Evidence map›Paper›PMID 30282948›Full record

ReviewInternational journal of molecular sciences2018

Protein Quality Control in the Endoplasmic Reticulum and Cancer.

Hye Won Moon, Hye Gyeong Han, Young Joo Jeon

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Article
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  4. Review
  5. Article
  6. Review
  7. Cellular Landscape of Synovial Chondromatosis Synovium Revealed by Single-Cell RNA Sequencing.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. An Overview of Adverse Outcome Pathway Links between PMEnvironment & health (Washington, D.C.) · 2024
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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.

Hye Won MoonDepartment of Biochemistry, Chungnam National University College of Medicine, Daejeon 35015, Korea. ansdj831@naver.com.
Hye Gyeong HanDepartment of Biochemistry, Chungnam National University College of Medicine, Daejeon 35015, Korea. hanhk0123@naver.com.
Young Joo JeonDepartment of Biochemistry, Chungnam National University College of Medicine, Daejeon 35015, Korea. yjjeon@cnu.ac.kr.ORCID 0000-0003-1004-5336

Funding

National Research Foundation of Korea NRF-2016R1A2B4006566
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is an essential compartment of the biosynthesis, folding, assembly, and trafficking of secretory and transmembrane proteins, and consequently, eukaryotic cells possess specialized machineries to ensure that the ER enables the proteins to acquire adequate folding and maturation for maintaining protein homeostasis, a process which is termed proteostasis. However, a large variety of physiological and pathological perturbations lead to the accumulation of misfolded proteins in the ER, which is referred to as ER stress. To resolve ER stress and restore proteostasis, cells have evolutionary conserved protein quality-control machineries of the ER, consisting of the unfolded protein response (UPR) of the ER, ER-associated degradation (ERAD), and autophagy. Furthermore, protein quality-control machineries of the ER play pivotal roles in the control of differentiation, progression of cell cycle, inflammation, immunity, and aging. Therefore, severe and non-resolvable ER stress is closely associated with tumor development, aggressiveness, and response to therapies for cancer. In this review, we highlight current knowledge in the molecular understanding and physiological relevance of protein quality control of the ER and discuss new insights into how protein quality control of the ER is implicated in the pathogenesis of cancer, which could contribute to therapeutic intervention in cancer.

Indexed as

Protein Processing, Post-TranslationalAnimalsAutophagyEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationEndoplasmic Reticulum StressHumansNeoplasmsProtein FoldingProtein TransportUnfolded Protein Responsecancerendoplasmic reticulum (ER) stressER-associated protein degradation (ERAD), autophagyprotein quality controlproteostasisunfolded protein response (UPR) of the ER

Identifiers

PMID30282948
PMCPMC6213883

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.