Results 211 to 220 of about 61,956 (252)
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Distinct Ribonuclease H Activities in Calf Thymus
European Journal of Biochemistry, 1975Three enzymes with ribonuclease H activity are present in calf thymus. They have been separated on the basis of chromatographic behaviour and molecular weight. They are further distinguished from one another by their ionic requirements and sensitivity to the −SH reagent N‐ethylmaleimide.
W, Büsen, P, Hausen
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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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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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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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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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Ribonuclease H activities associated with herpes simplex virus
Biochemical and Biophysical Research Communications, 1974Abstract Ribonuclease H activities were detected in purified particles of herpes simplex virus type 1 and 2. The RNase H specifically degrades the ribo moiety of the synthetic homopolymet [ 3 H]-poly rA·dT as well as the RNA part of the hybrid [ 3 H]-RNA·DNA duplex. Single-stranded polymers were not degraded under the conditions used.
C, Kleinicke, H, Fischer, R M, Flügel
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Biochemical and Biophysical Research Communications, 1978
Summary The specific activity of Mg 2+ -dependent ribonuclease H (RNase H) from rat liver nuclei increased three- to four-fold within 24 h of a single injection of thioacetamide, and decreased to normal values 48 h after administration. The response of RNase H activity to thioacetamide was very similar to that of RNA polymerase I after treatment. The
K, Tsukada, Y, Sawai, J, Saito, F, Sato
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Summary The specific activity of Mg 2+ -dependent ribonuclease H (RNase H) from rat liver nuclei increased three- to four-fold within 24 h of a single injection of thioacetamide, and decreased to normal values 48 h after administration. The response of RNase H activity to thioacetamide was very similar to that of RNA polymerase I after treatment. The
K, Tsukada, Y, Sawai, J, Saito, F, Sato
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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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Development of a Nonradioactive Ribonuclease H Assay
Analytical Biochemistry, 1996P, Rychetsky +3 more
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Journal of biochemistry, 1981
Rat liver nuclei were isolated in aqueous solutions of low ionic strength or anhydrous glycerol. The presence of ribonuclease H (RNase H) [EC 3.1.4.34] activity in the cytoplasm is due to extraction of the nuclear enzyme by buffer and inorganic salts.
Y, Sawai +4 more
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Rat liver nuclei were isolated in aqueous solutions of low ionic strength or anhydrous glycerol. The presence of ribonuclease H (RNase H) [EC 3.1.4.34] activity in the cytoplasm is due to extraction of the nuclear enzyme by buffer and inorganic salts.
Y, Sawai +4 more
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