Evidence map›Paper›PMID 31414713›Full record

ReviewAnnals of the New York Academy of Sciences2020

The E3 ubiquitin ligase CHIP in normal cell function and in disease conditions.

Tingyu Wang, Wenbo Wang, Qishan Wang, Rong Xie, Alan Landay, Di Chen

Open access · greenAbstract readReview
In one paragraph

Review in Annals of the New York Academy of Sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

43 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. The Ubiquitin-Proteasome System in Brain Disorders: Pathogenic Pathways, Post-Translational Tweaks, and Therapeutic Frontiers.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2025
    Review
  10. Article
  11. Ubiquitin E3 Ligases and p53 in Doxorubicin-Induced Cardiotoxicity.International journal of molecular sciences · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
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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

6 authors at 2 institutions in 2 countries.

Tingyu WangDepartment of Orthopedic Surgery, Rush University Medical Center, Chicago, Illinois.
Wenbo WangDepartment of Orthopedic Surgery, Rush University Medical Center, Chicago, Illinois.
Qishan WangDepartment of Pharmacy, Shanghai Ninth People's Hospital, Shanghai JiaoTong University School of Medicine, Shanghai, China.
Rong XieDepartment of Orthopedic Surgery, Rush University Medical Center, Chicago, Illinois.
Alan LandayDepartment of Microbial Pathogens and Immunity, Rush University Medical Center, Chicago, Illinois.
Di ChenDepartment of Orthopedic Surgery, Rush University Medical Center, Chicago, Illinois.
Rush University Medical Center · USShanghai Jiao Tong University · CN

Funding

The Mechanism through which TGF-Beta Maintains Chondrocytes in Proliferating StagR01AR054465 · NIAMS · UNIVERSITY OF ROCHESTER · PI CHEN, DI · 2007 to 2018
$2.7M
The Role of MicroRNA in Osteoarthritis: Alzheimer's Administrative SupplementR01AR070222 · NIAMS · RUSH UNIVERSITY MEDICAL CENTER · PI HUANG, JIAN, ZHAO, LAN · 2017 to 2022
$2.1M
Beta-Catenin Signaling and Pathogenesis of OsteoarthritisR01AR055915 · NIAMS · UNIVERSITY OF ROCHESTER · PI CHEN, DI · 2009 to 2013
$1.7M
National Natural Science Foundation of China 81301531National Natural Science Foundation of China 81572104National Natural Science Foundation of China 81874011NIAMS NIH HHS R01 AR054465NIAMS NIH HHS R01 AR055915NIAMS NIH HHS R01 AR070222NIH HHS R01AR054465NIH HHS R01AR070222
6 · The paper itself

Abstract

In eukaryotic cells, ubiquitination and proteasomal degradation is an essential mechanism for regulating protein functions. For example, critical signaling proteins play their roles by controlling different cellular functions. Once a signaling protein has been activated, its activity needs to be quickly downregulated by different mechanisms, including ubiquitination/proteasome regulation. Failure to regulate the activity or expression levels of these proteins may cause human diseases. Protein ubiquitination involves a cascade of biochemical processes and requires three types of ubiquitin enzymes: E1 activating enzyme, E2 conjugating enzyme, and E3 ligase. Among these enzymes, E3 ubiquitin ligases play a specific role in recognizing specific protein substrates. There are several structurally diverse groups of E3 ubiquitin ligases in eukaryotic cells, and one type of these E3 ligases is the U-box ubiquitin ligases. Carboxyl terminus of HSP70-interacting protein (CHIP) is a member of a family of U-box E3 ligases. It plays critical roles in multiple organs and tissues in the body. In this review article, we provide an update on some of the most recent discoveries about CHIP in normal physiological function and in disease.

Indexed as

DiseaseAgingCellsHumansImmunityInflammationUbiquitin-Protein LigasesUbiquitin-Protein Ligasesbone remodelingcarboxyl terminus of HSP70-interacting protein (CHIP)immunityinflammationneurodegenerative diseases

Identifiers

PMID31414713
PMCPMC6992472
OpenAlexW2969139018

What OpenQuestion holds

Textmetadata
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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.