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Number of items: 77.
Ashraf, Khuram U., Nygaard, Rie, Vickery, Owen N., Erramilli, Satchal K., Herrera, Carmen M., McConville, Thomas H., Petrou, Vasileios I., Giacometti, Sabrina I., Belcher Dufrisne, Meagan, Nosol, Kamil et al.
(2022)
Structural basis of lipopolysaccharide maturation by the WaaL O-antigen ligase.
Nature, 604
.
pp. 371-376.
doi:10.1038/s41586-022-04555-x
Tran, Wendy, Kusay, Ali S., Hawkins, Paige M. E., Cheung, Chen-Yi, Nagalingam, Gayathri, Pujari, Venugopal, Ford, Daniel J., Stoye, Alexander, Ochoa, Jessica L., Audette, Rebecca E. et al.
(2021)
Synthetic sansanmycin analogues as potent mycobacterium tuberculosis translocase I inhibitors.
Journal of Medicinal Chemistry, 64
(23).
pp. 17326-17345.
doi:10.1021/acs.jmedchem.1c01407
Graham, Chris L. B., Newman, Hector, Gillett, Francesca, Smart, Katie, Briggs, Nicholas, Banzhaf, Manuel and Roper, David I. (2021) A dynamic network of proteins facilitate cell envelope biogenesis in gram-negative bacteria. International Journal of Molecular Sciences, 22 (23). e12831. doi:10.3390/ijms222312831
Briggs, Nicholas, Bruce, Kevin E., Naskar, Souvik, Winkler, Malcolm E. and Roper, David I. (2021) The pneumococcal divisome : dynamic control of streptococcus pneumoniae cell division. Frontiers in Microbiology, 12 . 737396. doi:10.3389/fmicb.2021.737396
York, Anna, Lloyd, Adrian J., del Genio, Charo I., Shearer, Jonathan, Hinxman, Karen, Fritz, Konstantin, Fülöp, Vilmos, Dowson, Christopher G., Khalid, Syma and Roper, David I. (2021) Structure-based modeling and dynamics of MurM, a Streptococcus pneumoniae penicillin resistance determinant present at the cytoplasmic membrane. Structure, 29 (7). pp. 731-742. doi:10.1016/j.str.2021.03.001
Aggarwal, Surya D. , Lloyd, Adrian J., Yerneni, Saigopalakrishna S., Narciso, Ana Rita, Shepherd, Jennifer, Roper, David I., Dowson, Christopher G., Filipe, Sergio R and Hiller, N Luisa (2021) A molecular link between cell wall biosynthesis, translation fidelity, and stringent response in Streptococcus pneumoniae. Proceedings of the National Academy of Sciences of the United States of America, 118 (14). e2018089118. doi:10.1073/pnas.2018089118
Bryant, Jack Alfred, Morris, Faye C., Knowles, Timothy J., Maderbocus, Riyaz, Heinz, Eva, Boelter, Gabriela, Alodaini, Dema, Colyer, Adam, Wotherspoon, Peter J., Staunton, Kara A. et al.
(2020)
Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation.
eLife, 9
.
e62614.
doi:10.7554/eLife.62614
Cook, Jonathan P., Baverstock, Tyler, McAndrew, Martin B. L., Stansfeld, Phillip J., Roper, David I. and Crow, Allister (2020) Insights into intrinsic resistance and bacterial cell division from a structure of EnvC bound to the FtsX periplasmic domain. Proceedings of the National Academy of Sciences of the United States of America, 117 (45). pp. 28355-28365. doi:10.1073/pnas.2017134117
Lockey, Christine, Edwards, Richard J., Roper, David I. and Dixon, Ann M. (2020) Data for The extracellular domain of two-component system sensor kinase VanS from streptomyces coelicolor binds Vancomycin at a newly identified binding site. [Dataset]
Lockey, Christine, Edwards, Richard J., Roper, David I. and Dixon, Ann M. (2020) The extracellular domain of two-component system sensor kinase VanS from streptomyces coelicolor binds Vancomycin at a newly identified binding site. Scientific Reports, 10 (1). 5727.
