Michael B Sherman

Summary

Affiliation: University of Texas Medical Branch
Country: USA

Publications

  1. pmc Construction and organization of a BSL-3 cryo-electron microscopy laboratory at UTMB
    Michael B Sherman
    Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555 1055, USA
    J Struct Biol 181:223-33. 2013
  2. pmc Removal of divalent cations induces structural transitions in red clover necrotic mosaic virus, revealing a potential mechanism for RNA release
    Michael B Sherman
    Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA
    J Virol 80:10395-406. 2006
  3. pmc Single-particle cryo-electron microscopy of Rift Valley fever virus
    Michael B Sherman
    Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555 0647, USA
    Virology 387:11-5. 2009
  4. pmc Chikungunya virus: evolution and genetic determinants of emergence
    Konstantin A Tsetsarkin
    Institute for Human Infections and Immunity, University of Texas Medical Branch, Galveston, Texas USA
    Curr Opin Virol 1:310-7. 2011
  5. pmc Eilat virus, a unique alphavirus with host range restricted to insects by RNA replication
    Farooq Nasar
    Institute for Human Infections and Immunity and Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA
    Proc Natl Acad Sci U S A 109:14622-7. 2012
  6. pmc Structure of the recombinant alphavirus Western equine encephalitis virus revealed by cryoelectron microscopy
    Michael B Sherman
    W M Keck Center for Virus Imaging, University of Texas Medical Branch, Galveston, Texas, USA
    J Virol 84:9775-82. 2010
  7. pmc Three-dimensional organization of Rift Valley fever virus revealed by cryoelectron tomography
    Alexander N Freiberg
    Department of Pathology, Center for Biodefense and Emerging Infectious Diseases, University of Texas Medical Branch, Galveston, TX 77555 0647, USA
    J Virol 82:10341-8. 2008
  8. pmc Attenuation of Chikungunya virus vaccine strain 181/clone 25 is determined by two amino acid substitutions in the E2 envelope glycoprotein
    Rodion Gorchakov
    Institute for Human Infections and Immunity, Sealy Center for Vaccine Development, and Department of Pathology, University of Texas Medical Branch, Galveston, Texas, USA
    J Virol 86:6084-96. 2012
  9. ncbi request reprint Structure of the acrosomal bundle
    Michael F Schmid
    National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA
    Nature 431:104-7. 2004
  10. pmc The structure of p53 tumour suppressor protein reveals the basis for its functional plasticity
    Andrei L Okorokov
    Department of Pathology, Royal Free and University College Medical School, University College London, London, UK
    EMBO J 25:5191-200. 2006

Collaborators

Detail Information

Publications12

  1. pmc Construction and organization of a BSL-3 cryo-electron microscopy laboratory at UTMB
    Michael B Sherman
    Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555 1055, USA
    J Struct Biol 181:223-33. 2013
    ..The facility has successfully operated for more than a year without an incident and was certified as a select agent facility by the Centers for Disease Control...
  2. pmc Removal of divalent cations induces structural transitions in red clover necrotic mosaic virus, revealing a potential mechanism for RNA release
    Michael B Sherman
    Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA
    J Virol 80:10395-406. 2006
    ..These results indicate that divalent cations play a central role in capsid dynamics and suggest a mechanism for the release of viral RNA in low-divalent-cation environments such as those found within the cytoplasm of a cell...
  3. pmc Single-particle cryo-electron microscopy of Rift Valley fever virus
    Michael B Sherman
    Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555 0647, USA
    Virology 387:11-5. 2009
    ..This structure provides a detailed model for phleboviruses, opens new avenues for high-resolution structural studies of the bunyavirus family, and aids the design of antiviral diagnostics and effective subunit vaccines...
  4. pmc Chikungunya virus: evolution and genetic determinants of emergence
    Konstantin A Tsetsarkin
    Institute for Human Infections and Immunity, University of Texas Medical Branch, Galveston, Texas USA
    Curr Opin Virol 1:310-7. 2011
    ....
  5. pmc Eilat virus, a unique alphavirus with host range restricted to insects by RNA replication
    Farooq Nasar
    Institute for Human Infections and Immunity and Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA
    Proc Natl Acad Sci U S A 109:14622-7. 2012
    ..Reverse genetic studies of EILV may facilitate the discovery of determinants of alphavirus host range that mediate disease emergence...
  6. pmc Structure of the recombinant alphavirus Western equine encephalitis virus revealed by cryoelectron microscopy
    Michael B Sherman
    W M Keck Center for Virus Imaging, University of Texas Medical Branch, Galveston, Texas, USA
    J Virol 84:9775-82. 2010
    ..Surprisingly, the nucleocapsid of WEEV, a New World virus, is more similar to the Old World alphavirus Sindbis virus than to other New World alphaviruses...
  7. pmc Three-dimensional organization of Rift Valley fever virus revealed by cryoelectron tomography
    Alexander N Freiberg
    Department of Pathology, Center for Biodefense and Emerging Infectious Diseases, University of Texas Medical Branch, Galveston, TX 77555 0647, USA
    J Virol 82:10341-8. 2008
    ..Knowledge of the virus architecture may provide a structural template to develop vaccines and diagnostics, since no effective anti-RVFV treatments are available for human use...
  8. pmc Attenuation of Chikungunya virus vaccine strain 181/clone 25 is determined by two amino acid substitutions in the E2 envelope glycoprotein
    Rodion Gorchakov
    Institute for Human Infections and Immunity, Sealy Center for Vaccine Development, and Department of Pathology, University of Texas Medical Branch, Galveston, Texas, USA
    J Virol 86:6084-96. 2012
    ..These results indicate that the attenuation of strain 181/clone 25 is mediated by two point mutations, explaining the phenotypic instability observed in human vaccinees and also in our studies...
  9. ncbi request reprint Structure of the acrosomal bundle
    Michael F Schmid
    National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA
    Nature 431:104-7. 2004
    ....
  10. pmc The structure of p53 tumour suppressor protein reveals the basis for its functional plasticity
    Andrei L Okorokov
    Department of Pathology, Royal Free and University College Medical School, University College London, London, UK
    EMBO J 25:5191-200. 2006
    ..This architecture of p53 in toto suggests novel mechanisms for structural plasticity, which enables the protein to bind variably spaced DNA target sequences, essential for p53 transactivation and tumour suppressor functions...
  11. ncbi request reprint Electron beam coater for reduction of charging in ice-embedded biological specimens using Ti(88)Si(12) alloy
    Michael B Sherman
    National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA
    Microsc Microanal 9:566-73. 2003
    ..Images of the crystals after coating showed diffraction spots of up to 3 A resolution...
  12. ncbi request reprint Structure of triglyceride-rich human low-density lipoproteins according to cryoelectron microscopy
    Michael B Sherman
    Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA
    Biochemistry 42:14988-93. 2003
    ..This effect is likely achieved through changes in the conformation of apo-B-100. These data suggest that the physical state of the LDL core determines particle shape, surface structure, and metabolic fate...