A non-cytotoxic but ribonucleolytically specific ribotoxin variant: implication of tryptophan residues in the cytotoxicity of hirsutellin A.

doi:10.1515/hsz-2011-0278

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

Back to search

Article

A non-cytotoxic but ribonucleolytically specific ribotoxin variant: implication of tryptophan residues in the cytotoxicity of hirsutellin A.

Biological chemistry - 1 May 2012

Herrero-Galán Elías, García-Ortega Lucía, Lacadena Javier, Martínez-del-Pozo Álvaro, Olmo Nieves, Gavilanes José G, Oñaderra Mercedes

Abstract excerpt

Ribotoxins are a family of toxic proteins that exert a highly specific cleavage at the universally conserved sarcin/ricin loop (SRL) of the larger rRNA molecule. Before this ribonucleolytic action, passage through the cell membrane is a necessary step for ribotoxin internalization and the limiting factor for cytotoxicity. Although extensive knowledge of their ribonucleolytic activity and substrate recognition has...

Topics

Cell Line, Tumor
Cell Membrane
Conserved Sequence
Cytotoxins
Endoribonucleases
Fungal Proteins
Humans
Models, Molecular
Mutation
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Synthesis Inhibitors

Protein Transport

RNA, Ribosomal

Ribonucleases

Ricin

Substrate Specificity

Tryptophan

Source

Open in PubMed

Identifiers

PMID: 22628308
DOI: 10.1515/hsz-2011-0278

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A non-cytotoxic but ribonucleolytically specific ribotoxin variant: implication of tryptophan residues in the cytotoxicity of hirsutellin A.PMID 22628308Read ↗

Implication of an Asp residue in the ribonucleolytic activity of hirsutellin A reveals new electrostatic interactions at the active site of ribotoxins.Semantic proximity Read ↗

Role of the basic character of alpha-sarcin's NH2-terminal beta-hairpin in ribosome recognition and phospholipid interaction.Semantic proximity Read ↗

NMR structure of the noncytotoxic alpha-sarcin mutant Delta(7-22): the importance of the native conformation of peripheral loops for activity.Semantic proximity Read ↗

Minimized natural versions of fungal ribotoxins show improved active site plasticity.Semantic proximity Read ↗

Involvement of loop 5 lysine residues and the N-terminal β-hairpin of the ribotoxin hirsutellin A on its insecticidal activity.Semantic proximity Read ↗

Characterization of prokaryotic recombinant Aspergillus ribotoxin alpha-sarcin.Semantic proximity Read ↗

Identification of amino acids critical for the cytotoxicity of Shiga toxin 1 and 2 in Saccharomyces cerevisiae.Semantic proximity Read ↗

The ribotoxin restrictocin recognizes its RNA substrate by selective engagement of active site residues.Semantic proximity Read ↗

The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins.Semantic proximity Read ↗

Disruption of the CD Loop by Enzymatic Cleavage Promotes the Formation of Toxic Transthyretin Oligomers through a Common Transthyretin Misfolding Pathway.Semantic proximity Read ↗

Characterization of in vitro and in vivo mutations in non-conserved nucleotides in the ribosomal RNA recognition domain for the ribotoxins ricin and sarcin and the translation elongation factors.Semantic proximity Read ↗

Conserved Arginines at the P-Protein Stalk Binding Site and the Active Site Are Critical for Ribosome Interactions of Shiga Toxins but Do Not Contribute to Differences in the Affinity of the A1 Subunits for the Ribosome.Semantic proximity Read ↗

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