Asian Science Citation Index is committed to provide an authoritative, trusted and significant information by the coverage of the most important and influential journals to meet the needs of the global scientific community.  
ASCI Database
308-Lasani Town,
Sargodha Road,
Faisalabad, Pakistan
Fax: +92-41-8815544
Contact Via Web
Suggest a Journal
Articles by Yuan-Yuan Zhang
Total Records ( 3 ) for Yuan-Yuan Zhang
  Feng Tang , Hong-Lin Ren , Yun-Ming Xu , De-Ying Zou , Nan-Nan Liu , Yan-Song Li , Yu Zhou , Jie Song , Zhao-Hui Li , Yuan-Yuan Zhang , Shi-Ying Lu and Zeng-Shan Liu
  Brucellosis is a zoonosis which is caused by Brucella species and pruduces severe economic losses and a public health problem. At present, the diagonsis of Brucella infection mainly depends on serological tests to detect antibodies in sera and the animal brucellosis is prevented via vaccine. In this study, the kinetics and cross-reactivity of antibodies in sera were evaluated in Small Tail Han sheep (Ovis arie) infected with a virulent field strain of Brucella melitensis (BmF) and ones inoculated with a vaccine strain S2 of B. suis under laboratory conditions. Serum samples were collected at 0, 3, 7, 14, 21, 30, 40, 44, 50, 60 and 75 days post-challenge (dpc) and were analyzed by Rose Bengal Plate Agglutination Test (RBPT) and indirect Enzyme-Linked Immunosorbent Assay (iELISA). Sera samples of BmF-challenged and S2-challenged sheep groups at 40, 44, 50, 60 and 75 dpc were tested positive to Brucella by the RBPT, nevertheless the earliest positive reaction results were observed in sera at 21 dpc by iELISA. The virulent field strain BmF initiated a higher level of antibody titer than vaccine strain S2 without statistic significant difference (p>0.05). The cross-reactivities with the virulent and the vaccine stains were confirmed in serum antibodies between the BmF-challenged group and the S2-challenged group. The results indicated that the serodiagnosis is hard to distinguish the brucella-infected sheep from the vaccine-inoculated sheep. Diagnosis methods of identifying between the healthy and the infected animals need to further be studied in future.
  Xiao-Hui Yu , Yuan-Yuan Zhang , Na Tang , Li-Li Zhao and Guo-Zhong Zhang
  A recombinant Herpes Virus of Turkeys (HVT) vaccine expressing the key protective antigen of Newcastle Disease Virus (NDV) could facilitate in the prevention and control of both Marek’s Disease Virus (MDV) and NDV infections. The VECTORMUNE® HVT NDV vaccine is a recombinant vaccine in which the F gene of a NDV lentogenic strain has been inserted into the HVT genome. In the current study, this vaccine was assessed for its safety in chickens. Based on clinical observations, gross pathological examinations, histopathological examinations, virus shedding and tissue distribution, the VECTORMUNE® HVT NDV vaccine was determined to possess a high level of safety in chickens.
  Yuan-Yuan Zhang , Zi-Qing Mei , Jia-Wei Wu and Zhi-Xin Wang
  The mitogen-activated protein (MAP) kinases are essential signaling molecules that mediate many cellular effects of growth factors, cytokines, and stress stimuli. Full activation of the MAP kinases requires dual phosphorylation of the Thr and Tyr residues in the TXY motif of the activation loop by MAP kinase kinases. Down-regulation of MAP kinase activity can be initiated by multiple serine/threonine phosphatases, tyrosine-specific phosphatases, and dual specificity phosphatases (MAP kinase phosphatases). This would inevitably lead to the formation of monophosphorylated MAP kinases. However, the biological functions of these monophosphorylated MAP kinases are currently not clear. In this study, we have prepared MAP kinase p38α, a member of the MAP kinase family, in all phosphorylated forms and characterized their biochemical properties. Our results indicated the following: (i) p38α phosphorylated at both Thr-180 and Tyr-182 was 10–20-fold more active than p38α phosphorylated at Thr-180 only, whereas p38α phosphorylated at Tyr-182 alone was inactive; (ii) the dual-specific MKP5, the tyrosine-specific hematopoietic protein-tyrosine phosphatase, and the serine/threonine-specific PP2Cα are all highly specific for the dephosphorylation of p38α, and the dephosphorylation rates were significantly affected by different phosphorylated states of p38α; (iii) the N-terminal domain of MPK5 has no effect on enzyme catalysis, whereas deletion of the MAP kinase-binding domain in MKP5 leads to a 370-fold decrease in kcat/Km for the dephosphorylation of p38α. This study has thus revealed the quantitative contributions of phosphorylation of Thr, Tyr, or both to the activation of p38α and to the substrate specificity for various phosphatases.
Copyright   |   Desclaimer   |    Privacy Policy   |   Browsers   |   Accessibility