Evidence map›Paper›PMID 27284042›Full record

ReviewBiochemical Society transactions2016

Peroxisome protein import: a complex journey.

Alison Baker, Thomas Lanyon-Hogg, Stuart L Warriner

Erratum issuedAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026
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  9. mBio · 2023
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  12. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Alison BakerSchool of Molecular and Cellular Biology, Astbury Centre for Structural Molecular Biology and Centre for Plant Sciences, University of Leeds, Leeds LS2 9JT, U.K. a.baker@leeds.ac.uk.
Thomas Lanyon-HoggInstitute of Chemical Biology, Department of Chemistry, Imperial College London, London SW7 2AZ, U.K.
Stuart L WarrinerSchool of Chemistry, Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, U.K.

Funding

Biotechnology and Biological Sciences Research Council BB/D000904/1
6 · The paper itself

Abstract

The import of proteins into peroxisomes possesses many unusual features such as the ability to import folded proteins, and a surprising diversity of targeting signals with differing affinities that can be recognized by the same receptor. As understanding of the structure and function of many components of the protein import machinery has grown, an increasingly complex network of factors affecting each step of the import pathway has emerged. Structural studies have revealed the presence of additional interactions between cargo proteins and the PEX5 receptor that affect import potential, with a subtle network of cargo-induced conformational changes in PEX5 being involved in the import process. Biochemical studies have also indicated an interdependence of receptor-cargo import with release of unloaded receptor from the peroxisome. Here, we provide an update on recent literature concerning mechanisms of protein import into peroxisomes.

Indexed as

AnimalsEukaryotaHumansPeroxisomesProtein ConformationProtein Sorting SignalsProtein TransportReceptors, Cytoplasmic and NuclearPEX5L protein, humanProtein Sorting SignalsReceptors, Cytoplasmic and NuclearmechanismsmodelsperoxisomePEX5protein import cycletargeting signal

Identifiers

PMID27284042
PMCPMC4900764

What OpenQuestion holds

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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.