Ribonuclease, RNase A Family, 1 (Pancreatic) Proteins (RNASE1)

Arabidopsis thaliana Ribonuclease, RNase A Family, 1 (Pancreatic) (RNASE1) interaction partners

1. The wound induction of RNS1 is due in part to transcriptional regulation by wounding and abscisic acid.

Cow (Bovine) Ribonuclease, RNase A Family, 1 (Pancreatic) (RNASE1) interaction partners

1. In the regions involved in 3D swapping, the study observed an accumulation of weaknesses in the monomer, which disappear in the dimer and especially in the swapped dimer.

2. Thermal unfolding of ribonuclease A (RNase) was analyzed in various osmolyte solutions of glycine, proline, sarcosine, N,N-dimethylglycine, betaine, myo-inositol, taurine, and trimethylamine-N-oxide (TMAO).

3. Data suggest that dimerization of seminal ribonuclease (SRN) facilitates three-dimensional domain swapping; both swapped and un-swapped dimers of SRN exhibit increased flexibility as compared to monomeric subunit SRN.

4. A report of the first clear experimental evidence on the formation of a C-terminal swapped dimer of the monomeric BS-RNase derivatives.

5. investigation of structure/stability of native pancreatic RNase A compared to specific analogs: Results suggest that a reverse turn (Asn113-Pro114) exhibits great control over unfolding, conformational stability, and enzymatic activity of RNase A.

6. The initials steps of the molecular mechanism of Urea-RNase A interaction passes through the establishment of a three center four electron adduct.

7. Inactivation and reactivation of ribonuclease A studied by computer simulation.

8. Overexpression of bovine RNase in Toll-like receptor (TLR)7 transgenic mice results in reduction in splenomegaly, reduced numbers of activated B and T cells, fewer immune deposits in the kidney, reduced liver inflammation, and increased survival.

9. Data indicate that BS-RNase oligomers are more enzymatically active than the native dimer.

10. Data show that Asp83 replaced by Glu in ribonuclease A resulted in a comparable stabilization.

11. Effect of D-amino acids on the functional activity and conformational stability of ribonuclease-A

12. The domain swapping in BS-RNase must be influenced by the distinct features of the dimers, suggesting a prominent role for the interchain disulfide bridges.

13. The study suggests that domain swapping occurs via a local high-energy fluctuation at the C-terminus.

14. Folding, quality control, and secretion of pancreatic ribonuclease in live cells.

15. Hydrogen/deuterium (H/D) exchange of the RNase A C-dimer reveal that the H-bonds formed between the swapped C-terminal beta-strand and the other subunit are strong. Their rupture may be crucial for C-dimer dissociation.

16. the replacement of of Arg80 by Ser significantly decreases the cytotoxic activity of BS-RNase and the stability of the NCD form with respect to the parent protein, but does not affect the ribonucleolytic activity or the dissociation mechanism

17. These results provide support for a more general role for proline 114 isomerization as a conformational gatekeeper in domain swapping and oligomerization.

18. RNase A is chiefly unfolded in 40% acetic acid; it partially retains the native helices, whereas the beta-sheet is fully denatured and all X-Pro peptide bonds are predominantly in the trans conformation.

19. Data suggest that, in addition to Pro19 and Leu28, the presence of a glycine at the N-terminal end of the hinge peptide is also important to push the swapped form of RNase A dimer into the compact quaternary organization observed for NCD-BS.

Human Ribonuclease, RNase A Family, 1 (Pancreatic) (RNASE1) interaction partners

1. Data suggest that ribonuclease inhibitor (RNH1) protects HeLa cells from ribonuclease 1 (RNase 1).

2. Focusing on the increase in an N-glycosylated Asn residue of serum pancreatic ribonuclease 1, specifically Asn(88), affords a new diagnostic marker for pancreatic cancer

3. Deletion of five residues in the hinge loop of pancreatic ribonuclease induces formation of a domain-swapped dimer that leads to the generation of linear aggregates of pancreatic RNase, revealed by the crystal packing.

4. The reduced conformational flexibility of eosinophil cationic protein can be dynamically and functionally reproduced in the RNase A scaffold.

5. The nuclear transport of PE5 is critical for its cytotoxicity.

6. The role on the dimerization process of different residues of a domain-swapped dimer human pancreatic ribonuclease variant.

7. In human pancreatic ribonuclease both glutamine 28 and arginine 39 are important for the cleavage of dsRNA.

8. 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.

9. 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.

10. Human endothelial cells selectively express large amounts of pancreatic-type ribonuclease (RNase 1)

11. Results show that Glycine 38 is crucial for the full catalytic activity of the human enzyme on duplex RNA as its substitution with aspartate or alanine results in a drastic reduction in the dsRNA cleavage activity of HPR.

12. Results reveal the dendritic cell-activating activity of pancreatic ribonuclease and suggest that it is a likely participant of inflammatory and immune responses--an endogenous multifunctional immune alarmin.

13. Altogether the results suggest that the pressure-folding transition state of ribonuclease A looks like a collapsed globule with some secondary structure and a weakened hydrophobic core. This is the first direct comparison using a set of mutants.

14. RNase-1 has ribonuclease H activity.

15. Human pancreatic-ribonuclease interacts with importin alpha through different basic residues, including Lys1 and the arginine clusters 31-33 and 89-91.

16. The results were confirmed at the level of mRNA and protein, and suggested that four genes (OPCML, RNASE1, YES1 and ACK1) could play a key role in the tumorigenesis and metastasis of gastric cancer.

17. Structural and energetic aspects of the interaction between human RI (hRI) and human pancreatic ribonuclease (RNase 1), is reported.

18. Coulombic forces mediate extracellular and intracellular equilibria in a dichotomous manner that both endangers cells and defends them from the potentially lethal enzymatic activity of ribonucleases.

19. irrespective of differences in ethnic groups, RNASE1 might show markedly low heterogeneity in its genetic structure with regard to these SNPs

20. Multiple side chain conformations observed for key surface residues are proposed to be crucial for membrane binding as well as translocation and efficient RNA hydrolysis.

Mouse (Murine) Ribonuclease, RNase A Family, 1 (Pancreatic) (RNASE1) interaction partners

1. 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.