Research Topics
Genomes and GenesSpecies | Jeyanthy EswaranSummaryAffiliation: University of Oxford Country: UK Publications
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Detail Information
Publications
Three's company: component structures bring a closer view of tripartite drug efflux pumpsJeyanthy Eswaran
Cambridge University Department of Pathology, Tennis Court Road, Cambridge CB2 1QP, UK
Curr Opin Struct Biol 14:741-7. 2004..These structures have enhanced our understanding of the principles underlying pump assembly and operation, and present pumps as new drug targets...- UnPAKing the class differences among p21-activated kinasesJeyanthy Eswaran
University of Oxford, Structural Genomics, Old Road Campus Research Building, Old Road Campus, Roosevelt Drive, Headington, Oxford, UK
Trends Biochem Sci 33:394-403. 2008..We believe that a comprehensive understanding of the entire PAK family is essential for developing strategies towards PAK-targeted therapeutics... - Structure and functional characterization of the atypical human kinase haspinJeyanthy Eswaran
Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom
Proc Natl Acad Sci U S A 106:20198-203. 2009.... - Insights into protein kinase regulation and inhibition by large scale structural comparisonJeyanthy Eswaran
Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford Old Road Campus Building, Oxford OX3 7DQ, UK
Biochim Biophys Acta 1804:429-32. 2010..Here we discuss the currently available structural data and strategies that can be utilized for the development of highly selective inhibitors... - Targeting group II PAKs in cancer and metastasisJeyanthy Eswaran
Structural Genomics Consortium, University of Oxford, Old Road Campus, Roosevelt Drive, Oxford, OX3 7DQ, UK
Cancer Metastasis Rev 28:209-17. 2009.... - Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKsJeyanthy Eswaran
University of Oxford, Structural Genomics Consortium, Botnar Research Centre, Oxford OX3 7LD, United Kingdom
Structure 15:201-13. 2007..Inhibitor screening identified six potent PAK inhibitors from which a tri-substituted purine inhibitor was cocrystallized with PAK4 and PAK5... - The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1Jeyanthy Eswaran
Structural Genomics Consortium, University of Oxford, Botnar Research Centre, Oxford OX3 7LD, United Kingdom
Protein Sci 15:1500-5. 2006..In agreement, we show that RPTPkappa is monomeric in solution and crystal structure... - Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatasesJeyanthy Eswaran
Structural Genomics Consortium, University of Oxford, Botnar Research Centre, Oxford OX3 7LD, UK
Biochem J 395:483-91. 2006.... - Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-A resolutionAlastair J Barr
Structural Genomics Consortium, University of Oxford, Botnar Research Centre, Oxford, United Kingdom
Proteins 63:1132-6. 2006 - Structure of the human protein kinase MPSK1 reveals an atypical activation loop architectureJeyanthy Eswaran
Structural Genomics Consortium, Botnar Research Centre, University of Oxford, Oxford, United Kingdom
Structure 16:115-24. 2008..The presented data reveal an atypical kinase structural motif and suggest a role of MPSK1 regulating DRG1, a GTPase involved in regulation of cellular growth... - Atypical GTPases as drug targetsMeera Soundararajan
Structural Genomics Consortium, Nuffield Department of Clinical Medicine, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford, OX3 7DQ, UK
Anticancer Agents Med Chem 12:19-28. 2012..In summary, this review will highlight the emerging atypical GTPase family which allows us to understand novel regulatory mechanisms and thus providing new avenues for drug discovery programs... - Structure of the ligand-blocked periplasmic entrance of the bacterial multidrug efflux protein TolCMatthew K Higgins
Department of Pathology, Cambridge University, Tennis Court Road, Cambridge CB2 1QP, UK
J Mol Biol 342:697-702. 2004..As the electronegative entrance is widely conserved in the TolC family, it may be a useful target for the development of inhibitors against multidrug resistant pathogenic bacteria... - Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux systemThierry Touze
Cambridge University Department of Pathology, Tennis Court Road, Cambridge CB2 1QP, UK
Mol Microbiol 53:697-706. 2004..These in vivo and in vitro analyses establish the central role of the AcrA adaptor in drug-independent assembly of the tripartite drug efflux pump, specifically in coupling the inner membrane transporter and the outer membrane exit duct... - Structure and function of TolC: the bacterial exit duct for proteins and drugsVassilis Koronakis
Department of Pathology, Cambridge University, Cambridge CB2 1QP, United Kingdom
Annu Rev Biochem 73:467-89. 2004..TolC family proteins are ubiquitous among gram-negative bacteria, and the conserved entrance aperture presents a possible cheomotherapeutic target in multidrug-resistant pathogens... - Locking TolC entrance helices to prevent protein translocation by the bacterial type I export apparatusJeyanthy Eswaran
Department of Pathology, Cambridge University, Tennis Court Road, UK
J Mol Biol 327:309-15. 2003..The data show that untwisting the entrance helices is essential for the export function of TolC in E.coli, specifically to allow access and passage of substrates engaged at the inner membrane translocase... - Transition to the open state of the TolC periplasmic tunnel entranceChristian Andersen
Department of Pathology, Cambridge University, Tennis Court Road, Cambridge CB2 1QP, United Kingdom
Proc Natl Acad Sci U S A 99:11103-8. 2002..The results support a model in which transition to the open state of TolC is achieved by an iris-like realignment of the tunnel entrance helices...