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| 1 | The M Protein of SARS-CoV: Basic Structural and Immunological Properties显示文摘We studied structural and immunological properties of the SARS-CoV M (mem-brane) protein, based on comparative analyses of sequence features, phylogeneticinvestigation, and experimental results. The M protein is predicted to contain atriple-spanning transmembrane (TM) region, a single N-glycosylation site near itsN-terminus that is in the exterior of the virion, and a long C-terminal region inthe interior. The M protein harbors a higher substitution rate (0.6% correlated toits size) among viral open reading frames (ORFs) from published data. The foursubstitutions detected in the M protein, which cause non-synonymous changes,can be classified into three types. One of them results in changes of pI (isoelectricpoint) and charge, affecting antigenicity. The second changes hydrophobicity of theTM region, and the third one relates to hydrophilicity of the interior structure.Phylogenetic tree building based on the variations of the M protein appears tosupport the non-human origin of SARS-CoV. To investigate its immunogenicity,we synthesized eight oligopeptides covering 69.2% of the entire ORF and screenedthem by using ELISA (enzyme-linked immunosorbent assay) with sera from SARSpatients. The results confirmed our predictions on antigenic sites. | JunWang SiqiLiu ChangqingZeng JianWang HuanmingYang YongwuHu JieWen LinTang HaijunZhang XiaoweiZhang YahLi JingWang YujunHan GuoqingLi JianpingShi XiangjunTian FengJiang XiaoqianZhao | 2003 | Genomics, Proteomics & Bioinformatics2003，1，2： | 1 |
| 2 | Activated RSC–Nucleosome Complex and Persistently Altered Form of the Nucleosome显示文摘 | Yahli Lorch Bradley R Cairns Mincheng Zhang Roger D Kornberg | 1998 | Cell1998，，： | 1 |
| 3 | A Simple Method for Depletion High-abundant Proteins and Enriching Specific Proteins for Human Proteomic Analysis显示文摘 | Yun-ShanNING YahLI Cao-LingLUO NingLI Yun-DanWANG Fu-ChuHE Qi-HongSUN MingLI | 2004 | Acta Biochimica et Biophysica Sinica2004，36，1： | 0 |
| 4 | The R Protein of SARS-CoV: Analyses of Structure and Function Based on Four Complete Genome Sequences of Isolates BJ01-BJ04显示文摘The R (replicase) protein is the uniquely defined non-structural protein (NSP)responsible for RNA replication, mutation rate or fidelity, regulation of transcrip-tion in coronaviruses and many other ssRNA viruses. Based on our completegenome sequences of four isolates (BJ01-BJ04) of SARS-CoV from Beijing, China,we analyzed the structure and predicted functions of the R protein in comparisonwith 13 other isolates of SARS-CoV and 6 other coronaviruses. The entire ORF(open-reading frame) encodes for two major enzyme activities, RNA-dependentRNA polymerase (RdRp) and proteinase activities. The R polyprotein under-goes a complex proteolytic process to produce 15 function-related peptides. Ahydrophobic domain (HOD) and a hydrophilic domain (HID) are newly identifiedwithin NSP1. The substitution rate of the R protein is close to the average ofthe SARS-CoV genome. The functional domains in all NSPs of the R proteingive different phylogenetic results that suggest their different mutation rate underselective pressure. Eleven highly conserved regions in RdRp and twelve cleavagesites by 3CLP (chymotrypsin-like protein) have been identified as potential drugtargets. Findings suggest that it is possible to obtain information about the phy-logeny of SARS-CoV, as well as potential tools for drug design, genotyping anddiagnostics of SARS. | HaiyanSun XiaoweiZhang JunZhow SonggangLi JunWang JianWang ShenghBi HuanmingYang ZuyuanXu HaiqingZhang XiangjunTian JiaJi WeiLi YahLi WeiTian LiftWang ZizhangZhang JingXu WeiWei JinguiZhu | 2003 | Genomics, Proteomics & Bioinformatics2003，1，2： | 0 |
| 5 | Microdetermination of Residual Protein in Penicillin by Resonance Light Scattering Technique with m-Nitrophenylfluorone-Mo(Ⅳ) Complex显示文摘Based on the enhancement of resonance light scattering (RLS) of m-nitrophenylfluorone-Mo(Ⅵ) complex by protein, a novel method for protein microdetermination in Tween 20microemulsion has been developed. Under optimum condition, the linear ranges of bovine serum albumin are 0 ~ 0.03 μg.mL-1 with detection limits of 3.10 ng.mL-1. Most of amino acids and metal ions do not interfere. The method can be applied to determination of residual protein in penicillin Na salt and penicillin G potassium salt samples with satisfactory results. | QinWEI DanWU YahLI JunHongWANG YanLIU BinBU | 2005 | Chinese Chemical Letters2005，16，6： | 0 |
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