Search Results - "STAMMERS, D. K"

Crystal structure of the dimer of two essential Salmonella typhimurium proteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD–YeaZ–YjeE complex by Nichols, C. E., Lamb, H.K., Thompson, P., Omari, K. El, Lockyer, M., Charles, I., Hawkins, A. R., Stammers, D. K.

“…YgjD from COG0533 is amongst a small group of highly conserved proteins present in all three domains of life. Various roles and biochemical functions…”
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Structure of HIV-2 Reverse Transcriptase at 2.35-Å Resolution and the Mechanism of Resistance to Non-Nucleoside Inhibitors by Ren, J., Bird, L. E., Chamberlain, P. P., Stewart-Jones, G. B., Stuart, D. I., Stammers, D. K.

“…The HIV-2 serotype of HIV is a cause of disease in parts of the West African population, and there is evidence for its spread to Europe and Asia. HIV-2 reverse…”
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A Family of Insertion Mutations between Codons 67 and 70 of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Confer Multinucleoside Analog Resistance by LARDER, B. A, BLOOR, S, STUART, D. I, PAUWELS, R, KEMP, S. D, HERTOGS, K, DESMET, R. L, MILLER, V, STURMER, M, STASZEWSKI, S, REN, J, STAMMERS, D. K

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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 by Ren, J, Nichols, C, Bird, L, Chamberlain, P, Weaver, K, Short, S, Stuart, D I, Stammers, D K

“…Mutations at either Tyr181 or Tyr188 within HIV-1 reverse transcriptase (RT) give high level resistance to many first generation non-nucleoside inhibitors…”
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Crystal Structures of Zidovudine- or Lamivudine-Resistant Human Immunodeficiency Virus Type 1 Reverse Transcriptases Containing Mutations at Codons 41, 184, and 215 by Chamberlain, P P, Ren, J, Nichols, C E, Douglas, L, Lennerstrand, J, Larder, B A, Stuart, D I, Stammers, D K

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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…”
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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…”
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Design of MKC-442 (Emivirine) Analogues with Improved Activity Against Drug-Resistant HIV Mutants by Hopkins, Andrew L, Ren, Jingshan, Tanaka, Hiromichi, Baba, Masanori, Okamato, Mika, Stuart, David I, Stammers, David K

“…Two analogues of the nonnucleoside inhibitor of HIV-1 RT, MKC-442 (emivirine), containing different C6 substituents have been designed to be less susceptible…”
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Complexes of HIV-1 Reverse Transcriptase with Inhibitors of the HEPT Series Reveal Conformational Changes Relevant to the Design of Potent Non-Nucleoside Inhibitors by Hopkins, Andrew L, Ren, Jingshan, Esnouf, Robert M, Willcox, Benjamin E, Jones, E. Yvonne, Ross, Carl, Miyasaka, Tadashi, Walker, Richard T, Tanaka, Hiromichi, Stammers, David K, Stuart, David I

“…Crystal structures of HIV-1 reverse transcriptase (RT) complexed with a range of chemically diverse non-nucleoside inhibitors (NNIs) have shown a single pocket…”
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Correlation between Viral Resistance to Zidovudine and Resistance at the Reverse Transcriptase Level for a Panel of Human Immunodeficiency Virus Type 1 Mutants by Lennerstrand, J, Hertogs, K, Stammers, D K, Larder, B A

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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…”
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Continuous and Discontinuous Changes in the Unit Cell of HIV-1 Reverse Transcriptase Crystals on Dehydration by Esnouf, Robert M., Ren, Jingshan, Garman, Elspeth F., Somers, Don O'N., Ross, Carl K., Jones, E. Yvonne, Stammers, David K., Stuart, David I.

“…A crystal form of HIV‐1 reverse transcriptase (RT) complexed with inhibitors showed diffraction to a high‐resolution limit of 3.7 Å. Instability in the…”
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Crystal structures of Staphylococcus aureus type I dehydroquinase from enzyme turnover experiments by Nichols, C.E., Lockyer, M., Hawkins, A.R., Stammers, D.K.

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Biochemical Mechanism of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Resistance to Stavudine by LENNERSTRAND, Johan, STAMMERS, David K, LARDER, Brendan A

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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…”
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A procedure for setting up high-throughput nanolitre crystallization experiments. II. Crystallization results by Brown, J., Walter, T. S., Carter, L., Abrescia, N. G. A., Aricescu, A. R., Batuwangala, T. D., Bird, L. E., Brown, N., Chamberlain, P. P., Davis, S. J., Dubinina, E., Endicott, J., Fennelly, J. A., Gilbert, R. J. C., Harkiolaki, M., Hon, W.-C., Kimberley, F., Love, C. A., Mancini, E. J., Manso-Sancho, R., Nichols, C. E., Robinson, R. A., Sutton, G. C., Schueller, N., Sleeman, M. C., Stewart-Jones, G. B., Vuong, M., Welburn, J., Zhang, Z., Stammers, D. K., Owens, R. J., Jones, E. Y., Harlos, K., Stuart, D. I.

“…An initial tranche of results from day‐to‐day use of a robotic system for setting up 100 nl‐scale vapour‐diffusion sitting‐drop protein crystallizations has…”
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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…”
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Crystallographic Analysis of the Binding Modes of Thiazoloisoindolinone Non-Nucleoside Inhibitors to HIV-1 Reverse Transcriptase and Comparison with Modeling Studies by Ren, Jingshan, Esnouf, Robert M, Hopkins, Andrew L, Stuart, David I, Stammers, David K

“…We have determined the crystal structures of thiazoloisoindolinone non-nucleoside inhibitors in complex with HIV-1 reverse transcriptase to high-resolution…”
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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…”
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Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim by Matthews, D A, Bolin, J T, Burridge, J M, Filman, D J, Volz, K W, Kaufman, B T, Beddell, C R, Champness, J N, Stammers, D K, Kraut, J

“…Refined crystal structures are reported for complexes of Escherichia coli and chicken dihydrofolate reductase containing the antibiotic trimethoprim (TMP)…”
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