Catherwood, Anita C., Lloyd, Adrian J., Tod, Julie A., Chauhan, Smita, Slade, Susan E., Walkowiak, Grzegorz P., Galley, Nicola F., Punekar, Avinash S., Smart, Katie, Rea, Dean, Evans, Neil D., Chappell, Michael J., Roper, David I. and Dowson, Christopher G. (2020) Substrate and stereochemical control of peptidoglycan cross-linking by transpeptidation by Escherichia coli PBP1B. Journal of the American Chemical Society, 142 (11). pp. 5034-5048. doi:10.1021/jacs.9b08822
Kuru, Erkin, Radkov, Atanas, Meng, Xin, Egan, Alexander, Alvarez, Laura, Dowson, Amanda, Booher, Garrett, Breukink, Eefjan, Roper, David I., Cava, Felipe, Vollmer, Waldemar, Brun, Yves and VanNieuwenhze, Michael S. (2019) Mechanisms of incorporation for D-amino acid probes that target peptidoglycan biosynthesis. ACS Chemical Biology, 14 (12). pp. 2745-2756. doi:10.1021/acschembio.9b00664
Lee, Sarah C., Collins, Richard, Lin, Yu-pin, Jamshad, Mohammed, Broughton, Claire E., Harris, Sarah A., Hanson, Benjamin S, Tognoloni, Cecilia, Parslow, Rosemary A., Terry, Ann E., Rodger, Alison, Smith, Corinne J., Edler, Karen J., Ford, Robert, Roper, David I. and Dafforn, Timothy R. (2019) Nano-encapsulated escherichia coli divisome anchor ZipA, and in complex with FtsZ. Scientific Reports, 9 (1). 18712. doi:10.1038/s41598-019-54999-x
Cain, Ricky, Salimraj, Ramya, Punekar, Avinash S., Bellini, Dom, Fishwick, Colin W. G., Czaplewski, Lloyd, Scott, David J., Harris, Gemma, Dowson, Christopher G., Lloyd, Adrian J. and Roper, David I. (2019) Structure-guided enhancement of selectivity of chemical probe inhibitors targeting bacterial seryl-tRNA synthetase. Journal of Medicinal Chemistry, 62 (21). pp. 9703-9717. doi:10.1021/acs.jmedchem.9b01131
Simpson, Daniel H., Hapeshi, Alexia, Rogers, Nicola J., Brabec, Viktor, Clarkson, Guy J., Fox, David J., Hrabina, Ondrej, Kay, Gemma L., King, Andrew, Malina, Jaroslav, Millard, Andrew D., Moat, John, Roper, David I., Song, Hualong, Waterfield, Nicholas R. and Scott, Peter (2019) Metallohelices that kill Gram-negative pathogens using intracellular antimicrobial peptide pathways. Chemical Science, 10 . 9708-9720. doi:10.1039/C9SC03532J
Massarweh, Ahmad, Bosco, Michael, Chantret, Isabelle, Léger, Thibaut, Jamal, Layla, Roper, David I., Dowson, Christopher G., Busca, Patricia, Bouhss, Ahmed, Gravier-Pelletier, Christine and Moore, Stuart E. H. (2019) Bacterial lipid II analogs : novel in vitro substrates for mammalian oligosaccharyl diphosphodolichol diphosphatase (DLODP) activities. Molecules, 24 (11). 2135. doi:10.3390/molecules24112135
Pollock, Naomi, Rai, Megha, Simon, Kailene S., Hesketh, Sophie J., Teo, Alvin C. K. , Parmar, Mayuriben, Sridhar, Pooja, Collins, Richard, Lee, Sarah C., Stroud, Zoe N. et al.
(2019)
SMA-PAGE : a new method to examine complexes of membrane proteins using SMALP nano-encapsulation and native gel electrophoresis.
