ArticleBioMed research international2013
In silico prediction and in vitro characterization of multifunctional human RNase3.
Article in BioMed research international, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Candidate target genes in sepsis diagnosis and therapy: identifying hub genes with a spotlight on KLRB1.BMC infectious diseases · 2025Article
- Inflammation-related genes S100s, RNASE3, and CYBB and risk of leukemic transformation in patients with myelodysplastic syndrome with myelofibrosis.Biomarker research · 2021Article
- Heparan sulfate targeting strategy for enhancing liposomal drug accumulation and facilitating deep distribution in tumors.Drug delivery · 2020Article
- Cell Penetrating Peptide Derived from Human Eosinophil Cationic Protein Decreases Airway Allergic Inflammation.Scientific reports · 2017Article
- Exploring the mechanisms of action of human secretory RNase 3 and RNase 7 against Candida albicans.MicrobiologyOpen · 2016Article
- Insights into the Antimicrobial Mechanism of Action of Human RNase6: Structural Determinants for Bacterial Cell Agglutination and Membrane Permeation.International journal of molecular sciences · 2016Article
- A Heparan Sulfate-Binding Cell Penetrating Peptide for Tumor Targeting and Migration Inhibition.BioMed research international · 2015Article
- Basic amino acid residues of human eosinophil derived neurotoxin essential for glycosaminoglycan binding.International journal of molecular sciences · 2013Article
- Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human ribonucleases A (hRNaseA) superfamily consists of thirteen members with high-structure similarities but exhibits divergent physiological functions other than RNase activity. Evolution of hRNaseA superfamily has gained novel functions which may be preserved in a unique region or domain to account for additional molecular interactions. hRNase3 has multiple functions including ribonucleolytic, heparan sulfate (HS) binding, cellular binding, endocytic, lipid destabilization, cytotoxic, and antimicrobial activities. In this study, three putative multifunctional regions, (34)RWRCK(38) (HBR1), (75)RSRFR(79) (HBR2), and (101)RPGRR(105) (HBR3), of hRNase3 have been identified employing in silico sequence analysis and validated employing in vitro activity assays. A heparin binding peptide containing HBR1 is characterized to act as a key element associated with HS binding, cellular binding, and lipid binding activities. In this study, we provide novel insights to identify functional regions of hRNase3 that may have implications for all hRNaseA superfamily members.
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