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ndoG digests long non-coding RNA and produces 47-mer (show MERTK Proteins) RNA oligonucleotide complementary to hTERT pre-mRNA exon 8 and intron 8 junction place. Interaction of 47-mer (show MERTK Proteins) RNA oligonucleotide and hTERT pre-mRNA causes alternative splicing.
Overexpression of EndoG in CD4 (show CD4 Proteins)+ T cells downregulated the expression of the active full-length hTERT variant and upregulated the inactive alternatively spliced variant.
Overexpression of EndoG in capital ES, Cyrillicsmall a, Cyrilliccapital ES, Cyrillicsmall o, Cyrillic-2 cells downregulated the expression of active full-length hTERT variant and upregulated non-active spliced variant.
EndoG is not a mediator of exogenous DNA clearance, but in non-physiological circumstances, it may nonspecifically cleave intracellular DNA regardless of its origin.
These findings suggest that non-viral DNA vectors are also substrates for EndoG in its role in homologous recombination
our study established a link between Endo G and mitochondrial function during cardiac hypertrophy
Results show that BNIP3 (show BNIP3 Proteins) interacts with the voltage-dependent anion channel (VDAC) to directly induce mitochondrial release and nuclear translocation of EndoG.
Endonuclease G (EndoG), an apoptotic nuclease (show DCLRE1C Proteins), as an essential factor for MLLbcr-specific DNA recombination after induction of replication stress.
Ethyl gallate induces apoptosis of HL-60 cells by promoting the expression of caspases-8, -9, -3, apoptosis-inducing factor (show AIFM1 Proteins) and endonuclease G.
Data suggest that endonuclease G (EndoG) inhibitors have the potential to be utilized for amelioration of cell injuries in which participation of EndoG is essential.
This study demonistated that Endonuclease G knockout mice reveals a new putative molecular player in the regulation of anxiety.
These findings determine a role for EndoG in the generation of Switch region double-strand DNA breaks and class switch DNA recombination.
EndoG is essential during early embryogenesis and plays a critical role in normal apoptosis and nuclear DNA fragmentation
endonuclease G is essential for embryonic survival, but not through a mitochondrial or apoptosis function
These data suggest that the early nuclear translocation of endoG occurs and could induce DNA fragmentation in the ischemic brain after cerebral ischemia.
EndoG null mice are viable and develop to adulthood with no obvious abnormalities, suggesing that EndoG is not essential for early embryogenesis and apoptosis.
Overexpression of DNase I (show DNASE1 Proteins) in cultured mouse tubular epithelial cells also induced EndoG. Both DNase I (show DNASE1 Proteins) and EndoG mediate cisplatin injury to tubular epithelial cells.
high levels of EndoG were found in adult liver, heart, muscle & to a lesser extent, brain & kidney; EndoG had little or no expression in adult spleen & in embryonic organs at E13.5 stage
The translocation of EndoG to the nucleus of neurons in the infarct implicates EndoG in ischemic neuronal degeneration after permanent MCA (show RSPH1 Proteins) occlusion in mice.
Mouse EndoG without the mitochondrial localization signal (amino-acid residues 1-43) was successfully overexpressed, purified and crystallized using a microbatch method under oil
Results describe the mechanism of catalysis and substrate binding by the apoptotic mitochondrial nuclease (show DCLRE1C Proteins) EndoG, which belongs to the large family of DNA/RNA non-specific betabetaalpha-Me-finger nucleases.
The protein encoded by this gene is a nuclear encoded endonuclease that is localized in the mitochondrion. The encoded protein is widely distributed among animals and cleaves DNA at GC tracts. This protein is capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA.
, TBC1 domain family, member 13
, endonuclease G, mitochondrial
, endonuclease G, mitochondrial-like
, endo G
, mitochondrial endonuclease G