Evidence map›Paper›PMID 9112774›Full record

ArticlePlant physiology1997

Protein transport into higher plant peroxisomes. In vitro import assay provides evidence for receptor involvement.

D G Brickner, J J Harada, L J Olsen

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Inheritance of the Md-ACS1 gene and its relationship to fruit softening in apple ( Malus x domestica Borkh.).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2004
    Article
  6. Article
  7. Article
  8. Hydrogen peroxide homeostasis: activation of plant catalase by calcium/calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  9. Article
  10. Article
  11. Identification and analysis of the plant peroxisomal targeting signal 1 receptor NtPEX5.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  12. Review
  13. 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

3 authors at 1 institution in 1 country.

D G BricknerDepartment of Biology, University of Michigan, Ann Arbor 48109-1048, USA.
J J Harada
L J Olsen
University of Michigan–Ann Arbor · US

Funding

Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
NIGMS NIH HHS T32GM08353
6 · The paper itself

Abstract

Peroxisome biogenesis requires that proteins be transported from their site of synthesis in the cytoplasm to their final location in the peroxisome matrix or membrane. Glyoxysomes are a class of peroxisomes found primarily in germinating seedlings and are involved in mobilizing fatty acids via the glyoxylate cycle and the beta-oxidation pathway. We have used an in vitro assay to study the mechanism(s) of import of proteins into glyoxysomes. Results from this assay indicate that the transport process is time- and temperature-dependent and is specific for peroxisomal proteins. Isocitrate lyase, a glyoxysomal protein, and the leaf-type peroxisomal enzyme glycolate oxidase (GLO) were transported into pumpkin (Cucurbita pepo) glyoxysomes with no apparent differences in efficiency of import. Thus, this in vitro assay appears to be physiologically relevant and correlates well with expected in vivo conditions. Protein import was also energy-dependent and saturable. Nonradiolabeled GLO competed with radiolabeled, in vitro-synthesized GLO for components of the import machinery. Finally, pretreatment of the isolated glyoxysomes with protease virtually abolished subsequent import of GLO. Taken together, these results indicate that a proteinaceous receptor is involved in the import of peroxisomal proteins.

Indexed as

Adenosine TriphosphateAlcohol OxidoreductasesEndopeptidasesKineticsMicrobodiesOrganellesPlant LeavesPlantsReceptors, Cytoplasmic and NuclearVegetablesAdenosine TriphosphateAlcohol OxidoreductasesEndopeptidasesglycollate oxidaseReceptors, Cytoplasmic and Nuclear

Identifiers

PMID9112774
PMCPMC158244
OpenAlexW1996685702

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.