Nature of the N - terminal Amino Acid Residue of HIV - 1 RNase 2 H is Critical for the Stability of Reverse Transcriptase in Viral 3 Particles
نویسنده
چکیده
218 16
منابع مشابه
Synthesis and molecular docking of novel N-((2-chloroquinolin-3-yl) methylene)-4-methylbenzenamine derivatives as anti-HIV-1 reverse transcriptase inhibitors
In this research work, a proficient method has been developed for the preparation of novel N-((2-chloroquinolin-3-yl) methylene)-4-methylbenzenamine derivatives from 2-chloroquinoline-3-carbaldehyde derivatives and p-toluidine in ethanol as solvent and using catalytic amount of acetic acid under reflux conditions to obtain desired products in good yields. The identification of all the synthesiz...
متن کاملDrug- Resistance- Associated Mutations and HIV Sub-Type Determination in Drug-Naïve and HIV-Positive Patients under Treatment with Antiretroviral Drugs
Abstract Background and Objective: Resistance to antiretroviral agents is a significant concern in clinical management of HIV-infected individuals. Resistance is the result of mutations that develops in the viral protein targeted by antiretroviral agents. Material and Methods: In this cross-sectional study, the blood samples of 40 HIV-positive patients were collected. Twenty of them were d...
متن کاملThe isolated RNase H domain of murine leukemia virus reverse transcriptase. Retention of activity with concomitant loss of specificity.
Retroviral RNases H are similar in sequence and structure to Escherichia coli RNase HI and yet have differences in substrate specificities, metal ion requirements, and specific activities. Separation of reverse transcriptase (RT) into polymerase and RNase H domains yields an active RNase H from murine leukemia virus (MuLV) but an inactive human immunodeficiency virus (HIV) RNase H. The "handle ...
متن کاملConservation Patterns of HIV-1 RT Connection and RNase H Domains: Identification of New Mutations in NRTI-Treated Patients
BACKGROUND Although extensive HIV drug resistance information is available for the first 400 amino acids of its reverse transcriptase, the impact of antiretroviral treatment in C-terminal domains of Pol (thumb, connection and RNase H) is poorly understood. METHODS AND FINDINGS We wanted to characterize conserved regions in RT C-terminal domains among HIV-1 group M subtypes and CRF. Additional...
متن کاملMutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo.
Retroviral reverse transcriptases contain a DNA polymerase activity that can copy an RNA or DNA template and an RNase H activity that degrades the viral RNA genome during reverse transcription. RNase H makes both specific and nonspecific cleavages; specific cleavages are used to generate and remove the polypurine tract primer used for plus-strand DNA synthesis and to remove the tRNA primer used...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2014