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dc.contributor.authorTurek, Ilona
dc.contributor.authorWheeler, Janet I.
dc.contributor.authorGehring, Christoph A
dc.contributor.authorIrving, Helen R.
dc.contributor.authorMarondedze, Claudius
dc.date.accessioned2015-07-05T12:26:37Z
dc.date.available2015-07-05T12:26:37Z
dc.date.issued2015-06-30
dc.identifier.citationQuantitative proteome changes in Arabidopsis thaliana suspension-cultured cells in response to plant natriuretic peptides 2015 Data in Brief
dc.identifier.issn23523409
dc.identifier.pmid26217812
dc.identifier.doi10.1016/j.dib.2015.06.013
dc.identifier.urihttp://hdl.handle.net/10754/558855
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.
dc.publisherElsevier BV
dc.relation.urlhttp://linkinghub.elsevier.com/retrieve/pii/S2352340915001080
dc.rightsArchived with thanks to Data in Brief. Under a Creative Commons license http://creativecommons.org/licenses/by/4.0/
dc.subjectPlant natriuretic peptide
dc.subjectQuantitative proteomics
dc.subjectPeptide hormone signaling
dc.subjectPlant homeostasis
dc.subjectMolecular mimicry
dc.subjectSalt stress
dc.subjectReactive oxygen species
dc.titleQuantitative proteome changes in Arabidopsis thaliana suspension-cultured cells in response to plant natriuretic peptides
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.identifier.journalData in Brief
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Melbourne, VIC, Australia
dc.contributor.institutionCambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom
kaust.personTurek, Ilona
kaust.personGehring, Christoph A
kaust.personMarondedze, Claudius
refterms.dateFOA2018-06-13T14:57:15Z


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