Evidence map›Paper›PMID 30050548›Full record

ArticleFrontiers in plant science2018

Mapping of Plasma Membrane Proteins Interacting With

Petra Junková, Michal Daněk, Daniela Kocourková, Jitka Brouzdová, Kristýna Kroumanová, Enric Zelazny, Martin Janda, Radovan Hynek, Jan Martinec, Olga Valentová

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Involvement of the Membrane Nanodomain Protein,International journal of molecular sciences · 2023
    Article
  3. Article
  4. Article
  5. Interactome of Arabidopsis Thaliana.Plants (Basel, Switzerland) · 2022
    Article
  6. Review
  7. Article
  8. Flotillin membrane domains in cancer.Cancer metastasis reviews · 2020
    Review
  9. Dynamics and Endocytosis of Flot1 inInternational journal of molecular sciences · 2020
    Article
  10. Article
  11. Review
  12. Article
  13. 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

10 authors at 4 institutions in 2 countries.

Petra JunkováDepartment of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Prague, Czechia.
Michal DaněkInstitute of Experimental Botany of the Czech Academy of Sciences, Prague, Czechia.
Daniela KocourkováInstitute of Experimental Botany of the Czech Academy of Sciences, Prague, Czechia.
Jitka BrouzdováInstitute of Experimental Botany of the Czech Academy of Sciences, Prague, Czechia.
Kristýna KroumanováInstitute of Experimental Botany of the Czech Academy of Sciences, Prague, Czechia.
Enric ZelaznyInstitut de Biologie Intégrative de la Cellule (I2BC), CNRS-CEA-Université Paris Sud, Université Paris-Saclay, Gif-sur-Yvette, France.
Martin JandaDepartment of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Prague, Czechia.
Radovan HynekDepartment of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Prague, Czechia.
Jan MartinecInstitute of Experimental Botany of the Czech Academy of Sciences, Prague, Czechia.
Olga ValentováDepartment of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Prague, Czechia.
Czech Academy of Sciences, Institute of Experimental Botany · CZUniversity of Chemistry and Technology, Prague · CZCharles University · CZUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arabidopsis flotillin 2 (At5g25260) belongs to the group of plant flotillins, which are not well characterized. In contrast, metazoan flotillins are well known as plasma membrane proteins associated with membrane microdomains that act as a signaling hub. The similarity of plant and metazoan flotillins, whose functions most likely consist of affecting other proteins via protein-protein interactions, determines the necessity of detecting their interacting partners in plants. Nevertheless, identifying the proteins that form complexes on the plasma membrane is a challenging task due to their low abundance and hydrophobic character. Here we present an approach for mapping

Indexed as

Arabidopsis flotillin 2immunopurificationintracellular traffickingmass spectrometryplant–pathogen interactionprotein–protein interactionssplit-ubiquitin yeast systemwater transport

Identifiers

PMID30050548
PMCPMC6052134
OpenAlexW2809214902

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.