Biochimica et Biophysica Acta (BBA) - Biomembranes, 186
(8).
pp. 1437-1445.
doi:10.1016/j.bbamem.2019.05.011
Teo, Alvin C. K. , Lee, Sarah C., Pollock, Naomi L., Stroud, Zoe, Hall, Stephen, Thakker, Alpesh, Pitt, Andrew R., Dafforn, Timothy R., Spickett, Corinne M. and Roper, David I. (2019) Analysis of SMALP co-extracted phospholipids shows distinct membrane environments for three classes of bacterial membrane protein. Scientific Reports, 9 (1). 1813 . doi:10.1038/s41598-018-37962-0
Ábrányi-Balogh, Péter, Petri, László, Imre, Tímea, Szijj, Péter, Scarpino, Andrea, Hrast, Martina, Mitrović, Ana, Fonovič, Urša Pečar, Németh, Krisztina, Barreteau, Hélène, Roper, David I., Horváti, Kata, Ferenczy, György G, Kos, Janko, Ilaš, Janez, Gobec, Stanislav and Keserű, György M (2018) A road map for prioritizing warheads for cysteine targeting covalent inhibitors. European Journal of Medicinal Chemistry, 160 . pp. 94-107. doi:10.1016/j.ejmech.2018.10.010
Punekar, Avinash S., Samsudin, Firdaus, Lloyd, Adrian J., Dowson, Christopher G., Scott, David J., Khalid, Syma and Roper, David I. (2018) The role of the jaw subdomain of peptidoglycan glycosyltransferases for lipid II polymerization. The Cell Surface, 2 . pp. 54-66. doi:10.1016/j.tcsw.2018.06.002
Hrast, Martina, Jukič, Marko, Patin, Delphine, Tod, Julie, Dowson, Christopher G., Roper, David I., Barreteau, Hélène and Gobec, Stanislav (2018) In silico identification, synthesis and biological evaluation of novel tetrazole inhibitors of MurB. Chemical Biology & Drug Design, 91 (6). pp. 1101-1112. doi:10.1111/cbdd.13172
Meyer, Karen, Addy, Christine, Akashi, Satoko, Roper, David I. and Tame, Jeremy R. H. (2018) The crystal structure and oligomeric form of Escherichia coli L,D-carboxypeptidase A. Biochemical and Biophysical Research Communications, 499 (3). pp. 594-599. doi:10.1016/j.bbrc.2018.03.195
Batson, Sarah, de Chiara, Cesira, Majce, Vita, Lloyd, Adrian J., Gobec, Stanislav, Rea, Dean, Fülöp, Vilmos, Thoroughgood, Christopher W., Simmons, Katie J., Dowson, Christopher G., Fishwick, Colin W. G., de Carvalho, Luiz Pedro S. and Roper, David I. (2017) Inhibition of D-Ala : D-Ala ligase through a phosphorylated form of the antibiotic D-cycloserine. Nature Communications, 8 (1). 1939 . doi:10.1038/s41467-017-02118-7
Sychantha, David, Jones, Carys S., Little, Dustin J., Moynihan, Patrick J., Robinson, Howard, Galley, Nicola F., Roper, David I., Dowson, Christopher G., Howell, P. Lynne and Clarke, Anthony J. (2017) In vitro characterization of the antivirulence target of Gram-positive pathogens, peptidoglycan O-acetyltransferase A (OatA). PLOS Pathogens, 13 (10). e1006667. doi:10.1371/journal.ppat.1006667
Tran, Anh T., Watson, Emma E., Pujari, Venugopal, Conroy, Trent, Dowman, Luke J., Giltrap, Andrew M., Pang, Angel, Wong, Weng-Ruh, Linington, Roger G., Saunders, Jessica, Charman, Susan A., West, Nicholas P., Bugg, Tim, Tod, Julie, Dowson, Christopher G., Roper, David I., Crick, Dean C., Britton, Warwick J. and Payne, Richard J. (2017) Sansanmycin natural product analogues as potent and selective anti-mycobacterials that inhibit lipid I biosynthesis. Nature Communications, 8 . 14414 . doi:10.1038/ncomms14414
