Zobrazeno 1 - 10
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pro vyhledávání: '"C.E. Naylor"'
Akademický článek
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Autor:
Robert W. Evans, Henry K. Bayele, S. Kaila S. Srai, C.E. Naylor, Alpesh Patel, Nick Beaumont, Christopher L. Joannou, Basharut A. Syed, Peter S. N. Rowe
Publikováno v:
Protein Engineering, Design and Selection. 15:205-214
Hephaestin was implicated in mammalian iron homeostasis following its identification as the defective gene in murine sex-linked anaemia. It is a member of the family of copper oxidases that includes mammalian ceruloplasmin, factors V and VIII, yeast
Publikováno v:
Biochemistry. 39:15002-15011
The role of Asp-177 in the His-Asp catalytic dyad of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides has been investigated by a structural and functional characterization of the D177N mutant enzyme. Its three-dimensional structure ha
Autor:
Deborah A. Scopes, M.J. Adams, L. Vandeputte-Rutten, Veronica M.S. Lam, C.E. Naylor, Lucio Luzzatto, S. Gover, Philip J. Mason, S.W.N. Au
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 55:826-834
Recombinant human glucose 6-phosphate dehydrogenase (G6PD) has been crystallized and its structure solved by molecular replacement. Crystals of the natural mutant R459L grow under similar conditions in space groups P212121 and C2221 with eight or fou
Publikováno v:
Biochemistry. 37:2759-2767
The catalytic mechanism of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed mutagenesis. Each of the mutant enzymes w
Autor:
C.E. Naylor, L. Luzzatto, S. Gover, T. J. Vulliamy, M.J. Adams, José M. Bautista, P.J. Mason, A.K. Basak, P Rowland
Publikováno v:
Scopus-Elsevier
Human glucose 6-phosphate dehydrogenase (G6PD) has a particularly large number of variants resulting from point mutations; some 60 mutations have been sequenced to date. Many variants, some polymorphic, are associated with enzyme deficiency. Certain
Autor:
Nora Cronin, Orval A. Bateman, Nicholas H. Keep, Wilbert C. Boelens, Christine Slingsby, Claire Bagnéris, C.E. Naylor
Publikováno v:
Journal of molecular biology. 392(5)
Small heat shock proteins (sHsps) are a family of large and dynamic oligomers highly expressed in long-lived cells of muscle, lens and brain. Several family members are upregulated during stress, and some are strongly cytoprotective. Their polydisper
Akademický článek
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Autor:
Ali M. Al-Shangiti, Sean P. Nair, Brian Henderson, Benjamin M. Chain, David Briggs, C.E. Naylor
The staphylococcal superantigen-like proteins (SSLs) are a family of polymorphic paralogs encoded in the S taphylococcus aureus genome whose function is unknown. The crystal structure of SSL7 was determined and compared to that of SSL5 and that of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a9f80be771778f84d6e4923cbe94d86
https://europepmc.org/articles/PMC427445/
https://europepmc.org/articles/PMC427445/
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 57(Pt 5)
The reduced coenzymes NADH and NADPH only differ by one phosphate, but in the cell NADH provides reducing power for catabolism while NADPH is utilized in biosynthetic pathways. Enzymes almost invariably discriminate between the coenzymes, but glucose