Zobrazeno 1 - 10 of 43 pro vyhledávání: '"B F, ANDERSON"'
1
Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains
Autor: M, Paoli, B F, Anderson, H M, Baker, W T, Morgan, A, Smith, E N, Baker
Publikováno v: Nature structural biology. 6(10)
The ubiquitous use of heme in animals poses severe biological and chemical challenges. Free heme is toxic to cells and is a potential source of iron for pathogens. For protection, especially in conditions of trauma, inflammation and hemolysis, and to
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::acd9b7d183c0b0468070c219576bfad4
https://pubmed.ncbi.nlm.nih.gov/10504726
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3
Three-dimensional structure of lactoferrin in various functional states
Autor: E N, Baker, B F, Anderson, H M, Baker, C L, Day, M, Haridas, G E, Norris, S V, Rumball, C A, Smith, D H, Thomas
Publikováno v: Advances in experimental medicine and biology. 357
The three-dimensional structures of various forms of lactoferrin, determined by high resolution crystallographic studies, have been compared in order to determine the relationship between structure and biological function. These comparisons include h
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::980c7ffb6f72e5145513c411c7a8ebac
https://pubmed.ncbi.nlm.nih.gov/7762421
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7
Domain closure in lactoferrin. Two hinges produce a see-saw motion between alternative close-packed interfaces
Autor: M, Gerstein, B F, Anderson, G E, Norris, E N, Baker, A M, Lesk, C, Chothia
Publikováno v: Journal of molecular biology. 234(2)
Lactoferrin is an iron transport protein. Upon binding iron, the two domains in the N-terminal half of the molecule move together. Previous work has shown that this domain closure involves two hinges. Using the newly refined structure of the open for
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7d57b984895a3079ff90597353766e32
https://pubmed.ncbi.nlm.nih.gov/8230220
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