Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The structural integrity exerted by N-terminal pyroglutamate is crucial for the cytotoxicity of frog ribonuclease from Rana pipiens.

Nucleic acids research - 15 Sept 2003

Liao You-Di, Wang Sui-Chi, Leu Ying-Jen, Wang Chiu-Feng, Chang Shu-Ting, Hong Yu-Ting, Pan Yun-Ru, Chen Chinpan

Abstract excerpt

Onconase, a cytotoxic ribonuclease from Rana pipiens, possesses pyroglutamate (Pyr) at the N-terminus and has a substrate preference for uridine-guanine (UG). To identify residues responsible for onconase's cytotoxicity, we cloned the rpr gene from genomic DNA and expressed it in Escherichia coli BL21(DE3). The recombinant onconase with Met at the N-terminus had reduced thermostability, catalytic activity and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epitopes

Share to Gene Expression Regulation, Enzymologic

Share to Inhibitory Concentration 50

Share to K562 Cells

Share to Mass Spectrometry

Share to Ribonucleases

Source

Open in PubMed Open full text

Identifiers

PMID: 12954760
DOI: 10.1093/nar/gkg746
PMCID: PMC203329

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The structural integrity exerted by N-terminal pyroglutamate is crucial for the cytotoxicity of frog ribonuclease from Rana pipiens.PMID 12954760Read ↗

Residues involved in the catalysis, base specificity, and cytotoxicity of ribonuclease from Rana catesbeiana based upon mutagenesis and X-ray crystallography.Semantic proximity Read ↗

Removal of N-terminal methionine from recombinant proteins by engineered E. coli methionine aminopeptidase.Semantic proximity Read ↗

Structural analysis of a type 1 ribosome inactivating protein reveals multiple L‑asparagine‑N‑acetyl‑D‑glucosamine monosaccharide modifications: Implications for cytotoxicity.Semantic proximity Read ↗

The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants.Semantic proximity Read ↗

Structure-function relations in the NTPase domain of the antiviral tRNA ribotoxin Escherichia coli PrrC.Semantic proximity Read ↗

Specificity and evolutionary conservation of the Escherichia coli RNA pyrophosphohydrolase RppH.Semantic proximity Read ↗

Distinct roles of the R3H and RRM domains in poly(A)-specific ribonuclease structural integrity and catalysis.Semantic proximity Read ↗

Engineering Human Pancreatic RNase 1 as an Immunotherapeutic Agent for Cancer Therapy Through Computational and Experimental Studies.Semantic proximity Read ↗

A fungal anticodon nuclease ribotoxin exploits a secondary cleavage site to evade tRNA repair.Semantic proximity Read ↗

Mutants of Ustilago maydis defective in production of one of two polypeptides of KP6 toxin from the preprotoxin.Semantic proximity Read ↗

The essential role of the invariant GGQ motif in the function and stability <i>in vivo</i> of bacterial release factors RF1 and RF2Semantic proximity Read ↗

Prp8 intein in fungal pathogens: target for potential antifungal drugsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.