Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Melissa N. Wells"'
Autor:
David T. Auble, A. Butryn, Ramya Viswanathan, Karl-Peter Hopfner, Melissa N. Wells, Petra Wollmann, Gregor Witte, Roland Beckmann, Manuela Moldt, Sheng Cui, Petra Wendler, Otto Berninghausen
Publikováno v:
Nature. 475:403-407
The Swi2/Snf2 family of proteins uses the energy of ATP hydrolysis to disrupt protein-DNA interactions, a process known as remodelling. In this study, Karl-Peter Hopfner and colleagues have solved the structure of the Mot1 ATPase in complex with the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::623456da0d8cd8186111bcc31ea374bf
https://doi.org/10.1038/nature10215
https://doi.org/10.1038/nature10215
Autor:
Stefan Bekiranov, Melissa N. Wells, David T. Auble, Ramya Viswanathan, Rebekka O. Sprouse, Kunal Poorey
Publikováno v:
Genome research. 20(12)
TATA-binding protein (TBP) nucleates the assembly of the transcription preinitiation complex (PIC), and although TBP can bind promoters with high stability in vitro, recent results establish that virtually the entire TBP population is highly dynamic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f28108d39d75f4cb43362c2d199619b
https://pubmed.ncbi.nlm.nih.gov/20855454
https://pubmed.ncbi.nlm.nih.gov/20855454
Mot1 is an essential TATA-binding protein (TBP)-associated factor and Snf2/Swi2 ATPase that both represses and activates transcription. Biochemical and structural results support a model in which ATP binding and hydrolysis induce a conformational cha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9316fe9eca9226689a189fcd7e8cb4dd
https://europepmc.org/articles/PMC2640957/
https://europepmc.org/articles/PMC2640957/
