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Mammalian retrovirus-associated RNase H is virus coded

Journal of Virology, 1978
RNase H of a temperature-sensitive mutant of Rauscher murine leukemia virus is thermolabile, establishing this activity as a virus-coded function of the mammalian type C virus reverse transcriptase.
M H Lai   +3 more
openaire   +3 more sources

Molecular Cloning and Expression of cDNA for Human RNase H

Antisense and Nucleic Acid Drug Development, 1998
We have cloned, expressed, and purified to electrophoretic homogeneity a human RNase H. The enzyme has a molecular weight of 32 kDa, is Mg2+ dependent, and is inhibited by Mn2+ and N-ethylmaleimide. Its molecular weight and cleavage characteristics are consistent with type 2 human RNase H.
Hongjiang Wu   +2 more
openaire   +3 more sources

Recognition of Internal Cleavage Sites by Retroviral RNases H

Journal of Molecular Biology, 2004
The RNase H activity of reverse transcriptase is essential to complete retroviral replication. Many studies have characterized how reverse transcriptase associates with recessed and exposed DNA 3' ends or RNA 5' ends to position the RNase H domain for cleavage, but little is known about how a nick might affect RNase H cleavages, or how RNase H carries ...
James J. Champoux   +2 more
openaire   +3 more sources

Association of RNase H activity with yeast RNA polymerase A

Nature, 1976
EUKARYOTIC RNA polymerases were isolated as large multimeric protein complexes containing two high molecular weight subunits and a collection of smaller polypeptide chains1–3. This structural complexity suggests a multifunctional system, organised around a core enzyme combined with specificity determinants and possibly other proteins involved in ...
Françoise Wyers   +4 more
openaire   +3 more sources

Recent progress in the research of small molecule HIV-1 RNase H inhibitors.

Current Medicinal Chemistry, 2014
Reverse transcription of human immunodeficiency virus type 1 (HIV-1) is a crucial step in the life cycle initiated by the viral-coded reverse transcriptase (RT), functioning as RNA- and DNA-dependent DNA polymerase (RDDP and DDDP) and the ribonuclease H (
Lili Cao   +4 more
semanticscholar   +1 more source

The RNase H Domain: Structure, Function and Mechanism

2013
An essential step of proliferation of retroviruses and transposition of long terminal repeat-containing retrotransposons is conversion of their single-stranded RNA genome into integration-competent, double-stranded proviral DNA by the multifunctional reverse transcriptase (RT) (Gilboa et al. 1979). RT is an enzyme with two activities. RNA-dependent DNA
Marcin Nowotny, Małgorzata Figiel
openaire   +2 more sources

RNase H: Specificity, Mechanisms of Action, and Antiviral Target

2014
The Ribonuclease (RNase) H is one of the four enzymes encoded by all retroviruses, including HIV. Its main activity is the hydrolysis of the RNA moiety in RNA-DNA hybrids. The RNase H ribonuclease is essential in the retroviral life cycle, since it generates and removes primers needed by the Reverse Transcriptase (RT) for initiation of DNA synthesis ...
John E. Kerrigan   +3 more
openaire   +2 more sources

Sensitive aptamer-based fluorescene assay for ochratoxin A based on RNase H signal amplification.

Food Chemistry, 2019
Kefeng Wu   +4 more
semanticscholar   +1 more source

Human RNases H

2001
Walt F. Lima   +2 more
openaire   +3 more sources

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