Search Results - "Stammers, D.K."

The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases by Stammers, D.K., Ren, J., Leslie, K., Nichols, C.E., Lamb, H.K., Cocklin, S., Dodds, A., Hawkins, A.R.

“…NmrA is a negative transcriptional regulator involved in the post‐translational modulation of the GATA‐type transcription factor AreA, forming part of a system…”
Get full text

Crystal Structures of HIV-1 Reverse Transcriptases Mutated at Codons 100, 106 and 108 and Mechanisms of Resistance to Non-nucleoside Inhibitors by Ren, J, Nichols, C.E, Chamberlain, P.P, Weaver, K.L, Short, S.A, Stammers, D.K

“…Leu100Ile, Val106Ala and Val108Ile are mutations in HIV-1 reverse transcriptase (RT) that are observed in the clinic and give rise to resistance to certain…”
Get full text

Structural characterization of Salmonella typhimurium YeaZ, an M22 O-sialoglycoprotein endopeptidase homolog by Nichols, C.E., Johnson, C., Lockyer, M., Charles, I.G., Lamb, H.K., Hawkins, A.R., Stammers, D.K.

“…The Salmonella typhimurium “yeaZ” gene (StyeaZ) encodes an essential protein of unknown function (StYeaZ), which has previously been annotated as a putative…”
Get full text

Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors 1 1Edited by J. Karn by Ren, J, Nichols, C, Bird, L, Chamberlain, P, Weaver, K, Short, S, Stuart, D.I, Stammers, D.K

Get full text

Use of the Glu-Glu-Phe C-terminal epitope for rapid purification of the catalytic domain of normal and mutant ras GTPase-activating proteins by SKINNER, R. H, BRADLEY, S, BROWN, A. L, JOHNSON, N. J. E, RHODES, S, STAMMERS, D. K, LOWE, P. N

“…The C-terminal catalytic domain (residues 704-1047) of the human ras GTPase-activating protein (GAP) has been engineered so as to incorporate the tripeptide,…”
Get full text

Calcium regulation of chloroplast protein translocation is mediated by calmodulin binding to Tic32 by Chigri, F, Hörmann, F, Stamp, A, Stammers, D.K, Bölter, B, Soll, J, Vothknecht, U.C

“…The import of nuclear-encoded proteins into chloroplasts is tightly controlled on both sides of the envelope membranes. Regulatory circuits include…”
Get full text

High-resolution Structures Reveal Details of Domain Closure and “Half-of-sites-reactivity” in Escherichia coli Aspartate β-Semialdehyde Dehydrogenase by Nichols, C.E., Dhaliwal, B., Lockyer, M., Hawkins, A.R., Stammers, D.K.

“…Two high-resolution structures have been determined for Eschericia coli aspartate β-semialdehyde dehydrogenase ( ecASADH), an enzyme of the aspartate…”
Get full text

Crystal structures of Staphylococcus aureus type I dehydroquinase from enzyme turnover experiments by Nichols, C.E., Lockyer, M., Hawkins, A.R., Stammers, D.K.

Get full text

Comparison of Ligand-induced Conformational Changes and Domain Closure Mechanisms, Between Prokaryotic and Eukaryotic Dehydroquinate Synthases by Nichols, C.E., Ren, J., Leslie, K., Dhaliwal, B., Lockyer, M., Charles, I., Hawkins, A.R., Stammers, D.K.

“…Dehydroquinate synthase (DHQS) is a potential target for the development of novel broad-spectrum antimicrobial drugs, active against both prokaryotes and lower…”
Get full text

Ligand-induced Conformational Changes and a Mechanism for Domain Closure in Aspergillus nidulans Dehydroquinate Synthase by Nichols, C.E, Ren, J, Lamb, H.K, Hawkins, A.R, Stammers, D.K

“…In order to investigate systematically substrate and cofactor-induced conformational changes in the enzyme dehydroquinate synthase (DHQS), eight structures…”
Get full text

Biaryl acids: Novel non-nucleoside inhibitors of HIV reverse transcriptase types 1 and 2 by Milton, J., Slater, M.J., Bird, A.J., Spinks, D., Scott, G., Price, C.E., Downing, S., Green, D.V.S., Madar, S., Bethell, R., Stammers, D.K.

“…A series of biaryl acids has been found to show micromolar inhibition of the HIV reverse transcriptase (RT) from types 1 and 2 with IC 50s in the micromolar…”
Get full text

Rapid purification and characterisation of HIV-1 reverse transcriptase and RNaseH engineered to incorporate a C-terminal tripeptide α-tubulin epitope by Stammers, D.K., Tisdale, M., Court, S., Parmar, V., Bradley, C., Ross, C.K.

“…The C-termini of p66 and p51 forms of HIV-1 reverse transcriptase have been engineered to contain a Glu-Glu-Phe sequence recognized by a monoclonal antibody to…”
Get full text

The structure of mouse L1210 dihydrofolate reductase-drug complexes and the construction of a model of human enzyme by Stammers, D.K., Champness, J.N., Beddell, C.R., Dann, J.G., Eliopoulos, E., Geddes, A.J., Ogg, D., North, A.C.T.

“…The structure of mouse L1210 dihydrofolate reductase (DHFR) complexed with NADPH and trimethoprim has been refined at 2.0 Å resolution. The analogous complex…”
Get full text

Inhibition of HIV-1 reverse transcriptase by defined template/primer DNA oligonucleotides: effect of template length and binding characteristics by Idriss, H, Stammers, D K

“…The interaction of partially double stranded DNA oligonucleotides with HIV-1 RT was studied by investigating their ability to inhibit the homopolymeric…”
Get more information

Crystallographic investigation of the cooperative interaction between trimethoprim, reduced cofactor and dihydrofolate reductase by Champness, J.N., Stammers, D.K., Beddell, C.R.

“…The structure of the complex between E. coli (RT500) form I dihydrofolate reductase, the antibacterial trimethoprim and NADPH has been determined by X-ray…”
Get full text

Refolding of recombinant Pneumocystis carinii dihydrofolate reductase and characterization of the enzyme by Delves, C J, Ballantine, S P, Tansik, R L, Baccanari, D P, Stammers, D K

“…The isolation of dihydrofolate reductase (DHFR) cDNA sequences from the messenger RNA of Pneumocystis carinii using the polymerase chain reaction is described…”
Get more information

Preliminary crystallographic data for Pneumocystis carinii dihydrofolate reductase by Stammers, D K, Delves, C, Ballantine, S, Jones, E Y, Stuart, D I, Achari, A, Bryant, P K, Champness, J N

“…Dihydrofolate reductase from Pneumocystis carinii has been crystallized in a form suitable for high resolution X-ray diffraction studies. Recombinant enzyme…”
Get more information

Three-dimensional structure of cat muscle pyruvate kinase at 6 Angstrom resolution by Stammers, D K, Muirhead, H

Get more information

The binding of trimethoprim to bacterial dihydrofolate reductase by Baker, D.J., Beddell, C.R., Champness, J.N., Goodford, P.J., Norrington, F.E.A., Smith, D.R., Stammers, D.K.

Get full text

Comparison of angiotensinogen and tetradecapeptide as substrates for human renin. Substrate dependence of the mode of inhibition of renin by a statine-containing hexapeptide by Stammers, D K, Dann, J G, Harris, C J, Smith, D R

“…The kinetic properties of two different substrates for human renin, a synthetic tetradecapeptide and the natural substrate human angiotensinogen, have been…”
Get more information