Evidence map›Paper›PMID 23729811›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Simulating the pulling of stalled elongated peptide from the ribosome by the translocon.

Anna Rychkova, Shayantani Mukherjee, Ram Prasad Bora, Arieh Warshel

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Modeling protein folding in vivo.Biology direct · 2018
    Article
  7. The FPhotosynthesis research · 2017
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Electrostatic origin of the unidirectionality of walking myosin V motors.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Cotranslational folding of membrane proteins probed by arrest-peptide-mediated force measurements.Proceedings of the National Academy of Sciences of the United States of America · 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.

Anna RychkovaDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089-1062, USA.
Shayantani Mukherjee
Ram Prasad Bora
Arieh Warshel

Funding

COMPUTER SIMULATION OF ELECTRON TRANSFER REACTIONSR01GM040283 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI WARSHEL, ARIEH · 1988 to 2016
$4.2M
NIGMS NIH HHS GM02449NIGMS NIH HHS GM40283NIGMS NIH HHS R01 GM040283
6 · The paper itself

Abstract

The nature of the coupling between the stalling of the elongated nascent peptide chain in the ribosome and its insertion through the translocon is analyzed, focusing on the recently discovered biphasic force that overcomes the stalling barrier. The origin of this long-range coupling is explored by coarse-grained simulations that combine the translocon (TR) insertion profile and the effective chemical barrier for the extension of the nascent chain in the ribosome. Our simulation determined that the inserted H segment is unlikely to climb the TR barrier in parallel with the peptide synthesis chemical step and that the nascent chain should first overcome the chemical barriers and move into the ribosome-TR gap region before the insertion into the TR tunnel. Furthermore, the simulations indicate that the coupled TR-chemistry free energy profile accounts for the biphasic force. Apparently, although the overall elongation/insertion process can be depicted as a tug-of-war between the forces of the TR and the ribosome, it is actually a reflection of the combined free-energy landscape. Most importantly, the present study helps to relate the experimental observation of the biphasic force to crucial information about the elusive path and barriers of the TR insertion process.

Indexed as

Computer SimulationModels, MolecularAnimalsElectrochemistryEnergy MetabolismHumansPeptide Chain Elongation, TranslationalProtein BiosynthesisRibosomesarrest peptidecoarse grained modelempirical valence bondLangevin dynamicssecM

Identifiers

PMID23729811
PMCPMC3690858

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.