Evidence map›Paper›PMID 34881571›Full record

ArticleJournal of chemical theory and computation2022

Probing Interplays between Human XBP1u Translational Arrest Peptide and 80S Ribosome.

Francesco Di Palma, Sergio Decherchi, Fátima Pardo-Avila, Sauro Succi, Michael Levitt, Gunnar von Heijne, Andrea Cavalli

Open access · hybridAbstract read
In one paragraph

Article in Journal of chemical theory and computation, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Cotranslational folding and assembly of the dimericProceedings of the National Academy of Sciences of the United States of America · 2022
    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

7 authors at 4 institutions in 3 countries.

Francesco Di PalmaComputational & Chemical Biology, Fondazione Istituto Italiano di Tecnologia, Via Morego 30, I-16163 Genova, Italy.ORCID https://orcid.org/0000-0002-3758-9045
Sergio DecherchiComputational & Chemical Biology, Fondazione Istituto Italiano di Tecnologia, Via Morego 30, I-16163 Genova, Italy.ORCID https://orcid.org/0000-0001-8371-2270
Fátima Pardo-AvilaDepartment of Structural Biology, Stanford University, Palo Alto, California 94305, United States.
Sauro SucciComputational & Chemical Biology, Fondazione Istituto Italiano di Tecnologia, Via Morego 30, I-16163 Genova, Italy.
Michael LevittDepartment of Structural Biology, Stanford University, Palo Alto, California 94305, United States.
Gunnar von HeijneDepartment of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Andrea CavalliComputational & Chemical Biology, Fondazione Istituto Italiano di Tecnologia, Via Morego 30, I-16163 Genova, Italy.ORCID https://orcid.org/0000-0002-6370-1176
Italian Institute of Technology · ITPalo Alto University · USHarvard University Press · USStockholm University · SE

Funding

Emergent Properties of Complex Systems: From Atoms to Macromolecules; from Humans to SocietiesR35GM122543 · NIGMS · STANFORD UNIVERSITY · PI MICHAEL LEVITT · 2017 to 2026
$5.1M
NIGMS NIH HHS R35 GM122543
6 · The paper itself

Abstract

The ribosome stalling mechanism is a crucial biological process, yet its atomistic underpinning is still elusive. In this framework, the human XBP1u translational arrest peptide (AP) plays a central role in regulating the unfolded protein response (UPR) in eukaryotic cells. Here, we report multimicrosecond all-atom molecular dynamics simulations designed to probe the interactions between the XBP1u AP and the mammalian ribosome exit tunnel, both for the wild type AP and for four mutant variants of different arrest potencies. Enhanced sampling simulations allow investigating the AP release process of the different variants, shedding light on this complex mechanism. The present outcomes are in qualitative/quantitative agreement with available experimental data. In conclusion, we provide an unprecedented atomistic picture of this biological process and clear-cut insights into the key AP-ribosome interactions.

Indexed as

PeptidesRibosomesAnimalsCytosolHumansMammalsMolecular Dynamics SimulationPeptides

Identifiers

PMID34881571
PMCPMC8908735
OpenAlexW4221036694

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.