RNASEH1 Antibody

1. RNASEH1 gene variants associate with susceptibility/protection to T1 Diabetes in Colombia. PMID: 29204916
2. Studies indicate that ribonuclease H1 is essential for mitochondrial DNA replication. PMID: 27402764
3. 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. PMID: 29126318
4. 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. PMID: 28717002
5. RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability. PMID: 28257700
6. RNaseH1 maintains regulated levels of telomeric RNA-DNA hybrids at ALT telomeres to trigger homologous recombination without compromising telomere integrity too severely PMID: 25330849
7. 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 PMID: 26159921
8. Altered RNaseH1 has a reduced capability to remove the RNA from RNA-DNA hybrids leading to impaired mtDNA replication and adult-onset mitochondrial encephalomyopathy. PMID: 26094573
9. RNase H1 and protein P32 are involved in mitochondrial pre-rRNA processing PMID: 23990920
10. 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 PMID: 23078533
11. 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. PMID: 21443203
12. Observational study of gene-disease association. (HuGE Navigator) PMID: 20877624
13. 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. PMID: 12473655
14. Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3'-DNA/5'-RNA terminus of the heteroduplex substrate PMID: 14506260
15. in human cells RNase H1 is responsible for most of the activity of DNA-like antisense drugs PMID: 14960586
16. analysis of catalytic site of human RNase H1 for heteroduplex substrate catalysis PMID: 15205459
17. method for enhancing the human RNase H1 activity of chimeric antisense oligonucleotides PMID: 17028157
18. THE role substrate structure plays in directing human RNase H1 activity as well as the design of effective antisense oligodeoxyribonucleotides. PMID: 17028158
19. Report crystal structures of RNase H1 in complex with RNA/DNA hybrids. PMID: 17964265
20. 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. PMID: 18337749

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HGNC: 18466

OMIM: 604123

KEGG: hsa:246243

STRING: 9606.ENSP00000313350

UniGene: Hs.568006