Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Caroline E Weller"'
Autor:
Calvin Jon A Leonen, Miho Shimada, Caroline E Weller, Tomoyoshi Nakadai, Peter L Hsu, Elizabeth L Tyson, Arpit Mishra, Patrick MM Shelton, Martin Sadilek, R David Hawkins, Ning Zheng, Robert G Roeder, Champak Chatterjee
Publikováno v:
eLife, Vol 10 (2021)
The post-translational modification of histones by the small ubiquitin-like modifier (SUMO) protein has been associated with gene regulation, centromeric localization, and double-strand break repair in eukaryotes. Although sumoylation of histone H4 w
Externí odkaz:
https://doaj.org/article/30279bf7f3df4f09aea9e207bc1fc733
Autor:
Caroline E. Weller, Abhinav Dhall, Feizhi Ding, Edlaine Linares, Samuel D. Whedon, Nicholas A. Senger, Elizabeth L. Tyson, John D. Bagert, Xiaosong Li, Ohara Augusto, Champak Chatterjee
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
Chemical approaches to site-specifically ubiquitylate a target protein allow investigation of the biochemical effects of this modification, but they often destabilize the protein. Here, the authors report on a synthetic conjugation strategy that lead
Externí odkaz:
https://doaj.org/article/b48cef68f3dc4e9fa4b70b0add885ae3
Autor:
Elizabeth L. Tyson, Miho Shimada, Arpit Mishra, Peter L. Hsu, Caroline E. Weller, Martin Sadilek, Ning Zheng, Tomoyoshi Nakadai, Champak Chatterjee, Calvin Jon Antolin Leonen, Robert G. Roeder, Patrick M. M. Shelton, R. David Hawkins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b298b8926db9c9092119cb45d0aae510
https://doi.org/10.7554/elife.67952.sa2
https://doi.org/10.7554/elife.67952.sa2
Autor:
Tomoyoshi Nakadai, Miho Shimada, Champak Chatterjee, Patrick M. M. Shelton, Caroline E. Weller, Martin Sadilek, Ning Zheng, Calvin Jon Antolin Leonen, B. Roeder, Peter L. Hsu
Post-translational modification of histone H4 by the small ubiquitin-like modifier (SUMO) protein was associated with gene repression. However, this could not be proven due to the challenge of site-specifically sumoylating H4 in cells. Biochemical cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1205c5ee589f141fad356ee84ba1f62
https://doi.org/10.1101/2021.04.08.439039
https://doi.org/10.1101/2021.04.08.439039
Autor:
Arpit Mishra, Caroline E. Weller, Robert G. Roeder, Patrick M. M. Shelton, Miho Shimada, R. David Hawkins, Champak Chatterjee, Elizabeth L. Tyson, Peter L. Hsu, Ning Zheng, Martin Sadilek, Tomoyoshi Nakadai, Calvin Jon Antolin Leonen
Publikováno v:
eLife
eLife, Vol 10 (2021)
eLife, Vol 10 (2021)
The post-translational modification of histones by the small ubiquitin-like modifier (SUMO) protein has been associated with gene regulation, centromeric localization, and double-strand break repair in eukaryotes. Although sumoylation of histone H4 w
Autor:
Champak Chatterjee, Caroline E. Weller
Publikováno v:
Expressed Protein Ligation ISBN: 9781071604335
Methods Mol Biol
Methods Mol Biol
The post-translational modification of cellular proteins by ubiquitin (Ub), called ubiquitylation, is indispensable for the normal growth and development of eukaryotic organisms. In order to conduct studies that elucidate the precise mechanistic role
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b1dfd828c2f7a8cc8a7f7d7a62cbaaf
https://doi.org/10.1007/978-1-0716-0434-2_14
https://doi.org/10.1007/978-1-0716-0434-2_14
Publikováno v:
ACS Chemical Biology. 12:2275-2280
Lysine-specific demethylase 1 (LSD1) downregulates eukaryotic gene activity by demethylating mono and dimethylated Lys4 in histone H3. Elucidating the biochemical crosstalk of LSD1 with histone post-translational modifications (PTMs) is essential for
Autor:
Ukhyun Jo, Heng Li, Caroline E. Weller, Alan D. D'Andrea, Ning Zheng, Champak Chatterjee, Hyungjin Kim, Kah Suan Lim, Haibin Mao, Ji Sun, Thomas R. Hinds
Publikováno v:
Molecular Cell
Ubiquitin-specific proteases (USPs) constitute the largest family of deubiquitinating enzymes, whose catalytic competency is often modulated by their binding partners through unknown mechanisms. Here we report a series of crystallographic and biochem
Autor:
Christopher J. Schulze, Daniel M. Whalen, Adrian Liam Gill, Gert Kiss, Cregg James Joseph, Steve M. Kelsey, David Wildes, Abby Marquez, Alun Bermingham, Mae Saldajeno-Concar, Jacqueline Smith, Denise Reyes, Elena S. Koltun, Tiffany J. Choy, Robert J. Nichols, Yu C. Yang, Mallika Singh, Caroline E Weller, Mark A. Goldsmith, Richard Hansen
Publikováno v:
Molecular Cancer Therapeutics. 18:PR10-PR10
RAS proteins are small GTPases that drive cell proliferation and survival when bound to GTP. Mutant RAS proteins are found in approximately one-third of human cancers, and exist predominantly in the GTP-bound state, leading to excessive downstream si
Autor:
Caroline E. Weller, Champak Chatterjee
Publikováno v:
ChemBioChem. 16:2531-2536
Endless potential: The sixth Chemical Protein Synthesis Meeting, held recently in St. Augustine, Florida, showed the potential of peptide and protein chemistry when applied toward understanding and controlling complex biological processes. This repor