Adrian W R Serohijos

Summary

Affiliation: Harvard University
Country: USA

Publications

  1. doi Molecular modeling tools and approaches for CFTR and cystic fibrosis
    Adrian W R Serohijos
    Department of Physics and Astronomy, Program in Molecular and Cellular Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA
    Methods Mol Biol 741:347-63. 2011
  2. pmc Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating
    Lihua He
    Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599, USA
    J Biol Chem 283:26383-90. 2008
  3. pmc Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR
    Tamas Hegedus
    Department of Biochemistry and Biophysics, University of North Carolina Chapel Hill, Chapel Hill, NC 27599, USA
    J Mol Biol 378:1052-63. 2008
  4. pmc Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding
    Adrian W R Serohijos
    Department of Physics and Astronomy, University of North Carolina Chapel Hill, Chapel Hill, North Carolina, USA
    PLoS Comput Biol 4:e1000008. 2008
  5. pmc A structural model of the pore-forming region of the skeletal muscle ryanodine receptor (RyR1)
    Srinivas Ramachandran
    Department of Biochemistry and Biophysics, University of North Carolina Chapel Hill, Chapel Hill, North Carolina, USA
    PLoS Comput Biol 5:e1000367. 2009
  6. pmc A physical model reveals the mechanochemistry responsible for dynein's processive motion
    Denis Tsygankov
    Department of Pharmacology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA
    Biophys J 101:144-50. 2011
  7. pmc Structural basis for μ-opioid receptor binding and activation
    Adrian W R Serohijos
    Biochemistry and Biophysics Department, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
    Structure 19:1683-90. 2011
  8. pmc Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    Adrian W R Serohijos
    Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA
    Proc Natl Acad Sci U S A 105:3256-61. 2008
  9. pmc Kinetic models for the coordinated stepping of cytoplasmic dynein
    Denis Tsygankov
    Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
    J Chem Phys 130:025101. 2009

Collaborators

Detail Information

Publications9

  1. doi Molecular modeling tools and approaches for CFTR and cystic fibrosis
    Adrian W R Serohijos
    Department of Physics and Astronomy, Program in Molecular and Cellular Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA
    Methods Mol Biol 741:347-63. 2011
    ..Here, we describe molecular modeling tools that, in conjunction with complementary experimental tools, lead to significant findings on CFTR channel function and on the effect of the pathogenic mutant F508del...
  2. pmc Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating
    Lihua He
    Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599, USA
    J Biol Chem 283:26383-90. 2008
    ..These results reinforce the idea that mediation of regulatory signals between cytoplasmic- and membrane-integrated domains of the CFTR channel apparently relies on an array of precise but highly dynamic interdomain structural joints...
  3. pmc Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR
    Tamas Hegedus
    Department of Biochemistry and Biophysics, University of North Carolina Chapel Hill, Chapel Hill, NC 27599, USA
    J Mol Biol 378:1052-63. 2008
    ....
  4. pmc Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding
    Adrian W R Serohijos
    Department of Physics and Astronomy, University of North Carolina Chapel Hill, Chapel Hill, North Carolina, USA
    PLoS Comput Biol 4:e1000008. 2008
    ..The identified structural determinants of increased misfolding propensity of NBD1-DeltaF508 are essential information in correcting this pathogenic mutant...
  5. pmc A structural model of the pore-forming region of the skeletal muscle ryanodine receptor (RyR1)
    Srinivas Ramachandran
    Department of Biochemistry and Biophysics, University of North Carolina Chapel Hill, Chapel Hill, North Carolina, USA
    PLoS Comput Biol 5:e1000367. 2009
    ..Together, the computational and experimental results shed light on ion conductance and selectivity of RyR1 at an atomistic level...
  6. pmc A physical model reveals the mechanochemistry responsible for dynein's processive motion
    Denis Tsygankov
    Department of Pharmacology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA
    Biophys J 101:144-50. 2011
    ....
  7. pmc Structural basis for μ-opioid receptor binding and activation
    Adrian W R Serohijos
    Biochemistry and Biophysics Department, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
    Structure 19:1683-90. 2011
    ..In summary, the MOR1 model provides a tool for elucidating the structural mechanism of ligand-initiated cell signaling and for screening novel analgesics...
  8. pmc Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    Adrian W R Serohijos
    Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA
    Proc Natl Acad Sci U S A 105:3256-61. 2008
    ....
  9. pmc Kinetic models for the coordinated stepping of cytoplasmic dynein
    Denis Tsygankov
    Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
    J Chem Phys 130:025101. 2009
    ..Finally, we use the results of these investigations to develop a full model for dimeric dynein's chemomechanical cycle and analyze this model to make experimentally testable predictions...