Comprehensive profiling of lysine acetylation suggests the widespread function is regulated by protein acetylation in the silkworm, Bombyx mori

Lysine acetylation in proteins is a dynamic and reversible PTM and plays an important role in diverse cellular processes. In this study, using lysine‐acetylation (Kac) peptide enrichment coupled with nano HPLC/MS/MS, we initially identified the acetylome in the silkworms. Overall, a total of 342 ace...

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Veröffentlicht in:	Proteomics (Weinheim) 2015-09, Vol.15 (18), p.3253-3266
Hauptverfasser:	Nie, Zuoming, Zhu, Honglin, Zhou, Yong, Wu, Chengcheng, Liu, Yue, Sheng, Qing, Lv, Zhengbing, Zhang, Wenping, Yu, Wei, Jiang, Caiying, Xie, longfei, Zhang, Yaozhou, Yao, Juming
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylation Amino acids Animal proteomics Animals Biological activity Bombyx - metabolism Bombyx mori Chromatography, High Pressure Liquid Enrichment Functional analysis High-performance liquid chromatography Insect Proteins - analysis Insect Proteins - chemistry Insect Proteins - metabolism Insects Lepidoptera Liquid chromatography Lysine Lysine - analysis Lysine - chemistry Lysine - metabolism Lysine acetylation Nutrient utilization Nutrient-storage proteins Proteins Proteome - analysis Proteome - chemistry Proteome - metabolism Proteomics Regulation Regulatory mechanisms (biology) Ser2 proteins Silk Silkworms Storage proteins Substrates Tandem Mass Spectrometry Vitellogenin
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