Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Matthew R Marunde"'
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
Autor:
Kanishk Jain, Matthew R Marunde, Jonathan M Burg, Susan L Gloor, Faith M Joseph, Karl F Poncha, Zachary B Gillespie, Keli L Rodriguez, Irina K Popova, Nathan W Hall, Anup Vaidya, Sarah A Howard, Hailey F Taylor, Laylo Mukhsinova, Ugochi C Onuoha, Emily F Patteson, Spencer W Cooke, Bethany C Taylor, Ellen N Weinzapfel, Marcus A Cheek, Matthew J Meiners, Geoffrey C Fox, Kevin EW Namitz, Martis W Cowles, Krzysztof Krajewski, Zu-Wen Sun, Michael S Cosgrove, Nicolas L Young, Michael-Christopher Keogh, Brian D Strahl
Publikováno v:
eLife, Vol 12 (2023)
In nucleosomes, histone N-terminal tails exist in dynamic equilibrium between free/accessible and collapsed/DNA-bound states. The latter state is expected to impact histone N-termini availability to the epigenetic machinery. Notably, H3 tail acetylat
Externí odkaz:
https://doaj.org/article/4578fc571e78426c9ad347f2e09aa9c9
Autor:
Stefan A Zukin, Matthew R Marunde, Irina K Popova, Katarzyna M Soczek, Eva Nogales, Avinash B Patel
Publikováno v:
eLife, Vol 11 (2022)
The NuA4 protein complex acetylates histones H4 and H2A to activate both transcription and DNA repair. We report the 3.1-Å resolution cryo-electron microscopy structure of the central hub of NuA4, which flexibly tethers the histone acetyltransferase
Externí odkaz:
https://doaj.org/article/40a0833a16aa44ceba92ff7511f59cb4
Autor:
Kyle C Wilcox, Matthew R Marunde, Aditi Das, Pauline T Velasco, Benjamin D Kuhns, Michael T Marty, Haoming Jiang, Chi-Hao Luan, Stephen G Sligar, William L Klein
Publikováno v:
PLoS ONE, Vol 10, Iss 4, p e0125263 (2015)
Despite their value as sources of therapeutic drug targets, membrane proteomes are largely inaccessible to high-throughput screening (HTS) tools designed for soluble proteins. An important example comprises the membrane proteins that bind amyloid β
Externí odkaz:
https://doaj.org/article/09975a8c58e848ea9ad0aaa832ef9023
Autor:
Marcus A. Cheek, Aiping Dong, Renato Ferreira de Freitas, Dalia Barsyte-Lovejoy, Aliakbar Khalili Yazdi, Jinrong Min, Fengling Li, Victoria Vu, Albina Bolotokova, Lindsey I. James, Jack Greenblatt, Naimee Mehta, Irina K. Popova, David Dilworth, Ming Lei, Raquel Arminda Carvalho Machado, Ronan P Hanley, David Y Nie, Matthieu Schapira, Mengqi Zhou, Elisa Gibson, Cheryl H. Arrowsmith, Michael-Christopher Keogh, Suzanne Ackloo, Matthew R. Marunde, Mona Alqazzaz, Dmitri Kireev, Nathan W. Hall, Peter Brown, Abdellah Allali-Hassani, Sina Kazemzadeh, Edyta Marcon, Tigran M. Abramyan, Dominic D G Owens, Yanli Liu, Magdalena M. Szewczyk, Matthew J. Meiners, Irene Chau, Su Qin, Masoud Vedadi
Publikováno v:
Nat Chem Biol
Nuclear receptor-binding SET domain-containing 2 (NSD2) is the primary enzyme responsible for the dimethylation of lysine 36 of histone 3 (H3K36), a mark associated with active gene transcription and intergenic DNA methylation. In addition to a methy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a29b52d0f1e30e6d3bd73de3c2a5989b
https://doi.org/10.1038/s41589-021-00898-0
https://doi.org/10.1038/s41589-021-00898-0
The NuA4 protein complex acetylates histones H4 and H2A to activate both transcription and DNA repair. We report the 3.0 Å-resolution cryo-electron microscopy structure of the central hub of NuA4, which flexibly tethers the HAT and TINTIN modules. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3653070a7ae396ada1661196b4f9eaa3
https://doi.org/10.1101/2022.06.24.497536
https://doi.org/10.1101/2022.06.24.497536
Autor:
Douglas Barrows, Matthew R. Marunde, C. David Allis, Xiao Chen, Cynthia Horth, Phillip Rosenbaum, Michael-Christopher Keogh, Daniel N. Weinberg, Irina K. Popova, Chao Lu, Jacek Majewski, Zachary B. Gillespie
Publikováno v:
Nat Genet
Precise deposition of CpG methylation is critical for mammalian development and tissue homeostasis and is often dysregulated in human diseases. The localization of de novo DNA methyltransferase DNMT3A is facilitated by its PWWP domain recognizing his
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00a78d76b60034f02c0ddcd6a8fa163a
https://doi.org/10.1038/s41588-021-00856-5
https://doi.org/10.1038/s41588-021-00856-5
Autor:
Lu Sun, Hannah Willis, Matthew R. Marunde, Vishnu U. Kumary, Matthew J. Meiners, Saarang Gopinath, Jonathan M. Burg, Bryan J. Venters, Allison Hickman, Zu-Wen Sun, Martis W. Cowles, Pierre Esteve, Hang Gyeong Chin, Chaithanya Ponnaluri, Sriharsa Pradhan, Michael-Christopher Keogh
Publikováno v:
Cancer Research. 83:4728-4728
Chromatin remodeling is mediated by ATP-dependent enzymes that play key roles regulating gene expression and genome replication/repair. Aberrant nucleosome organization from dysregulated chromatin remodeling can severely alter chromatin accessibility
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea34cab5bb0c8f6e2385230ae125ff9d
https://doi.org/10.1158/1538-7445.am2023-4728
https://doi.org/10.1158/1538-7445.am2023-4728
Autor:
Karen C. Glass, Cameron Montgomery, Jonathan T. Lloyd, Kyle McLaughlin, Matthew R. Marunde, Chiara M. Evans, Samuel P. Boyson, Michael‐Christopher Keogh, Seth Frietze
Publikováno v:
The FASEB Journal. 36
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e82c9b73f62936c1df5f92796891fe4
https://doi.org/10.1096/fasebj.2022.36.s1.0r269
https://doi.org/10.1096/fasebj.2022.36.s1.0r269