Evidence map›Paper›PMID 20636328›Full record

ArticleMolecular microbiology2010

Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis.

Francisca A Cerda-Maira, Michael J Pearce, Michele Fuortes, William R Bishai, Stevan R Hubbard, K Heran Darwin

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

63 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Future Research Directions on Mycobacterium tuberculosis Proteins.Advances in experimental medicine and biology · 2026
    Review
  5. Review
  6. Identification of a depupylation regulator for an essential enzyme inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Macrocyclic Peptides that Selectively Inhibit theJournal of medicinal chemistry · 2021
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Protein post-translational modifications in bacteria.Nature reviews. Microbiology · 2019
    Review
  17. Article
  18. Review
  19. Article
  20. Article

3 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 3 institutions in 1 country.

Francisca A Cerda-MairaNew York University School of Medicine, Department of Microbiology, 550 First Avenue, New York, NY 10016, USA.
Michael J Pearce
Michele Fuortes
William R Bishai
Stevan R Hubbard
K Heran Darwin
New York University · USCornell University · USJohns Hopkins University · US

Funding

Mycobacterium tuberculosis Survival Regulatory GenesR01AI037856 · NIAID · JOHNS HOPKINS UNIVERSITY · PI BISHAI, WILLIAM RAMSES · 1997 to 2020
$7.2M
GENE REGULATION AND VIRULENCE IN TB AND MACR01AI036973 · NIAID · JOHNS HOPKINS UNIVERSITY · PI BISHAI, WILLIAM RAMSES · 1999 to 2014
$5.7M
Virulence Regulation by the Mycobacterium Tuberculosis ProteasomeR01HL092774 · NHLBI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DARWIN, KATERINA HERAN · 2007 to 2017
$4.0M
SEARCH FOR GENETIC REGULATORS OF LATENCY IN M TBR29AI036973 · NIAID · JOHNS HOPKINS UNIVERSITY · PI BISHAI, WILLIAM RAMSES · 1994 to 1998
–
NHLBI NIH HHS HL92774NHLBI NIH HHS R01 HL092774NIAID NIH HHS AI 36973NIAID NIH HHS AI 37856NIAID NIH HHS N01 AI030036
6 · The paper itself

Abstract

Proteins targeted for degradation by the Mycobacterium proteasome are post-translationally tagged with prokaryotic ubiquitin-like protein (Pup), an intrinsically disordered protein of 64 residues. In a process termed 'pupylation', Pup is synthesized with a terminal glutamine, which is deamidated to glutamate by Dop (deamidase of Pup) prior to attachment to substrate lysines by proteasome accessory factor A (PafA). Importantly, PafA was previously shown to be essential to cause lethal infections by Mycobacterium tuberculosis (Mtb) in mice. In this study we show that Dop, like PafA, is required for the full virulence of Mtb. Additionally, we show that Dop is not only involved in the deamidation of Pup, but also needed to maintain wild-type steady state levels of pupylated proteins in Mtb. Finally, using structural models and site-directed mutagenesis our data suggest that Dop and PafA are members of the glutamine synthetase fold family of proteins.

Indexed as

AmidohydrolasesAmino Acid SequenceAmino Acid SubstitutionAnimalsBacterial LoadBacterial ProteinsDisease Models, AnimalDNA, BacterialLungMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsMycobacterium tuberculosisSequence Analysis, DNAAmidohydrolasesBacterial ProteinsDNA, BacterialDop protein, Mycobacterium tuberculosisMutant ProteinsPup protein, Mycobacterium tuberculosisUbiquitinsVirulence Factors

Identifiers

PMID20636328
PMCPMC2975802
OpenAlexW1604716826

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.