Evidence map›Paper›PMID 25988164›Full record

ReviewFrontiers in molecular biosciences2014

Protein folding as a driving force for dual protein targeting in eukaryotes.

Bella Kalderon, Ophry Pines

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. The Mitochondrial Hsp90 TRAP1 and Alzheimer's Disease.Frontiers in molecular biosciences · 2021
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Cytosolic Hsp60 can modulate proteasome activity in yeast.The Journal of biological chemistry · 2015
    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

2 authors at 1 institution in 2 countries.

Bella KalderonDepartment of Microbiology and Molecular Genetics, Faculty of Medicine, Institute for Medical Research Israel-Canada, Hebrew University of Jerusalem Jerusalem, Israel.
Ophry PinesDepartment of Microbiology and Molecular Genetics, Faculty of Medicine, Institute for Medical Research Israel-Canada, Hebrew University of Jerusalem Jerusalem, Israel ; CREATE-NUS-HUJ Cellular and Molecular Mechanisms of Inflammation Program, National University of Singapore Singapore, Singapore.
Hebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is well documented that in eukaryotic cells molecules of one protein can be located in several subcellular locations, a phenomenon termed dual targeting, dual localization, or dual distribution. The differently localized identical or nearly identical proteins are termed "echoforms." Our conventional definition of dual targeted proteins refers to situations in which one of the echoforms is translocated through/into a membrane. Thus, dual targeted proteins are recognized by at least one organelle's receptors and translocation machineries within the lipid bilayer. In this review we attempt to evaluate mechanisms and situations in which protein folding is the major determinant of dual targeting and of the relative distribution levels of echoforms in the subcellular compartments of the eukaryotic cell. We show that the decisive folding step can occur prior, during or after translocation through the bilayer of a biological membrane. This phenomenon involves folding catalysts in the cell such as chaperones, proteases and modification enzymes, and targeting processes such as signal recognition, translocation through membranes, trapping, retrotranslocation and reverse translocation.

Indexed as

chaperonesechoformsmembranesMTS (mitochondrial targeting sequence)organellesretrotranslocationreverse translocationsignal peptide

Identifiers

PMID25988164
PMCPMC4428415
OpenAlexW2010353597

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.