Evidence map›Paper›PMID 33987870›Full record

ArticleBioEssays : news and reviews in molecular, cellular and developmental biology2021

Co-translational folding of nascent polypeptides: Multi-layered mechanisms for the efficient biogenesis of functional proteins.

Kevin Maciuba, Nandakumar Rajasekaran, Xiuqi Chen, Christian M Kaiser

Open access · hybridAbstract read
In one paragraph

Article in BioEssays : news and reviews in molecular, cellular and developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022
    Review
  5. 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 at 1 institution in 1 country.

Kevin MaciubaCMDB Graduate Program, Johns Hopkins University, Baltimore, Maryland, USA.
Nandakumar RajasekaranCMDB Graduate Program, Johns Hopkins University, Baltimore, Maryland, USA.
Xiuqi ChenCMDB Graduate Program, Johns Hopkins University, Baltimore, Maryland, USA.
Christian M KaiserDepartment of Biology, Johns Hopkins University, Baltimore, Maryland, USA.ORCID 0000-0001-9004-1882
Johns Hopkins University · US

Funding

CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
Folding and Chaperone Interactions of Multi-domain ProteinsR01GM121567 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HILSER, VINCENT J. · 2017 to 2025
$3.2M
NIGMS NIH HHS R01 GM121567NIGMS NIH HHS T32 GM007231
6 · The paper itself

Abstract

The coupling of protein synthesis and folding is a crucial yet poorly understood aspect of cellular protein folding. Over the past few years, it has become possible to experimentally follow and define protein folding on the ribosome, revealing principles that shape co-translational folding and distinguish it from refolding in solution. Here, we highlight some of these recent findings from biochemical and biophysical studies and their potential significance for cellular protein biogenesis. In particular, we focus on nascent chain interactions with the ribosome, interactions within the nascent protein, modulation of translation elongation rates, and the role of mechanical force that accompanies nascent protein folding. The ability to obtain mechanistic insight in molecular detail has set the stage for exploring the intricate process of nascent protein folding. We believe that the aspects discussed here will be generally important for understanding how protein synthesis and folding are coupled and regulated.

Indexed as

Protein FoldingRibosomesPeptidesProtein BiosynthesisProteinsPeptidesProteinsco-translational protein foldingfolding pathwaysmechanical forcemisfoldingmolecular chaperonesnascent proteinribosome

Identifiers

PMID33987870
PMCPMC8262109
OpenAlexW3163411493

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.