Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Oryza Sativa (rice)
TISSUE(S): Leaf
SUBMITTER: Iris Finkemeier
LAB HEAD: Prof. Iris Finkemeier
PROVIDER: PXD007175 | Pride | 2018-07-23
REPOSITORIES: Pride
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2017_Oryza_KSuc_Fr1.raw | Raw | |||
2017_Oryza_KSuc_Fr2.raw | Raw | |||
2017_Oryza_KSuc_Fr3.raw | Raw | |||
2017_Oryza_KSuc_Fr4.raw | Raw | |||
2017_Oryza_KSuc_Fr5.raw | Raw |
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Zhou Heng H Finkemeier Iris I Guan Wenxue W Tossounian Maria-Armineh MA Wei Bo B Young David D Huang Jingjing J Messens Joris J Yang Xibin X Zhu Jun J Wilson Michael H MH Shen Wenbiao W Xie Yanjie Y Foyer Christine H CH
Plant, cell & environment 20180109 5
Protein lysine acylations, such as succinylation and acetylation, are important post-translational modification (PTM) mechanisms, with key roles in cellular regulation. Antibody-based affinity enrichment, high-resolution liquid chromatography mass spectrometry analysis, and integrated bioinformatics analysis were used to characterize the lysine succinylome (K<sub>suc</sub> ) and acetylome (K<sub>ace</sub> ) of rice leaves. In total, 2,593 succinylated and 1,024 acetylated proteins were identifie ...[more]