Jin Shan Hu
Affiliation: University of Maryland
- Solution structure of a multifunctional DNA- and protein-binding motif of human Werner syndrome proteinJin 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...
- The nuclease domain of the Escherichia coli RecBCD enzyme catalyzes degradation of linear and circular single-stranded and double-stranded DNAJian 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...
- NMR assignments of the winged-helix domain of human werner syndrome proteinJian Zhong Sun
J Biomol NMR 32:261. 2005
- Modulation of Werner syndrome protein function by a single mutation in the conserved RecQ domainJae 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...
- Escherichia coli RecQ is a rapid, efficient, and monomeric helicaseXing 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...
- Backbone and side chain resonance assignmentsof a TRAV14-3 mouse T cell receptor domainJin Shan Hu
J Biomol NMR 31:271-2. 2005
- 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 enzymeHua 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...