Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Ruth B. Pritchard"'
Autor:
Nicolas D. Werbeck, Vaibhav Kumar Shukla, Micha B. A. Kunze, Havva Yalinca, Ruth B. Pritchard, Lucas Siemons, Somnath Mondal, Simon O. R. Greenwood, John Kirkpatrick, Charles M. Marson, D. Flemming Hansen
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Human Histone Deacetylases (HDACs) regulate gene expression and are important drug targets. Here, the authors combine NMR measurements, enzymatic assays and molecular dynamics simulations and show that HDAC8 samples a catalytically active and an inac
Externí odkaz:
https://doaj.org/article/e6e3823b97f04066b0453b2d183e0a76
Autor:
Ruth B. Pritchard, D. Flemming Hansen
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-7 (2019)
Analysis of side-chain motions by NMR has so far been restricted to small proteins and methyl-bearing side chains. Here, the authors present NMR methods based on 13C direct detection of highly deuterated protein samples that yield sharp and well-reso
Externí odkaz:
https://doaj.org/article/0da10a54a94e459fb2afae5adb60909a
Autor:
Lucas Siemons, Vaibhav Kumar Shukla, Havva Yalinca, Micha B. A. Kunze, Ruth B. Pritchard, Charles M. Marson, Nicolas D. Werbeck, Somnath Mondal, John Kirkpatrick, D. Flemming Hansen, Simon O. R. Greenwood
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Nature Communications
Nature Communications
Histone deacetylases (HDACs) are key enzymes in epigenetics and important drug targets in cancer biology. Whilst it has been established that HDACs regulate many cellular processes, far less is known about the regulation of these enzymes themselves.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb020fcb612a7bfdd48bafb085624bc1
http://link.springer.com/article/10.1038/s41467-020-17610-w
http://link.springer.com/article/10.1038/s41467-020-17610-w
Autor:
Ruth B. Pritchard, D. Flemming Hansen, Henrike Heise, Boran Uluca-Yazgi, Lucas Siemons, Stephen McCarthy
Publikováno v:
Chemical Communications. 55:14107-14110
Chemical shifts are often the only nuclear magnetic resonance parameter that can be obtained for challenging macromolecular systems. Here we present a framework to derive the conformational sampling of isoleucine side chains from 13C chemical shifts
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8349600b66c043776aebb7e341ed13d6
https://doi.org/10.1039/c9cc06496f
https://doi.org/10.1039/c9cc06496f
Publikováno v:
The journal of physical chemistry letters. 10(8)
[Image: see text] Whether recent updates and new releases of atomistic force fields can model the structural and dynamical properties of proteins containing both folded and partially disordered domains is still unclear. To address this fundamental qu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b370a18c8cc2d6172976ca08e47b9738
https://pubmed.ncbi.nlm.nih.gov/30933516
https://pubmed.ncbi.nlm.nih.gov/30933516