Evidence map›Paper›PMID 11053105›Full record

ArticleBiophysical journal2000

Models of post-translational protein translocation.

T C Elston

Abstract readComparative Study
In one paragraph

Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Simulating the pulling of stalled elongated peptide from the ribosome by the translocon.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  4. Article
  5. Article
  6. Article
  7. 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

1 author.

T C ElstonBiomathematics Graduate Program/Department of Statistics, North Carolina State University, Raleigh, North Carolina 27695-8203, USA. elston@stat.ncsu.edu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Organellar Hsp-70 is required for post-translational translocation into the endoplasmic reticulum and mitochondria. The functional role played by Hsp-70 is unknown. However, two operating principles have been suggested. The power stroke model proposes that Hsp-70 undergoes a conformational change, which pulls the precursor protein through the translocation pore, whereas, in the Brownian ratchet model, the role of Hsp-70 is simply to block backsliding through the pore. A mathematical analysis of both mechanisms is presented and reveals that qualitative differences between the models occur in the behavior of the mean velocity and effective diffusion coefficient as a function of Hsp-70 concentration. An experimental method is proposed for measuring these two quantities that only relies on current experimental techniques.

Indexed as

Models, BiologicalAnimalsBiological Transport, ActiveBiophysical PhenomenaBiophysicsEndoplasmic ReticulumHSP70 Heat-Shock ProteinsKineticsMitochondriaProtein ConformationProtein Processing, Post-TranslationalProteinsHSP70 Heat-Shock ProteinsProteins

Identifiers

PMID11053105
PMCPMC1301113

What OpenQuestion holds

Textmetadata
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.