Výsledky vyhledávání - "W. I. Lencer"

Entry of protein toxins into mammalian cells by crossing the endoplasmic reticulum membrane: co-opting basic mechanisms of endoplasmic reticulum-associated degradation

Autor: J M, Lord, L M, Roberts, W I, Lencer

Publikováno v: Current topics in microbiology and immunology. 300

The catalytic polypeptides of certain bacterial and plant protein toxins reach their substrates in the cytosol of mammalian cells by retro-translocation from the endoplasmic reticulum (ER). Emerging evidence indicates that these proteins subvert the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8830dfee3f96b17b3f8a727240505a92
https://pubmed.ncbi.nlm.nih.gov/16573240

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Microbes and microbial Toxins: paradigms for microbial-mucosal toxins. V. Cholera: invasion of the intestinal epithelial barrier by a stably folded protein toxin

Autor: W I, Lencer

Publikováno v: American journal of physiology. Gastrointestinal and liver physiology. 280(5)

Cholera toxin (CT) produced by Vibrio cholerae is the virulence factor responsible for the massive secretory diarrhea seen in Asiatic cholera. To cause disease, CT enters the intestinal epithelial cell as a stably folded protein by co-opting a lipid-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b26f97881f45a5dd368bbe1c276e2f9a
https://pubmed.ncbi.nlm.nih.gov/11292584

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Microbial invasion across the intestinal epithelial barrier

Autor: W I, Lencer

Publikováno v: Pediatric research. 49(1)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ee924bdf993cda6bf6600069e834215d
https://pubmed.ncbi.nlm.nih.gov/11134488

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Differential activity of cholera toxin and E. coli enterotoxin: construction and purification of mutant and hybrid derivatives

Autor: C, Rodighiero, A T, Aman, W I, Lencer, T R, Hirst

Publikováno v: Biochemical Society transactions. 26(4)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2457404334d2cd20e0eca40c55af1df4
https://pubmed.ncbi.nlm.nih.gov/10047878

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Structural basis for the differential toxicity of cholera toxin and Escherichia coli heat-labile enterotoxin. Construction of hybrid toxins identifies the A2-domain as the determinant of differential toxicity

Autor: C, Rodighiero, A T, Aman, M J, Kenny, J, Moss, W I, Lencer, T R, Hirst

Publikováno v: The Journal of biological chemistry. 274(7)

Cholera toxin (Ctx) and E. coli heat-labile enterotoxin (Etx) are structurally and functionally similar AB5 toxins with over 80% sequence identity. When their action in polarized human epithelial (T84) cells was monitored by measuring toxin-induced C

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a5607d170dedc0e056b13529013326bf
https://pubmed.ncbi.nlm.nih.gov/9933586

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Proteolytic activation of cholera toxin and Escherichia coli labile toxin by entry into host epithelial cells. Signal transduction by a protease-resistant toxin variant

Autor: W I, Lencer, C, Constable, S, Moe, P A, Rufo, A, Wolf, M G, Jobling, S P, Ruston, J L, Madara, R K, Holmes, T R, Hirst

Publikováno v: The Journal of biological chemistry. 272(24)

Cholera and Escherichia coli heat-labile toxins (CT and LT) require proteolysis of a peptide loop connecting two major domains of their enzymatic A subunits for maximal activity (termed "nicking"). To test whether host intestinal epithelial cells may

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e1db96271abd0fed0fc4821fe83f532c
https://pubmed.ncbi.nlm.nih.gov/9182593

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Carboxy-terminal vesicular stomatitis virus G protein-tagged intestinal Na+-dependent glucose cotransporter (SGLT1): maintenance of surface expression and global transport function with selective perturbation of transport kinetics and polarized expression

Autor: J R, Turner, W I, Lencer, S, Carlson, J L, Madara

Publikováno v: The Journal of biological chemistry. 271(13)

The Na+-dependent glucose transporter (SGLT1) mediates absorption of luminal glucose by the intestine. However, available intestinal cell lines that recapitulate a monolayer phenotype only express SGLT1 at low levels. Thus, to facilitate studies of t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::66507db173a677e6ba04e423aca718b5
https://pubmed.ncbi.nlm.nih.gov/8631815

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The A2b adenosine receptor mediates cAMP responses to adenosine receptor agonists in human intestinal epithelia

Autor: G R, Strohmeier, S M, Reppert, W I, Lencer, J L, Madara

Publikováno v: The Journal of biological chemistry. 270(5)

Adenosine is thought to be a major effector in immunological stimulation of Cl- secretion in intestinal epithelia. Previous studies indicate that both apical and basolateral domains of intestinal epithelial cells possess functionally defined adenosin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::74c233e0e8fb42ed1f74ec320404cad4
https://pubmed.ncbi.nlm.nih.gov/7836474

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[Characterization of proton pump and osmotic water transport in endocytic vesicles from rat kidney proximal tubule]

Autor: L B, Shi, R G, Ye, W I, Lencer, A S, Verkman

Publikováno v: Sheng li xue bao : [Acta physiologica Sinica]. 42(2)

The characteristics of ATP-driven proton and osmotic water transport were studied in endocytic vesicles isolated from rat kidney proximal tubule labelled in vivo with fluorescein isothiocyanate-dextran (FITC-dextran). ATP-driven proton transport was

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::248b0a27780a0ae53bd559e0803eee64
https://pubmed.ncbi.nlm.nih.gov/2142810

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