Evidence map›Paper›PMID 22942282›Full record

ArticleThe Journal of biological chemistry2012

Mycobacterium tuberculosis prokaryotic ubiquitin-like protein-deconjugating enzyme is an unusual aspartate amidase.

Kristin E Burns, Fiona E McAllister, Carsten Schwerdtfeger, Julian Mintseris, Francisca Cerda-Maira, Elke E Noens, Matthias Wilmanns, Stevan R Hubbard, Francesco Melandri, Huib Ovaa and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Bacterial Proteasomes: Mechanistic and Functional Insights.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  10. mBio · 2017
    Article
  11. Bacterial Proteasomes.Annual review of microbiology · 2015
    Review
  12. The Pup-Proteasome System of Mycobacteria.Microbiology spectrum · 2014
    Review
  13. Prokaryotic ubiquitin-like protein modification.Annual review of microbiology · 2014
    Review
  14. Prokaryotic proteasomes: nanocompartments of degradation.Journal of molecular microbiology and biotechnology · 2013
    Review
  15. 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

12 authors at 5 institutions in 3 countries.

Kristin E BurnsDepartment of Microbiology, New York University, New York, New York 10016, USA.
Fiona E McAllister
Carsten Schwerdtfeger
Julian Mintseris
Francisca Cerda-Maira
Elke E Noens
Matthias Wilmanns
Stevan R Hubbard
Francesco Melandri
Huib Ovaa
Steven P Gygi
K Heran Darwin
Harvard University · USNew York University · USBioChem Technology (United States) · USEuropean Molecular Biology Laboratory · DEOncode Institute · NL

Funding

New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
PROTEASOME-DEPENDENT DEGRADATION IN MYCOBACTERIUM TUBERCULOSISR01AI088075 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI Katerina Heran Darwin · 2011 to 2026
$6.5M
NIAID NIH HHS 1R01AI088075NIAID NIH HHS R01 AI088075NIGMS NIH HHS GM67945NIGMS NIH HHS R01 GM067945
6 · The paper itself

Abstract

Deamidase of Pup (Dop), the prokaryotic ubiquitin-like protein (Pup)-deconjugating enzyme, is critical for the full virulence of Mycobacterium tuberculosis and is unique to bacteria, providing an ideal target for the development of selective chemotherapies. We used a combination of genetics and chemical biology to characterize the mechanism of depupylation. We identified an aspartate as a potential nucleophile in the active site of Dop, suggesting a novel protease activity to target for inhibitor development.

Indexed as

AmidohydrolasesAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBiocatalysisCatalytic DomainDiazooxonorleucineEnzyme InhibitorsHydrolysisModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMycobacterium tuberculosisStructural Homology, ProteinAmidohydrolasesBacterial ProteinsDiazooxonorleucineEnzyme Inhibitors

Identifiers

PMID22942282
PMCPMC3481346
OpenAlexW2041286214

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.