Evidence map›Paper›PMID 29221924›Full record

ReviewMethods (San Diego, Calif.)2018

Unraveling co-translational protein folding: Concepts and methods.

Anton A Komar

Open access · greenAbstract readReview
In one paragraph

Review in Methods (San Diego, Calif.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. De novo biosynthesis of a nonnatural cobalt porphyrin cofactor inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. A Single Synonymous Variant (c.354G>A [p.P118P]) inInternational journal of molecular sciences · 2019
    Article
  16. Article
  17. Protein ensembles link genotype to phenotype.PLoS computational biology · 2019
    Review
  18. Article
  19. 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

1 author at 1 institution in 1 country.

Anton A KomarCenter for Gene Regulation in Health and Disease and Department of Biological, Geological and Environmental Sciences, Cleveland State University, Cleveland, OH 44115, USA; Department of Biochemistry and the Center for RNA Science and Therapeutics, Case Western Reserve University, Cleveland, OH 44106, USA; Genomic Medicine Institute, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA. Electronic address: a.komar@csuohio.edu.
Case Western Reserve University · US

Funding

Understanding the impact of disease causing mutations in FIXR15HL121779 · NHLBI · CLEVELAND STATE UNIVERSITY · PI KOMAR, ANTON A. · 2014 to 2014
$437k
NHLBI NIH HHS R15 HL121779
6 · The paper itself

Abstract

Advances in techniques such as nuclear magnetic resonance spectroscopy, cryo-electron microscopy, and single-molecule and time-resolved fluorescent approaches are transforming our ability to study co-translational protein folding both in vivo in living cells and in vitro in reconstituted cell-free translation systems. These approaches provide comprehensive information on the spatial organization and dynamics of nascent polypeptide chains and the kinetics of co-translational protein folding. This information has led to an improved understanding of the process of protein folding in living cells and should allow remaining key questions in the field, such as what structures are formed within nascent chains during protein synthesis and when, to be answered. Ultimately, studies using these techniques will facilitate development of a unified concept of protein folding, a process that is essential for proper cell function and organism viability. This review describes current methods for analysis of co-translational protein folding with an emphasis on some of the recently developed techniques that allow monitoring of co-translational protein folding in real-time.

Indexed as

Protein FoldingCell-Free SystemCryoelectron MicroscopyProtein BiosynthesisProtein Modification, TranslationalProteinsRibosomesProteinsCo-translational protein foldingProtein folding pathwayReal-time measurementsReconstituted cell-free translation systemsRibosome-bound nascent chain complexes (RNCs)

Identifiers

PMID29221924
PMCPMC5866750
OpenAlexW2771199102

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.