Evidence map›Paper›PMID 11854424›Full record

ArticleMolecular biology of the cell2002

Peroxisomes are formed from complex membrane structures in PEX6-deficient CHO cells upon genetic complementation.

Noriyo Hashiguchi, Tomoko Kojidani, Tsuneo Imanaka, Tokuko Haraguchi, Yasushi Hiraoka, Eveline Baumgart, Sadaki Yokota, Toshiro Tsukamoto, Takashi Osumi

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In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed, 26 citations in OpenAlex.

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  9. Opinion: peroxisomal-protein import: is it really that complex?Nature reviews. Molecular cell biology · 2002
    Review
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

9 authors at 4 institutions in 2 countries.

Noriyo HashiguchiDepartment of Life Science, Faculty of Science, Himeji Institute of Technology, Kamigori, Hyogo 678-1297, Japan.
Tomoko Kojidani
Tsuneo Imanaka
Tokuko Haraguchi
Yasushi Hiraoka
Eveline Baumgart
Sadaki Yokota
Toshiro Tsukamoto
Takashi Osumi
Himeji University · JPHeidelberg University · DETohoku Medical and Pharmaceutical University · JPUniversity of Yamanashi · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pex6p belongs to the AAA family of ATPases. Its CHO mutant, ZP92, lacks normal peroxisomes but contains peroxisomal membrane remnants, so called peroxisomal ghosts, which are detected with anti-70-kDa peroxisomal membrane protein (PMP70) antibody. No peroxisomal matrix proteins were detected inside the ghosts, but exogenously expressed green fluorescent protein (GFP) fused to peroxisome targeting signal-1 (PTS-1) accumulated in the areas adjacent to the ghosts. Electron microscopic examination revealed that PMP70-positive ghosts in ZP92 were complex membrane structures, rather than peroxisomes with reduced matrix protein import ability. In a typical case, a set of one central spherical body and two layers of double-membraned loops were observed, with endoplasmic reticulum present alongside the outer loop. In the early stage of complementation by PEX6 cDNA, catalase and acyl-CoA oxidase accumulated in the lumen of the double-membraned loops. Biochemical analysis revealed that almost all the peroxisomal ghosts were converted into peroxisomes upon complementation. Our results indicate that 1) Peroxisomal ghosts are complex membrane structures; and 2) The complex membrane structures become import competent and are converted into peroxisomes upon complementation with PEX6.

Indexed as

ATP-Binding Cassette TransportersAdenosine TriphosphatasesAnimalsATPases Associated with Diverse Cellular ActivitiesCHO CellsCricetinaeFibroblastsGenetic Complementation TestHumansMembrane ProteinsPeroxisomesABCD3 protein, humanAbcd3 protein, ratAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesATP-Binding Cassette TransportersMembrane ProteinsPEX6 protein, humanPex6 protein, rat

Identifiers

PMID11854424
PMCPMC65661
OpenAlexW2024603766

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.