Title : In vitro unfolding of retinol-binding protein by dithiothreitol. Endoplasmic reticulum-associated factors.

Pub. Date : 1993 Oct 15

PMID : 8408081






3 Functional Relationships(s)
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1 Protein disulfide isomerase is likely to be one such factor since it enhances the rate of RBP unfolding by DTT in vitro; protein disulfide isomerase-induced unfolding requires the absence of retinoids, similar to the DTT-induced unfolding in vivo. Dithiothreitol prolyl 4-hydroxylase subunit beta Homo sapiens
2 Protein disulfide isomerase is likely to be one such factor since it enhances the rate of RBP unfolding by DTT in vitro; protein disulfide isomerase-induced unfolding requires the absence of retinoids, similar to the DTT-induced unfolding in vivo. Dithiothreitol prolyl 4-hydroxylase subunit beta Homo sapiens
3 Protein disulfide isomerase is likely to be one such factor since it enhances the rate of RBP unfolding by DTT in vitro; protein disulfide isomerase-induced unfolding requires the absence of retinoids, similar to the DTT-induced unfolding in vivo. Dithiothreitol prolyl 4-hydroxylase subunit beta Homo sapiens