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6篇 您的检索式：作者名="HU Lianghai"

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		题名	作者	年代	出处	被引量
	1	Protein target discovery of drug and its reactive intermediate metabolite by using proteomic strategy显示文摘Identifying protein targets of bioactive compounds is an effective approach to discover unknown protein functions,identify molecular mechanisms of drug action,and obtain information for optimization of lead compounds.At the same time,metabolic activation of a drug can lead to cytotoxicities.Therefore,it is very important to systemically characterize the drug and its reactive intermediate.Mass spectrometry-based proteomic approach has emerged as the most efficient to study protein functions and modifications.This review will discuss method development for the drug target discovery and the application in different fields including the drug toxicity mechanism caused by reactive metabolites.	Lianghai Hu John Paul Fawcett Jingkai Gu	2012	Acta Pharmaceutica Sinica B2012，2，2：	2
	2	Analysis of the endogenous human serum peptides by on-line extraction with restricted-access material and HPLC-MS/MS identification显示文摘	Lianghai Hu Karl-Siegfried Boos Mingliang Ye Hanfa Zou	2014	Talanta2014，，：	1
	3	Determination of phenolic compounds in river water with on-line coupling bisphenol A imprinted monolithic precolumn with high perfor-mance liquid chromatography显示文摘	OU Junjie HU Lianghai HU Ligang	2006	Talanta2006，69，4：	1
	4	Profiling of endogenous serum phosphorylated peptides by titanium (Ⅳ) immobilized mesoporous silica particles enrichment and MALDI-TOFMS detection 显示文摘	HU Lianghai ZHOU Houjiang LI Yinghua	2008	Analytical Chemistry2008，81，1：	1
	5	Biological fingerprinting analysis of the traditional Chinese prescription Longdan Xiegan Decoction by on/off-line comprehensive two-dimensional biochromatography显示文摘	Yun Wang Liang Kong Lianghai Hu Xiaoyuan Lei Li Yang Guixin Chou Hanfa Zou Changhong Wang S.W. Annie Bligh Zhengtao Wang	2007	Journal of Chromatography B2007，，2：	1
	6	Comprehensive analysis of the N and C terminus of endogenous serum peptides reveals a highly conserved cleavage site pattern derived from proteolytic enzymes显示文摘The human serum proteome is closely associated with the state of the body.Endogenous peptides derived from proteolytic enzymes cleaving on serum proteins are widely studied due to their potential application in disease-specific marker discovery.However,the reproducibility of peptidome analysis of endogenous peptides is significantly influenced by the proteolytic enzymes within body fluids,thereby limiting the clinical use of the endogenous peptides.We comprehensively investigated the N and C terminus of endogenous peptides using peptidomics.The cleavage site patterns of the N and C terminus and adjacent sites from all the identified endogenous peptides were highly conserved under different sample preparation conditions,including long-term incubation at 37℃ and pretreatment with repeated freeze-thaw cycles.Furthermore,a distinguishable cleavage site pattern was obtained when a different disease serum was analyzed.The conserved cleavage site pattern derived from proteolytic enzymes holds potential in highly specific disease diagnosis.	Fangjun Wang Jun Zhu Lianghai Hu Hongqiang Qin Mingliang Ye Hanfa Zou	2012	Protein & Cell2012，3，9：	0

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