Acharya, Ravi - University of Bath - Department of Biology & Biochemistry

个人简介

PhD, Bangalore University, India (1982) Scientist at the National Chemical Laboratory, Pune, India (1982-1983) Post-doctoral Research Scientist, Laboratory of Molecular Biophysics, Oxford (1984-1990) Sir E.P.Abraham Junior Research Fellow, Linacre College, Oxford University (1988-1990) Lecturer (1990-1994), Reader (1994-1998), University of Bath Leverhulme Trust Research Fellow, University of Bath (1993-1994) Nuffield Foundation Science Research Fellow, University of Bath (1994-1995) Royal Society - Leverhulme Trust Senior Research Fellow, University of Bath (2001-2002) Wellcome Trust Research Leave Fellow, University of Bath (2004-2007) Royal Society Industry Research Fellow, University of Bath (2007-2011) Elected Fellow of Society of Biology (2011) Excellence in Doctoral Supervision Award - University of Bath (2012) Syntaxin Ltd (UK) Research Fellow (since October 2011) Professor of Structural Biology, University of Bath (since May 1998)

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Davies, A. H., McGlashan, J., Posner, M. G., Roberts, A. K., Shone, C. C. and Acharya, K. R., 2016. Forthcoming. Functional significance of active site residues in the enzymatic component of the Clostridium difficile binary toxin. Biochemistry and Biophysics Reports, 8, pp. 55-61. Liang, S. and Acharya, K. R., 2016. Structural basis of substrate specificity in porcine RNase 4. FEBS Journal, 283 (5), pp. 912-928. Larmuth, K. M., Masuyer, G., Douglas, R. G., Schwager, S. L., Acharya, K. R. and Sturrock, E. D., 2016. Kinetic and structural characterisation of amyloid-β peptides hydrolysis by human angiotensin-1-converting enzyme. FEBS Journal, 283 (6), pp. 1060-1076. Schmidt, A., Hammerbacher, A. S., Bastian, M., Nieken, K. J., Klockgether, J., Merighi, M., Lapouge, K., Poschgan, C., K?lle, J., Acharya, K. R., Ulrich, M., Tümmler, B., Unden, G., Kaever, V., Lory, S., Haas, D., Schwarz, S. and D?ring, G., 2016. Oxygen-dependent regulation of c-di-GMP synthesis by SadC controls alginate production in Pseudomonas aeruginosa. Environmental Microbiology Masuyer, G., Douglas, R. G., Sturrock, E. D. and Acharya, K. R., 2015. Structural basis of Ac-SDKP hydrolysis by Angiotensin-I converting enzyme. Scientific Reports, 5, 13742. Bradshaw, W. J., Davies, A. H., Chambers, C. J., Roberts, A. K., Shone, C. C. and Acharya, K. R., 2015. Molecular features of the sortase enzyme family. FEBS Journal, 282 (11), pp. 2097-2114. Chambers, C. J., Roberts, A. K., Shone, C. C. and Acharya, K. R., 2015. Structure and function of a Clostridium difficile sortase enzyme. Scientific Reports, 5, 9449. Bradshaw, W. J., Roberts, A. K., Shone, C. C. and Acharya, K. R., 2015. Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide. Acta Crystallographica Section F:Structural Biology Communications, 71, pp. 295-303. Harrison, C. and Acharya, K. R., 2015. A new high-resolution crystal structure of the Drosophila melanogaster angiotensin converting enzyme homologue, AnCE. FEBS Open Bio, 5, pp. 661-667. Iyer, S., La-Borde, P. J., Payne, K. A. P., Parsons, M. R., Turner, A. J., Isaac, R. E. and Acharya, K. R., 2015. Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans:a cytosolic enzyme with a di-nuclear active site. FEBS Open Bio, 5 (1), pp. 292-302. Masuyer, G., Davies, J. R., Moore, K., Chaddock, J. A. and Acharya, K. R., 2015. Structural analysis of Clostridium botulinum neurotoxin type D as a platform for the development of targeted secretion inhibitors. Scientific Reports, 5, 13397. Harrison, C. and Acharya, K. R., 2014. ACE for all:A molecular perspective. Journal of Cell Communication and Signaling, 8 (3), pp. 195-210. Bradshaw, W.J., Kirby, J.M., Thiyagarajan, N., Chambers, C.J., Davies, A.H., Roberts, A.K., Shone, C.C. and Acharya, K.R., 2014. The structure of the cysteine protease and lectin-like domains of Cwp84, a surface layer-associated protein from Clostridium difficile. Acta Crystallographica Section D-Biological Crystallography, 70 (7), pp. 1983-1993. Acharya, K.R. and Ackerman, S.J., 2014. Eosinophil granule proteins:Form and function. Journal of Biological Chemistry, 289 (25), pp. 17406-17415. Michaud, A., Acharya, K., Masuyer, G., Quenech'du, N., Gribouval, O., Morinière, V., Gubler, M.-C. and Corvol, P., 2014. Absence of cell surface expression of human ACE leads to perinatal death. Human Molecular Genetics, 23 (6), pp. 1479-1491. Douglas, R. G., Sharma, R. K., Masuyer, G., Lubbe, L., Zamora, I., Acharya, K. R., Chibale, K. and Sturrock, E. D., 2014. Fragment-based design for the development of N-domain-selective angiotensin-1-converting enzyme inhibitors. Clinical Science, 126 (4), pp. 305-313. Masuyer, G., Mohd, A., Czarny, B., Beau, F., Schwager, S. L. U., Sturrock, E. D., Isaac, R. E., Dive, V. and Acharya, K. R., 2014. Crystal structures of highly specific phosphinic tripeptide enantiomers in complex with the angiotensin-I converting enzyme. FEBS Journal, 281 (3), pp. 943-956. Yates, C. J., Masuyer, G., Schwager, S. L. U., Mohd, A., Sturrock, E. D. and Acharya, K. R., 2014. Molecular and thermodynamic mechanisms of the chloride-dependent human angiotensin-I-converting enzyme (ACE). Journal of Biological Chemistry, 289 (3), pp. 1798-1814. Iyer, S., Holloway, D. E. and Acharya, K. R., 2013. Crystal structures of murine angiogenin-2 and -3 - probing ‘structure - function’ relationships amongst angiogenin homologues. FEBS Journal, 280 (1), pp. 302-318. Thiyagarajan, N. and Acharya, K.R., 2013. Crystal structure of human angiogenin with an engineered loop exhibits conformational flexibility at the functional regions of the molecule. FEBS Open Bio, 3, pp. 65-70.