Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Paul J. Shrimpton"'
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 69:823-831
Despite the increased recent use of protein-ligand and protein-protein docking in the drug discovery process due to the increases in computational power, the difficulty of accurately ranking the binding affinities of a series of ligands or a series o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98849b5a737527333f76c114e83ca03c
https://doi.org/10.1002/prot.21782
https://doi.org/10.1002/prot.21782
Publikováno v:
Protein engineering, designselection : PEDS. 22(9)
Structural genomics initiatives are rapidly generating vast numbers of protein structures. Comparative modelling is also capable of producing accurate structural models for many protein sequences. However, for many of the known structures, functions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37e27965e4ff4d69ee9f9b5a2dd4e164
https://pubmed.ncbi.nlm.nih.gov/19574295
https://pubmed.ncbi.nlm.nih.gov/19574295
Autor:
Paul J. Shrimpton, Rudolf Konrad Allemann, Richard S. Swanwick, Jiayun Pang, Giovanni Maglia, Robert J. Rodriguez, Rhiannon M. Evans, Lai-Hock Tey
Publikováno v:
Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 361(1472)
Dihydrofolate reductase (DHFR) maintains the intracellular pool of tetrahydrofolate through catalysis of hydrogen transfer from reduced nicotinamide adenine dinucleotide to 7,8-dihydrofolate. We report results for pre-steady-state kinetic studies of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29dd90d5fbf10cb50ce229222d9e32b1
https://pubmed.ncbi.nlm.nih.gov/16873119
https://pubmed.ncbi.nlm.nih.gov/16873119
Autor:
Michael J.E. Sternberg, Srinivasan Madhusudan, Grigory L. Dianov, Paul J. Shrimpton, Timothy R. Hammonds, Fiona Smart, Paul A. Freemont, Jason L. Parsons, Sue Houlbrook, D Talbot, Ian D. Hickson, Laurence P. Gardiner
Publikováno v:
Nucleic Acids Research
The base excision repair (BER) pathway is essential for the removal of DNA bases damaged by alkylation or oxidation. A key step in BER is the processing of an apurinic/apyrimidinic (AP) site intermediate by an AP endonuclease. The major AP endonuclea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5b00ab5829aa99fe7f6741acbb670ef
http://ora.ox.ac.uk/objects/uuid:2aa7b80e-ba2c-41f6-8879-b2d6284c4a6d
http://ora.ox.ac.uk/objects/uuid:2aa7b80e-ba2c-41f6-8879-b2d6284c4a6d
Publikováno v:
Proteins. 51(2)
Despite much work, many key aspects of the mechanism of the dihydrofolate reductase (DHFR) catalyzed reduction of dihydrofolate remain unresolved. In bacterial forms of DHFR both substrate and water access to the active site are controlled by the con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::961f6f8ce05ddef51c6159f545344f8f
https://pubmed.ncbi.nlm.nih.gov/12660990
https://pubmed.ncbi.nlm.nih.gov/12660990
Dihydrofolate reductase (DHFR) catalyzes the nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reduction of 7,8-dihydrofolate (H2F) to 5,6,7,8-tetrahydrofolate (H4F). Because of the absence of any ionizable group in the vicinity of N5 of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20dd7ce75452b3a1a5e9bf0e4ac38334
https://europepmc.org/articles/PMC2373639/
https://europepmc.org/articles/PMC2373639/
Autor:
Rudolf K. Allemann, Rhiannon M. Evans, Lai-hock Tey, Giovanni Maglia, Jiayun Pang, Robert Rodriguez, Paul J. Shrimpton, Richard S. Swanwick
Publikováno v:
Philosophical Transactions of the Royal Society B: Biological Sciences; Aug2006, Vol. 361 Issue 1472, p1317-1321, 5p