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Infection and Immunity|March 23, 2006
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 cytosolKen Teter, Michael G Jobling, Danielle Sentz, et al.
The Analyst|December 10, 2015
A simple and fast method to study the hydrodynamic size difference of protein disulfide isomerase in oxidized and reduced form using gold nanoparticles and dynamic light scatteringTianyu Zheng, Patrick Cherubin, Lucia Cilenti, et al.
The Journal of Biological Chemistry|June 22, 2019
HSC70 and HSP90 chaperones perform complementary roles in translocation of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosolHelen Burress, Alisha Kellner, Jessica Guyette, et al.
The Journal of Biological Chemistry|October 17, 2014
Co- and post-translocation roles for HSP90 in cholera IntoxicationHelen Burress, Michael Taylor, Tuhina Banerjee, et al.
Infection and Immunity|October 16, 2002
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 pathwayKen Teter, Rebecca L Allyn, Michael G Jobling, et al.
The Journal of Biological Chemistry|July 13, 2012
Lipid rafts alter the stability and activity of the cholera toxin A1 subunitSupriyo Ray, Michael Taylor, Tuhina Banerjee, et al.
The Journal of Biological Chemistry|May 6, 2011
Protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunitMichael Taylor, Tuhina Banerjee, Supriyo Ray, et al.
Plos One|September 3, 2011
Modulation of toxin stability by 4-phenylbutyric acid and negatively charged phospholipidsSupriyo Ray, Michael Taylor, Mansfield Burlingame, et al.
Applied and Environmental Microbiology|January 14, 2009
Novel cell-based method to detect Shiga toxin 2 from Escherichia coli O157:H7 and inhibitors of toxin activityBeatriz Quiñones, Shane Massey, Mendel Friedman, et al.
Biochemistry|November 16, 2006
The pertussis toxin S1 subunit is a thermally unstable protein susceptible to degradation by the 20S proteasomeAbhay H Pande, David Moe, Maneesha Jamnadas, et al.
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