Evidence map›Paper›PMID 19595805›Full record

ReviewBiochimica et biophysica acta

A structural view on the mechanism of the ribosome-catalyzed peptide bond formation.

Miljan Simonović, Thomas A Steitz

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Targeting elongation factor 2 inFrontiers in insect science · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Relating Structure and Dynamics in RNA Biology.Cold Spring Harbor perspectives in biology · 2019
    Review
  15. Toward a Kinetic Understanding of Eukaryotic Translation.Cold Spring Harbor perspectives in biology · 2019
    Review
  16. Article
  17. Article
  18. Resistance to Macrolide Antibiotics in Public Health Pathogens.Cold Spring Harbor perspectives in medicine · 2016
    Review
  19. Bacterial Protein Synthesis as a Target for Antibiotic Inhibition.Cold Spring Harbor perspectives in medicine · 2016
    Review
  20. 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

2 authors.

Miljan SimonovićDepartment of Biochemistry and Molecular Genetics, University of Illinois at Chicago, MBRB 1170, 900 S Ashland Ave., Chicago, IL 60607, USA.
Thomas A Steitz

Funding

X-RAY ANALYSIS OF PROTEIN STRUCTURE AND FUNCTIONP01GM022778 · NIGMS · YALE UNIVERSITY · PI BREAKER, RONALD R · 1985 to 2019
$26.1M
Howard Hughes Medical InstituteNIGMS NIH HHS P01 GM022778
6 · The paper itself

Abstract

The ribosome is a large ribonucleoprotein particle that translates genetic information encoded in mRNA into specific proteins. Its highly conserved active site, the peptidyl-transferase center (PTC), is located on the large (50S) ribosomal subunit and is comprised solely of rRNA, which makes the ribosome the only natural ribozyme with polymerase activity. The last decade witnessed a rapid accumulation of atomic-resolution structural data on both ribosomal subunits as well as on the entire ribosome. This has allowed studies on the mechanism of peptide bond formation at a level of detail that surpasses that for the classical protein enzymes. A current understanding of the mechanism of the ribosome-catalyzed peptide bond formation is the focus of this review. Implications on the mechanism of peptide release are discussed as well.

Indexed as

Amino AcidsBinding SitesCatalysisCrystallography, X-RayGuanosine TriphosphateKineticsModels, ChemicalMolecular ConformationNucleic Acid ConformationPeptidesPeptidyl TransferasesRibosomesRNA, MessengerRNA, TransferThermusAmino AcidsGuanosine TriphosphatePeptidesPeptidyl TransferasesRNA, MessengerRNA, Transfer

Identifiers

PMID19595805
PMCPMC2783306

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.