Zobrazeno 1 - 10
of 17
pro vyhledávání: '"S J Yewdall"'
Autor:
G. C. Ford, Alisdair R Fernie, D. M. Lawson, Paul D. Hempstead, Pauline M. Harrison, S J Yewdall, Peter J. Artymiuk, David W. Rice
Publikováno v:
Journal of Molecular Biology. 268:424-448
Mammalian ferritins are 24-mers assembled from two types of polypeptide chain which provide the molecule with different functions. H(eavy) chains catalyse the first step in iron storage, the oxidation of iron(II). L(ight) chains promote the nucleatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85a8adeeb837deb61060842d2383dd78
https://doi.org/10.1006/jmbi.1997.0970
https://doi.org/10.1006/jmbi.1997.0970
Autor:
Amyra Treffry, J. C. Livingstone, John R. Guest, Peter J. Artymiuk, J. M. A. Smith, Pauline M. Harrison, D. M. Lawson, S J Yewdall, Simon C. Andrews, J. Hirzmann, G. C. Ford
Publikováno v:
ChemInform. 22
Publisher Summary This chapter compares the structures of the iron cores and protein coats of ferritins and the hemoferritins of bacteria, and the current state of knowledge concerning mineralization processes in these molecules is discussed in relat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ca6388cecc95ad929e7c3e8caf8bd875
https://doi.org/10.1002/chin.199150348
https://doi.org/10.1002/chin.199150348
Publikováno v:
Biochemical Journal. 288:931-939
The iron storage protein, ferritin, is widely distributed in the living kingdom. Here the complete cDNA and derived amino-acid sequence of pea seed ferritin are described, together with its predicted secondary structure, namely a four-helix-bundle fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d652e818a61423c119cbf0843a0f0cf5
https://doi.org/10.1042/bj2880931
https://doi.org/10.1042/bj2880931
Autor:
Sonia Levi, Werner Bottke, Pauline M. Harrison, M. von Darl, Jean-François Briat, Paolo Arosio, S J Yewdall, Simon C. Andrews, J. P. Laulhère, S. Lobreaux
Publikováno v:
Journal of Inorganic Biochemistry. 47:161-174
The ferritins of animals and plants and the bacterioferritins (BFRs) have a common iron-storage function in spite of differences in cytological location and biosynthetic regulation. The plant ferritins and BFRs are more similar to the H chains of mam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4721df47a6dac449fe71d22e1daaa031
https://doi.org/10.1016/0162-0134(92)84062-r
https://doi.org/10.1016/0162-0134(92)84062-r
Autor:
P D, Hempstead, S J, Yewdall, A R, Fernie, D M, Lawson, P J, Artymiuk, D W, Rice, G C, Ford, P M, Harrison
Publikováno v:
Journal of molecular biology. 268(2)
Mammalian ferritins are 24-mers assembled from two types of polypeptide chain which provide the molecule with different functions. H(eavy) chains catalyse the first step in iron storage, the oxidation of iron(II). L(ight) chains promote the nucleatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0a89506db7be35bf1466271f15ff5545
https://pubmed.ncbi.nlm.nih.gov/9159481
https://pubmed.ncbi.nlm.nih.gov/9159481
Publikováno v:
Advances in experimental medicine and biology. 356
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3abb7ea4d0c6b31e4f947d2fc6b4187d
https://pubmed.ncbi.nlm.nih.gov/7887213
https://pubmed.ncbi.nlm.nih.gov/7887213
Autor:
Amyra Treffry, D. Hechel, Pauline M. Harrison, S J Yewdall, Israel Nowik, E. R. Bauminger, Nigel Hodson
Publikováno v:
University of Manchester-PURE
The paper describes a study of Fe(II) oxidation and the formation of Fe(III)-apoferritin complexes in recombinant human H-chain ferritin and its variants. The effects of site-directed changes in the conserved residues associated with a proposed ferro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d2bd375d5b70bfcc686c2864a51815d
https://pubmed.ncbi.nlm.nih.gov/8280069
https://pubmed.ncbi.nlm.nih.gov/8280069
Autor:
S J Yewdall, Amyra Treffry, D. Hechel, E. R. Bauminger, Israel Nowik, Nigel Hodson, Pauline M. Harrison
Publikováno v:
University of Manchester-PURE
This paper aims to define the role of the threefold intersubunit channels in iron uptake and sequestration processes in the iron-storage protein, ferritin. Iron uptake, measured as loss of availability of Fe(II) to ferrozine (due to oxidation), has b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a3827d70b6b89338effa7a8869fa2ac
https://pubmed.ncbi.nlm.nih.gov/7506527
https://pubmed.ncbi.nlm.nih.gov/7506527
Autor:
S J Yewdall, Pauline M. Harrison, John R. Guest, F.H.A. Kadir, A J Thomson, Myles R. Cheesman, N.E. Le Brun, G.R. Moore, Simon C. Andrews, J. M. A. Smith
Publikováno v:
Scopus-Elsevier
The bacterioferritin (BFR) of Escherichia coli is an iron-storage protein containing 24 identical subunits and between three and 11 protohaem IX groups per molecule. Titration with additional haem gave a maximum loading of 12-14 haems per molecule. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b68acdd9147b2cd16bab77bd65d5abb7
https://pubmed.ncbi.nlm.nih.gov/8389131
https://pubmed.ncbi.nlm.nih.gov/8389131
Autor:
Anna Cozzi, Pauline M. Harrison, Paolo Santambrogio, Ermanna Rovida, Paolo Arosio, Alberto Albertini, S J Yewdall, Sonia Levi
Publikováno v:
Europe PubMed Central
The ability to incorporate iron in vitro was studied in homopolymers of human ferritin L-chain, human ferritin H-chain and its variants and in homopolymer mixtures. The H-chain variants carried amino acid substitutions in the ferroxidase centre and/o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8c544a1161f5e122951848d976fc6b2
https://pubmed.ncbi.nlm.nih.gov/1463463
https://pubmed.ncbi.nlm.nih.gov/1463463