Outputs (5)

Structural investigations on quinone methides for understanding their properties in confined media. (2006)
Journal Article
Szarma, R., Batsanov, A., Kataky, R., & Baruah, J. (2006). Structural investigations on quinone methides for understanding their properties in confined media. Journal of Inclusion Phenomena and Macrocyclic Chemistry, 55(1-2), 1-9. https://doi.org/10.1007/s10847-005-9001-1

Encapsulation of 4−[(4′-hydroxy−3′,5′-dimethylphenyl)(aryl)-methylene]−2,6−dimethyl-cyclohexa−2,5−dienones (when aryl=4−hydroxyphenyl 1, 4−methoxyphenyl 2, 2,3,4-trimethoxy phenyl 3) by β-cyclodextrin is studied. The compound 2 is selectively encapsu... Read More about Structural investigations on quinone methides for understanding their properties in confined media..

An introduction to thiol redox proteins in the endoplasmic reticulum and a review of current electrochemical methods of detection of thiols (2006)
Journal Article
Kruusma, J., Benham, A. M., Gareth Williams, J., & Kataky, R. (2006). An introduction to thiol redox proteins in the endoplasmic reticulum and a review of current electrochemical methods of detection of thiols. Analyst, 131(4), 459-473. https://doi.org/10.1039/b515874e

This aim of this paper is to expound the complexity of thiol redox systems in the endoplasmic reticulum of eukaryotic cells to the electroanalytical community. A summary of the state of the art in electrochemical methods for detection of thiols gives... Read More about An introduction to thiol redox proteins in the endoplasmic reticulum and a review of current electrochemical methods of detection of thiols.

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.

Recommendation for measuring and reporting chloride by ISEs in undiluted serum, plasma or blood. (2006)
Journal Article
Ben Rayana, M., Burnett, R., Covington, A., D'Orazio, P., Fogh-Andersen, N., Jacobs, E., …St John, A. (2006). Recommendation for measuring and reporting chloride by ISEs in undiluted serum, plasma or blood. Clinical Chemistry and Laboratory Medicine, 44(3), 346-352. https://doi.org/10.1515/cclm.2006.060

The proposed recommendation for measuring and reporting chloride in undiluted plasma or blood by ion-selective electrodes (ISEs) will provide results that are identical to chloride concentrations measured by coulometry for standardized normal plasma... Read More about Recommendation for measuring and reporting chloride by ISEs in undiluted serum, plasma or blood..

Expression, interactions and dynamics of the oxidoreductase Ero1Lbeta (2006)
Journal Article
Dias-Gunasekara, S., van Lith, M., Kataky, R., Williams, G., & Benham, A. (2006). Expression, interactions and dynamics of the oxidoreductase Ero1Lbeta. FASEB Journal, 20(4), https://doi.org/10.1096/fasebj.20.4.a500-c

Protein oxidation in the Endoplasmic Reticulum (ER) is catalysed by Endoplasmic reticulum oxidoreductases (EROs) that donate disulfide bonds to (and accept electrons from) Protein Disulfide Isomerase (PDI). Eros are essential for viability and protei... Read More about Expression, interactions and dynamics of the oxidoreductase Ero1Lbeta.