Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Steve Sarfaty"'
Publikováno v:
Structure. 5:1485-1499
Background: Escherichia coli heat-labile enterotoxin (LT) is the causative agent of traveller's diarrhoea, and it is also responsible for the deaths of hundreds of thousands of children per year in developing countries. LT is highly homologous in seq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c61b9359103ea3897112a8fc4f5f7ba8
https://doi.org/10.1016/s0969-2126(97)00298-0
https://doi.org/10.1016/s0969-2126(97)00298-0
Autor:
Michael G. Jobling, The-tsai Chang, Leslie M. Palmer, Steve Sarfaty, Ethan A. Merritt, Wim G. J. Hol, Randall K. Holmes
Publikováno v:
Structure. 3:561-570
Background: Because agents which inhibit the receptor binding of cholera toxin constitute possible lead compounds for the structure-based design of anti-cholera drugs, detailed investigation of the toxin's receptor-binding site is of key importance.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::215796db30e4dc84a1e9eb32c74eb6ff
https://doi.org/10.1016/s0969-2126(01)00190-3
https://doi.org/10.1016/s0969-2126(01)00190-3
Autor:
Steve Sarfaty, Mario Domenighini, Ethan A. Merritt, Mariagrazia Pizza, Wim G. J. Hol, Rino Rappuoli
Publikováno v:
Nature Structural & Molecular Biology. 2:269-272
The structure of an inactive mutant, heat-labile enterotoxin raises the possibility of a direct functional role for an internal, water-filled cavity.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::039ef3455bbb0cbc3d2af4d2af40fa44
https://doi.org/10.1038/nsb0495-269
https://doi.org/10.1038/nsb0495-269
Autor:
Hidong Kim, Ethan A. Merritt, I. K. Feil, Wim G. J. Hol, Philip H. Petra, L.F. Delboni, Christophe L. M. J. Verlinde, F. van den Akker, Shekhar C. Mande, Steve Sarfaty
Publikováno v:
Protein Science. 3:1670-1686
The current rapid growth in the number of known 3-dimensional protein structures is producing a database of structures that is increasingly useful as a starting point for the development of new medically relevant molecules such as drugs, therapeutic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::302307bdf8a4148d126fd52fd3ab67c9
https://doi.org/10.1002/pro.5560031006
https://doi.org/10.1002/pro.5560031006
Publikováno v:
Protein Science. 3:166-175
Cholera toxin (CT) is an AB5 hexameric protein responsible for the symptoms produced by Vibrio cholerae infection. In the first step of cell intoxication, the B-pentamer of the toxin binds specifically to the branched pentasaccharide moiety of gangli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12bc0a320d688c8c54e8daa54d2dff6a
https://doi.org/10.1002/pro.5560030202
https://doi.org/10.1002/pro.5560030202
Publikováno v:
Protein Science. 6:913-915
Members of the family of 2-oxoacid dehydrogenase multienzyme complexes catalyze the oxidative decarboxylation of alpha-keto acids and are among the most remarkable enzymatic machineries in the living cell. These multienzyme complexes combine a highly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1f9f47d9f7a6e8cc4925de648c565fe
https://doi.org/10.1002/pro.5560060419
https://doi.org/10.1002/pro.5560060419
Autor:
Wim G. J. Hol, Ethan A. Merritt, Steve Sarfaty, Jarrod L. Erbe, Randall K. Holmes, Peter Kuhn
Publikováno v:
Journal of molecular biology. 282(5)
Crystals of the 61 kDa complex of the cholera toxin B-pentamer with the ganglioside GM1 receptor pentasaccharide diffract to near-atomic resolution. We have refined the crystallographic model for this complex using anisotropic displacement parameters
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a36707b57f414244f690c3adaf35d30
https://pubmed.ncbi.nlm.nih.gov/9753553
https://pubmed.ncbi.nlm.nih.gov/9753553
Autor:
Timothy R. Hirst, Ethan A. Merritt, Steve Sarfaty, Michael G. Jobling, T. Chang, Randall K. Holmes, Wim G. J. Hol
Publikováno v:
Protein science : a publication of the Protein Society. 6(7)
The wide range of receptor binding affinities reported to result from mutations at residue Gly 33 of the cholera toxin B-pentamer (CTB) has been most puzzling. For instance, introduction of an aspartate at this position abolishes receptor binding, wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e2e0ffe89a54e47805cfd831c8074af
https://pubmed.ncbi.nlm.nih.gov/9232653
https://pubmed.ncbi.nlm.nih.gov/9232653
Autor:
Edda M. Twiddy, Wim G. J. Hol, Steve Sarfaty, Randall K. Holmes, Terry D. Connell, Focco van den Akker
Publikováno v:
Structure (London, England : 1993). 4(6)
Background: Cholera toxin from Vibrio cholerae and the type I heat-labile enterotoxins (LT-Is) from Escherichia coli are oligomeric proteins with AB 5 structures. The type II heat-labile enterotoxins (LT-IIs) from E. coli are structurally similar to,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81aeb3c715990b1f2f5e00f829cd7fa4
https://pubmed.ncbi.nlm.nih.gov/8805549
https://pubmed.ncbi.nlm.nih.gov/8805549
Publikováno v:
Biochemistry. 34(15)
Multiple sequence alignments including the enterococcal NADH peroxidase and NADH oxidase indicate that residues Ser38 and Cys42 align with the two cysteines of the redox-active disulfides found in glutathione reductase (GR), lipoamide dehydrogenase,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ef95926fba0a37df96962fb6c32bcdd
https://pubmed.ncbi.nlm.nih.gov/7711038
https://pubmed.ncbi.nlm.nih.gov/7711038