Evidence map›Paper›PMID 32045984›Full record

ReviewPlants (Basel, Switzerland)2020

Co-Translational Protein Folding and Sorting in Chloroplasts.

Fabian Ries, Claudia Herkt, Felix Willmund

Open access · goldAbstract readReview
In one paragraph

Review in Plants (Basel, Switzerland), 2020. 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
1.4field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  13. Structural features of chloroplast trigger factor determined at 2.6 Å resolution.Acta crystallographica. Section D, Structural biology · 2022
    Article
  14. Article
  15. Article
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  17. A VFrontiers in plant science · 2021
    Article
  18. 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

3 authors at 1 institution in 1 country.

Fabian RiesMolecular Genetics of Eukaryotes, University of Kaiserslautern, Paul-Ehrlich-Strasse 23, 67663 Kaiserslautern, Germany.ORCID 0000-0002-0964-3307
Claudia HerktMolecular Genetics of Eukaryotes, University of Kaiserslautern, Paul-Ehrlich-Strasse 23, 67663 Kaiserslautern, Germany.ORCID 0000-0002-7435-945X
Felix WillmundMolecular Genetics of Eukaryotes, University of Kaiserslautern, Paul-Ehrlich-Strasse 23, 67663 Kaiserslautern, Germany.
University of Kaiserslautern · DE

Funding

Carl-Zeiss Foundation FRDeutsche Forschungsgemeinschaft TRR175-A05Land Rheinland Pfalz BioComp
6 · The paper itself

Abstract

Cells depend on the continuous renewal of their proteome composition during the cell cycle and in order to replace aberrant proteins or to react to changing environmental conditions. In higher eukaryotes, protein synthesis is achieved by up to five million ribosomes per cell. With the fast kinetics of translation, the large number of newly made proteins generates a substantial burden for protein homeostasis and requires a highly orchestrated cascade of factors promoting folding, sorting and final maturation. Several of the involved factors directly bind to translating ribosomes for the early processing of emerging nascent polypeptides and the translocation of ribosome nascent chain complexes to target membranes. In plant cells, protein synthesis also occurs in chloroplasts serving the expression of a relatively small set of 60-100 protein-coding genes. However, most of these proteins, together with nucleus-derived subunits, form central complexes majorly involved in the essential processes of photosynthetic light reaction, carbon fixation, metabolism and gene expression. Biogenesis of these heterogenic complexes adds an additional level of complexity for protein biogenesis. In this review, we summarize the current knowledge about co-translationally binding factors in chloroplasts and discuss their role in protein folding and ribosome translocation to thylakoid membranes.

Indexed as

chloroplast gene expressionmolecular chaperonesprotein synthesisprotein targetingtranslocation

Identifiers

PMID32045984
PMCPMC7076657
OpenAlexW3005296459

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.