Evidence map›Paper›PMID 35247748›Full record

ReviewCurrent opinion in structural biology2022

Site-specific ubiquitination: Deconstructing the degradation tag.

Emma C Carroll, Susan Marqusee

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. The role of ubiquitin-conjugating enzyme in the process of spermatogenesis.Reproductive biology and endocrinology : RB&E · 2024
    Review
  10. Review
  11. Article
  12. Review
  13. Dysregulated proteostasis network in neuronal diseases.Frontiers in cell and developmental biology · 2023
    Review
  14. Article
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

2 authors at 2 institutions in 1 country.

Emma C CarrollInstitute for Neurodegenerative Diseases, University of California, San Francisco, San Francisco, CA, 94038, USA. Electronic address: emma.carroll@ucsf.edu.
Susan MarquseeDepartment of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA, 94720, USA; QB3 Institute for Quantitative Biosciences, University of California Berkeley, Berkeley, CA, 94720, USA; Department of Chemistry, University of California Berkeley, Berkeley, CA, 94720, USA. Electronic address: marqusee@berkeley.edu.
QB3 · USUniversity of California, San Francisco · US

Funding

Sequence and Environmental Determinants of the Protein Energy LandscapeR01GM050945 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI MARQUSEE, SUSAN · 1999 to 2022
$7.4M
NIGMS NIH HHS R01 GM050945
6 · The paper itself

Abstract

Ubiquitin is a small eukaryotic protein so named for its cellular abundance and originally recognized for its role as the posttranslational modification (PTM) "tag" condemning substrates to degradation by the 26S proteasome. Since its discovery in the 1970s, protein ubiquitination has also been identified as a key regulatory feature in dozens of non-degradative cellular processes. This myriad of roles illustrates the versatility of ubiquitin as a PTM; however, understanding the cellular and molecular factors that enable discrimination between degradative versus non-degradative ubiquitination events has been a persistent challenge. Here, we discuss recent advances in uncovering how site-specificity - the exact residue that gets modified - modulates distinct protein fates and cellular outcomes with an emphasis on how ubiquitination site specificity regulates proteasomal degradation. We explore recent advances in structural biology, biophysics, and cell biology that have enabled a broader understanding of the role of ubiquitination in altering the dynamics of the target protein, including implications for the design of targeted protein degradation therapeutics.

Indexed as

Proteasome Endopeptidase ComplexUbiquitinProtein Processing, Post-TranslationalProteinsProteolysisUbiquitinationProteasome Endopeptidase ComplexProteinsUbiquitin

Identifiers

PMID35247748
PMCPMC9208700
OpenAlexW4214878221

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.