Evidence map›Paper›PMID 21622956›Full record

ArticleNucleic acids research2011

The biological and structural characterization of Mycobacterium tuberculosis UvrA provides novel insights into its mechanism of action.

Franca Rossi, Jasbeer Singh Khanduja, Alessio Bortoluzzi, Joanna Houghton, Peter Sander, Carolin Güthlein, Elaine O Davis, Burkhard Springer, Erik C Böttger, Annalisa Relini and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. A Peek Inside the Machines of Bacterial Nucleotide Excision Repair.International journal of molecular sciences · 2021
    Review
  11. Review
  12. Targeting Genome Integrity inMolecules (Basel, Switzerland) · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

13 authors at 1 institution in 1 country.

Franca RossiDiSCAFF, University of Piemonte Orientale Amedeo Avogadro, Via Bovio 6, 28100 Novara, Italy.
Jasbeer Singh Khanduja
Alessio Bortoluzzi
Joanna Houghton
Peter Sander
Carolin Güthlein
Elaine O Davis
Burkhard Springer
Erik C Böttger
Annalisa Relini
Amanda Penco
K Muniyappa
Menico Rizzi
The Francis Crick Institute · GB

Funding

Medical Research Council
6 · The paper itself

Abstract

Mycobacterium tuberculosis is an extremely well adapted intracellular human pathogen that is exposed to multiple DNA damaging chemical assaults originating from the host defence mechanisms. As a consequence, this bacterium is thought to possess highly efficient DNA repair machineries, the nucleotide excision repair (NER) system amongst these. Although NER is of central importance to DNA repair in M. tuberculosis, our understanding of the processes in this species is limited. The conserved UvrABC endonuclease represents the multi-enzymatic core in bacterial NER, where the UvrA ATPase provides the DNA lesion-sensing function. The herein reported genetic analysis demonstrates that M. tuberculosis UvrA is important for the repair of nitrosative and oxidative DNA damage. Moreover, our biochemical and structural characterization of recombinant M. tuberculosis UvrA contributes new insights into its mechanism of action. In particular, the structural investigation reveals an unprecedented conformation of the UvrB-binding domain that we propose to be of functional relevance. Taken together, our data suggest UvrA as a potential target for the development of novel anti-tubercular agents and provide a biochemical framework for the identification of small-molecule inhibitors interfering with the NER activity in M. tuberculosis.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsDimerizationDNADNA-Binding ProteinsDNA DamageModels, MolecularMutationMycobacterium tuberculosisAdenosine TriphosphatasesBacterial ProteinsDNADNA-Binding Proteins

Identifiers

PMID21622956
PMCPMC3167621
OpenAlexW2135180456

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.