Professor Adam Benham's Outputs (2)

Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb (2005)
Journal Article
Dias-Gunasekara, S., Gubbens, J., van Lith, M., Dunne, C., Williams, J., Kataky, R., …Benham, A. (2005). Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb. Journal of Biological Chemistry, 280(38), 33066-33075. https://doi.org/10.1074/jbc.m505023200

Endoplasmic reticulum oxidoreductases (Eros) are essential for the formation of disulfide bonds. Understanding disulfide bond catalysis in mammals is important because of the involvement of protein misfolding in conditions such as diabetes, arthritis... Read More about Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb.

PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum (2005)
Journal Article
van Lith, M., Hartigan, N., Hatch, J., & Benham, A. (2005). PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum. Journal of Biological Chemistry, 280(2), 1376-1383. https://doi.org/10.1074/jbc.m408651200

Protein disulfide isomerase (PDI) is the archetypal enzyme involved in the formation and reshuffling of disulfide bonds in the endoplasmic reticulum (ER). PDI achieves its redox function through two highly conserved thioredoxin domains, and PDI can a... Read More about PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.