Calvez, Philippe, Breukink, Eefjan, Roper, David I., Dib, Mélanie, Contreras-Martel, Carlos and Zapun, André (2017) Substitutions in PBP2b from β-lactam resistant Streptococcus pneumoniae have different effects on enzymatic activity and drug reactivity. Journal of Biological Chemistry, 292 (7). pp. 2854-2865. doi: 10.1074/jbc.M116.764696
Vajs, Jure, Proud, Conor, Brozovic, Anamaria, Gazvoda, Martin, Lloyd, Adrian J., Roper, David I., Osmak, Maja, Košmrlj, Janez and Dowson, Christopher G. (2017) Diaryltriazenes as antibacterial agents against methicillin resistant Staphylococcus aureus (MRSA) and Mycobacterium smegmatis. European Journal of Medicinal Chemistry, 127 . pp. 223-234. doi:10.1016/j.ejmech.2016.12.060
Broughton, Claire E., Berg, Hugo van den, Wemyss, Alan M., Roper, David I. and Rodger, Alison (2016) Beyond the discovery void : new targets for antibacterial compounds. Science Progress, 99 (2). pp. 153-182. doi:10.3184/003685016X14616130512308
Usha, Veeraraghavan, Lloyd, Adrian J., Roper, David I., Dowson, Christopher G., Kozlov, Guennadi, Gehring, Kalle, Chauhan, Smita, Imam, Hasan T., Blindauer, Claudia A. and Besra, Gurdyal S. (2016) Reconstruction of diaminopimelic acid biosynthesis allows characterisation of Mycobacterium tuberculosis N-succinyl-L,L-diaminopimelic acid desuccinylase. Scientific Reports, 6 . 23191. doi:10.1038/srep23191
Kaner, Rebecca A., Allison, Simon A., Faulkner, Alan D., Simpson, Daniel H., Waterfield, Nicholas R., Phillips, Roger M., Roper, David I., Shepherd, Samantha L. and Scott, Peter (2016) Anticancer metallohelices : nanomolar potency and high selectivity. Chemical Science, 7 (2). pp. 951-958. doi:10.1039/c5sc03677a
Broughton, Claire E., Roper, David I., Berg, Hugo van den and Rodger, Alison (2015) Bacterial cell division : experimental and theoretical approaches to the divisome. Science Progress, 98 (4). pp. 313-345. doi:10.3184/003685015X14461391862881
Teo, Alvin and Roper, David I. (2015) Core steps of membrane-bound peptidoglycan biosynthesis : recent advances, insight and opportunities. Antibiotics, 4 (4). pp. 495-520. doi:10.3390/antibiotics4040495
Kaner, Rebecca A., Allison, Simon A., Faulkner, Alan D., Simpson, Daniel H., Waterfield, Nicholas R., Phillips, Roger M., Roper, David I., Shepherd, Samantha L. and Scott, Peter (2015) Data for Anticancer metallohelices : nanomolar potency and high selectivity. [Dataset]
Zuegg, Johannes, Muldoon, Craig, Adamson, George, McKeveney, Declan, Thanh, Giang Le, Premraj, Rajaratnam, Becker, Bernd, Cheng, Mu, Elliott, Alysha G., Huang, Johnny X. et al.
(2015)
Carbohydrate scaffolds as glycosyltransferase inhibitors with in vivo antibacterial activity.
Nature Communications, 6
.
pp. 1-11.
7719.
doi:10.1038/ncomms8719
Dow, Claire E., Berg, Hugo van den, Roper, David I. and Rodger, Alison (2015) Biological insights from a simulation model of the critical FtsZ accumulation required for prokaryotic cell division. Biochemistry, 54 (24). pp. 3803-3813. doi:10.1021/acs.biochem.5b00261
Li, Qiong, Cheng, Wang, Morlot, Cécile, Bai, Xiao-Hui, Jiang, Yong-Liang, Wang, Wenjia, Roper, David I., Vernet, Thierry, Dong, Yu-Hui, Chen, Yuxing and Zhou, Cong-Zhao (2015) Full-length structure of the major autolysin LytA. Acta Crystallographica Section D Biological Crystallography, 71 (6). pp. 1373-1381. doi:10.1107/S1399004715007403
