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

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

Biochemistry - 4 Feb 2020

Kundu Nidhi, Verma Pratima, Kumar Anil, Dhar Vinica, Dutta Somnath, Chattopadhyay Kausik

Abstract excerpt

Thermostable direct hemolysin (TDH) of Vibrio parahemolyticus is a membrane-damaging pore-forming toxin with potent cytolytic/cytotoxic activity. TDH exists as a tetramer consisting of protomers with a core β-sandwich domain, flanked by an 11-amino acid long N-terminal region (NTR). This NTR could not be modeled in the previously determined crystal structure of TDH. Moreover, the functional implication of NTR for...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Bacterial Toxins

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

Share to Biochemical Phenomena

Share to Biological Transport

Share to Hemolysin Proteins

Share to Hemolysis

Share to Protein Subunits

Share to Vibrio parahaemolyticus

Source

Identifiers

PMID: 31808340
DOI: 10.1021/acs.biochem.9b00937

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

N-Terminal Region of Vibrio parahemolyticus Thermostable Direct Hemolysin Regulates the Membrane-Damaging Action of the Toxin.PMID 31808340Read ↗

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

A mutant toxin of Vibrio parahaemolyticus thermostable direct hemolysin which has lost hemolytic activity but retains ability to bind to erythrocytes.Semantic proximity Read ↗

A High-Homology Region in Bacterial β-Barrel Pore-Forming ToxinsSemantic proximity Read ↗

Pore formation‐independent cell death induced by a β‐barrel pore‐forming toxinSemantic proximity Read ↗

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

Functional Study of Haemophilus ducreyi Cytolethal Distending Toxin Subunit B.Semantic proximity Read ↗

The aromatic ring of phenylalanine 334 is essential for oligomerization of Vibrio vulnificus hemolysin.Semantic proximity Read ↗

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

A peptide derived from the putative transmembrane domain in the tail region of E. coli toxin hemolysin E assembles in phospholipid membrane and exhibits lytic activity to human red blood cells: plausible implications in the toxic activity of the protein.Semantic proximity Read ↗

Mechanisms of assembly and cellular interactions for the bacterial genotoxin CDT.Semantic proximity Read ↗

Construction and characterization of an isogenic mutant of Vibrio parahaemolyticus having a deletion in the thermostable direct hemolysin-related hemolysin gene (trh)Semantic proximity Read ↗

Inactivation of Vibrio vulnificus hemolysin through mutation of the N- or C-terminus of the lectin-like domain.Semantic proximity Read ↗

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