Search Results - (Author, Cooperation:D. I. Stuart)
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1N. Hengrung ; K. El Omari ; I. Serna Martin ; F. T. Vreede ; S. Cusack ; R. P. Rambo ; C. Vonrhein ; G. Bricogne ; D. I. Stuart ; J. M. Grimes ; E. Fodor
Nature Publishing Group (NPG)
Published 2015Staff ViewPublication Date: 2015-10-28Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Apoenzymes/chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Endonucleases/chemistry/metabolism ; Enzyme Activation ; Influenzavirus C/*enzymology ; Models, Molecular ; Peptide Chain Initiation, Translational ; Promoter Regions, Genetic/genetics ; Protein Binding ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; RNA Caps/metabolism ; RNA Replicase/*chemistry/metabolism ; RNA, Viral/biosynthesis/metabolism ; Ribonucleoproteins/chemistryPublished by: -
2X. Wang ; J. Ren ; Q. Gao ; Z. Hu ; Y. Sun ; X. Li ; D. J. Rowlands ; W. Yin ; J. Wang ; D. I. Stuart ; Z. Rao ; E. E. Fry
Nature Publishing Group (NPG)
Published 2014Staff ViewPublication Date: 2014-10-21Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Capsid/chemistry ; Capsid Proteins/chemistry ; Crystallography, X-Ray ; *Evolution, Molecular ; Hepatitis A virus/*chemistry ; Hot Temperature ; Humans ; Hydrogen-Ion Concentration ; Insects/virology ; Models, Molecular ; Phylogeny ; Picornaviridae/*chemistry ; Transcytosis ; Virion/chemistry ; Virus InternalizationPublished by: -
3ROBINSON, R. C. ; GREY, L. M. ; STAUNTON, D. ; STUART, D. I. ; HEATH, J. K. ; JONES, E. Y.
Oxford, UK : Blackwell Publishing Ltd
Published 1995Staff ViewISSN: 1749-6632Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: Natural Sciences in GeneralType of Medium: Electronic ResourceURL: -
4Stuart, D. I. ; Acharya, K. R. ; Walker, N. P. C. ; Smith, S. G. ; Lewis, M. ; Phillips, D. C.
[s.l.] : Nature Publishing Group
Published 1986Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] 〈!--a-Lactalbumin acts as a specifier protein3, it comprises some 15% of total protein in human milk4 and is essential for the production of lactose. The attachment of a-lactalbumin to /3-galactosyl transferase on the luminal surface of the Golgi membrane results in a complex, lactose synthetase ...Type of Medium: Electronic ResourceURL: -
5Harlos, K. ; Martin, D. M. A. ; O'Brien, D. P. ; Jones, E. Y. ; Stuart, D. I. ; Polikarpov, I. ; Miller, A. ; Tuddenham, E. G. D. ; Boys, C. W. G.
[s.l.] : Nature Publishing Group
Published 1994Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] Residues 1-219 of tissue factor (TF2i9) were expressed in Escherichia coli, purified and crystallized as described previously5. TF2i9 was fully functional in assays for soluble tissue-factor activity6 and bound to factor VII in ligand blots7. The structure of TF219 was solved by multiple ...Type of Medium: Electronic ResourceURL: -
6Jones, E. Y. ; Harlos, K. ; Bottomley, M. J. ; Robinson, R. C. ; Driscoll, P. C. ; Edwards, R. M. ; Clements, J. M. ; Dudgeon, T. J. ; Stuart, D. I.
[s.l.] : Nature Publishing Group
Published 1995Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The soluble fragment VCAM-dl,2 (human VCAM-1 residues 1 to 202, with no TV-linked glycosylation sites, expressed in Escherichia coli) formed stable, highly ordered crystals which contained two molecules per crystallographic asymmetric unit9. Details of the crystallographic structure determination ...Type of Medium: Electronic ResourceURL: -
7Staff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] Tumour necrosis factor is a trimeric molecule, each subunit of which consists of an antiparallel β sandwich. Individual subunits form the trimer by a novel edge-to-face packing of β sheets. A comparison of the subunit fold with that of other proteins reveals a remarkable similarity to the ...Type of Medium: Electronic ResourceURL: -
8Sprang, S. R. ; Acharya, K. R. ; Goldsmith, E. J. ; Stuart, D. I. ; Varvill, K. ; Fletterick, R. J. ; Madsen, N. B. ; Johnson, L. N.
[s.l.] : Nature Publishing Group
Published 1988Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] A comparison of the refined crystal structures of dimeric glycogen phosphorylase b and a reveals structural changes that represent the first step in the activation of the enzyme. On phosphorylation of serine-14, the N-terminus of each subunit assumes an ordered helical conformation and binds to the ...Type of Medium: Electronic ResourceURL: