Zobrazeno 1 - 10 of 10 pro vyhledávání: '"M. A. Saper"'
1
Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase
Autor: C L, Smith, P, Khandelwal, K, Keliikuli, E R, Zuiderweg, M A, Saper
Publikováno v: Molecular microbiology. 42(4)
Pathogenic strains of Yersinia deploy a type III secretion system to inject the potent tyrosine phosphatase YopH into host cells, where it dephosphorylates focal adhesion-associated substrates. The amino-terminal, non-catalytic domain of YopH is bifu
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::eddc8d56e29ed48ee773cfe7c5585c50
https://pubmed.ncbi.nlm.nih.gov/11737640
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2
The 2.2 A crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity
Autor: J, Vijayalakshmi, M K, Mukhergee, J, Graumann, U, Jakob, M A, Saper
Publikováno v: Structure (London, England : 1993). 9(5)
One strategy that cells employ to respond to environmental stresses (temperature, oxidation, and pathogens) is to increase the expression of heat shock proteins necessary to maintain viability. Several heat shock proteins function as molecular chaper
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1c59a65add3f971c710296a2d04f777f
https://pubmed.ncbi.nlm.nih.gov/11377197
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3
Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase
Autor: Z Y, Zhang, J C, Clemens, H L, Schubert, J A, Stuckey, M W, Fischer, D M, Hume, M A, Saper, J E, Dixon
Publikováno v: The Journal of biological chemistry. 267(33)
The Yersinia protein tyrosine phosphatase (PTPase) Yop51, a C235R point mutation (Yop51*), and a protein lacking the first 162 amino acids at the NH2 terminus (Yop51*delta 162) have been overexpressed in Escherichia coli and purified to homogeneity t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5776c33aaf4fed2be0a1aaf6b035534c
https://pubmed.ncbi.nlm.nih.gov/1429715
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4
Novel tertiary structures and stereospecificities of periplasmic binding proteins involved in active transport and chemotaxis
Autor: M. A. Saper, Nand K. Vyas, J.W. Pflugrath, M.N. Vyas, Florante A. Quiocho, J. S. Sack
Publikováno v: Journal of Biosciences. 8:461-470
Binding proteins, which are located in the periplasmic space of Gram-negative bacteria, are essential components of osmotic shock-sensitive active transport systems and Chemotaxis. Described briefly herein are the high resolution molecular structures
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8b7d5a5741b7b8676df2c9a8585a8357
https://doi.org/10.1007/bf02703997
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5
Leucine, isoleucine, valine-binding protein from Escherichia coli. Structure at 3.0-A resolution and location of the binding site
Autor: F A Quiocho, M A Saper
Publikováno v: Journal of Biological Chemistry. 258:11057-11062
The structure of the leucine, isoleucine, valine-binding protein, an integral part of the high-affinity, branched-chain aliphatic amino acid transport system in Escherichia coli, has been solved at 3.0-A resolution by x-ray crystallography. Five isom
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::94fbe5a1de1e250803de3056116cc795
https://doi.org/10.1016/s0021-9258(17)44385-7
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7
Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine
Autor: J S, Sack, M A, Saper, F A, Quiocho
Publikováno v: Journal of molecular biology. 206(1)
The three-dimensional structure of the native unliganded form of the Leu/Ile/Val-binding protein (Mr = 36,700), an essential component of the high-affinity active transport system for the branched aliphatic amino acids in Escherichia coli, has been d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::50863bc938252dbcc96cbae07c00f176
https://pubmed.ncbi.nlm.nih.gov/2649682
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8
Leucine, isoleucine, valine-binding protein from Escherichia coli. Structure at 3.0-A resolution and location of the binding site
Autor: M A, Saper, F A, Quiocho
Publikováno v: The Journal of biological chemistry. 258(18)
The structure of the leucine, isoleucine, valine-binding protein, an integral part of the high-affinity, branched-chain aliphatic amino acid transport system in Escherichia coli, has been solved at 3.0-A resolution by x-ray crystallography. Five isom
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4fea79d009f8216268ca635fa2ce211f
https://pubmed.ncbi.nlm.nih.gov/6350301
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