Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Adewola Osunsade"'
Autor:
Tuan Nguyen, Sai Li, Jeremy T-H Chang, John W. Watters, Htet Ng, Adewola Osunsade, Yael David, Shixin Liu
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
Here the authors used single-molecule imaging and manipulation to study the mechanical effects of transcription factor Sox2 co-condensation with DNA and chromatin. They found that Sox2 condensates exert a high level of mechanical stress on DNA, but t
Externí odkaz:
https://doaj.org/article/a5fc41cecb574669a410977790cd6293
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-8 (2020)
Protein arginine deiminase 4 (PAD4) facilitates the posttranslational citrullination of histones H3 and H4. Here, the authors provide evidence that PAD4 antagonizes histone methylglyoxal-glycation by rewriting the glycated arginine into citrulline an
Externí odkaz:
https://doaj.org/article/fced30f35c3c4c4fa7ad21938c03dc03
Autor:
Qingfei Zheng, Nathaniel D. Omans, Rachel Leicher, Adewola Osunsade, Albert S. Agustinus, Efrat Finkin-Groner, Hannah D’Ambrosio, Bo Liu, Sarat Chandarlapaty, Shixin Liu, Yael David
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Proteins continuously undergo non-enzymatic modifications such as glycation, which accumulate under physiological conditions but can be enhanced in disease. Here the authors characterise histone glycation, provide evidence that it affects chromatin,
Externí odkaz:
https://doaj.org/article/d549df8147a043739d0eb71b8d597555
Autor:
Ethel Cesarman, Ashley S. Doane, Andreas Kloetgen, Joseph Conway, Jeannie M. Camarillo, Olivier Elemento, Neil L. Kelleher, Stephanie Portillo-Ledesma, Adewola Osunsade, Christopher E. Mason, Bryan J. Venters, Ari Melnick, Yael David, Alexey A. Soshnev, Tamar Schlick, Marcin Imielinski, David Scott, Aristotelis Tsirigos, Christopher R. Chin, Wendy Béguelin, Eftychia Apostolou, Arthur I. Skoultchi, Jonathan D. Licht, C. David Allis, Louis M. Staudt, Jude M. Phillip, Nevin Yusufova, Michael-Christopher Keogh, Matt Teater
Publikováno v:
Nature
Linker histone H1 proteins bind to nucleosomes and facilitate chromatin compaction1, although their biological functions are poorly understood. Mutations in the genes that encode H1 isoforms B–E (H1B, H1C, H1D and H1E; also known as H1-5, H1-2, H1-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57badeea50b93be34e01e83a6c86b178
http://europepmc.org/articles/PMC7855728
http://europepmc.org/articles/PMC7855728
Autor:
Rachel Leicher, Adewola Osunsade, Gabriella N. L. Chua, Sarah C. Faulkner, Andrew P. Latham, John W. Watters, Tuan Nguyen, Emily C. Beckwitt, Sophia Christodoulou-Rubalcava, Paul G. Young, Bin Zhang, Yael David, Shixin Liu
Publikováno v:
Nat Struct Mol Biol
The H1 linker histone family is the most abundant group of eukaryotic chromatin-binding proteins. However, their contribution to chromosome structure and function remains incompletely understood. Here we use single-molecule fluorescence and force mic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b13d9511e093efc8eba43aa873cd6fbc
https://europepmc.org/articles/PMC9117509/
https://europepmc.org/articles/PMC9117509/
Autor:
Tuan Nguyen, Sai Li, Jeremy T-H Chang, John W. Watters, Htet Ng, Adewola Osunsade, Yael David, Shixin Liu
Publikováno v:
Nature communications. 13(1)
Formation of biomolecular condensates constitutes an emerging mechanism for transcriptional regulation. Recent studies suggest that the co-condensation between transcription factors (TFs) and DNA can generate mechanical forces driving genome rearrang
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f19b56072e744a79346f5cfe5c7ab082
https://pubmed.ncbi.nlm.nih.gov/35810158
https://pubmed.ncbi.nlm.nih.gov/35810158
Autor:
Rachel Leicher, Adewola Osunsade, Gabriella N.L. Chua, Sarah C. Faulkner, Andrew P. Latham, John W. Watters, Tuan A. Nguyen, Emily C. Beckwitt, Sophia Christodoulou-Rubalcava, Paul G. Young, Bin Zhang, Yael David, Shixin Liu
Publikováno v:
Biophysical Journal. 121:357a-358a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1d755444ac58fb09e41371464a30fb3c
https://doi.org/10.1016/j.bpj.2021.11.974
https://doi.org/10.1016/j.bpj.2021.11.974
Autor:
Rachel Leicher, Albert S Agustinus, Qingfei Zheng, Bo Liu, Yael David, Adewola Osunsade, Efrat Finkin-Groner, Hannah K. D'Ambrosio, Shixin Liu, Nathaniel D. Omans, Sarat Chandarlapaty
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Nature Communications
Nature Communications
Cellular proteins continuously undergo non-enzymatic covalent modifications (NECMs) that accumulate under normal physiological conditions and are stimulated by changes in the cellular microenvironment. Glycation, the hallmark of diabetes, is a preval
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeb1ed10f1f1cd0b28b91fa3db2cea98
https://doaj.org/article/d549df8147a043739d0eb71b8d597555
https://doaj.org/article/d549df8147a043739d0eb71b8d597555
Autor:
Bin Zhang, Chua Gnl, Christodoulou-Rubalcava S, Rachel Leicher, Watters Jw, Adewola Osunsade, David Y, Shixin Liu, Andrew P. Latham
The linker histone H1 is the most abundant group of eukaryotic chromatin-binding proteins. The mechanism underlying the diverse physiological functions of H1 remains unclear. Here we used single-molecule fluorescence and force microscopy to observe t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dee473f92e672a9853326cd6b43bf4db
https://doi.org/10.1101/2021.03.17.435841
https://doi.org/10.1101/2021.03.17.435841
Autor:
Yael David, Karin A. Skalina, Benjamin A. Garcia, Cary N. Weiss, Adewola Osunsade, Chul Hwan Lee, Yair Botbol, Jie Zhao, Ari Melnick, Michael A. Willcockson, Sean E. Healton, Fernando Macian, Ethel Cesarman, Winfried Edelmann, Harry Hou, Arthur I. Skoultchi, Hugo Pinto, Boris Bartholdy, Dhruv S. Sidhwani, Maxim I. Maron, Laura Norwood Toro, Tommy J. Wilson, Simone Sidoli, Nevin Yusufova, Laxmi N. Mishra, Cem Meydan
Publikováno v:
Nature
H1 linker histones are the most abundant chromatin-binding proteins(1). In vitro studies indicate that their association with chromatin determines nucleosome spacing and enables arrays of nucleosomes to fold into more compact chromatin structures. Ho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4851ae9d104cc9b8e0ee822e8581f22d
https://europepmc.org/articles/PMC8110206/
https://europepmc.org/articles/PMC8110206/