Results 241 to 250 of about 11,347,920 (284)
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A capillary electrophoretic assay for ribonuclease H activity
Analytical Biochemistry, 2004A capillary electrophoretic assay was developed to measure the ribonuclease (RNase) H activity of human immunodeficiency virus (HIV) type 1 reverse transcriptase. Cleavage of a fluorescein-labeled RNA-DNA heteroduplex was monitored by capillary electrophoresis.
King C, Chan +9 more
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Ribonuclease H activity in developing rat brain
Life Sciences, 1977Abstract A ribonucleolytic enzyme (RNase H) which degrades the RNA strand of a RNA-DNA double stranded hybrid has been extracted from rat brain and characterized. RNase H activity in the cerebella increased up to around 6th day after birth and then decreased in adult rat cerebella, just as DNA polymerase and DNA ligase.
Y, Sawai, Y, Sawasaki, K, Tsukada
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Ribonuclease H evolution in retrotransposable elements
Cytogenetic and Genome Research, 2005Eukaryotic and prokaryotic genomes encode either Type I or Type II Ribonuclease H (RNH) which is important for processing RNA primers that prime DNA replication in almost all organisms. This review highlights the important role that Type I RNH plays in the life cycle of many retroelements, and its utility in tracing early events in retroelement ...
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Ribonuclease H activity in cultured plant cells
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1978Ribonuclease H (RNAase H) was extracted from cultured plant cells, strain GD-2 and characterized. RNAase H activity in logarithmical growing cells is much higher than that of stationary cells, and the response of RNAase H activity was very similar to that of DNA polymerase after culture.
Y, Sawai, N, Sugano, K, Tsukada
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Identification of a yeast ribonuclease H as an Sm antigen
European Journal of Biochemistry, 1989We have isolated a 55‐kDa enzyme from Saccharomyces cerevisiae on the basis of its ability to hydrolyze specifically the RNA moiety of RNA/DNA hybrids [RNase H(55)]. Remarkably, monospecific anti‐[R Nase H(55)] antibodies revealed that the protein associates with several small RNAs, including some of the essential yeast spliceosomal snRNAs.
R, Karwan, I, Kindås-Mügge
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A Thermodynamic Comparison of Mesophilic and Thermophilic Ribonucleases H
Biochemistry, 1999The mechanisms by which thermophilic proteins attain their increased thermostability remain unclear, as usually the sequence and structure of these proteins are very similar to those of their mesophilic homologues. To gain insight into the basis of thermostability, we have determined protein stability curves describing the temperature dependence of the
J, Hollien, S, Marqusee
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Ribonucleases H of retroviral and cellular origin
Pharmacology & Therapeutics, 1990Ribonucleases H (RNases H) are enzymes which catalyse the hydrolysis of the RNA-strand of an RNA-DNA hybrid. Retroviral reverse transcriptases possess RNase H activity in addition to their RNA- as well as DNA-dependent DNA-polymerizing activity. These enzymes transcribe the viral single stranded RNA-genome into double stranded DNA, which then can be ...
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Thermal and mechanical multistate folding of ribonuclease H
The Journal of Chemical Physics, 2009Two different classes of experimental techniques exist by which protein folding mechanisms are ascertained. The first class, of which circular dichroism is an example, probes thermally-induced folding. The second class, which includes atomic force microscopy and optical tweezers, measures mechanically-induced folding. In this article, we investigate if
Terry J, Schmitt +2 more
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Small molecule inhibitors of HIV RT Ribonuclease H
Bioorganic & Medicinal Chemistry Letters, 2010Two classes of compounds, thiocarbamates 1 and triazoles 2, have been identified as HIV RT RNase H inhibitors using a novel FRET-based HTS assay. The potent analogs in each series exhibited selectivity and were active in cell-based assays. In addition, saturable, 1:1 stoichiometric binding to target was established and time of addition studies were ...
Martin, Di Grandi +9 more
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Targeting the retroviral ribonuclease H by rational drug design
AIDS, 2012Ribonucleases H or RNases H are conserved and exist in almost every organism. They generate and remove RNA primers, which are required for DNA replication. RNases H hydrolyze RNA in RNA-DNA hybrids. RNases H and related enzymes contribute to reduction of gene expression in antisense and small-interfering RNA mechanisms for gene silencing.
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