Response of a protein disulfide isomerase-like activity of transitional endoplasmic reticulum to all-trans retinol
- 21 June 1996
- journal article
- Published by Elsevier in Life Sciences
- Vol. 59 (4) , 273-284
- https://doi.org/10.1016/0024-3205(96)00296-2
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Hormone- and growth factor-stimulated NADH oxidaseJournal of Bioenergetics and Biomembranes, 1994
- Intracellular Actions of Vitamin APublished by Elsevier ,1992
- Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomeraseBiochemistry, 1991
- Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox bufferBiochemistry, 1991
- Retinoid modulation of cell-free membrane transfer between endoplasmic reticulum and Golgi apparatusBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1990
- Transition vesicles of the cis Golgi apparatus face of rat liver are increased by retinolCell Biology International Reports, 1987
- Measurement of protein using bicinchoninic acidAnalytical Biochemistry, 1985
- Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerasePublished by Elsevier ,1984
- Kinetics of refolding of reduced ribonucleaseJournal of Molecular Biology, 1977
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959