Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Mekonnen Lemma Dechassa"'
Autor:
Payel Sen, Jie Luo, Arjan Hada, Solomon G. Hailu, Mekonnen Lemma Dechassa, Jim Persinger, Sandipan Brahma, Somnath Paul, Jeff Ranish, Blaine Bartholomew
Publikováno v:
Cell Reports, Vol 18, Iss 9, Pp 2135-2147 (2017)
Summary: The SWI/SNF chromatin remodeling complex is highly conserved from yeast to human, and aberrant SWI/SNF complexes contribute to human disease. The Snf5/SMARCB1/INI1 subunit of SWI/SNF is a tumor suppressor frequently lost in pediatric rhabdoi
Externí odkaz:
https://doaj.org/article/45e74331e16f4211a99bb29b8da26257
Autor:
Mekonnen Lemma Dechassa, Arjan Hada, Solomon G. Hailu, Blaine Bartholomew, Sandipan Brahma, Payel Sen, Jie Luo, Jeff Ranish, Somnath Paul, Jim Persinger
Publikováno v:
Cell Reports, Vol 18, Iss 9, Pp 2135-2147 (2017)
Summary: The SWI/SNF chromatin remodeling complex is highly conserved from yeast to human, and aberrant SWI/SNF complexes contribute to human disease. The Snf5/SMARCB1/INI1 subunit of SWI/SNF is a tumor suppressor frequently lost in pediatric rhabdoi
Autor:
Mekonnen Lemma Dechassa, Karolin Luger
Publikováno v:
Genome Organization and Function in the Cell Nucleus
Autor:
Jim Persinger, Bei Zhang, Blaine Bartholomew, Craig L. Peterson, Rachel A. Horowitz-Scherer, Christopher L. Woodcock, Mekonnen Lemma Dechassa
Publikováno v:
Molecular and Cellular Biology. 28:6010-6021
The SWI/SNF complex disrupts and mobilizes chromatin in an ATP-dependent manner. SWI/SNF interactions with nucleosomes were mapped by DNA footprinting and site-directed DNA and protein cross-linking when SWI/SNF was recruited by a transcription activ
Histone Acetylation near the Nucleosome Dyad Axis Enhances Nucleosome Disassembly by RSC and SWI/SNF
Autor:
Mridula Manohar, Justin A. North, Jennifer J. Ottesen, Nilanjana Chatterjee, Michael G. Poirier, Rashmi Prasad, Karolin Luger, Blaine Bartholomew, Mekonnen Lemma Dechassa
Signaling associated with transcription activation occurs through posttranslational modification of histones and is best exemplified by lysine acetylation. Lysines are acetylated in histone tails and the core domain/lateral surface of histone octamer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c85e774341e96b87c4f8f8cc46261c1
https://europepmc.org/articles/PMC4628061/
https://europepmc.org/articles/PMC4628061/
Autor:
Mekonnen Lemma Dechassa
Publikováno v:
Cancer Research. 77:5372-5372
Hepatocellular carcinoma (HCC) is one of the leading causes of cancer-related deaths worldwide. Accumulated evidence in the past decade has stablished that NASH, in addition to other well-identified risk factors, is becoming a major cause of HCC in U
Publikováno v:
Nucleic Acids Research
The assembly of centromeric nucleosomes is mediated by histone variant-specific chaperones. In budding yeast, the centromere-specific histone H3 variant is Cse4, and the histone chaperone Scm3 functions as a Cse4-specific nucleosome assembly factor.
Autor:
Barbara G. Mellone, Karolin Luger, Mekonnen Lemma Dechassa, Patrick Heun, Chin-Chi Chen, Emily Bettini, Christian Belisario, Mary B. Ledoux
Publikováno v:
Chen, C-C, Dechassa, M L, Bettini, E, Ledoux, M B, Belisario, C, Heun, P, Luger, K & Mellone, B G 2014, ' CAL1 is the Drosophila CENP-A assembly factor ', Journal of Cell Biology, vol. 204, no. 3, pp. 313-29 . https://doi.org/10.1083/jcb.201305036
The Journal of Cell Biology
The Journal of Cell Biology
Representing a unique family of histone assembly factors, CAL1 assembles the histone H3 variant CENP-A on centromeric DNA in Drosophila.
Centromeres are specified epigenetically by the incorporation of the histone H3 variant CENP-A. In humans, a
Centromeres are specified epigenetically by the incorporation of the histone H3 variant CENP-A. In humans, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::803c4d5ec4d37a647c6aef019ccaec6b
https://hdl.handle.net/20.500.11820/b12ad0b0-b5f0-46a9-b755-be65bc321b69
https://hdl.handle.net/20.500.11820/b12ad0b0-b5f0-46a9-b755-be65bc321b69
Publikováno v:
Cell. 138(1):22-24
The properties of centromeric nucleosomes have been the subject of considerable debate and controversy. Furuyama and Henikoff (2009) now provide surprising evidence that centromeric nucleosomes wrap DNA in an orientation that is opposite to that of c
Autor:
Alex M. Mooney, Blaine Bartholomew, Payel Sen, Mekonnen Lemma Dechassa, Paula Vivas, Michael G. Poirier
The SWI/SNF chromatin remodeling complex changes the positions where nucleosomes are bound to DNA, exchanges out histone dimers, and disassembles nucleosomes. All of these activities depend on ATP hydrolysis by the catalytic subunit Snf2, containing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b262d355fceae046c4f6114084b5cf9e
https://europepmc.org/articles/PMC3554119/
https://europepmc.org/articles/PMC3554119/