Analysis of HIV-1 replication block due to substitutions at F61 residue of reverse transcriptase reveals additional defects involving the RNase H function

Author： Mandal Dibyakanti   Dash Chandravanu   Le Grice Stuart F. J.   Prasad Vinayaka R.  

Publisher： Oxford University Press

ISSN： 1362-4962

Source： Nucleic Acids Research, Vol.34, Iss.10, 2006-01, pp. : 2853-2863

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Related content

Collective Motions in HIV-1 Reverse Transcriptase: Examination of Flexibility and Enzyme Function

By Bahar I.   Erman B.   Jernigan R.L.   Atilgan A.R.   Covell D.G.  

Journal of Molecular Biology, Vol. 285, Iss. 3, 1999-01 ,pp. : 1023-1037

Academic Press

Access to resources Recommend Favorite

Analysis of Amino Insertion Mutations in the Fingers Subdomain of HIV-1 Reverse Transcriptase

By Boyer P.L.   Lisziewicz J.   Lori F.   Hughes S.H.  

Journal of Molecular Biology, Vol. 286, Iss. 4, 1999-03 ,pp. : 995-1008

Academic Press

Access to resources Recommend Favorite

High-throughput sequence analysis reveals structural diversity and improved potency among RNA inhibitors of HIV reverse transcriptase

By Ditzler Mark A.  

Nucleic Acids Research, Vol. 41, Iss. 3, 2013-02 ,pp. : 1873-1884

Oxford University Press

Access to resources Recommend Favorite

Resistance to Nevirapine of HIV-1 Reverse Transcriptase Mutants: Loss of Stabilizing Interactions and Thermodynamic or Steric Barriers are Induced by Different Single Amino Acid Substitutions

By Maga G.   Amacker M.   Ruel N.   Hubscher U.   Spadari S.  

Journal of Molecular Biology, Vol. 274, Iss. 5, 1997-12 ,pp. : 738-747

Academic Press

Access to resources Recommend Favorite

Altered error specificity of RNase H-deficient HIV-1 reverse transcriptases during DNA-dependent DNA synthesis

By lvarez Mar   Barrioluengo Vernica   Afonso-Lehmann Raquel N.   Menndez-Arias Luis  

Nucleic Acids Research, Vol. 41, Iss. 8, 2013-04 ,pp. : 4601-4612

Oxford University Press

Access to resources Recommend Favorite