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Journal articleGoncalves V, Brannigan JA, Thinon E, et al., 2012,
A fluorescence-based assay for N-myristoyltransferase activity
, Analytical Biochemistry, Vol: 421, Pages: 342-344, ISSN: 1096-0309N-myristoylation is the irreversible attachment of a C14 fatty acid, myristic acid, to the N-terminal glycine of a protein via formation of an amide bond. This modification is catalyzed by myristoyl–coenzyme A (CoA):protein N-myristoyltransferase (NMT), an enzyme ubiquitous in eukaryotes that is up-regulated in several cancers. Here we report a sensitive fluorescence-based assay to study the enzymatic activity of human NMT1 and NMT2 based on detection of CoA by 7-diethylamino-3-(4-maleimido-phenyl)-4-methylcoumarin. We also describe expression and characterization of NMT1 and NMT2 and assay validation with small molecule inhibitors. This assay should be broadly applicable to NMTs from a range of organisms.
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Journal articleBroncel M, Serwa RA, Tate EW, 2012,
A New Chemical Handle for Protein AMPylation at the Host-Pathogen Interface
, Chembiochem, Vol: 13, Pages: 183-185, ISSN: 1439-7633agging protein AMPylation: A new chemical reporter for AMPylation, recently identified as a key post-translational modification during bacterial infection, is a robust tool for detecting and identifying AMPylated proteins in vitro.
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Journal articleDang THT, Fagan RP, Fairweather NF, et al., 2012,
Novel inhibitors of surface layer processing in Clostridium difficile
, Bioorganic & Medicinal Chemistry, Vol: 20, Pages: 614-621, ISSN: 1464-3391Clostridium difficile, a leading cause of hospital-acquired bacterial infection, is coated in a dense surface layer (S-layer) that is thought to provide both physicochemical protection and a scaffold for host-pathogen interactions. The key structural components of the S-layer are two proteins derived from a polypeptide precursor, SlpA, via proteolytic cleavage by the protease Cwp84. Here, we report the design, synthesis and in vivo characterization of a panel of protease inhibitors and activity-based probes (ABPs) designed to target S-layer processing in live C. difficile cells. Inhibitors based on substrate-mimetic peptides bearing a C-terminal Michael acceptor warhead were found to be promising candidates for further development.
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Journal articleHeal WP, Wright MH, Thinon E, et al., 2012,
Multifunctional protein labeling via enzymatic N-terminal tagging and elaboration by click chemistry
, NATURE PROTOCOLS, Vol: 7, Pages: 105-117, ISSN: 1754-2189- Author Web Link
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- Citations: 82
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Journal articleHeal WP, Tate EW, 2012,
Application of Activity-Based Protein Profiling to the Study of Microbial Pathogenesis
, ACTIVITY-BASED PROTEIN PROFILING, Vol: 324, Pages: 115-135, ISSN: 0340-1022- Author Web Link
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- Citations: 17
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Journal articleFurse S, Brooks NJ, Seddon AM, et al., 2012,
Lipid membrane curvature induced by distearoyl phosphatidylinositol 4-phosphate
, Soft Matter -
Journal articleBradshaw RT, Aronica PGA, Tate EW, et al., 2012,
Mutational Locally Enhanced Sampling (MULES) for quantitative prediction of the effects of mutations at protein-protein interfaces
, CHEMICAL SCIENCE, Vol: 3, Pages: 1503-1511, ISSN: 2041-6520- Author Web Link
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- Citations: 2
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Journal articleTate EW, Goss RJM, 2011,
Highlights from the 46th EUCHEM Conference on stereochemistry, Bürgenstock, Switzerland, May 2011.
, Chem Commun (Camb), Vol: 47, Pages: 10869-10873 -
Journal articleDelmotte A, Tate EW, Yaliraki SN, et al., 2011,
Protein multi-scale organization through graph partitioning and robustness analysis: application to the myosin-myosin light chain interaction
, PHYSICAL BIOLOGY, Vol: 8, ISSN: 1478-3975Despite the recognized importance of the multi-scale spatio-temporal organization of proteins, most computational tools can only access a limited spectrum of time and spatial scales, thereby ignoring the effects on protein behavior of the intricate coupling between the different scales. Starting from a physico-chemical atomistic network of interactions that encodes the structure of the protein, we introduce a methodology based on multi-scale graph partitioning that can uncover partitions and levels of organization of proteins that span the whole range of scales, revealing biological features occurring at different levels of organization and tracking their effect across scales. Additionally, we introduce a measure of robustness to quantify the relevance of the partitions through the generation of biochemically-motivated surrogate random graph models. We apply the method to four distinct conformations of myosin tail interacting protein, a protein from the molecular motor of the malaria parasite, and study properties that have been experimentally addressed such as the closing mechanism, the presence of conserved clusters, and the identification through computational mutational analysis of key residues for binding.
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Journal articlede la Riva L, Willing SE, Tate EW, et al., 2011,
Roles of Cysteine Proteases Cwp84 and Cwp13 in Biogenesis of the Cell Wall of <i>Clostridium difficile</i>
, JOURNAL OF BACTERIOLOGY, Vol: 193, Pages: 3276-3285, ISSN: 0021-9193- Author Web Link
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- Citations: 42
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