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Ribonuclease, RNase A family, 1

RNase A
This gene encodes a member of the pancreatic-type of secretory ribonucleases, a subset of the ribonuclease A superfamily. The encoded endonuclease cleaves internal phosphodiester RNA bonds on the 3'-side of pyrimidine bases. It prefers poly(C) as a substrate and hydrolyzes 2',3'-cyclic nucleotides, with a pH optimum near 8.0. The encoded protein is monomeric and more commonly acts to degrade ds-RNA over ss-RNA. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified. [provided by RefSeq, Jul 2008] (from NCBI)
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Top mentioned proteins: CAN, ACID, fibrillin-1, V1a, STEP
Papers using RNase A antibodies
Tilescope: online analysis pipeline for high-density tiling microarray data.
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Copenhaver Gregory P., In PLoS Genetics, 2006
... ChIP DNA was purified by incubation with 200 µg/ml RNase A (Qiagen #19101) for 1 h at ...
Sphingosine-1-phosphate lyase is involved in the differentiation of F9 embryonal carcinoma cells to primitive endoderm.
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Egli Martin, In PLoS ONE, 2002
... bovine serum albumin (BSA), resuspended in 1 ml Krishan Buffer containing 0.1% sodium citrate, 0.02 mg/ml RNase A (Qiagen, Valencia, CA), 0.20% NP40 ...
Evidence for a lack of DNA double-strand break repair in human cells exposed to very low x-ray doses.
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Jagetia Ganesh Chandra, In PLoS ONE, 2002
... BrdU was from Serva (Heidelberg, Germany), RNase A type III-A from Sigma and pepsin 0.7 FIP-U from Merck (Darmstadt, Germany) ...
Natural-killer like cells in the sheep: Functional characterization and regulation by pregnancy-associated proteins
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Hansen Peter J et al., In BMC Cell Biology, 2001
... deoxynucleotidyl transferase-mediated dUTP nick end labeling (TUNEL)] was purchased from Roche (Indianapolis, IN), the DNase-free RNase A was obtained from Qiagen (Valencia, CA), Precast Tris-HCl ...
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Papers on RNase A
pH-Reversible Cationic RNase A Conjugates for Enhanced Cellular Delivery and Tumor Cell Killing.
New
Lächelt et al., München, Germany. In Biomacromolecules, Feb 2016
Enhanced Green fluorescent protein (EGFP), as model for the visualization of protein transduction, and RNase A, as therapeutic protein with antitumoral effect, were modified with the pH-sensitive bifunctional AzMMMan linker and varying amounts of cationic oligomer.
Structural basis of substrate specificity in porcine RNase 4.
New
Acharya et al., Bath, United Kingdom. In Febs J, Feb 2016
UNASSIGNED: RNase 4, a member of the RNase A superfamily with substrate preference for uridine, has roles in host defence, angiogenesis and neurodegenerative diseases.
Perturbation of the Conformational Dynamics of an Active-Site Loop Alters Enzyme Activity.
New
Doucet et al., Québec, Canada. In Structure, Jan 2016
Using RNase A as a model, we demonstrate that elimination of a single methyl group located >10 Å away from the reaction site significantly alters conformational integrity and binding properties of the enzyme.
Integration of kinetic isotope effect analyses to elucidate ribonuclease mechanism.
Review
New
York et al., Cleveland, United States. In Biochim Biophys Acta, Nov 2015
The basic features of this mechanism are often cited to explain rate enhancement by both protein and RNA enzymes that catalyze RNA 2'-O-transphosphorylation. Recent kinetic isotope effect analyses and computational studies are providing a more chemically detailed description of the mechanism of RNase A and the rate limiting transition state.
Characterization of secretomes provides evidence for adipose-derived mesenchymal stromal cells subtypes.
Govorun et al., Moscow, Russia. In Stem Cell Res Ther, 2014
Hypoxia resulted in secretion of 6 proteins, the most prominent included EGF-like repeats and discoidin I-like domains 3, adrenomedullin and ribonuclease 4 of RNase A family.
Eosinophil-Derived Neurotoxin (EDN/RNase 2) and the Mouse Eosinophil-Associated RNases (mEars): Expanding Roles in Promoting Host Defense.
Review
Rosenberg, Bethesda, United States. In Int J Mol Sci, 2014
The eosinophil-derived neurotoxin (EDN/RNase2) and its divergent orthologs, the mouse eosinophil-associated RNases (mEars), are prominent secretory proteins of eosinophilic leukocytes and are all members of the larger family of RNase A-type ribonucleases.
[Ribonucleases as antiviral agents].
Review
Shakh Makhmud et al., In Mol Biol (mosk), 2014
The review observes the most known RNases which possess established antiviral effects, actually intracellular RNases (RNase L, MCPIPI protein, eosinophylic RNases) as well as exogenously applied ones (RNase A, BS-RNase, onconase, binase, synthetic RNases).
fireball/amber: An Efficient Local-Orbital DFT QM/MM Method for Biomolecular Systems.
