Soumya S Ray

Summary

Affiliation: Harvard University
Country: USA

Publications

  1. ncbi request reprint An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis
    Soumya S Ray
    Harvard Center for Neurodegeneration and Repair and Department of Neurology, Harvard Medical School, Boston, Massachusetts 02115, USA
    Biochemistry 43:4899-905. 2004
  2. pmc Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation
    Soumya S Ray
    Harvard Center for Neurodegeneration and Repair and Department of Neurology, Harvard Medical School, Boston, MA 02115, USA
    Proc Natl Acad Sci U S A 102:3639-44. 2005
  3. pmc Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods
    Richard J Nowak
    Harvard NeuroDiscovery Center, Harvard Medical School, Boston, Massachusetts, USA
    J Med Chem 53:2709-18. 2010
  4. pmc Fluorescence polarization assay for inhibitors of the kinase domain of receptor interacting protein 1
    Jenny L Maki
    Department of Biochemistry, School of Medicine, Tufts University, Boston, MA 02111, USA
    Anal Biochem 427:164-74. 2012
  5. pmc A possible therapeutic target for Lou Gehrig's disease
    Soumya S Ray
    Center for Neurologic Diseases, Brigham and Women s Hospital and Department of Neurology, Harvard Medical School, 65 Landsdowne Street, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 101:5701-2. 2004
  6. ncbi request reprint Cocrystal structures of diaminopimelate decarboxylase: mechanism, evolution, and inhibition of an antibiotic resistance accessory factor
    Soumya S Ray
    Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
    Structure 10:1499-508. 2002
  7. ncbi request reprint Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation
    Margareta K Sorenson
    The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
    Mol Cell 14:127-38. 2004
  8. pmc Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1
    Chittaranjan Das
    Department of Chemistry and Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454 9110, USA
    Proc Natl Acad Sci U S A 103:4675-80. 2006

Collaborators

Detail Information

Publications8

  1. ncbi request reprint An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis
    Soumya S Ray
    Harvard Center for Neurodegeneration and Repair and Department of Neurology, Harvard Medical School, Boston, Massachusetts 02115, USA
    Biochemistry 43:4899-905. 2004
    ..A drug-like molecule that could stabilize the A4V dimer could slow the onset and progression of FALS...
  2. pmc Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation
    Soumya S Ray
    Harvard Center for Neurodegeneration and Repair and Department of Neurology, Harvard Medical School, Boston, MA 02115, USA
    Proc Natl Acad Sci U S A 102:3639-44. 2005
    ..In the presence of several of these molecules, A4V and other FALS-linked SOD1 mutants such as G93A and G85R behaved similarly to wild-type SOD1, suggesting that these compounds could be leads toward effective therapeutics against FALS...
  3. pmc Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods
    Richard J Nowak
    Harvard NeuroDiscovery Center, Harvard Medical School, Boston, Massachusetts, USA
    J Med Chem 53:2709-18. 2010
    ..At least six of the new molecules exhibited high specificity of binding toward SOD-1 in the presence of blood plasma. These molecules represent a new class of molecules for further development into clinical candidates...
  4. pmc Fluorescence polarization assay for inhibitors of the kinase domain of receptor interacting protein 1
    Jenny L Maki
    Department of Biochemistry, School of Medicine, Tufts University, Boston, MA 02111, USA
    Anal Biochem 427:164-74. 2012
    ..62 (fluorescein-Nec-1) and 0.57 (fluorescein-Nec-3). In addition, results obtained from the FP assays and ligand docking studies provide insights into the putative binding sites of Nec-1, Nec-3, and Nec-4...
  5. pmc A possible therapeutic target for Lou Gehrig's disease
    Soumya S Ray
    Center for Neurologic Diseases, Brigham and Women s Hospital and Department of Neurology, Harvard Medical School, 65 Landsdowne Street, Cambridge, MA 02139, USA
    Proc Natl Acad Sci U S A 101:5701-2. 2004
  6. ncbi request reprint Cocrystal structures of diaminopimelate decarboxylase: mechanism, evolution, and inhibition of an antibiotic resistance accessory factor
    Soumya S Ray
    Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
    Structure 10:1499-508. 2002
    ..Implications for rational design of broad-spectrum antimicrobial agents targeted against DAPDCs of drug-resistant strains of bacterial pathogens, such as Staphylococcus aureus, are discussed...
  7. ncbi request reprint Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation
    Margareta K Sorenson
    The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
    Mol Cell 14:127-38. 2004
    ....
  8. pmc Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1
    Chittaranjan Das
    Department of Chemistry and Biochemistry, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454 9110, USA
    Proc Natl Acad Sci U S A 103:4675-80. 2006
    ..In particular, the geometry of the catalytic residues in the active site of UCH-L1 is distorted in such a way that the hydrolytic activity would appear to be impossible without substrate induced conformational rearrangements...