Evidence map›Paper›PMID 37665460›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Targeted Profiling of Protein Phosphorylation in Plants.

Xiangyu Xu, Kris Gevaert, Ive De Smet, Lam Dai Vu

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

4 authors.

Xiangyu XuGhent University, Department of Plant Biotechnology and Bioinformatics, Ghent, Belgium.
Kris GevaertVIB-UGent Center for Medical Biotechnology, Ghent, Belgium.
Ive De SmetGhent University, Department of Plant Biotechnology and Bioinformatics, Ghent, Belgium. ive.desmet@psb.vib-ugent.be.
Lam Dai VuGhent University, Department of Plant Biotechnology and Bioinformatics, Ghent, Belgium.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are crucial for controlling different cellular processes by perceiving and converting external environmental cues into cellular responses. Therefore, regulation of protein activities is pivotal for the development and survival of an organism. This is often mediated by posttranslational modifications, which usually are carried out on specific residues of a target protein by a "writer" protein. The (reversible) modifications of different residues may lead to different signaling outputs. In the case of protein phosphorylation, one of the most common posttranslational modifications, this writer protein is a protein kinase. In this chapter, we report a comprehensive and versatile workflow to identify the phosphorylation profile of a target protein in plants from a putative kinase-target pair by combining an in planta phosphorylation assay and mass spectrometry analysis.

Indexed as

Biological AssayProtein Processing, Post-TranslationalCuesMass SpectrometryPhosphorylationIn vivo phosphorylationKinase assayMass spectrometryPlant protein kinaseTransient protein expression

Identifiers

PMID37665460

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.