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

Construction by site-directed mutagenesis of a 39-kilodalton mosquitocidal protein similar to the larva-processed toxin of Bacillus sphaericus 2362.

Journal of bacteriology - 1 Jul 1990

Broadwell A H, Clark M A, Baumann L, Baumann P

Abstract excerpt

After ingestion of the parasporal crystals of Bacillus sphaericus, mosquito larvae process the 42-kilodalton (kDa) toxin to a protein of 39 kDa, which has an increased toxicity (A. H. Broadwell and P. Baumann, Appl. Environ. Microbiol. 53:1333-1337, 1987). A similar activation is performed by trypsin and chymotrypsin. Using site-directed mutagenesis, we have constructed derivatives of the 42-kDa toxin with a...

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 Bacterial Proteins

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

Share to Base Sequence

Share to Gene Expression

Share to Molecular Sequence Data

Share to Mutation

Share to Oligonucleotide Probes

Share to Restriction Mapping

Source

Open in PubMed Open full text

Identifiers

PMID: 2113918
DOI: 10.1128/jb.172.7.4032-4036.1990
PMCID: PMC213389

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

Construction by site-directed mutagenesis of a 39-kilodalton mosquitocidal protein similar to the larva-processed toxin of Bacillus sphaericus 2362.PMID 2113918Read ↗

The 42- and 51-kilodalton mosquitocidal proteins of Bacillus sphaericus 2362: construction of recombinants with enhanced expression and in vivo studies of processing and toxicity.Semantic proximity Read ↗

Functional complementation of nontoxic mutant binary toxins of Bacillus sphaericus 1593M generated by site-directed mutagenesis.Semantic proximity Read ↗

Identification of the functional site in the mosquito larvicidal binary toxin of Bacillus sphaericus 1593M by site-directed mutagenesis.Semantic proximity Read ↗

Development of mutants of the mosquitocidal bacterium Bacillus thuringiensis subspecies morrisoni (PG-14) toxic to lepidopterous or dipterous insects.Semantic proximity Read ↗

Binding of purified Bacillus sphaericus binary toxin and its deletion derivatives to Culex quinquefasciatus gut: elucidation of functional binding domains.Semantic proximity Read ↗

Targeted mutagenesis at charged residues in Bacillus sphaericus BinA toxin affects mosquito-larvicidal activity.Semantic proximity Read ↗

Directed mutagenesis of selected regions of a Bacillus thuringiensis entomocidal protein.Semantic proximity Read ↗

Toxicity of a Brevibacillus laterosporus strain lacking parasporal crystals against Musca domestica and Aedes aegyptiSemantic proximity Read ↗

Making 3D-Cry Toxin Mutants: Much More Than a Tool of Understanding Toxins Mechanism of Action.Semantic proximity Read ↗

Essential role of amino acids in αD-β4 loop of a Bacillus thuringiensis Cyt2Aa2 toxin in binding and complex formation on lipid membrane.Semantic proximity Read ↗

Site-directed mutations in the third domain of Bacillus thuringiensis delta-endotoxin CryIAa affect its ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles.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 ↗

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