Evidence map›Paper›PMID 30971450›Full record

ArticlePlant physiology2019

The Golgi Localization of GnTI Requires a Polar Amino Acid Residue within Its Transmembrane Domain.

Jennifer Schoberer, Eva Liebminger, Ulrike Vavra, Christiane Veit, Clemens Grünwald-Gruber, Friedrich Altmann, Stanley W Botchway, Richard Strasser

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.9field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Trafficking and localization of Golgi-residentFrontiers in plant science · 2025
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Prolyl Hydroxylase Paralogs inFrontiers in plant science · 2021
    Article
  13. Inactivation ofFrontiers in plant science · 2021
    Article
  14. Article
  15. Separating Golgi Proteins fromThe Plant cell · 2019
    Article
  16. 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

8 authors at 2 institutions in 2 countries.

Jennifer SchobererDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.ORCID 0000-0001-5102-7674
Eva LiebmingerDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Ulrike VavraDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Christiane VeitDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Clemens Grünwald-GruberDepartment of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.ORCID 0000-0002-6097-8348
Friedrich AltmannDepartment of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.ORCID 0000-0002-0112-7877
Stanley W BotchwayResearch Complex at Harwell, Central Laser Facility, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell-Oxford, Didcot OX11 0QX, United Kingdom.ORCID 0000-0002-3268-9303
Richard StrasserDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria richard.strasser@boku.ac.at.ORCID 0000-0001-8764-6530
BOKU University · ATRutherford Appleton Laboratory · GB

Funding

Austrian Science Fund FWF P 23906Austrian Science Fund FWF P 28218
6 · The paper itself

Abstract

The Golgi apparatus consists of stacked cisternae filled with enzymes that facilitate the sequential and highly controlled modification of glycans from proteins that transit through the organelle. Although the glycan processing pathways have been extensively studied, the underlying mechanisms that concentrate Golgi-resident glycosyltransferases and glycosidases in distinct Golgi compartments are poorly understood. The single-pass transmembrane domain (TMD) of n-acetylglucosaminyltransferaseI (GnTI) accounts for its steady-state distribution in the cis/medial-Golgi. Here, we investigated the contribution of individual amino acid residues within the TMD of Arabidopsis (

Indexed as

Amino AcidsArabidopsisCoat Protein Complex IGene Knockdown TechniquesGolgi ApparatusGreen Fluorescent ProteinsModels, BiologicalMutationNicotianaPlant ProteinsPolysaccharidesProtein DomainsProtein SubunitsProtein TransportVacuolesAmino AcidsCoat Protein Complex IGreen Fluorescent ProteinsPlant ProteinsPolysaccharidesProtein Subunits

Identifiers

PMID30971450
PMCPMC6548254
OpenAlexW2938572982

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.