Evidence map›Paper›PMID 26184179›Full record

ReviewInternational journal of molecular sciences2015

MD Simulations of tRNA and Aminoacyl-tRNA Synthetases: Dynamics, Folding, Binding, and Allostery.

Rongzhong Li, Lindsay M Macnamara, Jessica D Leuchter, Rebecca W Alexander, Samuel S Cho

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Coding of Class I and II Aminoacyl-tRNA Synthetases.Advances in experimental medicine and biology · 2017
    Review
  15. Article
  16. Peripheral neuropathy via mutant tRNA synthetases: Inhibition of protein translation provides a possible explanation.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  17. Article
  18. 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

5 authors.

Rongzhong LiDepartments of Physics and Computer Science, Wake Forest University, 1834 Wake Forest Road, Winston-Salem, NC 27109, USA. lir0@wfu.edu.
Lindsay M MacnamaraDepartment of Chemistry, Wake Forest University, 1834 Wake Forest Road, Winston-Salem, NC 27109, USA. lmacnama@wakehealth.edu.
Jessica D LeuchterDepartment of Physics, Wake Forest University, 1834 Wake Forest Road, Winston-Salem, NC 27109, USA. jessica.leuchter@gmail.com.
Rebecca W AlexanderDepartment of Chemistry, Wake Forest University, 1834 Wake Forest Road, Winston-Salem, NC 27109, USA. alexanr@wfu.edu.
Samuel S ChoDepartments of Physics and Computer Science, Wake Forest University, 1834 Wake Forest Road, Winston-Salem, NC 27109, USA. choss@wfu.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While tRNA and aminoacyl-tRNA synthetases are classes of biomolecules that have been extensively studied for decades, the finer details of how they carry out their fundamental biological functions in protein synthesis remain a challenge. Recent molecular dynamics (MD) simulations are verifying experimental observations and providing new insight that cannot be addressed from experiments alone. Throughout the review, we briefly discuss important historical events to provide a context for how far the field has progressed over the past few decades. We then review the background of tRNA molecules, aminoacyl-tRNA synthetases, and current state of the art MD simulation techniques for those who may be unfamiliar with any of those fields. Recent MD simulations of tRNA dynamics and folding and of aminoacyl-tRNA synthetase dynamics and mechanistic characterizations are discussed. We highlight the recent successes and discuss how important questions can be addressed using current MD simulations techniques. We also outline several natural next steps for computational studies of AARS:tRNA complexes.

Indexed as

Molecular Dynamics SimulationAllosteric RegulationAmino Acyl-tRNA SynthetasesNucleic Acid ConformationProtein BindingProtein Structure, TertiaryQuantum TheoryRNA, TransferAmino Acyl-tRNA SynthetasesRNA, Transferatomisticcatalytic mechanismcoarse-grainededitingempirical force field

Identifiers

PMID26184179
PMCPMC4519929

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.