Evidence map›Paper›PMID 8837511›Full record

ArticleThe Plant cell1996

Targeting and processing of a chimeric protein with the N-terminal presequence of the precursor to glyoxysomal citrate synthase.

A Kato, M Hayashi, M Kondo, M Nishimura

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Nuclear and peroxisomal targeting of catalase.Plant, cell & environment · 2022
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  9. Article
  10. Article
  11. Peroxisome biogenesis and function.The arabidopsis book · 2009
    Article
  12. Article
  13. Article
  14. Dual specificities of the glyoxysomal/peroxisomal processing protease Deg15 in higher plants.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

4 authors at 1 institution in 1 country.

A KatoDepartment of Cell Biology, National Institute for Basic Biology, Okazaki, Japan.
M Hayashi
M Kondo
M Nishimura
National Institute for Basic Biology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glyoxysomal citrate synthase in pumpkin is synthesized as a precursor that has a cleavable presequence at its N-terminal end. To investigate the role of the presequence in the transport of the protein to the microbodies, we generated transgenic Arabidopsis plants that expressed beta-glucuronidase with the N-terminal presequence of the precursor to the glyoxysomal citrate synthase of pumpkin. Immunogold labeling and cell fractionation studies showed that the chimeric protein was transported into microbodies and subsequently was processed. The chimeric protein was transported to functionally different microbodies, such as glyoxysomes, leaf peroxisomes, and unspecialized microbodies. These observations indicated that the transport of glyoxysomal citrate synthase is mediated by its N-terminal presequence and that the transport system is functional in all plant microbodies. Site-directed mutagenesis of the conserved amino acids in the presequence caused abnormal targeting and inhibition of processing of the chimeric protein, suggesting that the conserved amino acids in the presequence are required for recognition of the target or processing.

Indexed as

Amino Acid SequenceArabidopsisBase SequenceCitrate (si)-SynthaseConsensus SequenceDNA PrimersGene ExpressionGenes, PlantMicrobodiesMolecular Sequence DataMutagenesis, Site-DirectedPlant ProteinsPlants, Genetically ModifiedProtein PrecursorsProtein Processing, Post-TranslationalRecombinant Fusion ProteinsCitrate (si)-SynthaseDNA PrimersPlant ProteinsProtein PrecursorsRecombinant Fusion Proteins

Identifiers

PMID8837511
PMCPMC161301
OpenAlexW2144084133

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.