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Reduction of protein disulfide bonds in an oxidizing environment

Data up to Jan 2025

Published1997
Citations80
References12

Total Citations Per Year

Abstract

References (12)

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Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains.

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A new multiphasic buffer system for sodium dodecyl sulfate‐polyacrylamide gel electrophoresis of proteins and peptides with molecular masses 100 000–1000, and their detection with picomolar sensitivity

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Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase.

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Zur Reaktion von Cyclopropenonen mit Azomethinen, VIII Diphenylcyclopropenon und cyclische Imine

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Reduction of protein disulfide bonds in an oxidizing environment (1997) – FEBS Letters | Metascience Observatory Explorer