Label-free quantitative phosphoproteomic profiling of cellular response induced by an insect cytokine paralytic peptide

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• 作者：Liang Song¹ ; ^{songliang308@126.com} ; Fei Wang¹ ; ^{fwangswu@gmail.com} ; Zhaoming Dong ^{dong-zhaoming@163.com} ; Xiaoting Hua ^{huaxiaotingswu@126.com} ; Qingyou Xia ; ^{xiaqy@swu.edu.cn}
• 关键词：PP ; Paralytic peptide ; LC-MS/MS ; liquid chromatography-tandem mass spectrometry ; TFs ; transcription factors ; PKs ; protein kinases ; KEGG ; Kyoto Encyclopedia of Genes and Genomes ; MAPK ; mitogen-activated protein kinase ; PAK ; p21-activated kinase ; GBP ; growth-blocking peptide ; PSP ; plasmatocyte spreading peptide ; AMPs ; anti-microbial peptides ; JNK ; c-Jun terminal kinases ; p38 MAPK ; p38 mitogen-activated protein kinase ; PBS ; phosphate buffered saline ; IAA ; iodoacetamide ; DTT ; dithiotreitol ; TiO2 ; ti
• 刊名：Journal of Proteomics
• 出版年：2017
• 出版时间：10 February 2017
• 年：2017
• 卷：154
• 期：Complete
• 页码：49-58
• 全文大小：1455 K
• 卷排序：154

文摘

Some new phosphorylation targets of PP-stimulation were identified. Phosphorylation cascades play the crucial regulation roles in PP-dependent signaling pathways. The potential central position of the MAPKs was highlighted in PP-dependent signaling pathways.