Dataset Information

Maize leaf ESI-Q-TOF MS - Comparative analysis of salt-responsive phosphoproteins in maize leaves using Ti(4+)--IMAC enrichment and ESI-Q-TOF MS

ABSTRACT: Comparative analysis of salt-responsive phosphoproteins in maize leaves using Ti4+-IMAC enrichment and ESI-Q-TOF MS

INSTRUMENT(S): Synapt MS

ORGANISM(S): Zea Mays (maize)

TISSUE(S): Leaf

SUBMITTER: Yufeng Hu

LAB HEAD: Yufeng Hu

PROVIDER: PXD000027 | Pride | 2012-12-14

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	PRIDE_Exp_Complete_Ac_27239.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_27239.pride.mztab.gz	Mztab
	PRIDE_Exp_Complete_Ac_27239.xml.gz	Xml
	PRIDE_Exp_Complete_Ac_27240.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_27240.pride.mztab.gz	Mztab

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Publications

Comparative analysis of salt-responsive phosphoproteins in maize leaves using Ti(4+)--IMAC enrichment and ESI-Q-TOF MS.

Hu Yufeng Y Guo Shuangxi S Li Xuexian X Ren Xueqin X

Electrophoresis 20130122 4

Salinity is one of the most common abiotic stresses encountered by plants. Reversible protein phosphorylation is involved in plant defense processes against salinity stress. Here, we performed global phosphopeptide mapping through enrichment by our synthesized PVA-phosphate-Ti(4+) IMAC coupled with subsequent identification by ESI-Q-TOF MS. A total of 104 peptide sequences containing 139 phosphorylation sites were determined from 70 phosphoproteins of the control leaves. In contrast, 124 phosph ...[more]

PMID: 23172588

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