Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Alex M. Mooney"'
Autor:
Michelle B. Ferdinand, Alex M. Mooney, Cecil J. Howard, John van Noort, Michael G. Poirier, Justin A. North, Matthew A. Shoffner, Jonathan W. Picking, Marek Simon, Jennifer J. Ottesen
Publikováno v:
Nucleic Acids Research
Nucleosomes contain ∼146 bp of DNA wrapped around a histone protein octamer that controls DNA accessibility to transcription and repair complexes. Posttranslational modification (PTM) of histone proteins regulates nucleosome function. To date, only
Autor:
Ralf Bundschuh, Justin A. North, Richard Fishel, Michael G. Poirier, Jennifer J. Ottesen, Sarah Javaid, Matthew A. Shoffner, John C. Shimko, Alex M. Mooney, Sean D. Rose
Publikováno v:
Nucleic Acids Research
Eukaryotic genomes are repetitively wrapped into nucleosomes that then regulate access of transcription and DNA repair complexes to DNA. The mechanisms that regulate extrinsic protein interactions within nucleosomes are unresolved. We demonstrate tha
Autor:
Nidhi Punja, Richard Fishel, Alex M. Mooney, Jennifer J. Ottesen, Mridula Manohar, Michael G. Poirier, Sarah Javaid
Publikováno v:
Molecular Cell. 36(6):1086-1094
DNA nucleotide mismatches and lesions arise on chromosomes that are a complex assortment of protein and DNA (chromatin). The fundamental unit of chromatin is a nucleosome that contains approximately 146 bp DNA wrapped around an H2A, H2B, H3, and H4 h
Autor:
Richard Fishel, Annick Edon, Jonathan W. Picking, Jennifer J. Ottesen, Mridula Manohar, Michael G. Poirier, Alex M. Mooney, Justin A. North, Robin J. Nakkula
Publikováno v:
Journal of Biological Chemistry. 284:23312-23321
Histone post-translational modifications are essential for regulating and facilitating biological processes such as RNA transcription and DNA repair. Fifteen modifications are located in the DNA-histone dyad interface and include the acetylation of H
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/