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EC Number
Title
Organism
3.1.26.4
A two-nuclease pathway involving RNase H1 is required for primer removal at human mitochondrial OriL
Homo sapiens
3.1.26.4
An allosteric switch-based hairpin for label-free chemiluminescence detection of ribonuclease H activity and inhibitors
Homo sapiens
3.1.26.4
Atomistic details of the molecular recognition of DNA-RNA hybrid duplex by ribonuclease H enzyme
Halalkalibacterium halodurans
3.1.26.4
Characterization of Echinostoma cinetorchis endoribonuclease, RNase H
Echinostoma cinetorchis
3.1.26.4
Characterization of RNase HII substrate recognition using RNase HII-argonaute chimaeric enzymes from Pyrococcus furiosus
Pyrococcus horikoshii OT3
3.1.26.4
Characterization of RNase HII substrate recognition using RNase HII-argonaute chimaeric enzymes from Pyrococcus furiosus
Pyrococcus furiosus
3.1.26.4
Crystal structure of RNA-DNA duplex provides insight into conformational changes induced by RNase H binding
Halalkalibacterium halodurans
3.1.26.4
Crystal structure of RNA-DNA duplex provides insight into conformational changes induced by RNase H binding
Halalkalibacterium halodurans C-125
3.1.26.4
Division of labor among Mycobacterium smegmatis RNase H enzymes RNase H1 activity of RnhA or RnhC is essential for growth whereas RnhB and RnhA guard against killing by hydrogen peroxide in stationary phase
Mycolicibacterium smegmatis
3.1.26.4
Division of labor among Mycobacterium smegmatis RNase H enzymes RNase H1 activity of RnhA or RnhC is essential for growth whereas RnhB and RnhA guard against killing by hydrogen peroxide in stationary phase
Mycolicibacterium smegmatis ATCC 700084
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