Gly-PseAAC: Identifying protein lysine glycation through sequences.

	Gly-PseAAC: Identifying protein lysine glycation through sequences.
	Zhou, Fengfeng; Mai, Guoqin; Wu, Ling-Yun; Ding, Jun; Li, Li; Xu, Yan
刊名	GENE
	2017
文献子类	期刊论文
英文摘要	Background: Similar to the regular enzymatic glycosylation, glycation also attaches a sugar molecule to a peptide, but does not need the help of an enzyme. Glycation may occur both inside and outside the host body, and will compete with the glycosylation procedure for functional regulation of mature protein products. The glycated residues do not show significant patterns, which make both in silico sequence-level predictors and wet-lab validations a major challenge. This study hypothesizes that a better feature set formulated from the glycated flanking peptides may lead to a good glycation prediction program.
URL标识	查看原文
语种	英语
内容类型	期刊论文
源URL	[http://ir.siat.ac.cn:8080/handle/172644/12322]
专题	深圳先进技术研究院_医药所
作者单位	GENE
推荐引用方式 GB/T 7714	Zhou, Fengfeng,Mai, Guoqin,Wu, Ling-Yun,et al. Gly-PseAAC: Identifying protein lysine glycation through sequences.[J]. GENE,2017.
APA	Zhou, Fengfeng,Mai, Guoqin,Wu, Ling-Yun,Ding, Jun,Li, Li,&Xu, Yan.(2017).Gly-PseAAC: Identifying protein lysine glycation through sequences..GENE.
MLA	Zhou, Fengfeng,et al."Gly-PseAAC: Identifying protein lysine glycation through sequences.".GENE (2017).