Evidence map›Paper›PMID 11258479›Full record

ReviewEMBO reports2000

Protein unfolding by mitochondria. The Hsp70 import motor.

A Matouschek, N Pfanner, W Voos

Open access · bronzeAbstract readReview
In one paragraph

Review in EMBO reports, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

52 citing papers in PubMed, 168 citations in OpenAlex.

  1. Time and Length Scales of Incomplete Translocation through Nanopores.The journal of physical chemistry letters · 2025
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  7. American journal of cancer research · 2021
    Article
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  10. Isoforms of Base Excision Repair Enzymes Produced by Alternative Splicing.International journal of molecular sciences · 2019
    Review
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  12. Article
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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 2 institutions in 2 countries.

A MatouschekDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500, USA. matouschek@northwestern.edu
N Pfanner
W Voos
University of Freiburg · DENorthwestern University · US

Funding

Protein unfolding in a physiological systemR01GM063004 · NIGMS · NORTHWESTERN UNIVERSITY · PI MATOUSCHEK, ANDREAS · 2001 to 2012
$2.7M
NIGMS NIH HHS R01 GM063004
6 · The paper itself

Abstract

Protein unfolding is a key step in the import of some proteins into mitochondria and chloroplasts and in the degradation of regulatory proteins by ATP-dependent proteases. In contrast to protein folding, the reverse process has remained largely uninvestigated until now. This review discusses recent discoveries on the mechanism of protein unfolding during translocation into mitochondria. The mitochondria can actively unfold preproteins by unraveling them from the N-terminus. The central component of the mitochondrial import motor, the matrix heat shock protein 70, functions by both pulling and holding the preproteins.

Indexed as

Protein FoldingAdenosine TriphosphateAnimalsBacterial ProteinsCytosolHSP70 Heat-Shock ProteinsMitochondriaModels, BiologicalProtein BindingProtein Structure, TertiaryRibonucleasesAdenosine TriphosphateBacillus amyloliquefaciens ribonucleaseBacterial ProteinsHSP70 Heat-Shock ProteinsRibonucleases

Identifiers

PMID11258479
PMCPMC1083766
OpenAlexW2079110089

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.