Evidence map›Paper›PMID 23507200›Full record

ReviewBiochimica et biophysica acta2013

Orchestration of secretory protein folding by ER chaperones.

Tali Gidalevitz, Fred Stevens, Yair Argon

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
6.4field-weighted citation impact, top 3% of its field
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

85 citing papers in PubMed, 140 citations in OpenAlex.

  1. Review
  2. Article
  3. Conformational plasticity of a BiP-GRP94 chaperone complex.Nature structural & molecular biology · 2025
    Article
  4. Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  5. Review
  6. Structural Homology Fails to Predict Secretion Efficiency inInternational journal of molecular sciences · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Defective Thyroglobulin: Cell Biology of Disease.International journal of molecular sciences · 2022
    Review
  18. Article
  19. Review
  20. Article

25 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 at 3 institutions in 1 country.

Tali GidalevitzDepartment of Biology, Drexel University, Philadelphia, PA 19104, USA.
Fred Stevens
Yair Argon
Argonne National Laboratory · USChildren's Hospital of Philadelphia · USDrexel University · US

Funding

TRAINING GRANT IN GENETICST32GM007748 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Anne O'Donnell-Luria, Louise Wilkins-Haug · 1985 to 2026
$12.0M
Regulation of IGF Levels in Development and in AgingR01AG018001 · NIA · UNIVERSITY OF CHICAGO · PI ARGON, YAIR · 2000 to 2016
$5.9M
Regulation of insulin-like growth factors by the ER chaperone GRP94R01GM077480 · NIGMS · CHILDREN'S HOSP OF PHILADELPHIA · PI ARGON, YAIR · 2010 to 2013
$1.3M
NIA NIH HHS AG18001NIA NIH HHS R01 AG018001NIGMS NIH HHS GM07748NIGMS NIH HHS R01 GM077480NIGMS NIH HHS T32 GM007748
6 · The paper itself

Abstract

The endoplasmic reticulum is a major compartment of protein biogenesis in the cell, dedicated to production of secretory, membrane and organelle proteins. The secretome has distinct structural and post-translational characteristics, since folding in the ER occurs in an environment that is distinct in terms of its ionic composition, dynamics and requirements for quality control. The folding machinery in the ER therefore includes chaperones and folding enzymes that introduce, monitor and react to disulfide bonds, glycans, and fluctuations of luminal calcium. We describe the major chaperone networks in the lumen and discuss how they have distinct modes of operation that enable cells to accomplish highly efficient production of the secretome. This article is part of a Special Issue entitled: Functional and structural diversity of endoplasmic reticulum.

Indexed as

Molecular ChaperonesProtein FoldingProtein Processing, Post-TranslationalAnimalsEndoplasmic ReticulumHumansProtein BiosynthesisProteinsProtein TransportMolecular ChaperonesProteinsChaperonesEndoplasmic reticulumProtein foldingSecretome

Identifiers

PMID23507200
PMCPMC3729627
OpenAlexW1975334062

What OpenQuestion holds

Textmetadata
LicenceTDM
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.