Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase

By Kataropoulou Alexandra  

Nucleic Acids Research, Vol. 37, Iss. 11, 2009-06 ,pp. : 3660-3669

Oxford University Press

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Solution Structure of a Circular-permuted Variant of the Potent HIV-inactivating Protein Cyanovirin-N: Structural Basis for Protein Stability and Oligosaccharide Interaction

By Barrientos L.G.   Louis J.M.   Ratner D.M.   Seeberger P.H.   Gronenborn A.M.  

Journal of Molecular Biology, Vol. 325, Iss. 1, 2003-01 ,pp. : 211-223

Academic Press

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HIV-1 Vif-Derived Peptide Inhibits Drug-Resistant HIV Proteases

By Blumenzweig I.   Baraz L.   Friedler A.   Danielson U.H.   Gilon C.   Steinitz M.   Kotler M.  

Biochemical and Biophysical Research Communications, Vol. 292, Iss. 4, 2002-04 ,pp. : 832-840

Elsevier

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Modifications in host cell cytoskeleton structure and function mediated by intracellular HIV-1 Tat protein are greatly dependent on the second coding exon

By Lpez-Huertas M. R.  

Nucleic Acids Research, Vol. 38, Iss. 10, 2010-06 ,pp. : 3287-3307

Oxford University Press

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The RNA-binding domain of influenzavirus non-structural protein-1 cooperatively binds to virus-specific RNA sequences in a structure-dependent manner

By Marc Daniel  

Nucleic Acids Research, Vol. 41, Iss. 1, 2013-01 ,pp. : 434-449

Oxford University Press

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