Conformational Changes Induced in the Endoplasmic Reticulum Luminal Domain of Calnexin by Mg-ATP and Ca2+

This publication has 37 references indexed in Scilit:

• Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum.
  The Journal of cell biology, 1995
• Similarity of nucleotide interactions of BiP and GTP-binding proteins.
  Proceedings of the National Academy of Sciences, 1994
• Folding of VSV G Protein: Sequential Interaction with BiP and Calnexin
  Science, 1994
• Control of Expression, Glycosylation, and Secretion of HIV-1 gp120 by Homologous and Heterologous Signal Sequences
  Virology, 1994
• Calnexin: a membrane-bound chaperone of the endoplasmic reticulum
  Trends in Biochemical Sciences, 1994
• Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.
  Proceedings of the National Academy of Sciences, 1994
• Protein folding in the cell
  Nature, 1992
• Peptide Binding and Release by Proteins Implicated as Catalysts of Protein Assembly
  Science, 1989
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970