B
B J Sutton
Researcher at University of Oxford
Publications - 10
Citations - 1578
B J Sutton is an academic researcher from University of Oxford. The author has contributed to research in topics: Dinitrophenyl & Triple-resonance nuclear magnetic resonance spectroscopy. The author has an hindex of 9, co-authored 10 publications receiving 1518 citations. Previous affiliations of B J Sutton include University of Paris-Sud.
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Journal ArticleDOI
Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG.
Raj B. Parekh,Raymond A. Dwek,B J Sutton,Daryl L. Fernandes,A. Leung,D. R. Stanworth,Thomas W. Rademacher,T. Mizuochi,Tadatsugu Taniguchi,K. Matsuta,Fujio Takeuchi,Yasutaka Nagano,T Miyamoto,Akira Kobata +13 more
TL;DR: The results indicate that IgG isolated from normal individuals, patients with RA and patients with OA contains different distributions of asparagine-linked bi-antennary complex-type oligosaccharide structures, and these two arthritides may therefore be glycosylation diseases, reflecting changes in the intracellular processing, or post-secretory degradation of N-linked oligOSaccharides.
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Tertiary structural similarity between a class A β -lactamase and a penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase
Boudjéma Samraoui,Boudjéma Samraoui,Boudjéma Samraoui,B J Sutton,B J Sutton,R. J. Todd,R. J. Todd,Peter J. Artymiuk,Peter J. Artymiuk,S. G. Waley,David Phillips +10 more
TL;DR: The first evidence from a comparison of three-dimensional structures in support of the hypothesis that the β-lactamase I from Bacillus cereus is similar to that of the penicillin-sensitive D-alanyl-D-alanine carboxypeptidase-transpeptidases from Streptomyces R613 is presented.
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An X-ray-crystallographic study of beta-lactamase II from Bacillus cereus at 0.35 nm resolution.
TL;DR: Crystals of beta-lactamase II (EC 3.5.2.6., 'penicillinase') from Bacillus cereus were grown with Cd(II) in place of the natural Zn( II) cofactor and stabilized by cross-linking with glutaraldehyde to suggest the probable location of the active site of the enzyme.
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Structure of an antibody combining site by magnetic resonance.
Raymond A. Dwek,Simon Wain-Hobson,S K Dower,Peter G.W. Gettins,B J Sutton,Stephen J. Perkins,David Givol +6 more
TL;DR: The structure of the combining site of the DNP binding IgA mouse myeloma protein MOPC 315 has been determined by a combination of high resolution nuclear magnetic resonance, electron spin resonance, model building and chemical modifications.
Journal ArticleDOI
The combining site of the dinitrophenyl-binding immunoglobulin A myeloma protein MOPC 315
S K Dower,Simon Wain-Hobson,Peter G.W. Gettins,David Givol,W. Roland C. Jackson,Stephen J. Perkins,Christopher A. Sunderland,B J Sutton,Carolyn E. Wright,Raymond A. Dwek +9 more
TL;DR: In this article, Padlan, Davies, Pecht, Givol & Wright used magnetic resonance analysis to refine the model of the combining site of the Fv fragment of the dinitrophenyl-binding mouse myeloma protein MOPC 315.