Evidence map›Paper›PMID 8755875›Full record

ArticleJournal of bacteriology1996

Stationary phase-associated protein expression in Mycobacterium tuberculosis: function of the mycobacterial alpha-crystallin homolog.

Y Yuan, D D Crane, C E Barry

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed, 1 pooled it
6.5field-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

119 citing papers in PubMed, 1 synthesis or guideline pooled it, 319 citations in OpenAlex.

  1. A Systematic Review on NovelFrontiers in immunology · 2018
    Pooled it
  2. Trial
  3. Immunodominant Tuberculosis Antigens Recognized by Human CD4Cold Spring Harbor perspectives in medicine · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Evaluation of cytokine profiles related toFrontiers in immunology · 2024
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Understanding the early host immune response againstCentral-European journal of immunology · 2020
    Review
  17. Article
  18. Article
  19. CD4Frontiers in immunology · 2019
    Article
  20. A New Functional Model for Prediction of Chaperone Activity of the RecombinantThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2019
    Article

59 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

3 authors at 1 institution in 1 country.

Y YuanTuberculosis Research Unit, Laboratory of Intracellular Parasites, National Institutes for Allergy and Infectious Diseases, Rocky Mountain Laboratories, Hamilton, Montana 59840, USA.
D D Crane
C E Barry
National Institute of Allergy and Infectious Diseases · US

Funding

Pathogenesis, Latency and Drug Resistance Of Mycobacterium TuberculosisZ01AI000783 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI BARRY, CLIFTON · 1997 to 2008
$5.8M
Intramural NIH HHS Z01 AI000783
6 · The paper itself

Abstract

The majority of active tuberculosis cases arise as a result of reactivation of latent organisms which are quiescent within the host. The ability of mycobacteria to survive extended periods without active replication is a complex process whose details await elucidation. We used two-dimensional gel electrophoresis to examine both steady-state protein composition and time-dependent protein synthetic profiles in aging cultures of virulent Mycobacterium tuberculosis. At least seven proteins were maximally synthesized 1 to 2 weeks following the end of log-phase growth. One of these proteins accumulated to become a predominant stationary-phase protein. N-terminal amino acid sequencing and immunoreactivity identified this protein as the 16-kDa alpha-crystallin-like small heat shock protein. The gene for this protein was shown to be limited to the slowly growing M. tuberculosis complex of organisms as assessed by Southern blotting. Overexpression of this protein in wild-type M. tuberculosis resulted in a slower decline in viability following the end of log-phase growth. Accumulation of this protein was observed in log-phase cultures following a shift to oxygen-limiting conditions but not by other external stimuli. The protein was purified to homogeneity from overexpressing M. smegmatis in two steps and shown to have a significant ability to suppress the thermal denaturation of alcohol dehydrogenase. Collectively, these results suggest that the mycobacterial alpha-crystallin protein may play a role in enhancing long-term protein stability and therefore long-term survival of M. tuberculosis.

Indexed as

Antigens, BacterialBacterial ProteinsBase SequenceCrystallinsDNA, BacterialDNA PrimersGene ExpressionHeat-Shock ProteinsInterphaseMolecular ChaperonesMolecular Sequence DataMolecular WeightMycobacteriumMycobacterium tuberculosisPhenotypeSpecies SpecificityAntigens, BacterialBacterial ProteinsCrystallinsDNA, BacterialDNA PrimersHeat-Shock ProteinsMolecular Chaperones

Identifiers

PMID8755875
PMCPMC178214
OpenAlexW1851138068

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.