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Articles by Wei Zhao
Total Records ( 5 ) for Wei Zhao
  Yongming Liu , Nan Xia , Wanying Hu and Wei Zhao
  Background and Objectives: Ezetimibe/simvastatin and rosuvastatin drugs are two effective lipid-lowering therapies for hypercholesterolemic patients. However, whether the effect of ezetimibe/simvastatin is superior to rosuvastatin is is still controversial. Therefore, the purpose of this study was to compare the efficacy between ezetimibe/simvastatin and rosuvastatin for hypercholesterolemia treatment by a meta-analysis. Materials and Methods: Based on the predefined searching strategy and selection criteria, the eligible studies were selected. The quality of included study was evaluated using Cochrane Collaboration’s tool. The out come assessments indexes including low-density lipoprotein cholesterol (LDL-C), high density lipoprotein cholesterin (HDL-C), total cholesterin (Total C), triglycerides (TG) and apolipoprotein B (Apo B) were analyzed. In addition, the sub-group analysis was performed for comparing the efficacy of two groups with different dosages and sensitivity analysis was performed. Results: Totally, six studies were collected in the present study. The quality of the included studies were relatively high. Ezetimibe/simvastatin might result in greater LDL-C, Total C, TG and Apo B reductions than rosuvastatin for hypercholesterolemia. In addition, compared with 10 mg/day rosuvastatin, 10/20 mg/day ezetimibe/simvastatin had a better clinical efficacy in lipid-lowering of LDL-C, Total C, TG and Apo B. Moreover, no obvious changes of lipid-altering were observed between the rosuvastatin 40 mg/day and ezetimibe/simvastatin 10/40 mg/day. Conclusion: Ezetimibe/simvastatin was recommended to administrate hypercholesterolemia for providing greater reductions of LDL-C, Total C, TG and Apo B than rosuvastatin. Ezetimibe/simvastatin 10/20 mg/day had a better clinical efficacy than rosuvastatin 10 mg/day, while ezetimibe/simvastatin 10/40 mg/day had the same lipid-lowering than rosuvastatin 40 mg/day.
  Edi Erwan , Vebera Maslami , Elvy Chardila , Yulia Despika , Khalidah M. Noer Harahap , Hermawan , Zhefeng Li , Qianyun Zhang and Wei Zhao
  Background and Objective: An abundant studies show that leucine (Leu) acts as an anabolic agent that stimulates skeletal muscle growth in human as well as in animals. However, the effect of encapsulated leucine (CL) supplementation on growth performance of broiler chickens has not been evaluated. Therefore, the aim of this study was to determine initial metabolic responses to CL supplementation on food intake, plasma metabolites and branched chain amino acid concentration in 7-day-old broiler chicks. Materials and Methods: A total of 24 chicks were randomly assigned to the following treatments: (1) Control 4 h (C), (2) Free leucine 4h (L) and (3) Encapsulated-leucine 4h (CL). After 6 h of fasting, chicks were given a bolus of oral injection of distilled water, free leucine (6 mmol/10 mL kg1 BW) or encapsulated-leucine (6 mmol/10 mL kg1 BW). Immediately after the injection, chicks were allowed free access to a commercial starter diet for 1 h. Blood collections were obtained 4 h after the oral injection. Food intake, total glucose, total cholesterol, triacylglycerol, plasma leucine levels and the activity of glutamic oxaloacetic transaminase (GOT) were measured. Results: Food intake, glucose, total cholesterol and triacylglycerol levels were not affected by Leu supplementation. At 4 h, GOT levels were greater (p<0.05) in the CL group than that of the Leu groups. At 4 h, although plasma Leu levels were similar in all groups, Valine levels were lower (p<0.005) in the C and CL groups than that of the Leu group and isoleucine levels were lower (p<0.001) in the CL group than that of the C and Leu groups. Conclusion: The results of this study suggest that an oral administration of CL caused prolonged leucine-induced anabolic effects that may be beneficial for growth. Our observations also pave the way for studying the long-term effects of CL supplementation on performance of broiler chicks.
