Oxidoreductase Interactions Include a Role for ERp72 Engagement with Mutant Thyroglobulin from the rdw/rdw Rat Dwarf

This publication has 53 references indexed in Scilit:

• Protein disulfide isomerase–like proteins play opposing roles during retrotranslocation
  The Journal of cell biology, 2006
• From acute ER stress to physiological roles of the Unfolded Protein Response
  Cell Death & Differentiation, 2006
• Versatility of the Endoplasmic Reticulum Protein Folding Factory
  Critical Reviews in Biochemistry and Molecular Biology, 2005
• The Acetylcholinesterase Homology Region Is Essential for Normal Conformational Maturation and Secretion of Thyroglobulin
  Journal of Biological Chemistry, 2004
• Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
  Nature, 2002
• Linkage analysis identifies the thyroglobulin gene region as a major locus for familial congenital hypothyroidism
  Human Genetics, 2002
• Endoplasmic Reticulum (ER)-associated Degradation of Misfolded N-Linked Glycoproteins Is Suppressed upon Inhibition of ER Mannosidase I
  Journal of Biological Chemistry, 2000
• Graves-Basedow Disease Goiter: A Model of Bax-Bcl2 Regulated Apoptosis
  Thyroid®, 1999
• Enhanced Binding to the Molecular Chaperone BiP Slows Thyroglobulin Export from the Endoplasmic Reticulum
  Molecular Endocrinology, 1998
• Two resident ER‐proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase
  FEBS Letters, 1995