EC Number |
General Information |
Reference |
---|
3.1.31.1 | physiological function |
staphylococcal nuclease domain-containing protein 1 is a component of the RNA-induced splicing complex that mediates RNA interference, leading to degradation of specific mRNAs |
701613 |
3.1.31.1 | physiological function |
Staphylococcal nuclease degrades both DNA and RNA |
702789 |
3.1.31.1 | metabolism |
programmed cell death pathways, Tudor staphylococcal nuclease is a new component of the human programmed degradome and is cleaved by caspase-3 between the Tudor and SN5 domains |
705843 |
3.1.31.1 | metabolism |
programmed cell death, enzyme is a part of the stress-induced cell-death degradome during both developmental and stress-induced cell deaths |
705843 |
3.1.31.1 | physiological function |
ribonuclease activity, control of gene expression by activating transcription, subsequent mRNA splicing, regulation of RNA silencing and in the pathway that edits and destroys double-stranded RNA, uncleavable Tudor staphylococcal nuclease stimulates cell proliferation and protects cells from death |
705843 |
3.1.31.1 | more |
thermodynamic parameters derived from urea-induced unfolding of mutant SNase140 and mutant SNase141 in comparison with those of wild-type SNase and mutant SNase140 in the presence of calcium, backbone dynamics, detailed overview. Mutant SNase140 unfolds easily compared to mutant SNase141 and wild-type SNase |
717245 |
3.1.31.1 | more |
residue W140 is critical to SNase structure and function |
717382 |
3.1.31.1 | more |
MNase mapping of the enhancer chromatin structure in the Drosophila melanogaster embryo to analyse chromatin structure in a developmental setting, and identification of structural changes on a cis-regulatory element targeted by the Knirps repressor, method development and optimization, overview |
717620 |
3.1.31.1 | physiological function |
Staphylococcus aureus nuclease mediates resistance against entrapment and killing within neutrophil extracellular traps, which consist of a nuclear DNA backbone associated with antimicrobial peptides, histones and proteases that provide a matrix to entrap and kill various microbes. Promoting role of Staphylococcus aureus nuclease in neutrophil extracellular traps degradation and virulence in a murine respiratory tract infection model, overview. Staphylococcus aureus nuclease facilitates evasion from neutrophil extracellular trap entrapment, and mediates resistance against extracellular killing by neutrophils |
-, 717951 |
3.1.31.1 | physiological function |
presence and ionization of Lys66, buried in the hydrophobic core of a stabilized variant of staphylococcal nuclease, affect conformation and dynamics. The neutral Lys66 affects slow conformational fluctuations globally, whereas the effects of the charged form are localized to the region immediately surrounding position 66, when Lys66 is charged the protein expands, structural reorganization triggered by ionization of the internal Lys66, detailed overview |
718378 |