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Articles by Xiaodong Zhang
Total Records ( 4 ) for Xiaodong Zhang
  Yinghui Ling , Lijuan Wang , Xiaodong Zhang , Lina Xu , Jian-Ping Ding , Yun-Hai Zhang , Zijun Zhang and Xiao-Rong Zhang
  This study is about the correlation between COX II gene genetic variation and adult buck sperm motility traits, to provide genetics reference for the goat breeding. In this study, 120 adult male goat semen samples were collected from four populations. COX II gene polymorphism information was rapid screened using DNA pool and sequencing method. Each individual polymorphism of these goats was detected by RFLP. Sequencing results of DNA pool showed a single nucleotide mutation in COX II gene (A→G). The mutation caused a change of Hind III restriction site. RFLP results showed that the mutation associated with goat sperm traits. The vitality of fresh sperm and frozen sperm from BB-type goats was significantly higher than AA-type. This study provided foundation for establishment relationship between COX II gene SNP and goat sperm motility traits. It could be considered as a reference marker-assisted selection for buck semen quality traits and goat breeding.
  Jin Wang , Xiaodong Zhang , Shuo Zhang and Yingzi Li
  Open source design is a new mode which is composed of many agents who spontaneously cooperate to complete product design. A process model of open source design based on multi-agent is proposed in this paper with the purpose of studying the dynamic characteristics of product evolution and the ability of design-agent in the process of product design. A set of indexes which can evaluate the process of product evolution and the ability of agent is developed, including the weight of each module, product maturity, completion time of module for each agent and development ability of the agent. The algorithms of indexes are realized and verified in the simulation program. The simulation results show that the proposed simulation approach and evaluation indexes are effective for evaluation and management of open source design.
  Louise C. Briggs , Geoff S. Baldwin , Non Miyata , Hisao Kondo , Xiaodong Zhang and Paul S. Freemont
  p97, an essential chaperone in endoplasmic reticulum-associated degradation and organelle biogenesis, contains two AAA domains (D1 and D2) and assembles as a stable hexamer. We present a quantitative analysis of nucleotide binding to both D1 and D2 domains of p97, the first detailed study of nucleotide binding to both AAA domains for this type of AAA+ ATPase. We report that adenosine 5’-O-(thiotriphosphate) (ATPγS) binds with similar affinity to D1 and D2, but ADP binds with higher affinity to D1 than D2, offering an explanation for the higher ATPase activity in D2. Stoichiometric measurements suggest that although both ADP and ATPγS can saturate all 6 nucleotide binding sites in D1, only 3–4 of the 6 D2 sites can bind ATPγS simultaneously. ATPγS binding triggers a downstream cooperative conformational change of at least three monomers, which involves conserved arginine fingers and is necessary for ATP hydrolysis.
  Karen L. Murphy , Xiaodong Zhang , Raul R. Gainetdinov , Jean-Martin Beaulieu and Marc G. Caron
  Serotonin is involved in a variety of physiological processes in the central nervous system and the periphery. As the rate-limiting enzyme in serotonin synthesis, tryptophan hydroxylase plays an important role in modulating these processes. Of the two variants of tryptophan hydroxylase, tryptophan hydroxylase 2 (TPH2) is expressed predominantly in the central nervous system, whereas tryptophan hydroxylase 1 (TPH1) is expressed mostly in peripheral tissues. Although the two enzymes share considerable sequence homology, the regulatory domain of TPH2 contains an additional 41 amino acids at the N terminus that TPH1 lacks. Here we show that the extended TPH2 N-terminal domain contains a unique sequence involved in the regulation of enzyme expression. When expressed in cultured mammalian cells, TPH2 is synthesized less efficiently and is also less stable than TPH1. Removal of the unique portion of the N terminus of TPH2 results in expression of the enzyme at a level similar to that of TPH1, whereas protein chimeras containing this fragment are expressed at lower levels than their wild-type counterparts. We identify a region centered on amino acids 10–20 that mediates the bulk of this effect. We also demonstrate that phosphorylation of serine 19, a protein kinase A consensus site located in this N-terminal domain, results in increased TPH2 stability and consequent increases in enzyme output in cell culture systems. Because this domain is unique to TPH2, these data provide evidence for selective regulation of brain serotonin synthesis.
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