Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Colin C.F. Blake"'
Autor:
Colin C.F. Blake, Margaret Sunde
Publikováno v:
Quarterly Reviews of Biophysics. 31:1-39
The term ‘amyloid’ was used originally to describe certain deposits found post- mortem in organs and tissues, which gave a positive reaction when stained with iodine (Virchow, 1854). Only later was it realized that the material was in fact predom
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
Autor:
Vittorio Bellotti, Sheena E. Radford, Winston L. Hutchinson, Mark B. Pepys, Colin C.F. Blake, Paul E. Fraser, Carol V. Robinson, Christopher M. Dobson, Philip N. Hawkins, Margaret Sunde, David R. Booth
Publikováno v:
Nature. 385:787-793
Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with t
Publikováno v:
Proteins: Structure, Function, and Genetics. 24:292-303
The crystal structure of a ternary complex of pig muscle phosphoglycerate kinase (PGK) containing 3-phosphoglycerate (3-PG) and manganese adenylylimidodiphosphate (Mn AMP-PNP) has been determined and refined at 2.0 A resolution. The complex differs f
Autor:
Louise C. Serpell, O. Sangren, Pradeep K. Luther, Erik Lundgren, Paul E. Fraser, Colin C.F. Blake, Edward P. Morris, Margaret Sunde
Publikováno v:
Journal of Molecular Biology. 254:113-118
Familial amyloidotic polyneuropathies are autosomal-dominant, inherited disorders that are characterised by the aggregation of variant proteins in a fibrillar form and by the extracellular deposition of amyloid fibrils. In familial amyloidotic polyne
Publikováno v:
Structure. 3(2):177-187
Background: Methanol dehydrogenase (MDH) is a bacterial periplasmic quinoprotein; it has pyrrolo-quinoline quinone (PQQ) as its prosthetic group, requires Ca 2+ for activity and uses cytochrome c L as its electron acceptor. Low-resolution structures
Publikováno v:
Nature Structural & Molecular Biology. 1:102-105
Adjacent cysteine residues can only form disulphide bridges in a distorted structure containing a cis-peptide link. Such bridges are extremely uncommon, identified so far in the acetyl choline receptor alone where the structure of the bridge is undet
Autor:
F.M. Poulsen, Robert J. P. Williams, D.E.P. Grace, Christopher M. Dobson, David Phillips, Stephen J. Perkins, Colin C.F. Blake, Louise N. Johnson, R. Cassels
Publikováno v:
Ciba Foundation Symposium 60 - Molecular Interactions and Activity in Proteins
The conformations of lysozyme in crystals and in aqueous solution are discussed and it is shown that the basic conformation is similar in the two states. Certain parts of the molecule have mobility. The reactions of lysozyme with protons, metal ions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7c3251e44de5deb0c4add84cc4a362b5
https://doi.org/10.1002/9780470720424.ch10
https://doi.org/10.1002/9780470720424.ch10
Publikováno v:
Ciba Foundation Symposium 199 - The Nature and Origin of Amyloid Fibrils
We have investigated the ultrastructure of the homozygous amyloid fibrils from the vitreous humour of patients with Met30 familial amyloidotic polyneuropathy (FAP) by high-resolution electron microscopy and X-ray diffraction using synchrotron radiati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1ef5eea7ed0d228c796dbe7d8a02009
https://doi.org/10.1002/9780470514924.ch2
https://doi.org/10.1002/9780470514924.ch2
Autor:
Margaret Sunde, Colin C.F. Blake
Publisher Summary The chapter discusses the structural analysis of amyloid fibrils by electron microscopy and X-ray diffraction. A method to isolate amyloid fibrils from tissue was developed, and such preparations of purified fibrils exhibited the cl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cadb615a6d0ac2b2c50de781aad995be
https://doi.org/10.1016/s0065-3233(08)60320-4
https://doi.org/10.1016/s0065-3233(08)60320-4
Autor:
Samantha J. Richardson, Margaret Sunde, Tom Pettersson, Linus Chang, Gerhard Schreiber, Colin C.F. Blake
Publikováno v:
Scopus-Elsevier
The crystal structure of chicken transthyretin has been solved at 290-pm resolution by molecular-replacement techniques. Transthyretin is the protein component of the amyloid fibrils found in patients suffering from either familial amyloidotic polyne