Faulkner, Alan D., Kaner, Rebecca A., Abdallah, Qasem M. A., Clarkson, Guy J., Fox, David J., Gurnani, Pratik, Howson, Suzanne E., Phillips, Roger M. , Roper, David I., Simpson, Daniel H. and Scott, Peter (2014) Asymmetric triplex metallohelices with high and selective activity against cancer cells. Nature Chemistry, Volume 6 (Number 9). pp. 797-803. doi:10.1038/nchem.2024
Braddick, Darren, Sandhu, Sandeep, Roper, David I., Chappell, M. J. (Michael J.) and Bugg, Tim (2014) Observation of the time-course for peptidoglycan lipid intermediate II polymerization by Staphylococcus aureus monofunctional transglycosylase. Microbiology, Volume 160 (Part 8). pp. 1628-1636. doi:10.1099/mic.0.079442-0
Galley, Nicola F., O'Reilly, Amy M. and Roper, David I. (2014) Prospects for novel inhibitors of peptidoglycan transglycosylase. Bioorganic Chemistry, Volume 55 (Number 100). pp. 16-26. doi:10.1016/j.bioorg.2014.05.007
Paulin, Sarah, Jamshad, Mohammed, Dafforn, Tim, Garcia-Lara, Jorge, Foster, Simon J., Galley, Nicola F., Roper, David I., Rosado, Helena and Taylor, Peter W. (2014) Surfactant-free purification of membrane protein complexes from bacteria : application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a. Nanotechnology, Volume 25 (Number 28). Article number 285101. doi:10.1088/0957-4484/25/28/285101
Rodolis, Maria T., Mihalyi, Agnes, O'Reilly, Amy M., Slikas, Justinas, Roper, David I., Hancock, Robert E. W. and Bugg, Tim (2014) Identification of a novel inhibition site in Translocase MraY based upon the site of interaction with Lysis Protein E from Bacteriophage ϕX174. Chembiochem, Volume 15 (Number 9). pp. 1300-1308. doi:10.1002/cbic.201402064
Lloyd, Adrian J., Potter, Nicola J., Fishwick, Colin W. G., Roper, David I. and Dowson, Christopher G. (2013) Adenosine Tetraphosphoadenosine drives a continuous ATP-release assay for Aminoacyl-tRNA synthetases and other Adenylate-forming enzymes. ACS Chemical Biology, 8 (10). pp. 2157-2163. doi:10.1021/cb400248f
Lloyd, Adrian J., Potter, Nicola J., Fishwick, Colin W. G., Roper, David I. and Dowson, Christopher G. (2013) Adenosine tetraphosphoadenosine drives a continuous ATP-release assay for aminoacyl-tRNA synthetases and other adenylate-forming enzymes. ACS Chemical Biology, 8 (10). pp. 2157-2163. doi:10.1021/cb400248f
Valegård, Karin, Iqbal, Aman, Kershaw, Nadia J., Ivison, David, Généreux, Catherine, Dubus, Alain, Blikstad, Cecilia, Demetriades, Marina, Hopkinson, Richard J., Lloyd, Adrian J., Roper, David I., Schofield, Christopher J., Andersson, Inger and McDonough, Michael A. (2013) Structural and mechanistic studies of theorf12 gene product from the clavulanic acid biosynthesis pathway. Acta Crystallographica Section D Biological Crystallography, Volume 69 (Number 8). pp. 1567-1579. doi:10.1107/S0907444913011013
Dow, Claire E., Rodger, Alison, Roper, David I. and Berg, Hugo van den (2013) A model of membrane contraction predicting initiation and completion of bacterial cell division. Integrative Biology (Number 5). pp. 778-795. doi:10.1039/c3ib20273a
Majce, Vita, Ruane, Karen M., Gobec, Stanislav and Roper, David I. (2013) Crystallization and preliminary X-ray analysis of a UDP-MurNAc-tripeptideD-alanyl-D-alanine-adding enzyme (PaMurF) from Pseudomonas aeruginosa. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, Volume 69 (number 5). pp. 503-505. doi:10.1107/S1744309113005344
Pacheco‑Gómez, Raúl, Cheng, Xi, Hicks, Matthew R., Smith, Corinne J., Roper, David I., Addinall, Stephen G., Rodger, Alison and Dafforn, Tim (2013) Tetramerization of ZapA is required for FtsZ bundling. Biochemical Journal, Volume 449 (Number 3). pp. 795-802. doi:10.1042/BJ20120140
