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Annual Report 2011 - Center for Advanced Biotechnology and ...

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The long-term goals of our studies are to provide a structural <strong>and</strong> mechanistic<br />

underst<strong>and</strong>ing <strong>for</strong> how the HCV glycoproteins (E1 <strong>and</strong> E2) interact with each other<br />

<strong>and</strong> with cellular receptors. Also we are focused on how HCV evades the host<br />

antiviral response <strong>and</strong> how RIG-I discriminates viral from cellular RNAs.<br />

Publications:<br />

Structure of RIG-I helicase-<br />

RD bound to dsRNA <strong>and</strong><br />

ADP-BeF<br />

Jiang, F., Ramanathan, A., Miller, M.T., Tang, G.Q., Gale, M. Jr., Patel, S.S.,<br />

Marcotrigiano, J. Structural basis of RNA recognition <strong>and</strong> activation by innate<br />

immune receptor RIG-I. Nature <strong>2011</strong> 479(7373):423-7<br />

Whidby, J., Mateu, G., Scarborough, H., Demeler, B., Grakoui, A. <strong>and</strong><br />

Marcotrigiano, J.<br />

Blocking hepatitis C virus infection with recombinant <strong>for</strong>m of envelope protein 2<br />

ectodomain. J. Virol. 2009 83(21):11078-89.<br />

Saito, T., Owen, D.M., Jiang, F., Marcotrigiano, J., Gale, M. Jr. Innate immunity<br />

induced by composition-dependent RIG-I recognition of hepatitis C virus RNA.<br />

Nature 2008 454(7203):523-7<br />

53

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