Evidence map›Paper›PMID 22155179›Full record

ReviewCurrent opinion in structural biology2012

Structural analyses clarify the complex control of mistranslation by tRNA synthetases.

Min Guo, Paul Schimmel

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Mammalian Tolerance to Amino Acid Heterochirality.Chembiochem : a European journal of chemical biology · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. A molecular link between cell wall biosynthesis, translation fidelity, and stringent response inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Chiral checkpoints during protein biosynthesis.The Journal of biological chemistry · 2019
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Bacterial transfer RNAs.FEMS microbiology reviews · 2015
    Review
  16. The ribosome challenge to the RNA world.Journal of molecular evolution · 2015
    Review
  17. Emergence and evolution.Topics in current chemistry · 2014
    Review
  18. Article
  19. Transfer RNA and human disease.Frontiers in genetics · 2014
    Review
  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

2 authors at 1 institution in 1 country.

Min GuoDepartment of Cancer Biology, The Scripps Research Institute, Scripps Florida, Jupiter, FL 33458, United States.
Paul Schimmel
Scripps Research Institute · US

Funding

INVESTIGATIONS OF REACTIONS OF PHYSIOLOGICAL IMPORTANCER01GM015539 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHIMMEL, PAUL R · 1985 to 2011
$6.6M
GENETIC APPROACHES TO PROTEIN/NUCLEIC ACID INTERACTIONSR01GM023562 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHIMMEL, PAUL R · 1985 to 2012
$4.9M
REACTIONS OF PHYSIOLOGICAL IMPORTANCER37GM015539 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI SCHIMMEL, PAUL R · 1989 to 1998
–
NIGMS NIH HHS GM 15539NIGMS NIH HHS R01 GM015539NIGMS NIH HHS R01 GM023562PHS HHS 23562
6 · The paper itself

Abstract

Proteins are precisely assembled with amino acids by matching the anticodons of charged transfer RNAs to nucleotide triplets in mRNA sequences. Accurate translation depends on the specific coupling of cognate amino acids and tRNAs - a step carried out by aminoacyl-tRNA synthetases (aaRSs) and that generates the genetic code. Owing to their intrinsic similarity, aaRSs developed highly differentiated structures to discriminate between amino acids at the active site for aminoacylation. Because this discrimination is not sufficient to prevent toxic mistranslation, aaRSs developed separate structures to further refine recognition by proofreading. From comprehensive structural studies on aaRSs, many of the molecular details have been elucidated for the recognition of cognate amino acids and for the misactivation and editing of noncognate amino acids, Here we review recent advances in the structural description of the binding, activation and editing of amino acids, which collectively reveal many aspects of the fine-tuned systems that resulted in a robust and universal genetic code.

Indexed as

Protein BiosynthesisAminoacylationAmino Acyl-tRNA SynthetasesAnimalsHumansLigandsRNA, TransferSubstrate SpecificityAmino Acyl-tRNA SynthetasesLigandsRNA, Transfer

Identifiers

PMID22155179
PMCPMC3288634
OpenAlexW2137532652

What OpenQuestion holds

Textmetadata
LicenceTDM
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.