Evidence map›Paper›PMID 28271482›Full record

ReviewSub-cellular biochemistry

Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction.

Henry C Nguyen, Wei Wang, Yong Xiong

Open access · greenAbstract readReview
In one paragraph

Review in Sub-cellular biochemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

52 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. 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
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The Role of CELMoD Agents in Multiple Myeloma.OncoTargets and therapy · 2025
    Review
  18. Review
  19. Ubiquitin system mutations in neurological diseases.Trends in biochemical sciences · 2024
    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 at 2 institutions in 1 country.

Henry C NguyenDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06511, USA.
Wei WangDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06511, USA.
Yong XiongDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06511, USA. yong.xiong@yale.edu.
Yale University · USUniversity of California, San Francisco · US

Funding

Multifaceted interactions between lentiviral Vif and host molecules for viral infectivity enhancementR37AI116313 · NIAID · YALE UNIVERSITY · PI Yong Xiong · 2021 to 2026
$3.2M
Recognition of Viral DNA by APOBEC3 Proteins and their Antagonization by HIV VifR01AI116313 · NIAID · YALE UNIVERSITY · PI XIONG, YONG · 2015 to 2019
$2.1M
Structural Studies of HIV Vif and Its Cellular Binding PartnersR33AI078831 · NIAID · YALE UNIVERSITY · PI XIONG, YONG · 2010 to 2012
$1.1M
Structural Studies of HIV Vif and Its Cellular Binding PartnersR21AI078831 · NIAID · YALE UNIVERSITY · PI XIONG, YONG · 2008 to 2009
$441k
NIAID NIH HHS R01 AI116313NIAID NIH HHS R21 AI078831NIAID NIH HHS R33 AI078831NIAID NIH HHS R37 AI116313
6 · The paper itself

Abstract

Ubiquitination is a highly conserved post-translational modification in eukaryotes, well known for targeting proteins for degradation by the 26S proteasome. Proteins destined for proteasomal degradation are selected by E3 ubiquitin ligases. Cullin-RING E3 ubiquitin ligases (CRLs) are the largest superfamily of E3 ubiquitin ligases, with over 400 members known in mammals. These modular complexes are tightly regulated in the cell. In this chapter, we highlight recent structural and biochemical advances shedding light on the assembly and architecture of cullin-RING ligases, their dynamic regulation by a variety of host factors, and their manipulation by viral pathogens and small molecules.

Indexed as

UbiquitinationAnimalsCullin ProteinsProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein LigasesATP dependent 26S proteaseCullin ProteinsProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein LigasesCullinCullin-RING ligaseE3 ligaseNEDD8NeddylationProtein-protein interactionUbiquitinUbiquitinationUbiquitylationViral hijacking

Identifiers

PMID28271482
PMCPMC7205596
OpenAlexW2593126736

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.