Synapse
⌘+K
Synapse
PulseExploreClubsResearchersJournals
Instagram
HomeClubsExplore
February 1, 1999Journal of Biological ChemistryOpen Access

The Requirement for Molecular Chaperones during Endoplasmic Reticulum-associated Protein Degradation Demonstrates That Protein Export and Import Are Mechanistically Distinct

View Full Paper
Ask AI
Bookmark
Share

Authors

JBJeffrey L. BrodskyUniversity of PittsburghEWEric D. WernerHarvard UniversityMDMaria E. Dubas

Discussion

Loading...

Member takes

Overview

Key Points

Key points are not available for this paper at this time.

Cite This Study

Brodsky et al. (1999) studied this question.

synapsesocial.com/papers/6a71b05db27f15817827d3cbhttps://doi.org/10.1074/jbc.274.6.3453
View Full Paper
Ask AI
Bookmark
Share

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Complex Interactions Among Members of an Essential Subfamily of hsp70 Genes in Saccharomyces Cerevisiae1987 · 359 citations
  2. 2Association between calnexin and a secretion-incompetent variant of human alpha 1-antitrypsin.1994 · 113 citations
  3. 3Protein quality control: triage by chaperones and proteases.1997 · 552 citations
  4. 4Calnexin and Other Factors That Alter Translocation Affect the Rapid Binding of Ubiquitin to ApoB in the Sec61 Complex1998 · 95 citations
  5. 5Der3p/Hrd1p Is Required for Endoplasmic Reticulum-associated Degradation of Misfolded Lumenal and Integral Membrane Proteins1998 · 382 citations