Faculty of Biological Sciences

Dr Louise Kime

BSc (Hons) Medical Sciences, PhD Leeds
Research Fellow
School of Molecular and Cellular Biology

Contact:  Garstang 8.52, email address for  

Kime L, Vincent HA, Gendoo DMA, Jourdan SS, Fishwick CWG, Callaghan AJ, McDowall KJ The First Small-Molecule Inhibitors of Members of the Ribonuclease E Family (vol 5, 8028, 2015) SCIENTIFIC REPORTS 5 -, 2015
DOI:10.1038/srep09781

Kime L, Vincent HA, Gendoo DMA, Jourdan SS, Fishwick CWG, Callaghan AJ, McDowall KJ The first small-molecule inhibitors of members of the ribonuclease E family Scientific Reports 5 8028-, 2015
DOI:10.1038/srep08028
View abstract

Clarke JE, Kime L, Romero A D, McDowall KJ Direct entry by RNase e is a major pathway for the degradation and processing of RNA in Escherichia coli Nucleic Acids Research 42 11733-11751, 2014
DOI:10.1093/nar/gku808
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Kime L, Clarke JE, Romero A D, Grasby JA, McDowall KJ Adjacent single-stranded regions mediate processing of tRNA precursors by RNase E direct entry. Nucleic Acids Res 42 4577-4589, 2014
DOI:10.1093/nar/gkt1403
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Romero DA, Hasan AH, Lin YF, Kime L, Ruiz-Larrabeiti O, Urem M, Bucca G, Mamanova L, Laing EE, van Wezel GP, Smith CP, Kaberdin VR, Mcdowall KJ A comparison of key aspects of gene regulation in Streptomyces coelicolor and Escherichia coli using nucleotide-resolution transcription maps produced in parallel by global and differential RNA sequencing Molecular Microbiology 94 963-987, 2014
DOI:10.1111/mmi.12810
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Kime L, Jourdan SS, Stead JA, Hidalgo-Sastre A, McDowall KJ Rapid cleavage of RNA by RNase E in the absence of 5' monophosphate stimulation. Mol Microbiol 76 590-604, 2010
DOI:10.1111/j.1365-2958.2009.06935.x
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Jourdan SS, Kime L, McDowall KJ The sequence of sites recognised by a member of the RNase E/G family can control the maximal rate of cleavage, while a 5'-monophosphorylated end appears to function cooperatively in mediating RNA binding. Biochem Biophys Res Commun 391 879-883, 2010
DOI:10.1016/j.bbrc.2009.11.156
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Kime L, Jourdan SS, McDowall KJ Chapter 12 Identifying and Characterizing Substrates of the RNase E/G Family of Enzymes Methods in Enzymology 447 215-241, 2008
DOI:10.1016/S0076-6879(08)02212-X
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Kime L, Jourdan SS, McDowall KJ IDENTIFYING AND CHARACTERIZING SUBSTRATES OF THE RNASE E/G FAMILY OF ENZYMES, 2008
DOI:10.1016/S0076-6879(08)02212-X

Kime L, Wright SC Mad4 is regulated by a transcriptional repressor complex that contains Miz-1 and c-Myc. Biochem J 370 291-298, 2003
DOI:10.1042/BJ20021679
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Barnes K, Walkden BJ, Kime L, Turner AJ Localization and regulation of the isoforms of brain endothelin converting enzyme-1 ESN/ISN Meeting, JOURNAL OF NEUROCHEMISTRY 71 pp.43-, 1998