Evidence map›Paper›PMID 32690719›Full record

ArticleThe Plant cell2020

SEIPIN Isoforms Interact with the Membrane-Tethering Protein VAP27-1 for Lipid Droplet Formation.

Michael Scott Greer, Yingqi Cai, Satinder K Gidda, Nicolas Esnay, Franziska K Kretzschmar, Damien Seay, Elizabeth McClinchie, Till Ischebeck, Robert T Mullen, John M Dyer and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 62 citations in OpenAlex.

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  17. Review
  18. Seipin-still a mysterious protein?Frontiers in cell and developmental biology · 2023
    Review
  19. Article
  20. Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

11 authors at 3 institutions in 2 countries.

Michael Scott GreerDepartment of Biological Sciences, BioDiscovery Institute, University of North Texas, Denton, Texas 76203.ORCID 0000-0002-0608-9531
Yingqi CaiDepartment of Biological Sciences, BioDiscovery Institute, University of North Texas, Denton, Texas 76203.ORCID 0000-0002-0357-5809
Satinder K GiddaDepartment of Molecular Cell Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.ORCID 0000-0002-4722-0006
Nicolas EsnayDepartment of Biological Sciences, BioDiscovery Institute, University of North Texas, Denton, Texas 76203.ORCID 0000-0002-2477-8306
Franziska K KretzschmarAlbrecht-von-Haller-Institute for Plant Sciences and Goettingen Center for Molecular Biosciences (GZMB), Department of Plant Biochemistry, University of Goettingen, Justus-von-Liebig Weg 11, 37077 Goettingen, Germany.ORCID 0000-0001-8875-6336
Damien SeayU.S. Department of Agriculture-Agricultural Research Service, U.S. Arid-Land Agricultural Research Center, Maricopa, Arizona 85138.ORCID 0000-0003-3869-6325
Elizabeth McClinchieDepartment of Biological Sciences, BioDiscovery Institute, University of North Texas, Denton, Texas 76203.ORCID 0000-0001-8508-6947
Till IschebeckAlbrecht-von-Haller-Institute for Plant Sciences and Goettingen Center for Molecular Biosciences (GZMB), Department of Plant Biochemistry, University of Goettingen, Justus-von-Liebig Weg 11, 37077 Goettingen, Germany.ORCID 0000-0003-0737-3822
Robert T MullenDepartment of Molecular Cell Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.ORCID 0000-0002-6915-7407
John M DyerU.S. Department of Agriculture-Agricultural Research Service, U.S. Arid-Land Agricultural Research Center, Maricopa, Arizona 85138.ORCID 0000-0001-6215-0053
Kent D ChapmanDepartment of Biological Sciences, BioDiscovery Institute, University of North Texas, Denton, Texas 76203 chapman@unt.edu.ORCID 0000-0003-0489-3072
University of North Texas · USAgricultural Research Service · USUniversity of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SEIPIN proteins are localized to endoplasmic reticulum (ER)-lipid droplet (LD) junctions where they mediate the directional formation of LDs into the cytoplasm in eukaryotic cells. Unlike in animal and yeast cells, which have single SEIPIN genes, plants have three distinct SEIPIN isoforms encoded by separate genes. The mechanism of SEIPIN action remains poorly understood, and here we demonstrate that part of the function of two SEIPIN isoforms in Arabidopsis (

Indexed as

ArabidopsisArabidopsis ProteinsEndoplasmic ReticulumLipid DropletsNicotianaPhylogenyPlant CellsPlants, Genetically ModifiedProtein DomainsR-SNARE ProteinsSeedsTwo-Hybrid System TechniquesArabidopsis ProteinsAt3g60600 protein, ArabidopsisR-SNARE Proteins

Identifiers

PMID32690719
PMCPMC7474298
OpenAlexW3044761442

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.