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

Disulphide bond restrains the C-terminal region of thermostable direct hemolysin during folding to promote oligomerization.

The Biochemical journal - 15 Jan 2017

Kundu Nidhi, Tichkule Swapnil, Pandit Shashi Bhushan, Chattopadhyay Kausik

Abstract excerpt

Pore-forming toxins (PFTs) are typically produced as water-soluble monomers, which upon interacting with target cells assemble into transmembrane oligomeric pores. Vibrio parahaemolyticus thermostable direct hemolysin (TDH) is an atypical PFT that exists as a tetramer in solution, prior to membrane binding. The TDH structure highlights a core β-sandwich domain similar to those found in the eukaryotic actinoporin...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Toxins
Share to Disulfides

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hemolysin Proteins

Share to Hemolysis

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Share to Vibrio parahaemolyticus

Source

Identifiers

PMID: 27784764
DOI: 10.1042/BCJ20160728

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disulphide bond restrains the C-terminal region of thermostable direct hemolysin during folding to promote oligomerization.PMID 27784764Read ↗

N-Terminal Region of Vibrio parahemolyticus Thermostable Direct Hemolysin Regulates the Membrane-Damaging Action of the Toxin.Semantic proximity Read ↗

Sequence Diversity in the Pore-Forming Motifs of the Membrane-Damaging Protein Toxins.Semantic proximity Read ↗

Structural basis for self-assembly of a cytolytic pore lined by protein and lipid.Semantic proximity Read ↗

Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysins.Semantic proximity Read ↗

Structural Basis of the Pore-Forming Toxin/Membrane InteractionSemantic proximity Read ↗

An intermolecular electrostatic interaction controls the prepore-to-pore transition in a cholesterol-dependent cytolysin.Semantic proximity Read ↗

Pore formation by equinatoxin, a eukaryotic pore-forming toxin, requires a flexible N-terminal region and a stable beta-sandwich.Semantic proximity Read ↗

Auto-Assembling Detoxified Staphylococcus aureus Alpha-Hemolysin Mimicking the Wild-Type Cytolytic ToxinSemantic proximity Read ↗

A molecular pin to study the dynamics of beta-barrel formation in pore-forming toxins on erythrocytes: a sliding model.Semantic proximity Read ↗

Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit beta-strand alignment.Semantic proximity Read ↗

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

Partial oligomerization of pyolysin induced by a disulfide-tethered mutant.Semantic proximity Read ↗

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