yunhe Bao, Sean R. Collins, Jung-Ae Kim, Nevan J. Krogan, Jeff Delrow, Jessica Highland, Maria D. Person, James E. Haber, Jing Xiao, Jonathan S. Weissman
Publikováno v:
Cell. 130(3):499-511
SummaryThe yeast Mec1/Tel1 kinases, ATM/ATR in mammals, coordinate the DNA damage response by phosphorylating proteins involved in DNA repair and checkpoint pathways. Recently, ATP-dependent chromatin remodeling complexes, such as the INO80 complex,
Autor:
Yunhe Bao, Xuetong Shen
Publikováno v:
Current Opinion in Genetics & Development. 17:126-131
ATP-dependent chromatin remodeling complexes use ATP hydrolysis to remodel nucleosomes and have well-established functions in transcription. However, emerging lines of evidence suggest that chromatin remodeling complexes are important players in DNA
Autor:
Jeff Ranish, Jianfeng Shen, Jie Luo, Xuetong Shen, Guang Peng, Yunhe Bao, Jing Xiao, Jim Persinger, Blaine Bartholomew, Prabodh Kapoor
ATP-dependent chromatin remodeling complexes alter chromatin structure through interactions with chromatin substrates such as DNA, histones, and nucleosomes. However, whether chromatin remodeling complexes have the ability to regulate nonchromatin su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ba92106e1960d18fa740297c7b1da5b
https://europepmc.org/articles/PMC4378192/
https://europepmc.org/articles/PMC4378192/
Publikováno v:
Journal of Molecular Biology. 361:617-624
Poly(dA.dT) DNA sequence elements are thought to promote transcription by either excluding nucleosomes or by altering their structural or dynamic properties. Here, the stability and structure of a defined nucleosome core particle containing a 16 base
Publikováno v:
Journal of Biological Chemistry. 280:1817-1825
Eukaryotic chromatin is highly dynamic and turns over rapidly even in the absence of DNA replication. Here we show that the acidic histone chaperone nucleosome assembly protein 1 (NAP-1) from yeast reversibly removes and replaces histone protein dime
Autor:
David J. Tremethick, Danny Rangasamy, Young-Jun Park, Paul J. Laybourn, Yunhe Bao, Simona Rosu, Karolin Luger, Kasey L. Konesky, Pamela N. Dyer
Publikováno v:
The EMBO Journal. 23:3314-3324
H2A.Bbd is an unusual histone variant whose sequence is only 48% conserved compared to major H2A. The major sequence differences are in the docking domain that tethers the H2A-H2B dimer to the (H3-H4)(2) tetramer; in addition, the C-terminal tail is
Publikováno v:
Cold Spring Harbor Symposia on Quantitative Biology. 69:227-234
protein to form chromatin, the fundamental unit of which is the nucleosome core particle (NCP). An NCP consists of two copies each of the four core histones H2A, H2B, H3, and H4. This histone octamer binds 147 base pairs of DNA around its outer surfa
Autor:
Yunhe Bao
Publikováno v:
Epigenomics. 3(3)
Manipulation of chromatin, in which genomic DNA is packaged, is a fundamental requirement for all DNA-based metabolic processes in eukayotic cells. Histone variant incorporation, histone post-translational modifications, and ATP-dependent chromatin r