Zobrazeno 1 - 10
of 61
pro vyhledávání: '"Robert O J, Weinzierl"'
Autor:
Sven Nottebaum, Robert O. J. Weinzierl
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
Nanoarchaea represent a highly diverged archaeal phylum that displays many unusual biological features. The Nanoarchaeum equitans genome encodes a complete set of RNA polymerase (RNAP) subunits and basal factors. Several of the standard motifs in the
Externí odkaz:
https://doaj.org/article/35aceeb8d0e94eb3b97dc2b7d8de1cc2
Publikováno v:
Biomolecules, Vol 10, Iss 9, p 1289 (2020)
Mapping the route of nucleoside triphosphate (NTP) entry into the sequestered active site of RNA polymerase (RNAP) has major implications for elucidating the complete nucleotide addition cycle. Constituting a dichotomy that remains to be resolved, tw
Externí odkaz:
https://doaj.org/article/adbc9368db32426c9fb75674528637ee
Publikováno v:
Biomolecules, Vol 10, Iss 9, p 1205 (2020)
The human mediator subunit MED25 acts as a coactivator that binds the transcriptional activation domains (TADs) present in various cellular and viral gene-specific transcription factors. Previous studies, including on NMR measurements and site-direct
Externí odkaz:
https://doaj.org/article/0f3d5a1ee59f44e287ad2f93d1816f73
Autor:
Robert O J, Weinzierl
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2466
A completely automated purification of glutathione-S-transferase (GST) fusion proteins, either in soluble form or after renaturation of insoluble inclusion bodies, is described. Depending on the expression levels and the amount of glutathione affinit
Publikováno v:
PLoS Computational Biology, Vol 12, Iss 5, p e1004935 (2016)
Transcriptional activation domains (ADs) are generally thought to be intrinsically unstructured, but capable of adopting limited secondary structure upon interaction with a coactivator surface. The indeterminate nature of this interface made it hithe
Externí odkaz:
https://doaj.org/article/8c416b49fbd64c4b83f874c19d3272a9
Autor:
Robert O. J. Weinzierl
Publikováno v:
Methods in Molecular Biology ISBN: 9781071621752
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b1857dd796898d33ea8640da98218f56
https://doi.org/10.1007/978-1-0716-2176-9_7
https://doi.org/10.1007/978-1-0716-2176-9_7
Autor:
Robert O. J. Weinzierl
Publikováno v:
Biomolecules, Vol 11, Iss 856, p 856 (2021)
Biomolecules
Volume 11
Issue 6
Biomolecules
Volume 11
Issue 6
The human transcription factor FOXO3 (a member of the ‘forkhead’ family of transcription factors) controls a variety of cellular functions that make it a highly relevant target for intervention in anti-cancer and anti-aging therapies. FOXO3 is a
Publikováno v:
Biomolecules
Volume 10
Issue 9
Biomolecules, Vol 10, Iss 1289, p 1289 (2020)
Volume 10
Issue 9
Biomolecules, Vol 10, Iss 1289, p 1289 (2020)
Mapping the route of nucleoside triphosphate (NTP) entry into the sequestered active site of RNA polymerase (RNAP) has major implications for elucidating the complete nucleotide addition cycle. Constituting a dichotomy that remains to be resolved, tw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e556a08966f97777721c5eebcf1b7ac
http://hdl.handle.net/10044/1/83088
http://hdl.handle.net/10044/1/83088
Publikováno v:
Biomolecules, Vol 10, Iss 1205, p 1205 (2020)
Biomolecules
Volume 10
Issue 9
Biomolecules
Volume 10
Issue 9
The human mediator subunit MED25 acts as a coactivator that binds the transcriptional activation domains (TADs) present in various cellular and viral gene-specific transcription factors. Previous studies, including on NMR measurements and site-direct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50af9ad736a0138f97c25c69fdcdbfc0
http://hdl.handle.net/10044/1/82333
http://hdl.handle.net/10044/1/82333
Publikováno v:
Life, Vol 10, Iss 109, p 109 (2020)
Life
Volume 10
Issue 7
Life
Volume 10
Issue 7
Many of the proteins involved in key cellular regulatory events contain extensive intrinsically disordered regions that are not readily amenable to conventional structure/function dissection. The oncoprotein c-MYC plays a key role in controlling cell