Platinum(II) Complexes of N^C^N‑Coordinating 1,3-Bis(2-pyridyl)benzene Ligands: Thiolate Coligands Lead to Strong Red Luminescence from Charge-Transfer States (2014)
Journal Article
Tarran, W., Freeman, G., Murphy, L., Benham, A., Kataky, R., & Williams, J. (2014). Platinum(II) Complexes of N^C^N‑Coordinating 1,3-Bis(2-pyridyl)benzene Ligands: Thiolate Coligands Lead to Strong Red Luminescence from Charge-Transfer States. Inorganic Chemistry, 53(11), 5738-5749. https://doi.org/10.1021/ic500555w

A new family of platinum(II) complexes of the form PtLnSR have been prepared, where Ln represents a cyclometalating, NCN-bound tridentate ligand and SR is a monodentate thiolate ligand. The complexes fall into two groups, those of PtL1SR where HL1 =... Read More about Platinum(II) Complexes of N^C^N‑Coordinating 1,3-Bis(2-pyridyl)benzene Ligands: Thiolate Coligands Lead to Strong Red Luminescence from Charge-Transfer States.

Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1b (2006)
Journal Article
Dias-Gunasekara, S., van Lith, M., Williams, J., Kataky, R., & Benham, A. (2006). Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1b. Journal of Biological Chemistry, 281(35), 25018-25025. https://doi.org/10.1074/jbc.m602354200

Disulfide bond catalysis is an essential component of protein biogenesis in the secretory pathway, from yeast through to man. In the endoplasmic reticulum (ER), protein-disulfide isomerase (PDI) catalyzes the oxidation and isomerization of disulfide... Read More about Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1b.

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.