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Articles by Wei Shen
Total Records ( 2 ) for Wei Shen
  Qing-Wei Yang , Cheng Zhen , Song Chen , Ying Zhang , Wei Shen , Shi-Shi Chen and Guang-Rong Huang
  Marine fish processing byproducts were considered as potential good protein resource for producing bioactive peptides by enzymatic hydrolysis. In this study, hydrolysates with high ferrous binding ability were prepared by enzymatic hydrolysis from mackerel (Trachurus japonicus) processing byproducts. In order to get hydrolysates of high ferrous binding ability and degree of hydrolysis, the enzymatic hydrolysis conditions were optimized, including proteases type, hydrolysis time, temperature, pH and enzyme to substrate ratio. The results showed that the hydrolysate by alcalase had the highest ferrous binding ability and degree of hydrolysis, reaching to 9.8 and 49.0%, respectively. The best hydrolysis conditions of alcalase were optimized using response surface methodology to be: pH 9.0, temperature of 50°C, enzyme substrate ratio of 160 mg/100 mL, hydrolysis time of 100 min. The ferrous binding ability and degree of hydrolysis were reached to 48.0 and 45.4%, respectively, at these optimized hydrolysis conditions.
  Shenyuan L. Zhang , J. Ashot Kozak , Weihua Jiang , Andriy V. Yeromin , Jing Chen , Ying Yu , Aubin Penna , Wei Shen , Victor Chi and Michael D. Cahalan
  We evaluated currents induced by expression of human homologs of Orai together with STIM1 in human embryonic kidney cells. When co-expressed with STIM1, Orai1 induced a large inwardly rectifying Ca2+-selective current with Ca2+-induced slow inactivation. A point mutation of Orai1 (E106D) altered the ion selectivity of the induced Ca2+ release-activated Ca2+ (CRAC)-like current while retaining an inwardly rectifying I-V characteristic. Expression of the C-terminal portion of STIM1 with Orai1 was sufficient to generate CRAC current without store depletion. 2-APB activated a large relatively nonselective current in STIM1 and Orai3 co-expressing cells. 2-APB also induced Ca2+ influx in Orai3-expressing cells without store depletion or co-expression of STIM1. The Orai3 current induced by 2-APB exhibited outward rectification and an inward component representing a mixed calcium and monovalent current. A pore mutant of Orai3 inhibited store-operated Ca2+ entry and did not carry significant current in response to either store depletion or addition of 2-APB. Analysis of a series of Orai1-3 chimeras revealed the structural determinant responsible for 2-APB-induced current within the sequence from the second to third transmembrane segment of Orai3. The Orai3 current induced by 2-APB may reflect a store-independent mode of CRAC channel activation that opens a relatively nonselective cation pore.
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