Evidence map›Paper›PMID 7638178›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

An Arabidopsis syntaxin homologue isolated by functional complementation of a yeast pep12 mutant.

D C Bassham, S Gal, A da Silva Conceição, N V Raikhel

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
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  3. Phylogeny of endocytic components yields insight into the process of nonendosymbiotic organelle evolution.Proceedings of the National Academy of Sciences of the United States of America · 2008
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  13. AtVPS45 complex formation at the trans-Golgi network.Molecular biology of the cell · 2000
    Article
  14. Article
  15. Article
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  17. Article
  18. Exocytosis in plants.Plant molecular biology · 1998
    Review
  19. Review
  20. A putative vacuolar cargo receptor partially colocalizes with AtPEP12p on a prevacuolar compartment in Arabidopsis roots.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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

4 authors at 1 institution in 1 country.

D C BasshamDepartment of Energy Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA.
S Gal
A da Silva Conceição
N V Raikhel
Michigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The syntaxin family of integral membrane proteins are thought to function as receptors for transport vesicles, with different isoforms of this family localized to various membranes throughout the cell. The yeast Pep12 protein is a syntaxin homologue which may function in the trafficking of vesicles from the trans-Golgi network to the vacuole. We have isolated an Arabidopsis thaliana cDNA by functional complementation of a yeast pep12 mutant. The Arabidopsis cDNA (aPEP12) potentially encodes a 31-kDa protein which is homologous to yeast Pep12 and to other members of the syntaxin family, indicating that this protein may function in the docking or fusion of transport vesicles with the vacuolar membrane in plant cells. Northern blot analysis indicates that the mRNA is expressed in all tissues examined, although at a very low level in leaves. The mRNA is found in all cell types in roots and leaves, as shown by in situ hybridization experiments. The existence of plant homologues of proteins of the syntaxin family indicates that the basic vesicle docking and fusion machinery may be conserved in plants as it is in yeast and mammals.

Indexed as

Arabidopsis ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceArabidopsisDNA, ComplementaryDNA, FungalDNA, PlantFungal ProteinsGenes, PlantGenetic Complementation TestMembrane ProteinsMolecular Sequence DataMutationPlant ProteinsQa-SNARE ProteinsRNA, MessengerArabidopsis ProteinsATPEP12 protein, ArabidopsisDNA, ComplementaryDNA, FungalDNA, PlantFungal ProteinsMembrane ProteinsPEP12 protein, S cerevisiaePlant ProteinsQa-SNARE ProteinsRNA, MessengerRNA, PlantSaccharomyces cerevisiae Proteins

Identifiers

PMID7638178
PMCPMC41319
OpenAlexW2079927453

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.