Zobrazeno 1 - 10
of 136
pro vyhledávání: '"David K. Stammers"'
Autor:
C.E. Nichols, Alastair R. Hawkins, Ian G. Charles, Heather K. Lamb, K. El Omari, Paul Thompson, David K. Stammers, Michael Lockyer
Publikováno v:
Protein Science. 22:628-640
YgjD from COG0533 is amongst a small group of highly conserved proteins present in all three domains of life. Various roles and biochemical functions (including sialoprotease and endonuclease activities) have been ascribed to YgjD and orthologs, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::360a7a04457713509253a645070f5018
https://doi.org/10.1002/pro.2247
https://doi.org/10.1002/pro.2247
Autor:
Annelies Bronckaers, Jan Balzarini, Sandra Liekens, David K. Stammers, María-Jesús Pérez-Pérez, Kamel El Omari
HTP (human thymidine phosphorylase), also known as PD-ECGF (platelet-derived endothelial cell growth factor) or gliostatin, has an important role in nucleoside metabolism. HTP is implicated in angiogenesis and apoptosis and therefore is a prime targe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a85abbefbbda9c588d3c9925214d5b87
https://ora.ox.ac.uk/objects/uuid:aa21ad13-4440-4ebd-b7bb-6a9873781e61
https://ora.ox.ac.uk/objects/uuid:aa21ad13-4440-4ebd-b7bb-6a9873781e61
Autor:
J.N. Champness, Janice M Garvey, Lee F. Kuyper, Christopher R Beddell, David P. Baccanari, David K. Stammers
Conformationally restricted analogues of the antibacterial agent trimethoprim (TMP) were designed to mimic the conformation of drug observed in its complex with bacterial dihydrofolate reductase (DHFR). This conformation of TMP was achieved by linkin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::126edf956a8b4405069d2a3c1c0b3460
https://ora.ox.ac.uk/objects/uuid:d3b2050e-70c1-4f03-8cd4-50611776f0af
https://ora.ox.ac.uk/objects/uuid:d3b2050e-70c1-4f03-8cd4-50611776f0af
Autor:
G S Lowell, John Milton, David I. Stuart, Joseph H. Chan, George Andrew Freeman, S S Gonzales, Steven A. Short, Jingshan Ren, Andrew L. Hopkins, K L Creech, Richard J. Hazen, R G Ferris, G W Koszalka, L T Schaller, G B Roberts, Cowan, C W Andrews Iii, Kurt Weaver, L R Boone, David K. Stammers, D J Reynolds
HIV-1 nonnucleoside reverse transcriptase inhibitors (NNRTIs) are part of the combination therapy currently used to treat HIV infection. The features of a new NNRTI drug for HIV treatment must include selective potent activity against both wild-type
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dba0381a0617d10120e121697f22e025
https://doi.org/10.1021/jm040072r
https://doi.org/10.1021/jm040072r
Autor:
David K. Stammers, D.E. Davies, C.J. Harris, G.W. Hardy, J.G. Dann, R.J. Arrowsmith, J.A. Morton
A new class of human renin inhibitor is described, containing a novel analogue of the peptide bond. High inhibitory potency was observed for octapeptide-length substrate analogues but inhibition progressively weakened as the molecule was shortened fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4869a299b646fb2601708ca062ce5571
https://ora.ox.ac.uk/objects/uuid:e1fecdd7-ef6d-4cf7-a05f-6785235bf15f
https://ora.ox.ac.uk/objects/uuid:e1fecdd7-ef6d-4cf7-a05f-6785235bf15f
Autor:
Alastair R. Hawkins, C.E. Nichols, David K. Stammers, Simon Cocklin, Jingshan Ren, A. Dodds, Kris Leslie, Heather K. Lamb
NmrA is a negative transcriptional regulator involved in the post-translational modulation of the GATA-type transcription factor AreA, forming part of a system controlling nitrogen metabolite repression in various fungi. X-ray structures of two NmrA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::718a9e48cef112363aecb4ff0c85e080
https://ora.ox.ac.uk/objects/uuid:d9424090-00c9-4d58-87a5-a8d8b279ce74
https://ora.ox.ac.uk/objects/uuid:d9424090-00c9-4d58-87a5-a8d8b279ce74
Autor:
David K. Stammers, Anthony C.T. North, C. R. Beddell, D. Ogg, Elias Eliopoulos, J.N. Champness, A.J. Geddes, J.G. Dann
The structure of mouse L1210 dihydrofolate reductase (DHFR) complexed with NADPH and trimethoprim has been refined at 2.0 Å resolution. The analogous complex with NADPH and methotrexate has been refined at 2.5 Å resolution. These structures reveal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::575a083bd3bd04e0023f31bf2835e5c9
https://ora.ox.ac.uk/objects/uuid:b55acfb9-a49d-4914-a21d-eaba9309d917
https://ora.ox.ac.uk/objects/uuid:b55acfb9-a49d-4914-a21d-eaba9309d917
We have found a close correlation between viral stavudine (d4T) resistance and resistance to d4T-triphosphate at the human immunodeficiency virus type 1 reverse transcriptase (RT) level. RT from site-directed mutants with 69S-XX codon insertions and/
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9311f28fead4b816bb9a176154a4b50d
https://ora.ox.ac.uk/objects/uuid:fb6cd7fd-57fe-4f4f-99ac-104c88a03c3d
https://ora.ox.ac.uk/objects/uuid:fb6cd7fd-57fe-4f4f-99ac-104c88a03c3d
Autor:
Kurt Hertogs, R Pauwels, S. D. Kemp, Schlomo Staszewski, Veronica Miller, Martin Stürmer, Jingshan Ren, B. A. Larder, David I. Stuart, David K. Stammers, R. L. Desmet, Stuart Bloor
Publikováno v:
Scopus-Elsevier
To investigate the occurrence of multinucleoside analog resistance during therapy failure, we surveyed the drug susceptibilities and genotypes of nearly 900 human immunodeficiency virus type 1 (HIV-1) samples. For 302 of these, the 50% inhibitory con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0c8f4e46ae7c1f82b43696643b47260
https://ora.ox.ac.uk/objects/uuid:c02b6582-c197-4b96-8d40-3b9caf461d22
https://ora.ox.ac.uk/objects/uuid:c02b6582-c197-4b96-8d40-3b9caf461d22
The structure of pyruvate kinase (EC 2.7.1.40) has been determined from a 2.6 A resolution electron density map. This map shows more detail than the previous 3.1 A map (Stammers & Muirhead, 1977) and has enabled a detailed chain folding to be establi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3305f1a313b91cbffa7199e612fc972a
https://ora.ox.ac.uk/objects/uuid:17335be5-adda-483a-b3cd-49193c1e3d74
https://ora.ox.ac.uk/objects/uuid:17335be5-adda-483a-b3cd-49193c1e3d74