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

Mass spectrometric-based revision of the structure of a cysteine-rich peptide toxin with gamma-carboxyglutamic acid, TxVIIA, from the sea snail, Conus textile.

Protein science : a publication of the Protein Society - 1 Mar 1996

Nakamura T, Yu Z, Fainzilber M, Burlingame A L

Abstract excerpt

A mollusk-specific toxin, TxVIIA, having potent paralytic activity was isolated from the venom of sea snail Conus textile (Fainzilber M et al., 1991, Eur J Biochem 202:589-595). The structure reported above was based upon amino acid analysis and the Edman degradation. We have recently reinvestigated this toxin employing some of the most novel techniques in mass spectrometry. We now report a revised structure...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Amino Acids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine

Share to Membrane Glycoproteins

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Molecular Weight

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 8868490
DOI: 10.1002/pro.5560050315
PMCID: PMC2143357

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mass spectrometric-based revision of the structure of a cysteine-rich peptide toxin with gamma-carboxyglutamic acid, TxVIIA, from the sea snail, Conus textile.PMID 8868490Read ↗

Production in Escherichia coli, folding, purification and characterization of notexin with wild type sequence and with N-terminal and catalytic site mutations.Semantic proximity Read ↗

Isolation and Characterization of a Cone Snail Protease with Homology to CRISP Proteins of the Pathogenesis-related Protein SuperfamilySemantic proximity Read ↗

Vexitoxins: a novel class of conotoxin-like venom peptides from predatory gastropods of the genus <i>Vexillum</i>Semantic proximity Read ↗

Transcriptomic messiness in the venom duct of Conus miles contributes to conotoxin diversity.Semantic proximity Read ↗

Overview of scorpion toxins specific for Na+ channels and related peptides: biodiversity, structure-function relationships and evolution.Semantic proximity Read ↗

Extensive multiplicity of the miscellaneous type of neurotoxins from the venom of the cobra Naja naja naja and structural characterization of major components.Semantic proximity Read ↗

Constant and hypervariable regions in conotoxin propeptides.Semantic proximity Read ↗

High conopeptide diversity in Conus tribblei revealed through analysis of venom duct transcriptome using two high-throughput sequencing platforms.Semantic proximity Read ↗

Exploring snake venom proteomes: multifaceted analyses for complex toxin mixtures.Semantic proximity Read ↗

Categorizing Molecular Features Of Venom Toxins Using Bioinformatics Tools.Semantic proximity Read ↗

Cone Snails Broad-Transcriptomics Elucidate the Evolutionary Diversification and Anti-Microbial Potential of ConopeptidesSemantic proximity Read ↗

Widespread Evolution of Molecular Resistance to Snake Venom α-Neurotoxins in Vertebrates.Semantic proximity Read ↗

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