scholarly journals Defining HIV-1 Vif residues that interact with CBFβ by site-directed mutagenesis

Virology ◽  
2014 ◽  
Vol 449 ◽  
pp. 82-87 ◽  
Author(s):  
Yusuke Matsui ◽  
Keisuke Shindo ◽  
Kayoko Nagata ◽  
Katsuhiro Io ◽  
Kohei Tada ◽  
...  
Keyword(s):  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Hiv 1

Site-directed mutagenesis of two trans-regulatory genes (tat-III,trs) of HIV-1

Science ◽  
1988 ◽  
Vol 239 (4842) ◽  
pp. 910-913 ◽  
Author(s):  
M. Sadaie ◽  
T Benter ◽  
F Wong-Staal
Keyword(s):  
Regulatory Genes ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Hiv 1

Probing the RNA Binding Surface of the HIV-1 Nucleocapsid Protein by Site-Directed Mutagenesis

Biochemistry ◽  
2013 ◽  
Vol 52 (19) ◽  
pp. 3358-3368 ◽  
Author(s):  
Wei Ouyang ◽  
Stephen Okaine ◽  
Mark P. McPike ◽  
Yong Lin ◽  
Philip N. Borer
Keyword(s):  
Nucleocapsid Protein ◽  
Rna Binding ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Binding Surface ◽  
Hiv 1

scholarly journals Site-directed mutagenesis of the conserved Asp-443 and Asp-498 carboxy-terminal residues of HIV-1 reverse transcriptase

1990 ◽  
Vol 18 (18) ◽  
pp. 5359-5363 ◽  
Author(s):  
Valerie Mizrahi ◽  
Martine T. Usdin ◽  
Alexis Harington ◽  
Lindsay R. Dudding
Keyword(s):  
Reverse Transcriptase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Carboxy Terminal ◽  
Hiv 1

scholarly journals Structure-guided approach identifies a novel class of HIV-1 ribonuclease H inhibitors: binding mode insights through magnesium complexation and site-directed mutagenesis studies

MedChemComm ◽  
2018 ◽  
Vol 9 (3) ◽  
pp. 562-575 ◽  
Author(s):  
Vasanthanathan Poongavanam ◽  
Angela Corona ◽  
Casper Steinmann ◽  
Luigi Scipione ◽  
Nicole Grandi ◽  
...  
Keyword(s):  
In Silico ◽  
Binding Mode ◽  
Rnase H ◽  
Site Directed Mutagenesis ◽  
Ribonuclease H ◽  
Directed Mutagenesis ◽  
New Class ◽  
Hiv 1

In silico methods identified a new class of inhibitors for HIV-1 RT RNase H and magnesium complexation study reveals the binding mode of these compounds.

scholarly journals Prevalent Polymorphisms in Wild-Type HIV-1 Integrase Are Unlikely To Engender Drug Resistance to Dolutegravir (S/GSK1349572)

2013 ◽  
Vol 57 (3) ◽  
pp. 1379-1384 ◽  
Author(s):  
Cindy Vavro ◽  
Samiul Hasan ◽  
Heather Madsen ◽  
Joseph Horton ◽  
Felix DeAnda ◽  
...  
Keyword(s):  
Additional Data ◽  
Integrase Inhibitor ◽  
Acid Sites ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Wild Type ◽  
Functional Roles ◽  
Hiv 1

ABSTRACTThe majority of HIV-1 integrase amino acid sites are highly conserved, suggesting that most are necessary to carry out the critical structural and functional roles of integrase. We analyzed the 34 most variable sites in integrase (>10% variability) and showed that prevalent polymorphic amino acids at these positions did not affect susceptibility to the integrase inhibitor dolutegravir (S/GSK1349572), as demonstrated bothin vitro(in site-directed mutagenesis studies) andin vivo(in a phase IIa study of dolutegravir monotherapy in HIV-infected individuals). Ongoing clinical trials will provide additional data on the virologic activity of dolutegravir across subject viruses with and without prevalent polymorphic substitutions.

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