Models for the structure and function of the Bacillus thuringiensis δ-endotoxins determined by compilational analysis
- 1 January 1990
- journal article
- research article
- Published by Taylor & Francis in DNA Sequence
- Vol. 1 (2) , 97-106
- https://doi.org/10.3109/10425179009016037
Abstract
The protein δ-endotoxins of Bacillus thuringiensis are a commercially and environmentally important class of highly specific insecticides. From an alignment of their sequences, certain structural and functional domains can be inferred which may shed light on the mode of action of these toxins.Keywords
This publication has 32 references indexed in Scilit:
- Helix geometry in proteinsPublished by Elsevier ,2004
- Proteolytic processing of a coleopteran-specific δ-endotoxin produced by Bacillus thuringiensis var. tenebrionisBiochemical Journal, 1989
- Location of the Bombyx mori specificity domain on a Bacillus thuringiensis delta-endotoxin protein.Proceedings of the National Academy of Sciences, 1989
- Molecular characterization of a gene encoding a 72-kilodalton mosquito-toxic crystal protein from Bacillus thuringiensis subsp. israelensisJournal of Bacteriology, 1988
- Common features of Bacillus thuringiensis toxins specific for Diptera and LepidopteraEuropean Journal of Biochemistry, 1988
- Nucleotide sequence of an additional crystal protein gene cloned fromBacillus thuringiensissubsp.thuringiensisNucleic Acids Research, 1988
- The hypervariable region in the genes coding for entomopathogenic crystal proteins of Bacillus thuringiensis: nucleotide sequence of the kurhd1 gene of subsp. kurstaki HD1Gene, 1986
- THREE-DIMENSIONAL STRUCTURE OF MEMBRANE AND SURFACE PROTEINSAnnual Review of Biochemistry, 1984
- The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesisCell, 1981
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978