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Deoxyribonuclease I-like 1

DNase I-like, XIB, DNase X, DNASE1L1
This gene encodes a member of the deoxyribonuclease family and the protein shows high sequence similarity to lysosomal DNase I. Alternate transcriptional splice variants, encoding the same protein, have been characterized. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, DNase I, Actin, CAN, HAD
Papers on DNase I-like
Molecular Pathogenesis of Ehrlichia chaffeensis Infection.
Rikihisa, Columbus, United States. In Annu Rev Microbiol, Nov 2015
E. chaffeensis has a multigene family of major outer membrane proteins with porin activity and induces infectious entry using its entry-triggering protein to bind the human cell surface protein DNase X.
Helicobacter pylori HP0425 Targets the Nucleus with DNase I-Like Activity.
Baik et al., Chinju, South Korea. In Helicobacter, Oct 2015
CONCLUSIONS: These results suggest that HP0425 carrying a nuclear localization signal sequence translocates into the nucleus of host cells and degrades genomic DNA by DNase I-like enzymatic activity, which is a new pathogenic strategy of H. pylori in the host.
Regulation of Apoptotic Endonucleases by EndoG.
Basnakian et al., Little Rock, United States. In Dna Cell Biol, May 2015
The study showed that overexpression of mature EndoG in kidney tubular epithelial NRK-52E cells can increase expression of caspase-activated DNase (CAD) and four endonucleases that belong to DNase I group including DNase I, DNase X, DNase IL2, and DNase γ, but not endonucleases of the DNase 2 group.
Identification of functional SNPs potentially served as a genetic risk factor for the pathogenesis of parakeratosis in the gene encoding human deoxyribonuclease I-like 2 (DNase 1L2) implicated in terminal differentiation of keratinocytes.
Yasuda et al., Fukui, Japan. In Gene, May 2015
In the present study, we evaluated all of the 35 non-synonymous SNPs in the gene encoding DNase I-like 2 (DNase 1L2), implicated in terminal differentiation of keratinocytes, to seek a functional SNP that would potentially affect the levels of in vivo DNase 1L2 activity.
EtpE Binding to DNase X Induces Ehrlichial Entry via CD147 and hnRNP-K Recruitment, Followed by Mobilization of N-WASP and Actin.
Rikihisa et al., Columbus, United States. In Mbio, 2014
To infect cells, Ehrlichia uses the C terminus of the outer membrane invasin entry-triggering protein (EtpE) of Ehrlichia (EtpE-C), which directly binds the mammalian cell surface glycosylphosphatidyl inositol-anchored protein, DNase X.
Cytolethal distending toxin (CDT) is a radiomimetic agent and induces persistent levels of DNA double-strand breaks in human fibroblasts.
Fritz et al., Mainz, Germany. In Dna Repair (amst), 2014
In line with its in vitro DNase I-like activity on plasmid DNA, neutral and alkaline Comet assay revealed predominant induction of DSBs in CDT-treated fibroblasts, whereas irradiation of cells generated higher amounts of SSBs and alkali-labile sites.
Evaluation of all non-synonymous single nucleotide polymorphisms (SNPs) in the genes encoding human deoxyribonuclease I and I-like 3 as a functional SNP potentially implicated in autoimmunity.
Yasuda et al., Fukui, Japan. In Febs J, 2014
The objectives of this study were to evaluate all the non-synonymous single nucleotide polymorphisms (SNPs) in the DNase I and DNase I-like 3 (1L3) genes potentially implicated in autoimmune diseases as a functional SNP in terms of alteration of the activity levels.
The structure of human DNase I bound to magnesium and phosphate ions points to a catalytic mechanism common to members of the DNase I-like superfamily.
Bourne et al., Marseille, France. In Biochemistry, 2013
Complementary mutagenesis data of rhDNase I coupled to a comprehensive structural analysis of the DNase I-like superfamily argue for the key catalytic role of Asn7, which is invariant among mammalian DNase I enzymes and members of this superfamily, through stabilization of the magnesium ion coordination sphere.
In silico and in vitro characterization of phospholipase A₂ isoforms from soybean (Glycine max).
Fidelio et al., Córdoba, Argentina. In Biochimie, 2012
According to PLA₂ superfamily, two of G. max sPLA₂s are grouped as XIA and the rest of sequences as XIB, on the basis of differences found in their molecular weights and deviating sequences especially in the N- and C-terminal regions of the isoenzymes.
A biomarker based detection and characterization of carcinomas exploiting two fundamental biophysical mechanisms in mammalian cells.
Coy et al., Tübingen, Germany. In Bmc Cancer, 2012
The biochemical suicide molecule endonuclease DNaseX (DNaseI-like 1) has been used to identify the Apo10 protein epitope that marks tumor cells with abnormal apoptosis and proliferation.
Ehrlichia chaffeensis uses its surface protein EtpE to bind GPI-anchored protein DNase X and trigger entry into mammalian cells.
Rikihisa et al., Columbus, United States. In Plos Pathog, 2012
Yeast two-hybrid screening revealed that DNase X, a glycosylphosphatidyl inositol-anchored mammalian cell-surface protein binds EtpE-C.
Global analysis of single nucleotide polymorphisms in the exons of human deoxyribonuclease I-like 1 and 2 genes.
Takeshita et al., Japan. In Electrophoresis, 2010
Several SNPs in the deoxyribonuclease I-like 1 (DNase 1L1) and DNase 1L2 were investigated.
Genetic and expression analysis of all non-synonymous single nucleotide polymorphisms in the human deoxyribonuclease I-like 1 and 2 genes.
Yasuda et al., Fukui, Japan. In Electrophoresis, 2010
Genotyping of all the non-synonymous SNPs of was performed in three ethnic groups including six different populations using the PCR-RFLP method newly developed.
[Structure and function of sphingomyelinase].
Oda, Tokushima, Japan. In Yakugaku Zasshi, 2009
Based on the highly conserved nature of amino acid residues of the binding sites, the crystal structure of Bc-SMase with Mg(2+) or Co(2+) provided a common structural framework applicable to phosphohydrolases belonging to the DNase I-like folding superfamily.
In vivo virulence properties of bacterial cytolethal-distending toxin.
Fox et al., Cambridge, United States. In Cell Microbiol, 2008
CDT is typically composed of three subunits: the catalytic subunit CdtB has DNase I-like activity, whereas CdtA and CdtC are binding proteins for delivering CdtB into target cells.
The contribution of cytolethal distending toxin to bacterial pathogenesis.
Bayles et al., United States. In Crit Rev Microbiol, 2006
Once inside the cell, CdtB enters the nucleus and exhibits a DNase I-like activity that results in DNA double-strand breaks.
Cytolethal distending toxins and activation of DNA damage-dependent checkpoint responses.
Thelestam et al., Stockholm, Sweden. In Int J Med Microbiol, 2002
CDTs are encoded by three linked genes (cdtA, cdtB and cdtC), and CdtB is the toxin subunit which possesses the DNase I-like activity.
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