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

Functional domains of a pore-forming cardiotoxic protein, volvatoxin A2.

The Journal of biological chemistry - 20 Feb 2004

Weng Yui-Ping, Lin Ya-Ping, Hsu Chyong-Ing, Lin Jung-Yaw

Abstract excerpt

Volvatoxin A2 (VVA2), a novel pore-forming cardiotoxic protein was isolated from the mushroom Volvariella volvacea. We identified an N-terminal fragment (NTF) (1-127 residues) of VVA2 as a domain for oligomerization by limited tryptic digestion. On preincubation of NTF with VVA2, NTF was found to inhibit VVA2 hemolytic activity by inducing VVA2 oligomerization in the solution in the same manner as liposomes. By...

Read the complete abstract on PubMed

Topics

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

Share to Agaricales
Share to Bacillus thuringiensis
Share to Chromatography

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosaminoglycans

Share to Hemolysis

Share to Heparin

Share to Liposomes

Share to Mycotoxins

Source

Identifiers

PMID: 14645370
DOI: 10.1074/jbc.M308675200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional domains of a pore-forming cardiotoxic protein, volvatoxin A2.PMID 14645370Read ↗

Computational Exploration of Plant Ribosome Inactivating Proteins (RIPs) in Countering Snake Venom: A Novel Therapeutic Opportunity and ChallengesSemantic proximity Read ↗

A new Kunitz-type snake toxin family associated with an original mode of interaction with the vasopressin 2 receptor.Semantic proximity Read ↗

Presence of WH2 like domain in VgrG-1 toxin of <i>Vibrio cholerae</i> reveals the molecular mechanism of actin cross-linkingSemantic proximity Read ↗

Integrative multi-omics analysis reveals the contribution of neoVTX genes to venom diversity of Synanceia verrucosaSemantic proximity Read ↗

Clostridium perfringens Delta Toxin Is Sequence Related to Beta Toxin, NetB, and Staphylococcus Pore-Forming Toxins, but Shows Functional DifferencesSemantic proximity Read ↗

Hydralysins, a new category of beta-pore-forming toxins in cnidaria.Semantic proximity Read ↗

Analysis of the interaction of tarantula toxin Jingzhaotoxin-III (β-TRTX-Cj1α) with the voltage sensor of Kv2.1 uncovers the molecular basis for cross-activities on Kv2.1 and Nav1.5 channels.Semantic proximity Read ↗

Differential structural characteristics, physicochemical properties, and calcium-binding capabilities of annexin A2 wild-type versus E53A, E96A, D162A, E247A and D322A mutants.Semantic proximity Read ↗

High throughput screening and identification of coagulopathic snake venom proteins and peptides using nanofractionation and proteomics approachesSemantic proximity Read ↗

Deciphering the venomic transcriptome of killer-wasp Vespa velutina.Semantic proximity Read ↗

Bioinformatic design of venom toxin-specific antivenom to improve the treatment of snakebite in AfricaSemantic proximity Read ↗

Novel antioxidant peptides from hydrolyzed proteins of Volvariella volvacea: Purification, characterization and protective effects on H2O2-induced human skin fibroblastsSemantic proximity Read ↗

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