Meigh, Louise, Greenhalgh, Sophie A., Rodgers, Thomas L., Cann, Martin J., Roper, David I. and Dale, Nicholas (2013) CO2 directly modulates connexin 26 by formation of carbamate bridges between subunits. eLife, Volume 2 . Article number e01213. doi:10.7554/eLife.01213
Zapun, André, Philippe, Jules, Abrahams, Katherine A., Signor, Luca, Roper, David I., Breukink, Eefjan and Vernet, Thierry (2013) In vitro reconstitution of peptidoglycan assembly from the gram-positive pathogen streptococcus pneumoniae. ACS Chemical Biology, Volume 8 (Number 12). pp. 2688-2696. doi:10.1021/cb400575t
Ruane, Karen M., Lloyd, Adrian J., Fülöp, Vilmos, Dowson, Christopher G., Barreteau, Hélène, Boniface, Audrey, Dementin, Sébastien, Blanot, Didier, Mengin-Lecreulx, Dominique, Gobec, Stanislav, Dessen, Andréa and Roper, David I. (2013) Specificity determinants for lysine incorporation in staphylococcus aureus peptidoglycan as revealed by the structure of a MurE enzyme ternary complex. Journal of Biological Chemistry, Volume 288 (Number 46). Article number 33439. doi:10.1074/jbc.M113.508135
Yoshida, Hisashi, Kawai, Fumihiro, Obayashi, Eiji, Akashi, Satoko, Roper, David I., Tame, Jeremy R.H. and Park, Sam-Yong (2012) Crystal structures of penicillin-binding protein 3 (PBP3) from methicillin-resistant staphylococcus aureus in the apo and cefotaxime‐bound forms. Journal of Molecular Biology, Volume 423 (Number 3). pp. 351-364. doi:10.1016/j.jmb.2012.07.012
Turner, Daniel J., Portman, Ian, Dafforn, Tim, Rodger, Alison, Roper, David I., Smith, Corinne J. and Turner, Matthew S. (2012) The Mechanics of FtsZ fibers. Biophysical Journal, Vol.102 (No.4). pp. 731-738. doi:10.1016/j.bpj.2012.01.015
Pacheco-Gómez, Raúl, Roper, David I., Dafforn, Tim and Rodger, Alison (2011) The pH dependence of polymerization and bundling by the essential bacterial cytoskeltal protein FtsZ. PLoS One, Vol.6 (No.6). e19369. doi:10.1371/journal.pone.0019369
Bugg, Tim, Braddick, Darren, Dowson, Christopher G. and Roper, David I. (2011) Bacterial cell wall assembly : still an attractive antibacterial target. Trends in Biotechnology, Vol.29 (No.4). pp. 167-173. doi:10.1016/j.tibtech.2010.12.006
Hattersley, John G., Pérez-Velázquez, J., Chappell, M. J. (Michael J.), Bearup, Daniel James, Roper, David I., Dowson, Christopher G., Bugg, Tim and Evans, Neil D. (2011) Indistinguishability and identifiability of kinetic models for the MurC reaction in peptidoglycan biosynthesis. Computer Methods and Programs in Biomedicine, Vol.104 (No.2). pp. 70-80. doi:10.1016/j.cmpb.2010.07.009
Batson, Sarah, Rea, Dean, Fülöp, Vilmos and Roper, David I. (2010) Crystallization and preliminary X-ray analysis of a D-alanyl-D-alanine ligase (EcDdlB) from Escherichia coli. Journal of Experimental Psychology: Human Perception and Performance, Vol.66 (No.4). pp. 405-408. doi:10.1107/S1744309110003970
Kawai, Fumihiro, Clarke, Thomas B., Roper, David I., Han, Gab-Jo, Hwang, Kwang Yeon, Unzai, Satoru, Obayashi, Eiji, Park, Sam-Yong and Tame, Jeremy R. H. (2010) Crystal structures of penicillin-binding proteins 4 and 5 from Haemophilus influenzae. Journal of Molecular Biology, Vol.396 (No.3). pp. 634-645. doi:10.1016/j.jmb.2009.11.055
