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Articles by Yong Yang
Total Records ( 3 ) for Yong Yang
  Go Kawamura , Yong Yang , Koichiro Fukuda and Masayuki Nogami
  Multi-branched gold nanoparticles (MBGNs) were prepared by a seed-mediated growth method using assistance of AgNO3 and cetyltrimethylammonium bromide (CTAB) acting as the surface modifiers of the particle. The size of MBGNs was changed from 150 to 1500 nm, in which the branches with length up to 100 nm were formed. The formation of the branches was discussed as the selective growth of surfaces restricted by the Ag+–CTAB complex. The surface plasmon resonance properties were strongly affected by the morphology of MBGNs and tuned over the wide wavelengths.
  Yong Yang , Fang Wu , Tarsha Ward , Feng Yan , Quan Wu , Zhaoyang Wang , Tanisha McGlothen , Wei Peng , Tianpa You , Mingkuan Sun , Taixing Cui , Renming Hu , Zhen Dou , Jingde Zhu , Wei Xie , Zihe Rao , Xia Ding and Xuebiao Yao
  Chromosome movements in mitosis are orchestrated by dynamic interactions between spindle microtubules and the kinetochore, a multiprotein complex assembled onto centromeric DNA of the chromosome. Here we show that phosphorylation of human HsMis13 by Aurora B kinase is required for functional kinetochore assembly in HeLa cells. Aurora B interacts with HsMis13 in vitro and in vivo. HsMis13 is a cognate substrate of Aurora B, and the phosphorylation sites were mapped to Ser-100 and Ser-109. Suppression of Aurora B kinase by either small interfering RNA or chemical inhibitors abrogates the localization of HsMis13 but not HsMis12 to the kinetochore. In addition, non-phosphorylatable but not wild type and phospho-mimicking HsMis13 failed to localize to the kinetochore, demonstrating the requirement of phosphorylation by Aurora B for the assembly of HsMis13 to kinetochore. In fact, localization of HsMis13 to the kinetochore is spatiotemporally regulated by Aurora B kinase, which is essential for recruiting outer kinetochore components such as Ndc80 components and CENP-E for functional kinetochore assembly. Importantly, phospho-mimicking mutant HsMis13 restores the assembly of CENP-E to the kinetochore, and tension developed across the sister kinetochores in Aurora B-inhibited cells. Thus, we reason that HsMis13 phosphorylation by Aurora B is required for organizing a stable bi-oriented microtubule kinetochore attachment that is essential for faithful chromosome segregation in mitosis.
  Ingrid Tessmer , Yong Yang , Jie Zhai , Chungwei Du , Peggy Hsieh , Manju M. Hingorani and Dorothy A. Erie
  DNA mismatch repair is initiated by the recognition of mismatches by MutS proteins. The mechanism by which MutS searches for and recognizes mismatches and subsequently signals repair remains poorly understood. We used single-molecule analyses of atomic force microscopy images of MutS-DNA complexes, coupled with biochemical assays, to determine the distributions of conformational states, the DNA binding affinities, and the ATPase activities of wild type and two mutants of MutS, with alanine substitutions in the conserved Phe-Xaa-Glu mismatch recognition motif. We find that on homoduplex DNA, the conserved Glu, but not the Phe, facilitates MutS-induced DNA bending, whereas at mismatches, both Phe and Glu promote the formation of an unbent conformation. The data reveal an unusual role for the Phe residue in that it promotes the unbending, not bending, of DNA at mismatch sites. In addition, formation of the specific unbent MutS-DNA conformation at mismatches appears to be required for the inhibition of ATP hydrolysis by MutS that signals initiation of repair. These results provide a structural explanation for the mechanism by which MutS searches for and recognizes mismatches and for the observed phenotypes of mutants with substitutions in the Phe-Xaa-Glu motif.
 
 
 
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