Evidence map›Paper›PMID 26225950›Full record

ReviewMolecules (Basel, Switzerland)2015

Glycoprotein Quality Control and Endoplasmic Reticulum Stress.

Qian Wang, Jody Groenendyk, Marek Michalak

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

44 citing papers in PubMed, 83 citations in OpenAlex.

  1. High-Throughput Proteomic and Glycoproteomic Analyses in Benign Prostatic Hyperplasia.Journal of the American Society for Mass Spectrometry · 2026
    Article
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  4. Review
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  11. CaFrontiers in endocrinology · 2024
    Review
  12. Article
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  16. GANAB andInternational journal of molecular sciences · 2022
    Review
  17. Article
  18. Review
  19. Article
  20. Emerging roles of N-linked glycosylation in brain physiology and disorders.Trends in endocrinology and metabolism: TEM · 2021
    Review
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 1 institution in 1 country.

Qian WangDepartment of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada. qw7@ualberta.ca.
Jody GroenendykDepartment of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada. jlg2@ualberta.ca.
Marek MichalakDepartment of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada. marek.michalak@ualberta.ca.
University of Alberta · CA

Funding

Canadian Institutes of Health Research MOP15291
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) supports many cellular processes and performs diverse functions, including protein synthesis, translocation across the membrane, integration into the membrane, folding, and posttranslational modifications including N-linked glycosylation; and regulation of Ca2+ homeostasis. In mammalian systems, the majority of proteins synthesized by the rough ER have N-linked glycans critical for protein maturation. The N-linked glycan is used as a quality control signal in the secretory protein pathway. A series of chaperones, folding enzymes, glucosidases, and carbohydrate transferases support glycoprotein synthesis and processing. Perturbation of ER-associated functions such as disturbed ER glycoprotein quality control, protein glycosylation and protein folding results in activation of an ER stress coping response. Collectively this ER stress coping response is termed the unfolded protein response (UPR), and occurs through the activation of complex cytoplasmic and nuclear signaling pathways. Cellular and ER homeostasis depends on balanced activity of the ER protein folding, quality control, and degradation pathways; as well as management of the ER stress coping response.

Indexed as

Protein FoldingProteolysisAnimalsEndoplasmic Reticulum StressGlycoproteinsGlycosylationHumansProtein Processing, Post-TranslationalProtein TransportUnfolded Protein ResponseGlycoproteinscalnexincalreticulinchaperoneendoplasmic reticulumstress

Identifiers

PMID26225950
PMCPMC6331979
OpenAlexW1912803548

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.