Evidence map›Paper›PMID 34270043›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2021

Phosphorylation Site Motifs in Plant Protein Kinases and Their Substrates.

Lin Xi, Zhaoxia Zhang, Sandra Herold, Sarah Kassem, Xu Na Wu, Waltraud X Schulze

Abstract readReview
PubMed Publisher
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. AUXIN RESPONSE FACTOR protein accumulation and function.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  3. Review
  4. Characterization ofPlants (Basel, Switzerland) · 2023
    Article
  5. Review
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 at 2 institutions in 2 countries.

Lin XiDepartment of Plant Systems Biology, University of Hohenheim, Stuttgart, Germany. lin.xi.260@uni-hohenheim.de.
Zhaoxia ZhangDepartment of Plant Systems Biology, University of Hohenheim, Stuttgart, Germany.
Sandra HeroldDepartment of Plant Systems Biology, University of Hohenheim, Stuttgart, Germany.
Sarah KassemDepartment of Plant Systems Biology, University of Hohenheim, Stuttgart, Germany.
Xu Na WuState Key Laboratory of Conservation and Utilization of Bio-Resources in Yunnan and Center for Life Science, School of Life Sciences, Yunnan University, Kunming, China.
Waltraud X SchulzeDepartment of Plant Systems Biology, University of Hohenheim, Stuttgart, Germany.
University of Hohenheim · DEYunnan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphorylation is an important cellular regulatory mechanism affecting the activity, localization, conformation, and interaction of proteins. Protein phosphorylation is catalyzed by kinases, and thus kinases are the enzymes regulating cellular signaling cascades. In the model plant Arabidopsis, 940 genes encode for kinases. The substrate proteins of kinases are phosphorylated at defined sites, which consist of common patterns around the phosphorylation site, known as phosphorylation motifs. The discovery of kinase specificity with a preference of phosphorylation of certain motifs and application of such motifs in deducing signaling cascades helped to reveal underlying regulation mechanisms, and facilitated the prediction of kinase-target pairs. In this mini-review, we took advantage of retrieved data as examples to present the functions of kinase families along with their commonly found phosphorylation motifs from their substrates.

Indexed as

Amino Acid MotifsArabidopsisHumansPhosphorylationPlant ProteinsPlantsProtein KinasesSignal TransductionSubstrate SpecificityPlant ProteinsProtein KinasesBiological functionKinase familiesPhosphorylationPhosphorylation motifs

Identifiers

PMID34270043
OpenAlexW3182105967

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.