Evidence map›Paper›PMID 25804536›Full record

ArticleThe Plant cell2015

Identification and Characterization of a Golgi-Localized UDP-Xylose Transporter Family from Arabidopsis.

Berit Ebert, Carsten Rautengarten, Xiaoyuan Guo, Guangyan Xiong, Solomon Stonebloom, Andreia M Smith-Moritz, Thomas Herter, Leanne Jade G Chan, Paul D Adams, Christopher J Petzold and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
15.0field-weighted citation impact, top 1% 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

36 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. ACS omega · 2024
    Article
  6. Identification of QTLs for symbiotic nitrogen fixation and related traits in a soybean recombinant inbred line population.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. The Xyloglucan Endotransglucosylase/Hydrolase GeneInternational journal of molecular sciences · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. ThePlant direct · 2021
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

14 authors at 3 institutions in 3 countries.

Berit EbertJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720 Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, C 1871 Copenhagen, Denmark ARC Centre of Excellence in Plant Cell Walls, School of BioSciences, The University of Melbourne, Victoria 3010, Australia.
Carsten RautengartenJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720 ARC Centre of Excellence in Plant Cell Walls, School of BioSciences, The University of Melbourne, Victoria 3010, Australia.
Xiaoyuan GuoDepartment of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, C 1871 Copenhagen, Denmark.
Guangyan XiongDepartment of Plant and Microbial Biology, University of California, Berkeley, California 94720.
Solomon StonebloomJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
Andreia M Smith-MoritzJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
Thomas HerterJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
Leanne Jade G ChanJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
Paul D AdamsJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720 Department of Bioengineering, University of California, Berkeley, California 94720.
Christopher J PetzoldJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
Markus PaulyDepartment of Plant and Microbial Biology, University of California, Berkeley, California 94720.
William G T WillatsDepartment of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, C 1871 Copenhagen, Denmark.
Joshua L HeazlewoodJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720 ARC Centre of Excellence in Plant Cell Walls, School of BioSciences, The University of Melbourne, Victoria 3010, Australia.
Henrik Vibe SchellerJoint BioEnergy Institute and Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720 Department of Plant and Microbial Biology, University of California, Berkeley, California 94720 hscheller@lbl.gov.
Lawrence Berkeley National Laboratory · USUniversity of California, Berkeley · USUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most glycosylation reactions require activated glycosyl donors in the form of nucleotide sugars to drive processes such as posttranslational modifications and polysaccharide biosynthesis. Most plant cell wall polysaccharides are biosynthesized in the Golgi apparatus from cytosolic-derived nucleotide sugars, which are actively transferred into the Golgi lumen by nucleotide sugar transporters (NSTs). An exception is UDP-xylose, which is biosynthesized in both the cytosol and the Golgi lumen by a family of UDP-xylose synthases. The NST-based transport of UDP-xylose into the Golgi lumen would appear to be redundant. However, employing a recently developed approach, we identified three UDP-xylose transporters in the Arabidopsis thaliana NST family and designated them UDP-XYLOSE TRANSPORTER1 (UXT1) to UXT3. All three transporters localize to the Golgi apparatus, and UXT1 also localizes to the endoplasmic reticulum. Mutants in UXT1 exhibit ∼30% reduction in xylose in stem cell walls. These findings support the importance of the cytosolic UDP-xylose pool and UDP-xylose transporters in cell wall biosynthesis.

Indexed as

ArabidopsisArabidopsis ProteinsGolgi ApparatusMonosaccharide Transport ProteinsUridine Diphosphate XyloseArabidopsis ProteinsMonosaccharide Transport ProteinsUridine Diphosphate Xylose

Identifiers

PMID25804536
PMCPMC4558686
OpenAlexW2117414049

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.