Evidence map›Paper›PMID 11566882›Full record

ArticleThe EMBO journal2001

A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14.

A Borodovsky, B M Kessler, R Casagrande, H S Overkleeft, K D Wilkinson, H L Ploegh

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 259 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
259citing papers in PubMed, 1 pooled it
5.8field-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

259 citing papers in PubMed, 1 synthesis or guideline pooled it, 508 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Synthetic Strategies for Activity-Based Probes to Decode Ubiquitin-Like Modifiers.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Internal Ubiquitin Electrophiles for Covalent Trapping and Inhibition of Deubiquitinases.Chembiochem : a European journal of chemical biology · 2025
    Article
  10. Review
  11. AKT and DUBs: a bidirectional relationship.Cellular & molecular biology letters · 2025
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  20. Deubiquitinases and Cancer.Journal of pharmacy & bioallied sciences · 2024
    Review

199 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

6 authors at 2 institutions in 1 country.

A BorodovskyDepartment of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
B M Kessler
R Casagrande
H S Overkleeft
K D Wilkinson
H L Ploegh
Harvard University · USEmory University · US

Funding

UBIQUITIN-DEPENDENT PROTEOLYSIS--SPECIFICITY/MECHANISMR01GM030308 · NIGMS · EMORY UNIVERSITY · PI WILKINSON, KEITH D · 1985 to 2010
$3.9M
NIGMS NIH HHS GM30308NIGMS NIH HHS R01 GM030308
6 · The paper itself

Abstract

A C-terminally modified ubiquitin (Ub) derivative, ubiquitin vinyl sulfone (UbVS), was synthesized as an active site-directed probe that irreversibly modifies a subset of Ub C-terminal hydrolases (UCHs) and Ub-specific processing proteases (UBPs). Specificity of UbVS for deubiquitylating enzymes (DUBs) is demonstrated not only by inhibition of [(125)I]UbVS labeling with N-ethylmaleimide and Ub aldehyde, but also by genetic analysis. [(125)I]UbVS modifies six of the 17 known and putative yeast deubiquitylating enzymes (Yuh1p, Ubp1p, Ubp2p, Ubp6p, Ubp12p and Ubp15p), as revealed by analysis of corresponding mutant strains. In mammalian cells, greater numbers of polypeptides are labeled, most of which are likely to be DUBs. Using [(125)I]UbVS as a probe, we report the association of an additional DUB with the mammalian 26S proteasome. In addition to the 37 kDa enzyme reported to be part of the 19S cap, we identified USP14, a mammalian homolog of yeast Ubp6p, as being bound to the proteasome. Remarkably, labeling of 26S-associated USP14 with [(125)I]UbVS is increased when proteasome function is impaired, suggesting functional coupling between the activities of USP14 and the proteasome.

Indexed as

Proteasome Endopeptidase ComplexSaccharomyces cerevisiae Proteins3T3 CellsAnimalsBinding SitesCell ExtractsCell LineEndopeptidasesEnzyme InhibitorsFungal ProteinsGene DeletionIodine RadioisotopesMacromolecular SubstancesMiceOligopeptidesPeptide Hydrolases4-hydroxy-3-iodo-2-nitrophenyl-leucyl-leucyl-leucine vinyl sulfoneATP dependent 26S proteaseCell ExtractsEndopeptidasesEnzyme InhibitorsFungal ProteinsIodine RadioisotopesMacromolecular SubstancesOligopeptidesPeptide HydrolasesProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsSulfonesThiolester HydrolasesUbiquitinsUbiquitin Thiolesteraseubiquitin vinyl sulfoneUBP6 protein, S cerevisiae

Identifiers

PMID11566882
PMCPMC125629
OpenAlexW2001234769

What OpenQuestion holds

Textmetadata
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.