Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Keith J. Moore"'
Autor:
Keith J. Moore, Augustin Amour, Gareth Wayne, Steven J. Ratcliffe, Peter Francis, Steve L. Martin, Carla Smith, Nicholas J. Ede, Corinne Kay, Nigel M. Hooper, Daniel Thomas
Publikováno v:
PROTEOMICS. 6:2112-2120
Identification of peptide substrates for proteases can be a major undertaking. To overcome issues such as feasibility and deconvolution, associated with large peptide libraries, a 'small but smart' generic fluorescence resonance energy transfer rapid
Publikováno v:
SLAS Discovery. 7:35-44
A method is described for measuring the activity of G(s)-coupled receptors in a nonradioactive homogeneous membrane-based assay. This method has several major advantages over currently used methods for measuring functional activity of G(s)-coupled re
Autor:
Susan E. Hodge, Nieves Cuervo, Eftihia Cayanis, Sergey Kalachikov, Keith J. Moore, George Venetos, Stuart G. Fischer, Jane H. Morse, James A. Knowles, Susan L. Slager, Robyn J. Barst, Zemin Deng
Publikováno v:
The American Journal of Human Genetics. 67:737-744
Familial primary pulmonary hypertension is a rare autosomal dominant disorder that has reduced penetrance and that has been mapped to a 3-cM region on chromosome 2q33 (locus PPH1). The phenotype is characterized by monoclonal plexiform lesions of pro
Autor:
Keith J. Moore, Hakim Djaballah, David L. Earnshaw, Catherine J. Greenwood, Anthony J. Jurewicz, Andrew J. Pope, Kenneth J. Murray
Publikováno v:
SLAS Discovery. 4:239-248
DNA helicases are responsible for the unwinding of double-stranded DNA, facilitated by the binding and hydrolysis of 5'-nucleoside triphosphates. These enzymes represent an important class of targets for the development of novel anti-infective agents
Autor:
Jacques Lapointe, Keith J. Moore, Lucy Mensah, Murray J. B. Brown, Andrew J. Pope, Neil Benson
Publikováno v:
Journal of Biological Chemistry. 273:31680-31690
The kinetic mechanism for the amino acid activation reaction of Staphylococcus aureus isoleucyl-tRNA synthetase (IleRS; E) has been determined from stopped-flow measurements of the tryptophan fluorescence associated with the formation of the enzyme-b
Publikováno v:
Journal of Biological Chemistry. 273:31702-31706
Binding of ligands to isoleucyl-tRNA synthetase (IleRS; E) from Staphylococcus aureus was investigated through effects on proteolytic digestion. Approximately 50-fold higher concentrations of protease (trypsin or chymotrypsin) were required to inacti
Autor:
Neil Benson, Lucy Mensah, Andrew J. Pope, Keith J. Moore, Mary McVey, Murray J. B. Brown, Neal Osbourne, Nigel J. P. Broom, Peter J. O'Hanlon
Publikováno v:
Journal of Biological Chemistry. 273:31691-31701
The interactions of isoleucyl-tRNA synthetase (IleRS, E) from Staphylococcus aureus with both intermediate analogues and pseudomonic acid (PS-A) have been investigated using transient and steady-state techniques. Non-hydrolyzable analogues of isoleuc
Autor:
Andrew J Pope, Manfred Auer, Rolf Guenther, Franz-Josef Meyer-Almes, Keith J Moore, Kurt A. Stoeckli
Publikováno v:
Drug Discovery Today. 3:457-465
Miniaturized high-throughput screening offers great promise for increasing the productivity of the pharmaceutical drug discovery process. By monitoring interactions of single molecules in femtoliter volumes, fluorescence correlation spectroscopy (FCS
Autor:
Ulrich Haupts, Andrew J. Pope, Sandra Turconi, Charlotte Wharton, Martin Rüdiger, Jonathan P. Hutchinson, Charlotte Carey, Stephen Ashman, Ryan P. Bingham, Keith J. Moore
Publikováno v:
Journal of biomolecular screening. 8(1)
Single-molecule detection technologies are becoming a powerful readout format to support ultra-high-throughput screening. These methods are based on the analysis of fluorescence intensity fluctuations detected from a small confocal volume element. Th
Autor:
Murray J. B. Brown, Karen O'Dwyer, Drake Eggleston, Simon A. Readshaw, Stephen Ashman, Lei Wang, Andrew West, Gordon Bruton, Andrew J. Pope, Keith J. Moore, John Humphries, Peter J. O'Hanlon, Anthony Huxley, Barry Sidney Orlek
Publikováno v:
European journal of medicinal chemistry. 38(4)
Pre-protein sequence data was used to design substrates for SpsB, the bacterial signal peptidase I enzyme from Staphylococcus aureus. Key elements were an alkyl membrane anchor, proline at P5 and lysine at P2. The proline at P5 induced a helical turn