Timothy J. Tavender

发表

Substrate Specificity of the Oxidoreductase ERp57 Is Determined Primarily by Its Interaction with Calnexin and Calreticulin*

N. Bulleid, Joseph E Chambers, C. E. Jessop, 2009, Journal of Biological Chemistry.

Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum

N. Bulleid, Jennifer J Springate, Timothy J. Tavender, 2010, The EMBO journal.

Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation

N. Bulleid, Timothy J. Tavender, 2010, Journal of Cell Science.

Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum.

N. Bulleid, Timothy J. Tavender, 2010, Antioxidants & redox signaling.

The Reduction Potential of the Active Site Disulfides of Human Protein Disulfide Isomerase Limits Oxidation of the Enzyme by Ero1α*

N. Bulleid, David Knight, Stacey Warwood, 2010, The Journal of Biological Chemistry.

Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells.

N. Bulleid, Timothy J. Tavender, Alyson M Sheppard, 2008, The Biochemical journal.

Crystal Structure of Reduced and of Oxidized Peroxiredoxin IV Enzyme Reveals a Stable Oxidized Decamer and a Non-disulfide-bonded Intermediate in the Catalytic Cycle

R. Cogdell, A. Roszak, Zhenbo Cao, 2011, The Journal of Biological Chemistry.

LuxS-independent formation of AI-2 from ribulose-5-phosphate

K. Winzer, K. Hardie, N. Halliday, 2008, BMC Microbiology.

AI-2 does not function as a quorum sensing molecule in Campylobacter jejuni during exponential growth in vitro

K. Winzer, K. Hardie, J. Wells, 2009, BMC Microbiology.