Evidence map›Paper›PMID 29686160›Full record

ArticlePlant physiology2018

Variable Effects of C-Terminal Fusions on FLS2 Function: Not All Epitope Tags Are Created Equal.

Charlotte H Hurst, Dionne Turnbull, Sally M Myles, Kerry Leslie, Nana F Keinath, Piers A Hemsley

Abstract read
In one paragraph

Article in Plant physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Overexpression ofInternational journal of molecular sciences · 2019
    Article
  5. Article
  6. 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

6 authors.

Charlotte H HurstDivision of Plant Sciences, School of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.
Dionne TurnbullDivision of Plant Sciences, School of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.
Sally M MylesDivision of Plant Sciences, School of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.
Kerry LeslieDivision of Plant Sciences, School of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.
Nana F KeinathDepartment of Plant Developmental Biology, Centre for Organismal Studies, Heidelberg University, 69120 Heidelberg, Germany.
Piers A HemsleyDivision of Plant Sciences, School of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom p.a.hemsley@dundee.ac.uk.ORCID 0000-0003-2950-0634

Funding

Mapping of spatiotemporal code features to neural and perceptual spacesR01NS109961 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI PANZERI, STEFANO VT, RINBERG, DMITRY · 2018 to 2022
$2.4M
Biotechnology and Biological Sciences Research Council BB/M010996/1Biotechnology and Biological Sciences Research Council BB/M024911/1NINDS NIH HHS R01 NS109961
6 · The paper itself

Abstract

Receptor-like kinases (RLKs) are the largest family of proteins in plants and are responsible for perceiving the vast majority of extracellular stimuli. Thus, RLKs function in diverse processes, including sensing pathogen attacks, regulating symbiotic interactions, transducing hormone and peptide signals, and monitoring cell wall status. However, despite their fundamental role in plant biology, very few antibodies are available against RLKs, which necessitates the use of epitope tags and fluorescent protein fusions in biochemical analyses such as immunoblot analysis and intracellular visualization. Epitope tags are widely used and are typically assumed to be benign, with no influence on protein function. FLAGELLIN SENSITIVE2 (FLS2) is the receptor for bacterial flagellin and often is used as a model for RLK function. Previous work implies that carboxyl-terminal epitope fusions to FLS2 maintain protein function. Here, a detailed complementation analysis of Arabidopsis (

Indexed as

ArabidopsisArabidopsis ProteinsEpitopesGenetic Complementation TestMAP Kinase Signaling SystemMutationPlants, Genetically ModifiedProtein KinasesRecombinant Fusion ProteinsSignal TransductionArabidopsis ProteinsEpitopesFLS2 protein, ArabidopsisProtein KinasesRecombinant Fusion Proteins

Identifiers

PMID29686160
PMCPMC6001324

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.