Ken Teter

The cholera toxin A1(3) subdomain is essential for interaction with ADP-ribosylation factor 6 and full toxic activity but is not required for translocation from the endoplasmic reticulum to the cytosol.

Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathway.

Inhibition of endoplasmic reticulum-associated degradation in CHO cells resistant to cholera toxin, Pseudomonas aeruginosa exotoxin A, and ricin.

A class of mutant CHO cells resistant to cholera toxin rapidly degrades the catalytic polypeptide of cholera toxin and exhibits increased endoplasmic reticulum-associated degradation.

Characterization of mammalian Ecm29, a 26 S proteasome-associated protein that localizes to the nucleus and membrane vesicles.

Vesicular transport is not required for the cytoplasmic pool of cholera toxin to interact with the stimulatory alpha subunit of the heterotrimeric g protein.

Cellular internalization of cytolethal distending toxin: a new end to a known pathway.

The pertussis toxin S1 subunit is a thermally unstable protein susceptible to degradation by the 20S proteasome.

Pet, a non-AB toxin, is transported and translocated into epithelial cells by a retrograde trafficking pathway.

Lipopolyamine treatment increases the efficacy of intoxication with saporin and an anticancer saporin conjugate.

Conformational instability of the cholera toxin A1 polypeptide.

Structural characteristics of the plasmid-encoded toxin from enteroaggregative Escherichia coli.

A novel mode of translocation for cytolethal distending toxin.

Novel cell-based method to detect Shiga toxin 2 from Escherichia coli O157:H7 and inhibitors of toxin activity.

Stabilization of the tertiary structure of the cholera toxin A1 subunit inhibits toxin dislocation and cellular intoxication.

A host-specific factor is necessary for efficient folding of the autotransporter plasmid-encoded toxin.

Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol.

Contribution of subdomain structure to the thermal stability of the cholera toxin A1 subunit.

Identification of molecular-mimicry-based ligands for cholera diagnostics using magnetic relaxation.

Host-Toxin Interactions Involving EspC and Pet, Two Serine Protease Autotransporters of the Enterobacteriaceae.

A therapeutic chemical chaperone inhibits cholera intoxication and unfolding/translocation of the cholera toxin A1 subunit.

Protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit.

A cell-based fluorescent assay to detect the activity of Shiga toxin and other toxins that inhibit protein synthesis.

Structural and functional interactions between the cholera toxin A1 subunit and ERdj3/HEDJ, a chaperone of the endoplasmic reticulum.

Modulation of toxin stability by 4-phenylbutyric acid and negatively charged phospholipids.