Skip to search formSkip to main content
You are currently offline. Some features of the site may not work correctly.

endoribonuclease activity

Catalysis of the hydrolysis of ester linkages within ribonucleic acid by creating internal breaks. [GOC:mah, ISBN:0198547684]
National Institutes of Health

Related topics

Related topics

3 relations
Endoribonucleasesendonuclease G activitypositive regulation of endoribonuclease activity

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2017
Highly Cited
2017
Structural Basis for Guide RNA Processing and Seed-Dependent DNA Targeting by CRISPR-Cas12a.
The CRISPR-associated protein Cas12a (Cpf1), which has been repurposed for genome editing, possesses two distinct nuclease… Expand
  • figure 1
  • table 1
  • figure 2
  • figure 3
  • figure 4
Is this relevant?
Highly Cited
2011
Highly Cited
2011
Argonaute protein identity and pairing geometry determine cooperativity in mammalian RNA silencing.
Small RNAs loaded into Argonaute proteins direct silencing of complementary target mRNAs. It has been proposed that multiple… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • table 1
Is this relevant?
Highly Cited
2009
Highly Cited
2009
Identification of Apurinic/apyrimidinic endonuclease 1 (APE1) as the endoribonuclease that cleaves c-myc mRNA
Endonucleolytic cleavage of the coding region determinant (CRD) of c-myc mRNA appears to play a critical role in regulating c-myc… Expand
  • figure 1
  • table 1
  • figure 2
  • figure 3
  • figure 4
Is this relevant?
Highly Cited
2008
Highly Cited
2008
A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity.
Many plant pentatricopeptide repeat (PPR) proteins are known to contain a highly conserved C-terminal DYW domain whose function… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 5
  • figure 4
Is this relevant?
Highly Cited
2004
Highly Cited
2004
Interference of mRNA Function by Sequence-specific Endoribonuclease PemK*
In Escherichia coli, programmed cell death is mediated through the system called “addiction module,” which consists of a pair of… Expand
Is this relevant?
Highly Cited
2003
Highly Cited
2003
Bypassing a Kinase Activity with an ATP-Competitive Drug
Unfolded proteins in the endoplasmic reticulum cause trans-autophosphorylation of the bifunctional transmembrane kinase Ire1… Expand
Is this relevant?
Highly Cited
2000
Highly Cited
2000
The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response.
The unfolded protein response (UPR) is a signal transduction pathway that is activated by the accumulation of unfolded proteins… Expand
Is this relevant?
Highly Cited
2000
Highly Cited
2000
The poly(A)-binding protein and an mRNA stability protein jointly regulate an endoribonuclease activity.
We previously identified a sequence-specific erythroid cell-enriched endoribonuclease (ErEN) activity involved in the turnover of… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Is this relevant?
Highly Cited
1998
Highly Cited
1998
A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells.
Eukaryotes respond to the presence of unfolded protein in the endoplasmic reticulum (ER) by up-regulating the transcription of… Expand
Is this relevant?
Highly Cited
1988
Highly Cited
1988
Sequence-specific endoribonuclease activity of the Tetrahymena ribozyme: enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes.
A shortened form of the self-splicing intervening sequence RNA of Tetrahymena acts as a sequence-specific endoribonuclease… Expand
Is this relevant?
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy, Terms of Service, and Dataset License
ACCEPT & CONTINUE