Ortega et al., Madrid, Spain. In J Chem Theory Comput, 2014
We also present examples of the application of this QM/MM approach to three representative biomolecular systems: the analysis of the effect of electrostatic embedding in the behavior of a salt bridge between an aspartic acid and a lysine residue, a study of the intermediate states for the triosephosphate isomerase catalyzed conversion of dihydroxyacetone phosphate into glyceraldehyde 3-phosphate, and the detailed description, using DFT QM/MM molecular dynamics, of the cleavage of a phosphodiester bond in RNA catalyzed by the enzyme RNase A.
Highly sensitive nuclease assays based on chemically modified DNA or RNA.
Review
Takenaka et al., Kitakyūshū, Japan. In Sensors (basel), 2013
Angiogenin, an angiogenic factor, is a member of the RNase A family.
Structural and functional relationships of natural and artificial dimeric bovine ribonucleases: new scaffolds for potential antitumor drugs.
Review
Spadaccini et al., Verona, Italy. In Febs Lett, 2013
In this context, RNase A represents a fascinating model system, since by dislocating different polypeptide chain regions, it forms many diverse oligomers.
Site-specific DICER and DROSHA RNA products control the DNA-damage response.
Impact
d'Adda di Fagagna et al., Milano, Italy. In Nature, 2012
DDR foci are sensitive to RNase A treatment, and DICER- and DROSHA-dependent RNA products are required to restore DDR foci in RNase-A-treated cells.
The nuclear transport capacity of a human-pancreatic ribonuclease variant is critical for its cytotoxicity.
GeneRIF
Vilanova et al., Girona, Spain. In Invest New Drugs, 2011
The nuclear transport of PE5 is critical for its cytotoxicity.
Interactions crucial for three-dimensional domain swapping in the HP-RNase variant PM8.
GeneRIF
Benito et al., Girona, Spain. In Biophys J, 2011
The role on the dimerization process of different residues of a domain-swapped dimer human pancreatic ribonuclease variant.
Expression and localisation of vascular ribonucleases in endothelial cells.
GeneRIF
Preissner et al., Gießen, Germany. In Thromb Haemost, 2011
Vascular RNase1 and RNase5 are mainly produced by vascular endothelial cells and can serve, depending on the vascular bed, different functions in vascular homeostasis and endothelial cell responses.
Functional role of glutamine 28 and arginine 39 in double stranded RNA cleavage by human pancreatic ribonuclease.
GeneRIF
Batra et al., New Delhi, India. In Plos One, 2010
In human pancreatic ribonuclease both glutamine 28 and arginine 39 are important for the cleavage of dsRNA.
It takes two to flirt with a dimeric RNase.
GeneRIF
D'Alessio, Napoli, Italy. In Biopolymers, 2009
Studies illustrate of the making dimeric pancreatic RNase through removal by directed mutagenesis of most of the N-terminal alpha-helix to the remainder of the protein.
Catalytic strategies of self-cleaving ribozymes.
Review
Impact
Strobel et al., New Haven, United States. In Acc Chem Res, 2008
All of these RNA enzymes catalyze self-scission of the RNA backbone using a chemical mechanism equivalent to that of RNase A. RNase A uses four basic strategies to promote this reaction: geometric constraints, activation of the nucleophile, transition-state stabilization, and leaving group protonation.
Characterization of enzyme motions by solution NMR relaxation dispersion.
Review
Impact
Watt et al., New Haven, United States. In Acc Chem Res, 2008
The CPMG experiments were applied to the backbone N-H positions of ribonuclease A (RNase A).
Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.
Impact
Eisenberg et al., Los Angeles, United States. In Nature, 2005
Here we show that a designed amyloid-like fibril of the well-characterized enzyme RNase A contains native-like molecules capable of enzymatic activity.
Oxidative folding of proteins.
Impact
Scheraga et al., Ithaca, United States. In Acc Chem Res, 2000
The oxidative folding of proteins is reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A).
More papers using RNase A antibodies
Processing of colicin V-1, a secretable marker protein of a bacterial ATP binding cassette export system, requires membrane integrity, energy, and cytosolic factors
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Sykes Kathryn F. et al., In Frontiers in Microbiology, 1995
... The cells were resuspended in 1 ml of buffer B1 (with RNase A; Qiagen, Valencia, CA, USA) to ...
Migration patterns and breast cancer risk in Asian-American women
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Jirtle Randy L. et al., In Environmental Health Perspectives, 1992
... 150 liver, day 150 brain, and day 150 kidney using buffer ATL, proteinase K, and Rnase A (Qiagen Inc., Valencia, CA) followed ...
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