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In combination with previously published in vivo data, the findings presented here suggest a model, in which R-loop processing by RNase H1 directs origin-specific initiation of DNA replication in human mitochondria.
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RNASEH1 gene variants associate with susceptibility/protection to T1 Diabetes in Colombia.
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Studies indicate that ribonuclease H1 is essential for mitochondrial DNA replication.
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Data show that the catalytic domains of E. coli and human RNase H have nearly identical sequence preferences, which correlate with the efficiency of RNase H-recruiting antisense oligonucleotides.
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Data suggest that ribonuclease H1 (RNASEH1) plays important role in replication fork movement by resolving R-loops (RNA-DNA hybrids); RNASEH1 depletion results in accumulation of RNA-DNA hybrids, slowing of replication forks, and increased DNA damage; RNASEH1 appears to contribute to genome stability and preserves telomere integrity.
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RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability.
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RNaseH1 maintains regulated levels of telomeric RNA-DNA hybrids at ALT telomeres to trigger homologous recombination without compromising telomere integrity too severely
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found that the 3' fragments of target pre-mRNA generated by ASO were almost completely degraded from their 5' ends by nuclear XRN2 after RNase H1-mediated cleavage
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Altered RNaseH1 has a reduced capability to remove the RNA from RNA-DNA hybrids leading to impaired mtDNA replication and adult-onset mitochondrial encephalomyopathy.
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RNase H1 and protein P32 are involved in mitochondrial pre-rRNA processing
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data implicate the H264 side chain in phosphodiester hydrolysis as well as in product release, and are consistent with a proposed model in which the RNAse H1 H264 side chain interacts with a divalent metal ion to support catalysis
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On the basis of its nuclear magnetic resonance (NMR) nucleic acid structure, a boranophosphonate-modified, fully R(P) BH(3) DNA/RNA hybrid is predicted not to be a substrate for RNase H1.
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The cysteine residues responsible for the redox-dependent activity of RNase H1 were determined by site-directed mutagenesis to involve Cys(147) and Cys(148), producing an inactive enzyme conformation by disulfide bond formation.
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Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3'-DNA/5'-RNA terminus of the heteroduplex substrate
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in human cells RNase H1 is responsible for most of the activity of DNA-like antisense drugs
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analysis of catalytic site of human RNase H1 for heteroduplex substrate catalysis
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method for enhancing the human RNase H1 activity of chimeric antisense oligonucleotides
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THE role substrate structure plays in directing human RNase H1 activity as well as the design of effective antisense oligodeoxyribonucleotides.
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Report crystal structures of RNase H1 in complex with RNA/DNA hybrids.
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Characterization of full-length enzymes with defective hybrid binding domain indicates that this domain dramatically enhances both the specific activity and processivity of RNase H1.
