S
Stephen J. Yeaman
Researcher at Newcastle University
Publications - 119
Citations - 5967
Stephen J. Yeaman is an academic researcher from Newcastle University. The author has contributed to research in topics: Pyruvate dehydrogenase complex & Oxoglutarate dehydrogenase complex. The author has an hindex of 43, co-authored 119 publications receiving 5851 citations. Previous affiliations of Stephen J. Yeaman include University of Dundee.
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Journal ArticleDOI
The 2-oxo acid dehydrogenase complexes: recent advances.
TL;DR: The 2-oxo acid dehydrogenase complexes represent the classic examples of multienzyme complexes, a knowledge of whose structure and function has wide implications for our understanding of macromolecular assembly and organization and of protein structures and function as mentioned in this paper.
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Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism.
Andrew J. Garton,David G. Campbell,David Carling,D. Grahame Hardie,Roger J. Colbran,Stephen J. Yeaman +5 more
TL;DR: Phosphorylation of site 2 has been found to inhibit subsequent phosphorylation and activation of hormone-sensitive lipase by the cyclic-AMP-dependent and cyclic -GMP-dependent protein kinases, indicating that site-2 phosphorylated may have an antilipolytic role in vivo.
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Primary biliary cirrhosis: identification of two major m2 mitochondrial autoantigens
Stephen J. Yeaman,D.J. Danner,David Mutimer,S. P. M. Fussey,O.F.W. James,Margaret F. Bassendine +5 more
TL;DR: Identification of the PBC-specific, immunoreactive, trypsin-sensitive antigens on the inner mitochondrial membrane (M2) should facilitate the development of a specific serological test for PBC and the study of autoimmunising epitopes.
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Identification and analysis of the major M2 autoantigens in primary biliary cirrhosis
Shelley P. M. Fussey,John R. Guest,Oliver F. W. James,Margaret F. Bassendine,Stephen J. Yeaman +4 more
TL;DR: Analysis of the primary structure of the E2 components of all three 2-oxo acid dehydrogenase complexes reveals a high degree of homology with a similar highly segmented structure including lipoyl domains, E3-binding domains, C-terminal catalytic domains, and interdomain linker sequences.
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Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart
Stephen J. Yeaman,Eldridge T. Hutcheson,Thomas E. Roche,Flora H. Pettit,James R. Brown,Lester J. Reed,David C. Watson,Gordon H. Dixon +7 more
TL;DR: Phosphorylation proceeded markedly faster at site 1 than at sites 2 and 3, and phosphorylation at site 2 correlated closely with inactivation of pyruvate dehydrogenase, indicating the possibility of half-site reactivity.