Evidence map›Paper›PMID 15995195›Full record

ArticleJournal of bacteriology2005

Mutational analysis of 16S and 23S rRNA genes of Thermus thermophilus.

Steven T Gregory, Jennifer F Carr, Daniel Rodriguez-Correa, Albert E Dahlberg

Abstract read
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

35 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Hibernating ribosomes as drug targets?Frontiers in microbiology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Tiamulin-Resistant Mutants of the Thermophilic BacteriumAntibiotics (Basel, Switzerland) · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Antimicrobial agents and chemotherapy · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Tools for characterizing bacterial protein synthesis inhibitors.Antimicrobial agents and chemotherapy · 2013
    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

4 authors at 1 institution in 1 country.

Steven T GregoryDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02912, USA.
Jennifer F Carr
Daniel Rodriguez-Correa
Albert E Dahlberg
Brown University · US

Funding

POLYSOMES &SUBUNITS: STRUCTURE-FUNCTION RELATIONSHIPSR01GM019756 · NIGMS · BROWN UNIVERSITY · PI DAHLBERG, ALBERT E · 1985 to 2013
$8.5M
INDENTATION WITH ATOMIC FORCE MICROSCOPYF32GM019756 · NIGMS · BARNES-JEWISH HOSPITAL · PI COSTA, KEVIN D · 1998 to 1998
–
NIGMS NIH HHS F32 GM019756NIGMS NIH HHS GM19756NIGMS NIH HHS R01 GM019756
6 · The paper itself

Abstract

Structural studies of the ribosome have benefited greatly from the use of organisms adapted to extreme environments. However, little is known about the mechanisms by which ribosomes or other ribonucleoprotein complexes have adapted to functioning under extreme conditions, and it is unclear to what degree mutant phenotypes of extremophiles will resemble those of their counterparts adapted to more moderate environments. It is conceivable that phenotypes of mutations affecting thermophilic ribosomes, for instance, will be influenced by structural adaptations specific to a thermophilic existence. This consideration is particularly important when using crystal structures of thermophilic ribosomes to interpret genetic results from nonextremophilic species. To address this issue, we have conducted a survey of spontaneously arising antibiotic-resistant mutants of the extremely thermophilic bacterium Thermus thermophilus, a species which has featured prominently in ribosome structural studies. We have accumulated over 20 single-base substitutions in T. thermophilus 16S and 23S rRNA, in the decoding site and in the peptidyltransferase active site of the ribosome. These mutations produce phenotypes that are largely identical to those of corresponding mutants of mesophilic organisms encompassing a broad phylogenetic range, suggesting that T. thermophilus may be an ideal model system for the study of ribosome structure and function.

Indexed as

Anti-Bacterial AgentsBase SequenceDNA PrimersModels, MolecularMolecular Sequence DataMutagenesisMutationNucleic Acid ConformationRNA, BacterialRNA, Ribosomal, 16SRNA, Ribosomal, 23SThermus thermophilusAnti-Bacterial AgentsDNA PrimersRNA, BacterialRNA, Ribosomal, 16SRNA, Ribosomal, 23S

Identifiers

PMID15995195
PMCPMC1169515
OpenAlexW2102630710

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.