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  • Kannan Gunasekaran, Chung-Jung Tsai, Ruth Nussinov
  • Chemistry, Medicine
  • Journal of molecular biology
  • 2004 (First Publication: 1 August 2004)
  • Most proteins exist in the cell as multi-component assemblies. However, which proteins need to be present simultaneously in order to perform a given function is frequently unknown. The first stepContinue Reading
  • Hui-Hsu Gavin Tsai, Meital Reches, Chung-Jung Tsai, Kannan Gunasekaran, Ehud Gazit, Ruth Nussinov
  • Medicine, Chemistry
  • Proceedings of the National Academy of Sciences…
  • 2005 (First Publication: 7 June 2005)
  • Recent evidence suggests that amyloidogenic oligomers may be the toxic species in cell cultures. Thus, it is crucial to understand their structure and oligomerization mechanism in atomistic detail.Continue Reading
  • David Zanuy, Kannan Gunasekaran, Arthur M. Lesk, Ruth Nussinov
  • Chemistry, Medicine
  • Journal of molecular biology
  • 2006 (First Publication: 1 April 2006)
  • The formation of fibril aggregates by long polyglutamine sequences is assumed to play a major role in neurodegenerative diseases such as Huntington. Here, we model peptides rich in glutamine, throughContinue Reading
  • Kannan Gunasekaran, Ruth Nussinov
  • Chemistry, Medicine
  • Journal of molecular biology
  • 2007
  • Proteins are dynamic molecules and often undergo conformational change upon ligand binding. It is widely accepted that flexible loop regions have a critical functional role in enzymes. Lack ofContinue Reading
  • David Zanuy, Nurit Haspel, +4 authors Ruth Nussinov
  • Medicine, Chemistry
  • Physical biology
  • 2004 (First Publication: 1 June 2004)
  • In this paper we present a detailed atomic model for a protofilament, the most basic organization level, of the amyloid fibre formed by the peptide DFNKF. This pentapeptide is a segment derived fromContinue Reading
  • Buyong Ma, Yongping Pan, Kannan Gunasekaran, Rajanarayana Venkataraghavan, Arnold J. Levine, Ruth Nussinov
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences…
  • 2005 (First Publication: 15 March 2005)
  • p53, the tumor suppressor protein, functions as a dimer of dimers. However, how the tetramer binds to the DNA is still an open question. In the crystal structure, three copies of the p53 monomersContinue Reading
  • Ramil F. Latypov, Dingjiang Liu, Kannan Gunasekaran, Timothy S. Harvey, Vladimir I. Razinkov, Andrei A. Raibekas
  • Chemistry, Medicine
  • Protein science : a publication of the Protein…
  • 2008 (First Publication: 1 April 2008)
  • Although 8-anilinonaphthalene-1-sulfonic acid (ANS) is frequently used in protein folding studies, the structural and thermodynamic effects of its binding to proteins are not well understood. UsingContinue Reading