Quantitative proteome changes in Arabidopsis thaliana suspension-cultured cells in response to plant natriuretic peptides

Handle URI:
http://hdl.handle.net/10754/558855
Title:
Quantitative proteome changes in Arabidopsis thaliana suspension-cultured cells in response to plant natriuretic peptides
Authors:
Turek, Ilona ( 0000-0001-6457-7456 ) ; Wheeler, Janet I.; Gehring, Christoph A. ( 0000-0003-4355-4591 ) ; Irving, Helen R.; Marondedze, Claudius ( 0000-0002-2113-904X )
Abstract:
Proteome changes in the Arabidopsis thaliana suspension cells in response to the A. thaliana plant natriuretic peptide (PNP), AtPNP-A (At2g18660) were assessed using quantitative proteomics employing tandem mass tag (TMT) labeling and tandem mass spectrometry (LC–MS/MS). In this study, we characterized temporal responses of suspension-cultured cells to 1 nM and 10 pM AtPNP-A at 0, 10 and 30 min post-treatment. Both concentrations we found to yield a distinct differential proteome signature. The data shown in this article are associated with the article “Plant natriuretic peptides induce a specific set of proteins diagnostic for an adaptive response to abiotic stress” by Turek et al. (Front. Plant Sci. 5 (2014) 661) and have been deposited to the ProteomeXchange with identifier PXD001386.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Quantitative proteome changes in Arabidopsis thaliana suspension-cultured cells in response to plant natriuretic peptides 2015 Data in Brief
Journal:
Data in Brief
Issue Date:
30-Jun-2015
DOI:
10.1016/j.dib.2015.06.013
Type:
Article
ISSN:
23523409
Additional Links:
http://linkinghub.elsevier.com/retrieve/pii/S2352340915001080
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorTurek, Ilonaen
dc.contributor.authorWheeler, Janet I.en
dc.contributor.authorGehring, Christoph A.en
dc.contributor.authorIrving, Helen R.en
dc.contributor.authorMarondedze, Claudiusen
dc.date.accessioned2015-07-05T12:26:37Zen
dc.date.available2015-07-05T12:26:37Zen
dc.date.issued2015-06-30en
dc.identifier.citationQuantitative proteome changes in Arabidopsis thaliana suspension-cultured cells in response to plant natriuretic peptides 2015 Data in Briefen
dc.identifier.issn23523409en
dc.identifier.doi10.1016/j.dib.2015.06.013en
dc.identifier.urihttp://hdl.handle.net/10754/558855en
dc.description.abstractProteome changes in the Arabidopsis thaliana suspension cells in response to the A. thaliana plant natriuretic peptide (PNP), AtPNP-A (At2g18660) were assessed using quantitative proteomics employing tandem mass tag (TMT) labeling and tandem mass spectrometry (LC–MS/MS). In this study, we characterized temporal responses of suspension-cultured cells to 1 nM and 10 pM AtPNP-A at 0, 10 and 30 min post-treatment. Both concentrations we found to yield a distinct differential proteome signature. The data shown in this article are associated with the article “Plant natriuretic peptides induce a specific set of proteins diagnostic for an adaptive response to abiotic stress” by Turek et al. (Front. Plant Sci. 5 (2014) 661) and have been deposited to the ProteomeXchange with identifier PXD001386.en
dc.relation.urlhttp://linkinghub.elsevier.com/retrieve/pii/S2352340915001080en
dc.rightsArchived with thanks to Data in Brief. Under a Creative Commons license http://creativecommons.org/licenses/by/4.0/en
dc.subjectPlant natriuretic peptideen
dc.subjectQuantitative proteomicsen
dc.subjectPeptide hormone signalingen
dc.subjectPlant homeostasisen
dc.subjectMolecular mimicryen
dc.subjectSalt stressen
dc.subjectReactive oxygen speciesen
dc.titleQuantitative proteome changes in Arabidopsis thaliana suspension-cultured cells in response to plant natriuretic peptidesen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalData in Briefen
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Melbourne, VIC, Australiaen
dc.contributor.institutionCambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, United Kingdomen
kaust.authorTurek, Ilonaen
kaust.authorGehring, Christoph A.en
kaust.authorMarondedze, Claudiusen
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