Evidence map›Paper›PMID 27012468›Full record

ReviewCell research2016

Substrate specificity of the ubiquitin and Ubl proteases.

Judith A Ronau, John F Beckmann, Mark Hochstrasser

Open access · hybridAbstract readReview
In one paragraph

Review in Cell research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

74 citing papers in PubMed, 127 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

14 more citing papers are in PubMed but not listed here.

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.

Judith A RonauDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA.
John F BeckmannDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA.
Mark HochstrasserDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA.
Yale University · USWhitney Museum of American Art · US

Funding

FUNCTIONS AND MECHANISMS OF DEUBIQUITINATING ENZYMESR01GM053756 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 1996 to 2019
$6.5M
Function and Assembly of Eukaryotic ProteasomesR01GM083050 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 2008 to 2019
$3.8M
Degradation of Short Lived Regulatory Protein in YeastR37GM046904 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 2009 to 2018
$3.6M
DEGRADTION OF SHORT-LIVED REGULATORY PROTEINS IN YEASTR01GM046904 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 1992 to 2020
$3.6M
NIGMS NIH HHS GM046904NIGMS NIH HHS GM053756NIGMS NIH HHS GM083050NIGMS NIH HHS R01 GM046904NIGMS NIH HHS R01 GM053756NIGMS NIH HHS R01 GM083050NIGMS NIH HHS R37 GM046904
6 · The paper itself

Abstract

Conjugation and deconjugation of ubiquitin and ubiquitin-like proteins (Ubls) to cellular proteins are highly regulated processes integral to cellular homeostasis. Most often, the C-termini of these small polypeptides are attached to lysine side chains of target proteins by an amide (isopeptide) linkage. Deubiquitinating enzymes (DUBs) and Ubl-specific proteases (ULPs) comprise a diverse group of proteases that recognize and remove ubiquitin and Ubls from their substrates. How DUBs and ULPs distinguish among different modifiers, or different polymeric forms of these modifiers, remains poorly understood. The specificity of ubiquitin/Ubl-deconjugating enzymes for particular substrates depends on multiple factors, ranging from the topography of specific substrate features, as in different polyubiquitin chain types, to structural elements unique to each enzyme. Here we summarize recent structural and biochemical studies that provide insights into mechanisms of substrate specificity among various DUBs and ULPs. We also discuss the unexpected specificities of non-eukaryotic proteases in these families.

Indexed as

Catalytic DomainDeubiquitinating EnzymesHumansProtein ConformationStructure-Activity RelationshipSubstrate SpecificityUbiquitinUbiquitinsDeubiquitinating EnzymesUbiquitinUbiquitins

Identifiers

PMID27012468
PMCPMC4822132
OpenAlexW2316880913

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.