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

Structural and functional studies of alpha-helix 5 region from Bacillus thuringiensis Cry1Ab delta-endotoxin.

Biochimica et biophysica acta - 9 Mar 2001

Nuñez-Valdez M, Sánchez J, Lina L, Güereca L, Bravo A

Abstract excerpt

The crystal insecticidal proteins from Bacillus thuringiensis are modular proteins comprised of three domains connected by single linkers. Domain I is a seven alpha-helix bundle, which has been involved in membrane insertion and pore formation activity. Site-directed mutagenesis has contributed to identify regions that might play an important role in the structure of the pore-forming domain within the membrane....

Read the complete abstract on PubMed

Topics

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

Share to Bacillus thuringiensis
Share to Bacillus thuringiensis Toxins

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

Share to Cell Membrane Permeability

Share to Endotoxins

Share to Hemolysin Proteins

Share to Insecticides

Share to Manduca

Share to Pest Control, Biological

Source

Identifiers

PMID: 11257515
DOI: 10.1016/s0167-4838(01)00132-7

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

Structural and functional studies of alpha-helix 5 region from Bacillus thuringiensis Cry1Ab delta-endotoxin.PMID 11257515Read ↗

Analysis of mutations in the pore-forming region essential for insecticidal activity of a Bacillus thuringiensis delta-endotoxin.Semantic proximity Read ↗

The alpha-helix 4 residue, Asn135, is involved in the oligomerization of Cry1Ac1 and Cry1Ab5 Bacillus thuringiensis toxins.Semantic proximity Read ↗

Specific mutations within the alpha4-alpha5 loop of the Bacillus thuringiensis Cry4B toxin reveal a crucial role for Asn-166 and Tyr-170.Semantic proximity Read ↗

Bacillus thuringiensis Cry1Ab mutants affecting oligomer formation are non-toxic to Manduca sexta larvae.Semantic proximity Read ↗

Rearrangement of N-Terminal α-Helices of Bacillus thuringiensis Cry1Ab Toxin Essential for Oligomer Assembly and Toxicity.Semantic proximity Read ↗

The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta.Semantic proximity Read ↗

Bacillus thuringiensis Cry4Aa insecticidal protein: functional importance of the intrinsic stability of the unique α4-α5 loop comprising the Pro-rich sequence.Semantic proximity Read ↗

N546 in beta18-beta19 loop is important for binding and toxicity of the Bacillus thuringiensis Cry1Ac toxin.Semantic proximity Read ↗

Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation.Semantic proximity Read ↗

Evidence for intermolecular interaction as a necessary step for pore-formation activity and toxicity of Bacillus thuringiensis Cry1Ab toxin.Semantic proximity Read ↗

The role of a proline-induced broken-helix motif in alpha-helix 2 of Bacillus thuringiensis delta-endotoxins.Semantic proximity Read ↗

Characterization of the mechanism of action of the genetically modified Cry1AbMod toxin that is active against Cry1Ab-resistant insects.Semantic proximity Read ↗

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