Zobrazeno 1 - 10
of 111
pro vyhledávání: '"Catherine A Musselman"'
Autor:
Matthew R Marunde, Harrison A Fuchs, Jonathan M Burg, Irina K Popova, Anup Vaidya, Nathan W Hall, Ellen N Weinzapfel, Matthew J Meiners, Rachel Watson, Zachary B Gillespie, Hailey F Taylor, Laylo Mukhsinova, Ugochi C Onuoha, Sarah A Howard, Katherine Novitzky, Eileen T McAnarney, Krzysztof Krajewski, Martis W Cowles, Marcus A Cheek, Zu-Wen Sun, Bryan J Venters, Michael-C Keogh, Catherine A Musselman
Publikováno v:
eLife, Vol 13 (2024)
Histone post-translational modifications (PTMs) play a critical role in chromatin regulation. It has been proposed that these PTMs form localized ‘codes’ that are read by specialized regions (reader domains) in chromatin-associated proteins (CAPs
Externí odkaz:
https://doaj.org/article/bb8066ecda624cd69e4af12da10f5a2d
Publikováno v:
STAR Protocols, Vol 4, Iss 2, Pp 102229- (2023)
Summary: Single-molecule fluorescence microscopy (SMFM) has been shown to be informative in understanding the interaction of chromatin-associated factors with nucleosomes, the basic building unit of chromatin. Here, we present a protocol for preparin
Externí odkaz:
https://doaj.org/article/c2930184011c480aafd9cde4a56594fb
Autor:
Saumya M De Silva, Alisha Dhiman, Surbhi Sood, Kilsia F Mercedes, William J Simmons, Morkos A Henen, Beat Vögeli, Emily C Dykhuizen, Catherine A Musselman
Publikováno v:
Nucleic Acids Research. 51:3631-3649
PBRM1 is a subunit of the PBAF chromatin remodeling complex, which is mutated in 40–50% of clear cell renal cell carcinoma patients. It is thought to largely function as a chromatin binding subunit of the PBAF complex, but the molecular mechanism u
Publikováno v:
iScience, Vol 24, Iss 2, Pp 102070- (2021)
Summary: Intrinsically disordered regions (IDRs) are abundant and play important roles in the function of chromatin-associated proteins (CAPs). These regions are often found at the N- and C-termini of CAPs and between structured domains, where they c
Externí odkaz:
https://doaj.org/article/8320e64705284e6eb079d57a69ef1798
Autor:
Jovylyn Gatchalian, Xiaodong Wang, Jinzen Ikebe, Khan L. Cox, Adam H. Tencer, Yi Zhang, Nathaniel L. Burge, Luo Di, Matthew D. Gibson, Catherine A. Musselman, Michael G. Poirier, Hidetoshi Kono, Jeffrey J. Hayes, Tatiana G. Kutateladze
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
The chromatin remodeller CHD4 contains two PHD finger reader domains that have been shown to bivalently recognize H3 histone tails. Here, the authors describe a mechanism by which the PHD fingers bind to the intact nucleosome core particle, revealing
Externí odkaz:
https://doaj.org/article/80503b36d74a4bc3b72aa20bc28f7b84
Autor:
Adam H. Tencer, Khan L. Cox, Luo Di, Joseph B. Bridgers, Jie Lyu, Xiaodong Wang, Jennifer K. Sims, Tyler M. Weaver, Hillary F. Allen, Yi Zhang, Jovylyn Gatchalian, Michael A. Darcy, Matthew D. Gibson, Jinzen Ikebe, Wei Li, Paul A. Wade, Jeffrey J. Hayes, Brian D. Strahl, Hidetoshi Kono, Michael G. Poirier, Catherine A. Musselman, Tatiana G. Kutateladze
Publikováno v:
Cell Reports, Vol 21, Iss 2, Pp 455-466 (2017)
Summary: Chromatin remodeling is required for genome function and is facilitated by ATP-dependent complexes, such as nucleosome remodeling and deacetylase (NuRD). Among its core components is the chromodomain helicase DNA binding protein 3 (CHD3) who
Externí odkaz:
https://doaj.org/article/7ca566c3011e443687e83fac93b1d9f8
Autor:
Ehsan Akbari, Eui-Jin Park, Ajit K. Singh, Vinayak Vinayak, Ranya K. A. Virk, Jeff Wereszczynksi, Catherine A. Musselman
Publikováno v:
Biophysical Reviews.
Autor:
Emma A. Morrison, Julio C. Sanchez, Jehnna L. Ronan, Daniel P. Farrell, Katayoun Varzavand, Jenna K. Johnson, Brian X. Gu, Gerald R. Crabtree, Catherine A. Musselman
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
BRG1 and BRM are central components of the BAF (mSWI/SNF) chromatin remodelling complex, which is critical for regulation of chromatin structure. Here, the authors provide evidence that both the BRG1 and hBRM bromodomains have DNA-binding activity an
Externí odkaz:
https://doaj.org/article/3649bcbbddde4952a8a4555506942341
Autor:
Catherine A. Musselman, Eugene Valkov
Publikováno v:
Current opinion in structural biology. 77
Publikováno v:
Journal of fluorescence.
Single molecule FRET (Forster resonance energy transfer) is very powerful method for studying biomolecular binding dynamics and conformational transitions. Only a few donor - acceptor dye pairs have been characterized for use in single-molecule FRET