Evidence map›Paper›PMID 31004255›Full record

ReviewThe protein journal2019

Protein Quality Control in the Endoplasmic Reticulum.

Benjamin M Adams, Michela E Oster, Daniel N Hebert

Abstract readReview
In one paragraph

Review in The protein journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

72 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The murine MHC-E molecule Qa-1Frontiers in immunology · 2026
    Article
  7. Review
  8. Journal of proteome research · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Insights into the interaction between UGGT, the gatekeeper of folding in the ER, and its partner, the selenoprotein SEP15.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Benjamin M AdamsDepartment of Biochemistry and Molecular Biology, University of Massachusetts, 240 Thatcher Road, Amherst, MA, 01003, USA.
Michela E OsterDepartment of Biochemistry and Molecular Biology, University of Massachusetts, 240 Thatcher Road, Amherst, MA, 01003, USA.
Daniel N HebertDepartment of Biochemistry and Molecular Biology, University of Massachusetts, 240 Thatcher Road, Amherst, MA, 01003, USA. dhebert@biochem.umass.edu.ORCID 0000-0003-1537-4446

Funding

Cellular protein maturation and degradationR01GM086874 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI RAUCH, JENNIFER NICOLE · 2009 to 2025
$4.5M
CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
NIGMS NIH HHS GM086874NIGMS NIH HHS R01 GM086874NIGMS NIH HHS T32 GM008515NIH HHS GM008515
6 · The paper itself

Abstract

The site of protein folding and maturation for the majority of proteins that are secreted, localized to the plasma membrane or targeted to endomembrane compartments is the endoplasmic reticulum (ER). It is essential that proteins targeted to the ER are properly folded in order to carry out their function, as well as maintain protein homeostasis, as accumulation of misfolded proteins could lead to the formation of cytotoxic aggregates. Because protein folding is an error-prone process, the ER contains protein quality control networks that act to optimize proper folding and trafficking of client proteins. If a protein is unable to reach its native state, it is targeted for ER retention and subsequent degradation. The protein quality control networks of the ER that oversee this evaluation or interrogation process that decides the fate of maturing nascent chains is comprised of three general types of families: the classical chaperones, the carbohydrate-dependent system, and the thiol-dependent system. The cooperative action of these families promotes protein quality control and protein homeostasis in the ER. This review will describe the families of the ER protein quality control network and discuss the functions of individual members.

Indexed as

Endoplasmic ReticulumEukaryotic CellsGlycosylationMolecular ChaperonesProtein FoldingSecretory PathwayMolecular ChaperonesEndoplasmic reticulumMolecular chaperonesN-linked glycosylationOxidoreductasesQuality controlSecretory pathway

Identifiers

PMID31004255
PMCPMC6589386

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.