James Feeney, D.Sc

Affiliations: 
MRC Biomedical NMR Centre National Institute for Medical Research, London, England, United Kingdom 
Area:
Use of NMR in Biochemistry
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"James Feeney"
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http://onlinelibrary.wiley.com/doi/10.1002/9780470034590.emrhp0053/pdf

Mean distance: 10.61
 
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Publications

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Feeney J, Birdsall B, Kovalevskaya NV, et al. (2011) NMR structures of apo L. casei dihydrofolate reductase and its complexes with trimethoprim and NADPH: contributions to positive cooperative binding from ligand-induced refolding, conformational changes, and interligand hydrophobic interactions. Biochemistry. 50: 3609-20
Babon JJ, Morgan WD, Kelly G, et al. (2007) Structural studies on Plasmodium vivax merozoite surface protein-1. Molecular and Biochemical Parasitology. 153: 31-40
Kovalevskaya NV, Smurnyi ED, Birdsall B, et al. (2007) Structural factors determining the binding selectivity of the antibacterial drug trimethoprim to dihydrofolate reductase Pharmaceutical Chemistry Journal. 41: 350-353
Polshakov VI, Birdsall B, Feeney J. (2006) Effects of co-operative ligand binding on protein amide NH hydrogen exchange. Journal of Molecular Biology. 356: 886-903
Kovalevskaya N, Polshakov V, Birdsall B, et al. (2006) 1H, 15N and 13C resonance assignments of human dihydrofolate reductase in its complex with trimethoprim and NADPH Journal of Back and Musculoskeletal Rehabilitation
Martin SR, Biekofsky RR, Skinner MA, et al. (2004) Interaction of calmodulin with the phosphofructokinase target sequence. Febs Letters. 577: 284-8
Biekofsky RR, Turjanski AG, Estrin DA, et al. (2004) Ab initio study of NMR 15N chemical shift differences induced by Ca2+ binding to EF-hand proteins. Biochemistry. 43: 6554-64
Muskett FW, May FE, Westley BR, et al. (2003) Solution structure of the disulfide-linked dimer of human intestinal trefoil factor (TFF3): the intermolecular orientation and interactions are markedly different from those of other dimeric trefoil proteins. Biochemistry. 42: 15139-47
Biekofsky RR, Martin SR, McCormick JE, et al. (2002) Thermal stability of calmodulin and mutants studied by (1)H-(15)N HSQC NMR measurements of selectively labeled [(15)N]Ile proteins. Biochemistry. 41: 6850-9
Polshakov VI, Biekofsky RR, Birdsall B, et al. (2002) Towards understanding the origins of the different specificities of binding the reduced (NADPH) and oxidised (NADPH+) forms of nicotinamide adenine dinucleotide phosphate coenzyme to dihydrofolate reductase Journal of Molecular Structure. 602: 257-267
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