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Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells.

Data up to Jan 2025

Published1995
Citations112
References22

Total Citations Per Year

Abstract

References (22)

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IpaB of Shigella flexneri causes entry into epithelial cells and escape from the phagocytic vacuole.

1992 • 316 citations

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1994 • 298 citations

MxiD, an outer membrane protein necessary for the secretion of the Shigella flexneri Ipa invasins

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1992 • 228 citations

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1994 • 213 citations

Surface presentation of Shigella flexneri invasion plasmid antigens requires the products of the spa locus

1992 • 183 citations

Protein folding in the periplasm of Escherichia coli

1994 • 175 citations

MxiJ, a lipoprotein involved in secretion of Shigella Ipa invasins, is homologous to YscJ, a secretion factor of the Yersinia Yop proteins

1992 • 172 citations

Eight genes in region 5 that form an operon are essential for invasion of epithelial cells by Shigella flexneri 2a

1993 • 140 citations

Two novel virulence loci, mxiA and mxiB, in Shigella flexneri 2a facilitate excretion of invasion plasmid antigens

1991 • 137 citations

A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae

1992 • 130 citations

In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product.

1992 • 127 citations

mxiA of Shigella flexneri 2a, which facilitates export of invasion plasmid antigens, encodes a homolog of the low-calcium-response protein, LcrD, of Yersinia pestis

1992 • 122 citations

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Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa… (1995) – Proceedings of the National Academy of Sciences | Metascience Observatory Explorer