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Recognition of Internal Cleavage Sites by Retroviral RNases H
Journal of Molecular Biology, 2004The 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 ...
Sharon J, Schultz +2 more
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Molecular Cloning and Expression of cDNA for Human RNase H
Antisense and Nucleic Acid Drug Development, 1998We 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.
H, Wu, W F, Lima, S T, Crooke
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Structure and Function of RNase H Enzymes
2011RNase H enzymes are endonucleases that specifically cleave ribonucleotides within an RNA:DNA duplex. RNase H proteins are divided into type 1 and type 2 enzymes based on amino acid sequence similarities, substrate specificity, and structure. Both RNase H1 and RNase H2 enzymes play important roles in DNA replication, repair and transcription, and at ...
Thomas Hollis, Nadine M. Shaban
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Association of RNase H activity with yeast RNA polymerase A
Nature, 1976EUKARYOTIC 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 ...
J, Huet +4 more
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RNase H: Specificity, Mechanisms of Action, and Antiviral Target
2014The 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 ...
Moelling K, Broecker F, Kerrigan JE
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FEBS letters, 1998
We cloned the Saccharomyces cerevisiae homologue of mammalian RNase HI, which itself is related to the prokaryotic RNase HII, an enzyme of unknown function and previously described as having minor activity in Escherichia coli. Expression of the corresponding yeast 35 kDa protein (named by us RNase H(35)) in E.
P, Frank +2 more
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We cloned the Saccharomyces cerevisiae homologue of mammalian RNase HI, which itself is related to the prokaryotic RNase HII, an enzyme of unknown function and previously described as having minor activity in Escherichia coli. Expression of the corresponding yeast 35 kDa protein (named by us RNase H(35)) in E.
P, Frank +2 more
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An RNase H‐Assisted Fluorescent Biosensor for Aptamers
ChemBioChem, 2007Dae-Ro, Ahn, Eun Gyeong, Yang
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