Is protein disulfide isomerase a redox-dependent molecular chaperone?

Protein disulfide isomerase (PDI) is a multifunctional protein catalysing the formation of disulfide bonds, acting as a molecular chaperone and being a component of the enzymes prolyl 4‐hydroxylase (P4H) and microsomal triglyceride transfer protein. The role of PDI as a molecular chaperone or polype...

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Veröffentlicht in:	The EMBO journal 2002-12, Vol.21 (24), p.6763-6770
Hauptverfasser:	Lumb, Richard A., Bulleid, Neil J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Catalysis Cell Line Cross-Linking Reagents - pharmacology Disulfides Endoplasmic Reticulum - metabolism glutathione Glutathione - metabolism Humans molecular chaperone Molecular Chaperones - metabolism Oxidation-Reduction Oxidizing agents Peptides - chemistry Precipitin Tests procollagen Procollagen - chemistry Procollagen-Proline Dioxygenase - metabolism prolyl 4-hydroxylase Protein Binding Protein Biosynthesis Protein Conformation protein disulfide isomerase Protein Disulfide-Isomerases - metabolism Protein Disulfide-Isomerases - physiology Protein Folding Protein Structure, Tertiary Recombinant Proteins - metabolism Transcription, Genetic
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