Paradis-Bleau, Catherine, Lloyd, Adrian, Sanschagrin, Francois, Maaroufi, Halim, Clarke, Thomas B., Blewett, Ann, Dowson, Christopher G., Roper, David I., Bugg, Tim and Levesque, Roger C. (2009) Pseudomonas aeruginosa MurE amide ligase : enzyme kinetics and peptide inhibitor. Biochemical Journal, Vol.421 (No. 2). pp. 263-272. doi:10.1042/BJ20081395
Cressina, Elena, Lloyd, Adrian J., De Pascale, Gianfranco, Mok, B. James, Caddick, Stephen, Roper, David I., Dowson, Christopher G. and Bugg, Tim (2009) Inhibition of tRNA-dependent ligase MurM from Streptococcus pneumoniae by phosphonate and sulfonamide inhibitors. Bioorganic & Medicinal Chemistry, Vol.17 (No.9). pp. 3443-3455. doi:10.1016/j.bmc.2009.03.028
Usha, Veeraraghavan, Dover, Lynn G., Roper, David I., Fuetterer, Klaus and Besra, Gurdyal S. (2009) Structure of the diaminopimelate epimerase DapF from Mycobacterium tuberculosis. Acta Crystallographica Section D: Biological Crystallography, Vol.65 (No.4). pp. 383-387. doi:10.1107/S0907444909002522
Clarke, Thomas B., Kawai, Fumihiro, Park, Sam-Yong, Tame, Jeremy R. H., Dowson, Christopher G. and Roper, David I. (2009) Mutational analysis of the substrate specificity of Escherichia coli penicillin binding protein 4. Biochemistry, Vol.48 (No.12). pp. 2675-2683. doi:10.1021/bi801993x
Sova, Matej, Cadez, Gasper, Turk, Samo, Majce, Vita, Polanc, Slovenko, Batson, Sarah, Lloyd, Adrian, Roper, David I., Fishwick, Colin W. G. and Gobec, Stanislav (2009) Design and synthesis of new hydroxyethylamines as inhibitors of D-alanyl-D-lactate ligase (VanA) and D-alanyl-D-alanine ligase (DdlB). Bioorganic & Medicinal Chemistry Letters, Vol.19 (No.5). pp. 1376-1379. doi:10.1016/j.bmcl.2009.01.034
De Pascale, Gianfranco, Lloyd, Adrian J., Schouten, James A., Gilbey, Andrea M., Roper, David I., Dowson, Christopher G. and Bugg, Tim (2008) Kinetic characterization of lipid II-Ala:Alanyl-tRNA ligase (MurN) from streptococcus pneumoniae using semisynthetic aminoacyl-lipid II substrates. Journal of Biological Chemistry, Vol.283 (No.50). pp. 34571-34579. doi:10.1074/jbc.M805807200
Rea, Dean, Hovington, Rebecca, Rakus, John F., Gerlt, John A., Fülöp, Vilmos, Bugg, Tim and Roper, David I. (2008) Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12. Biochemistry, Vol.47 (No.38). pp. 9955-9965. doi:10.1021/bi800943g
Alderwick, Luke J., Dover, Lynn G., Veerapen, Natacha, Gurcha, Sudagar S., Kremer, Laurent, Roper, David I., Pathak, Ashish K., Reynolds, Robert C. and Besra, Gurdyal S. (2008) Expression, purification and characterisation of soluble GlfT and the identification of a novel galactofuranosyltransferase Rv3782 involved in priming GlfT-mediated galactan polymerisation in Mycobacterium tuberculosis. Protein Expression and Purification, Vol.58 (No.2). pp. 332-341. doi:10.1016/j.pep.2007.11.012
Lloyd, Adrian J., Gilbey, Andrea M., Blewett, Anne M., De Pascale, Gianfranco, El Zoeiby, Ahmed, Levesque, Roger C., Catherwood, Anita C., Tomasz, Alexander, Bugg, Tim, Roper, David I. and Dowson, Christopher G. (2008) Characterization of tRNA-dependent peptide bond formation by MurM in the synthesis of Streptococcus pneumoniae peptidoglycan. Journal of Biological Chemistry, Vol.283 (No.10). pp. 6402-6417. doi:10.1074/jbc.M708105200
Usha, Veeraraghavan, Dover, Lynn G., Roper, David I. and Besra, Gurdyal S. (2008) Characterization of Mycobacterium tuberculosis diaminopimelic acid epimerase: paired cysteine residues are crucial for racemization. FEMS Microbiology Letters, Vol.280 (No.1). pp. 57-63. doi:10.1111/j.1574-6968.2007.01049.x