  Wei Zhao , Peter Langfelder , Tova Fuller , Jun Dong , Ai Li and Steve Hovarth
  Weighted gene coexpression network analysis (WGCNA) has been applied to many important studies since its introduction in 2005. WGCNA can be used as a data exploratory tool or as a gene screening method; WGCNA can also be used as a tool to generate testable hypothesis for validation in independent data sets. In this article, we review key concepts of WGCNA and some of its applications in gene expression analysis of oncology, brain function, and protein interaction data.
  Pascal Loyer , Janeen H. Trembley , Jose A. Grenet , Adeline Busson , Anne Corlu , Wei Zhao , Mehmet Kocak , Vincent J. Kidd and Jill M. Lahti
  Although it has been reported that cyclin L1α and L2α proteins interact with CDK11p110, the nature of the cyclin L transcripts, the formation of complexes between the five cyclin L and the three CDK11 protein isoforms, and the influence of these complexes on splicing have not been thoroughly investigated. Here we report that cyclin L1 and L2 genes generate 14 mRNA variants encoding six cyclin L proteins, one of which has not been described previously. Using cyclin L gene-specific antibodies, we demonstrate expression of multiple endogenous cyclin L proteins in human cell lines and mouse tissues. Moreover, we characterize interactions between CDK11p110, mitosis-specific CDK11p58, and apoptosis-specific CDK11p46 with both cyclin Lα and -β proteins and the co-elution of these proteins following size exclusion chromatography. We further establish that CDK11p110 and associated cyclin Lα/β proteins localize to splicing factor compartments and nucleoplasm and interact with serine/arginine-rich proteins. Importantly, we also determine the effect of CDK11-cyclin L complexes on pre-mRNA splicing. Preincubation of nuclear extracts with purified cyclin Lα and -β isoforms depletes the extract of in vitro splicing activity. Ectopic expression of cyclin L1α, L1β, L2α, or L2β or active CDK11p110 individually enhances intracellular intron splicing activity, whereas expression of CDK11p58/p46 or kinase-dead CDK11p110represses splicing activity. Finally, we demonstrate that expression of cyclins Lα and -β and CDK11p110 strongly and differentially affects alternative splicing in vivo. Together, these data establish that CDK11p110 interacts physically and functionally with cyclin Lα and -β isoforms and SR proteins to regulate splicing.
  Kenjiro Ono , Margaret M. Condron , Lap Ho , Jun Wang , Wei Zhao , Giulio M. Pasinetti and David B. Teplow
  Epidemiological evidence suggests that moderate consumption of red wine reduces the incidence of Alzheimer disease (AD). To study the protective effects of red wine, experiments recently were executed in the Tg2576 mouse model of AD. These studies showed that a commercially available grape seed polyphenolic extract, MegaNatural-AZ (MN), significantly attenuated AD-type cognitive deterioration and reduced cerebral amyloid deposition (Wang, J., Ho, L., Zhao, W., Ono, K., Rosensweig, C., Chen, L., Humala, N., Teplow, D. B., and Pasinetti, G. M. (2008) J. Neurosci. 28, 6388–6392). To elucidate the mechanistic bases for these observations, here we used CD spectroscopy, photo-induced cross-linking of unmodified proteins, thioflavin T fluorescence, size exclusion chromatography, and electron microscopy to examine the effects of MN on the assembly of the two predominant disease-related amyloid β-protein alloforms, Aβ40 and Aβ42. We also examined the effects of MN on Aβ-induced cytotoxicity by assaying 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide metabolism and lactate dehydrogenase activity in Aβ-treated, differentiated pheochromocytoma (PC12) cells. Initial studies revealed that MN blocked Aβ fibril formation. Subsequent evaluation of the assembly stage specificity of the effect showed that MN was able to inhibit protofibril formation, pre-protofibrillar oligomerization, and initial coil → α-helix/β-sheet secondary structure transitions. Importantly, MN had protective effects in assays of cytotoxicity in which MN was mixed with Aβ prior to peptide assembly or following assembly and just prior to peptide addition to cells. These data suggest that MN is worthy of consideration as a therapeutic agent for AD.
 
 
 
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