Jin Shan Hu

Summary

Affiliation: University of Maryland
Country: USA

Publications

  1. pmc Solution structure of a multifunctional DNA- and protein-binding motif of human Werner syndrome protein
    Jin Shan Hu
    Department of Chemistry and Biochemistry and Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA
    Proc Natl Acad Sci U S A 102:18379-84. 2005
  2. ncbi request reprint The nuclease domain of the Escherichia coli RecBCD enzyme catalyzes degradation of linear and circular single-stranded and double-stranded DNA
    Jian Zhong Sun
    Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA
    Biochemistry 45:131-40. 2006
  3. ncbi request reprint NMR assignments of the winged-helix domain of human werner syndrome protein
    Jian Zhong Sun
    J Biomol NMR 32:261. 2005
  4. ncbi request reprint Modulation of Werner syndrome protein function by a single mutation in the conserved RecQ domain
    Jae Wan Lee
    Laboratory of Molecular Gerontology, NIA, National Institutes of Health, Baltimore, Maryland 21224 6825, USA
    J Biol Chem 280:39627-36. 2005
  5. ncbi request reprint Escherichia coli RecQ is a rapid, efficient, and monomeric helicase
    Xing Dong Zhang
    Laboratory of Soft Matter Physics, Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100080, China
    J Biol Chem 281:12655-63. 2006
  6. ncbi request reprint Backbone and side chain resonance assignmentsof a TRAV14-3 mouse T cell receptor domain
    Jin Shan Hu
    J Biomol NMR 31:271-2. 2005
  7. doi request reprint The zinc-binding motif of human RECQ5beta suppresses the intrinsic strand-annealing activity of its DExH helicase domain and is essential for the helicase activity of the enzyme
    Hua Ren
    CNRS, UMR 2027, Institut Curie Section de Recherche, Centre Universitaire, Batiment 110, F 91405 Orsay, France
    Biochem J 412:425-33. 2008

Collaborators

  • Ping Xie
  • Xu Guang Xi
  • Vilhelm A Bohr
  • R M Brosh
  • Pavel Janscak
  • Jian Zhong Sun
  • Xing Dong Zhang
  • Hua Ren
  • Peng Ye Wang
  • Shuo Xing Dou
  • Wangyong Zeng
  • Guang Xin Lin
  • Jae Wan Lee
  • Jie Lin Liu
  • Radhakrishnan Kanagaraj
  • Douglas A Julin
  • Han Qiao Feng
  • Cayetano Von Kobbe
  • Rika Kusumoto
  • Wen Hsing Cheng
  • Kevin M Doherty

Detail Information

Publications7

  1. pmc Solution structure of a multifunctional DNA- and protein-binding motif of human Werner syndrome protein
    Jin Shan Hu
    Department of Chemistry and Biochemistry and Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA
    Proc Natl Acad Sci U S A 102:18379-84. 2005
    ..Furthermore, we propose that DPBD functions as a regulatory domain to regulate the enzymatic activity of WRN and to direct cellular localization of WRN through protein-protein interaction...
  2. ncbi request reprint The nuclease domain of the Escherichia coli RecBCD enzyme catalyzes degradation of linear and circular single-stranded and double-stranded DNA
    Jian Zhong Sun
    Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA
    Biochemistry 45:131-40. 2006
    ..A new model has been proposed to explain the regulation of the RecB30 nuclease in RecBCD...
  3. ncbi request reprint NMR assignments of the winged-helix domain of human werner syndrome protein
    Jian Zhong Sun
    J Biomol NMR 32:261. 2005
  4. ncbi request reprint Modulation of Werner syndrome protein function by a single mutation in the conserved RecQ domain
    Jae Wan Lee
    Laboratory of Molecular Gerontology, NIA, National Institutes of Health, Baltimore, Maryland 21224 6825, USA
    J Biol Chem 280:39627-36. 2005
    ..Our nuclear magnetic resonance data on the three-dimensional structure of the wild-type RQC and Lys-1016 mutant proteins display a remarkable similarity in their structures...
  5. ncbi request reprint Escherichia coli RecQ is a rapid, efficient, and monomeric helicase
    Xing Dong Zhang
    Laboratory of Soft Matter Physics, Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100080, China
    J Biol Chem 281:12655-63. 2006
    ..These kinetic results not only further support our previous conclusion that E. coli RecQ functions as a monomer but also suggest that some of the Superfamily 2 helicases may function through an "inchworm" mechanism...
  6. ncbi request reprint Backbone and side chain resonance assignmentsof a TRAV14-3 mouse T cell receptor domain
    Jin Shan Hu
    J Biomol NMR 31:271-2. 2005
  7. doi request reprint The zinc-binding motif of human RECQ5beta suppresses the intrinsic strand-annealing activity of its DExH helicase domain and is essential for the helicase activity of the enzyme
    Hua Ren
    CNRS, UMR 2027, Institut Curie Section de Recherche, Centre Universitaire, Batiment 110, F 91405 Orsay, France
    Biochem J 412:425-33. 2008
    ..The novel intramolecular modulation of RECQ5beta catalytic activity mediated by the zinc-binding motif may represent a universal regulation mode for all RecQ family helicases...