Rea, Dean, Fülöp, Vilmos, Bugg, Tim and Roper, David I. (2007) Structure and mechanism of HpcH : a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli. Journal of Molecular Biology, Vol.373 (No.4). pp. 866-876. doi:10.1016/j.jmb.2007.06.048
Lysenko, Elena S., Clarke, Thomas B., Shchepetov, Mikhail, Ratner, Adam J., Roper, David I., Dowson, Christopher G. and Weiser, Jeffrey N. (2007) Nod1 signaling overcomes resistance of S. pneumoniae to opsonophagocytic killing. PL o S Pathogens , Vol.3 (No.8). pp. 1073-1081. doi:10.1371/journal.ppat.0030118
Cressina, Elena, Lloyd, Adrian J., De Pascale, Gianfranco, Roper, David I., Dowson, Christopher G. and Bugg, Tim (2007) Adenosine phosphonate inhibitors of lipid II: Alanyl tRNA ligase MurM from Streptococcus pneumoniae. Bioorganic & Medicinal Chemistry Letters, Vol.17 (No.16). pp. 4654-4656. doi:10.1016/j.bmcl.2007.05.071
Lysenko, Elena S., Clarke, Thomas B., Shchepetov, Mikhail, Ratner, Adam J., Roper, David I., Dowson, Christopher G. and Weiser, Jeffrey N. (2007) Nod1 signaling overcomes resistance of S. pneumoniae to opsonophagocytic killing. PLoS Pathogens, Vol.3 (No.8). pp. 1073-1081. doi:10.1371/journal.ppat.0030118
Izumi, Atsushi, Rea, Dean, Adachi, Tomoko, Unzai, Satoru, Park, Sam-Yong, Roper, David I. and Tame, Jeremy R. H. (2007) Structure and mechanism of HpcG, a hydratase in the homoprotocatechuate degradation pathway of Escherichia coli. Journal of Molecular Biology, Vol.370 (No.5). pp. 899-911. doi:10.1016/j.jmb.2007.05.006
Lee, Sarah C., Stoilova-Mcphie, Svetla, Baxter, Laura, Fülöp, Vilmos, Henderson, Janey, Rodger, Alison, Roper, David I., Scott, David J., Smith, Corinne J. and Morgan, J. Alun W. (2007) Structural characterisation of the insecticidal toxin XptA1, reveals a 1.15 MDa tetramer with a cage-like structure. Journal of Molecular Biology, Vol.366 (No.5). pp. 1558-1568. doi:10.1016/j.jmb.2006.12.057
Adachi, Tomoko, Izumi, Atsushi, Rea, Dean, Park, Sam-Yong, Tame, Jeremy R. H. and Roper, David I. (2006) Expression, purification and crystallization of 2-oxo-hept-4-ene-1,7-dioate hydratase (HpcG) from Escherichia coli C. Acta Crystallographica Section F-Structural Biology And Crystallization Communicati, 62 (Part 10). pp. 1010-1012. doi:10.1107/S1744309106035901
Usha, Veeraraghavan, Dover, Lynn G., Roper, David I., Lloyd, Adrian J. and Besra, Gurdyal S. (2006) Use of a codon alteration strategy in a novel approach to cloning the Mycobacterium tuberculosis diaminopimelic acid epimerase. FEMS Microbiology Letters, Volume 262 (Number 1). pp. 39-47. doi:10.1111/j.1574-6968.2006.00356.x
Tötemeyer, Sabine, Sheppard, Mark, Lloyd, Adrian, Roper, David I., Dowson, Christopher G., Underhill, David, Murray, Peter, Maskell, Duncan and Bryant, Clare (2006) IFN-gamma enhances production of nitric oxide from macrophages via a mechanism that depends on nucleotide oligomerization domain-2. Journal of Immunology, Vol.176 (No.8). pp. 4804-4810.
Kishida, H., Unzai, Satoru, Roper, David I., Lloyd, A, Park, S.Y. and Tame, Jeremy R. H. (2006) Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics. Biochemistry, Vol.45 (No.3). pp. 783-792. doi:10.1021/bi051533t
This list was generated on Sat Jun 25 21:31:23 2022 BST.