Evidence map›Paper›PMID 23289948›Full record

ArticleCell communication and signaling : CCS2013

Structural and functional characteristics of cGMP-dependent methionine oxidation in Arabidopsis thaliana proteins.

Claudius Marondedze, Ilona Turek, Brian Parrott, Ludivine Thomas, Boris Jankovic, Kathryn S Lilley, Chris Gehring

Open access · goldAbstract read
In one paragraph

Article in Cell communication and signaling : CCS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
6.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 122 citations in OpenAlex.

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  11. Downstream Targets of Cyclic Nucleotides in Plants.Frontiers in plant science · 2018
    Article
  12. Discovery of Novel Functional Centers With Rationally Designed Amino Acid Motifs.Computational and structural biotechnology journal · 2018
    Review
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Claudius MarondedzeDivision of Chemical and Life Sciences and Engineering, King Abdullah University of Science and Technology, Thuwal, 23955-6900, Saudi Arabia. Christoph.Gehring@KAUST.edu.sa.
Ilona Turek
Brian Parrott
Ludivine Thomas
Boris Jankovic
Kathryn S Lilley
Chris Gehring
King Abdullah University of Science and Technology · SAUniversity of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

unlabelled

backgroundIncreasing structural and biochemical evidence suggests that post-translational methionine oxidation of proteins is not just a result of cellular damage but may provide the cell with information on the cellular oxidative status. In addition, oxidation of methionine residues in key regulatory proteins, such as calmodulin, does influence cellular homeostasis. Previous findings also indicate that oxidation of methionine residues in signaling molecules may have a role in stress responses since these specific structural modifications can in turn change biological activities of proteins.

findingsHere we use tandem mass spectrometry-based proteomics to show that treatment of Arabidopsis thaliana cells with a non-oxidative signaling molecule, the cell-permeant second messenger analogue, 8-bromo-3,5-cyclic guanosine monophosphate (8-Br-cGMP), results in a time-dependent increase in the content of oxidised methionine residues. Interestingly, the group of proteins affected by cGMP-dependent methionine oxidation is functionally enriched for stress response proteins. Furthermore, we also noted distinct signatures in the frequency of amino acids flanking oxidised and un-oxidised methionine residues on both the C- and N-terminus.

conclusionsGiven both a structural and functional bias in methionine oxidation events in response to a signaling molecule, we propose that these are indicative of a specific role of such post-translational modifications in the direct or indirect regulation of cellular responses. The mechanisms that determine the specificity of the modifications remain to be elucidated.

Identifiers

PMID23289948
PMCPMC3544604
OpenAlexW2115643744

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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.