Soumya S Ray
Affiliation: Harvard University
- An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosisSoumya 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...
- Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregationSoumya 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...
- Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methodsRichard 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...
- Fluorescence polarization assay for inhibitors of the kinase domain of receptor interacting protein 1Jenny 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...
- A possible therapeutic target for Lou Gehrig's diseaseSoumya 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
- Enzymatic Characterization of ER Stress-Dependent Kinase, PERK, and Development of a High-Throughput Assay for Identification of PERK InhibitorsDariusz Pytel
The Abramson Family Cancer Research Institute, University of Pennsylvania, Philadelphia, PA, USA Department of Cancer Biology, University of Pennsylvania, Philadelphia, PA, USA Abramson Cancer Center and Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA Laboratory for Drug Discovery in Neurodegeneration, Harvard NeuroDiscovery Center, Brigham and Women s Hospital, Harvard Medical School, Cambridge, MA, USA
J Biomol Screen 19:1024-34. 2014..This approach yielded one compound that exhibited good in vitro and cellular activity. These results demonstrate the validity of this screen and represent starting points for drug discovery efforts...
- Cocrystal structures of diaminopimelate decarboxylase: mechanism, evolution, and inhibition of an antibiotic resistance accessory factorSoumya 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...
- Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformationMargareta K Sorenson
The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
Mol Cell 14:127-38. 2004....
- Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1Chittaranjan 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...