Dissociation from BiP and Retrotranslocation of Unassembled Immunoglobulin Light Chains Are Tightly Coupled to Proteasome Activity

Míreanna Comhchosúla

• Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release.
  le: Knittler, M R, et al.
  Foilsithe: (1992)
• BiP and Immunoglobulin Light Chain Cooperate to Control the Folding of Heavy Chain and Ensure the Fidelity of Immunoglobulin Assembly
  le: Lee, Young-Kwang, et al.
  Foilsithe: (1999)
• The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP
  le: Skowronek, Markus H., et al.
  Foilsithe: (1998)
• Intracellular dissociation and reassembly of prolyl 4-hydroxylase:the alpha-subunits associated with the immunoglobulin-heavy-chain binding protein (BiP) allowing reassembly with the beta-subunit.
  le: John, D C, et al.
  Foilsithe: (1996)
• Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum.
  le: Knittler, M R, et al.
  Foilsithe: (1995)