C. E. Jessop

The role of glutathione in disulphide bond formation and endoplasmic‐reticulum‐generated oxidative stress

N. Bulleid, S. Chakravarthi, C. E. Jessop, 2006, EMBO reports.

Oxidative protein folding in the mammalian endoplasmic reticulum.

N. Bulleid, S. Chakravarthi, C. E. Jessop, 2004, Biochemical Society transactions.

Glutathione Directly Reduces an Oxidoreductase in the Endoplasmic Reticulum of Mammalian Cells*

N. Bulleid, C. E. Jessop, 2004, Journal of Biological Chemistry.

Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins

J. J. Simmons, N. Bulleid, C. E. Jessop, 2009, Journal of Cell Science.

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.

Formation of a Major Histocompatibility Complex Class I Tapasin Disulfide Indicates a Change in Spatial Organization of the Peptide-loading Complex during Assembly*

N. Bulleid, Joseph E Chambers, C. E. Jessop, 2008, Journal of Biological Chemistry.

Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1.

N. Bulleid, C. Stirling, S. Chakravarthi, 2007, The Biochemical journal.

ERp57 is essential for efficient folding of glycoproteins sharing common structural domains

S. Lovell, N. Bulleid, G. Hämmerling, 2007, The EMBO journal.