Evidence map›Paper›PMID 11463335›Full record

ArticleThe Biochemical journal2001

Identification of PEX5p-related novel peroxisome-targeting signal 1 (PTS1)-binding proteins in mammals.

L Amery, H Sano, G P Mannaerts, J Snider, J Van Looy, M Fransen, P P Van Veldhoven

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

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  14. Alternatively spliced isoforms of TRIP8b differentially control h channel trafficking and function.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  15. Regulation of HCN channel surface expression by a novel C-terminal protein-protein interaction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004
    Article
  16. Peroxisome senescence in human fibroblasts.Molecular biology of the cell · 2002
    Article
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  19. 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

7 authors at 3 institutions in 3 countries.

L AmeryKatholieke Universiteit Leuven, Campus Gasthuisberg (O/N), Departement Moleculaire Celbiologie, Afdeling Farmacologie, Herestraat 49, B-3000 Leuven, Belgium.
H Sano
G P Mannaerts
J Snider
J Van Looy
M Fransen
P P Van Veldhoven
KU Leuven · BEFood Research Institute · JPMerck (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Based on peroxin protein 5 (Pex5p) homology searches in the expressed sequence tag database and sequencing of large full-length cDNA inserts, three novel and related human cDNAs were identified. The brain-derived cDNAs coded for two related proteins that differ only slightly at their N-terminus, and exhibit 39.8% identity to human PEX5p. The shorter liver-derived cDNA coded for the C-terminal tetratricopeptide repeat-containing domain of the brain cDNA-encoded proteins. Since these three proteins specifically bind to various C-terminal peroxisome-targeting signals in a manner indistinguishable from Pex5p and effectively compete with Pex5p in an in vitro peroxisome-targeting signal 1 (PTS1)-binding assay, we refer to them as 'Pex5p-related proteins' (Pex5Rp). In contrast to Pex5p, however, human PEX5Rp did not bind to Pex14p or to the RING finger motif of Pex12p, and could not restore PTS1 protein import in Pex5(-/-) mouse fibroblasts. Immunofluorescence analysis of epitope-tagged PEX5Rp in Chinese hamster ovary cells suggested an exclusively cytosolic localization. Northern-blot analysis showed that the PEX5R gene, which is localized to chromosome 3q26.2--3q27, is expressed preferentially in brain. Mouse PEX5Rp was also delineated. In addition, experimental evidence established that the closest-related yeast homologue, YMR018wp, did not bind PTS1. Based on its subcellular localization and binding properties, Pex5Rp may function as a regulator in an early step of the PTS1 protein import process.

Indexed as

Amino Acid SequenceAnimalsBrainCHO CellsCloning, MolecularCricetinaeCytosolDNA, ComplementaryFibroblastsHumansMaleMiceMolecular Sequence DataPeroxisome-Targeting Signal 1 ReceptorRabbitsRatsDNA, ComplementaryPeroxisome-Targeting Signal 1 ReceptorPEX5 protein, humanPex5 protein, mouseReceptors, Cytoplasmic and Nuclear

Identifiers

PMID11463335
PMCPMC1221994
OpenAlexW2044055574

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.