S
Stephen J. Perkins
Researcher at University College London
Publications - 260
Citations - 9741
Stephen J. Perkins is an academic researcher from University College London. The author has contributed to research in topics: Neutron scattering & Factor H. The author has an hindex of 54, co-authored 251 publications receiving 9253 citations. Previous affiliations of Stephen J. Perkins include University of North London & Royal Free Hospital.
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Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences.
TL;DR: In this paper, an intermediate consensus volume set of amino acid-residue volumes is proposed in order to predict experimental v values using sequence information, and the method is extended to carbohydrates and glycoproteins.
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The fab and fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling
TL;DR: The IgAA1 hinge is structurally distinct from that in IgG, and this results in a markedly different antibody structure that may account for a unique immune role of monomeric IgA1 in plasma and mucosa.
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Autosomal dominant reticuloendothelial iron overload associated with a 3–base pair deletion in the ferroportin 1 gene(SLC11A3)
Vinod Devalia,Kymberley Carter,Ann P. Walker,Stephen J. Perkins,Mark Worwood,Alison May,James Dooley +6 more
TL;DR: Results indicate that this extracellular cluster is functionally important for iron transport, and its disruption leads to iron overload.
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Deletion of Lys224 in regulatory domain 4 of Factor H reveals a novel pathomechanism for dense deposit disease (MPGN II)
Christoph Licht,Stefan Heinen,Mihály Józsi,Ina Löschmann,Rebecca E. Saunders,Stephen J. Perkins,Ruediger Waldherr,Christine Skerka,Michael Kirschfink,Bernd Hoppe,Peter F. Zipfel,Peter F. Zipfel +11 more
TL;DR: Replacement of functional Factor H by fresh frozen plasma was well tolerated, prevented so far disease progression in both patients, and is in the long run expected to preserve kidney function.
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His-384 allotypic variant of factor H associated with age-related macular degeneration has different heparin binding properties from the non-disease-associated form.
Simon J. Clark,Victoria A. Higman,Barbara Mulloy,Stephen J. Perkins,Susan M. Lea,Robert B. Sim,Anthony J. Day,Anthony J. Day +7 more
TL;DR: Using a recombinant construct, it is shown that amino acid 384 is adjacent to a heparin-binding site in CCP7 of factor H and demonstrated that the allotypic variants differentially recognize heparine, potentially influencing complement activation, immune complex clearance, and inflammation in the macula of AMD patients.