(Q27648943)

1

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Laurie Betts

2

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James G Smedley

3

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Bruce A McClane

4

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James M Anderson

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

4 January 2008

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published in

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volume

283

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issue

1

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page(s)

268-74

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cites work

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Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo

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Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: Evidence for direct involvement of claudins in tight junction barrier.

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CaCo-2 cells treated with Clostridium perfringens enterotoxin form multiple large complex species, one of which contains the tight junction protein occludin

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Prevalence of hepatitis G virus among intravenous drug abusers in Los Angeles

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A novel strategy for the enhancement of drug absorption using a claudin modulator

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Claudin proteins in human cancer: promising new targets for diagnosis and therapy

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Claudin-4: a new target for pancreatic cancer treatment using Clostridium perfringens enterotoxin.

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Treatment of chemotherapy-resistant human ovarian cancer xenografts in C.B-17/SCID mice by intraperitoneal administration of Clostridium perfringens enterotoxin

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Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases

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Substructure solution with SHELXD

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Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein

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A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation

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Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications

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Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex

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Tocopherol-binding proteins: their function and physiological significance

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N-acetylgalactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin

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Role of receptors in Bacillus thuringiensis crystal toxin activity

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