Evidence map›Paper›PMID 8589629›Full record

ArticleThe Plant cell1995

Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine.

A Heese-Peck, R N Cole, O N Borkhsenious, G W Hart, N V Raikhel

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  3. Article
  4. Glycosylation of the nuclear pore.Traffic (Copenhagen, Denmark) · 2014
    Review
  5. Article
  6. The roles of O-linked β-N-acetylglucosamine in cardiovascular physiology and disease.American journal of physiology. Heart and circulatory physiology · 2012
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
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  16. Review
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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

5 authors at 1 institution in 1 country.

A Heese-PeckMichigan State University, Department of Energy Plant Research Laboratory, East Lansing 48824-1312, USA.
R N Cole
O N Borkhsenious
G W Hart
N V Raikhel
Michigan State University · US

Funding

ROLE OF O-GLCNAC ON SYNAPSIN IF32NS009415 · NINDS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI COLE, ROBERT N · 1993 to 1994
–
NINDS NIH HHS F32-NS09415
6 · The paper itself

Abstract

Only a few nuclear pore complex (NPC) proteins, mainly in vertebrates and yeast but none in plants, have been well characterized. As an initial step to identify plant NPC proteins, we examined whether NPC proteins from tobacco are modified by N-acetylglucosamine (GlcNAc). Using wheat germ agglutinin, a lectin that binds specifically to GlcNAc in plants, specific labeling was often found associated with or adjacent to NPCs. Nuclear proteins containing GlcNAc can be partially extracted by 0.5 M salt, as shown by a wheat germ agglutinin blot assay, and at least eight extracted proteins were modified by terminal GlcNAc, as determined by in vitro galactosyltransferase assays. Sugar analysis indicated that the plant glycans with terminal GlcNAc differ from the single O-linked GlcNAc of vertebrate NPC proteins in that they consist of oligosaccharides that are larger in size than five GlcNAc residues. Most of these appear to be bound to proteins via a hydroxyl group. This novel oligosaccharide modification may convey properties to the plant NPC that are different from those of vertebrate NPCs.

Indexed as

AcetylglucosamineCells, CulturedNicotianaNuclear EnvelopeNuclear ProteinsOligosaccharidesPlant ProteinsPlants, ToxicAcetylglucosamineNuclear ProteinsOligosaccharidesPlant Proteins

Identifiers

PMID8589629
PMCPMC160971
OpenAlexW2096693374

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.