Evidence map›Paper›PMID 19963078›Full record

ArticleInfection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases2010

Peruvian and globally reported amino acid substitutions on the Mycobacterium tuberculosis pyrazinamidase suggest a conserved pattern of mutations associated to pyrazinamide resistance.

Mirko Zimic, Patricia Sheen, Miguel Quiliano, Andrés Gutierrez, Robert H Gilman

Open access · greenAbstract read
In one paragraph

Article in Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
0.5field-weighted citation impact, top 37% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Structural and Dynamic Insights into the W68L, L85P, and T87A Mutations ofInternational journal of environmental research and public health · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Role of metal ions on the activity of Mycobacterium tuberculosis pyrazinamidase.The American journal of tropical medicine and hygiene · 2012
    Article
  11. Article
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

5 authors at 1 institution in 2 countries.

Mirko ZimicUnidad de Bioinformática, Laboratorios de Investigación y Desarrollo, Facultad de Ciencias y Filosofía, Universidad Peruana Cayetano Heredia, Av. Honorio Delgado 430, SMP, Lima, Peru. mzimic@jhsph.edu <mzimic@jhsph.edu>
Patricia Sheen
Miguel Quiliano
Andrés Gutierrez
Robert H Gilman
Universidad Peruana Cayetano Heredia · PE

Funding

Serological &Molecular Techniques-- Epidemiology of Cyclospora cayetanensisP01AI051976 · NIAID · UNIVERSIDAD PERUANA CAYETANO HEREDIA · PI GARCIA, HECTOR HUGO · 2002 to 2006
$3.3M
Infectious Diseases Training Program in PeruD43TW006581 · FIC · JOHNS HOPKINS UNIVERSITY · PI GILMAN, ROBERT H · 2003 to 2012
$2.4M
PERU EMERGING INFECTIONS TRAINING AND RESEARCHD43TW000910 · FIC · JOHNS HOPKINS UNIVERSITY · PI GILMAN, ROBERT H · 1997 to 2002
$784k
Towards tuberculosis control: pyrazinamide susceptibility and resistant mechanismR03AI067608 · NIAID · UNIVERSIDAD PERUANA CAYETANO HEREDIA · PI SHEEN, PATRICIA · 2006 to 2007
$106k
FIC NIH HHS D43 TW000910FIC NIH HHS D43 TW006581NIAID NIH HHS 1 R03 AI067608-0NIAID NIH HHS P01 AI051976NIAID NIH HHS R03 AI067608
6 · The paper itself

Abstract

Resistance to pyrazinamide in Mycobacterium tuberculosis is usually associated with a reduction of pyrazinamidase activity caused by mutations in pncA, the pyrazinamidase coding gene. Pyrazinamidase is a hydrolase that converts pyrazinamide, the antituberculous drug against the latent stage, to the active compound, pyrazinoic acid. To better understand the relationship between pncA mutations and pyrazinamide resistance, it is necessary to analyze the distribution of pncA mutations from pyrazinamide resistant strains. We determined the distribution of Peruvian and globally reported pncA missense mutations from M. tuberculosis clinical isolates resistant to pyrazinamide. The distributions of the single amino acid substitutions were compared at the secondary structure domains level. The distribution of the Peruvian mutations followed a similar pattern as the mutations reported globally. A consensus clustering of mutations was observed in hot-spot regions located in the metal coordination site and to a lesser extent in the active site of the enzyme. The data was not able to reject the null hypothesis that both distributions are similar, suggesting that pncA mutations associated to pyrazinamide resistance in M. tuberculosis, follow a conserved pattern responsible to impair the pyrazinamidase activity.

Indexed as

AmidohydrolasesAmino Acid SubstitutionAntitubercular AgentsBacterial ProteinsBinding SitesCluster AnalysisDrug Resistance, BacterialHumansMycobacterium tuberculosisPeruProtein Structure, SecondaryPyrazinamideStatistics, NonparametricTuberculosisAmidohydrolasesAntitubercular AgentsBacterial ProteinsPncA protein, Mycobacterium tuberculosisPyrazinamide

Identifiers

PMID19963078
PMCPMC2845309
OpenAlexW1964997170

What OpenQuestion holds

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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.