An ADAM metalloprotease is a Cry3Aa Bacillus thuringiensis toxin receptor.
Ochoa-Campuzano, Camila
An ADAM metalloprotease is a Cry3Aa Bacillus thuringiensis toxin receptor. [electronic resource] - Biochemical and biophysical research communications Oct 2007 - 437-42 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-291X
10.1016/j.bbrc.2007.07.197 doi
ADAM Proteins--chemistry
Amino Acid Sequence
Animals
Bacillus thuringiensis Toxins
Bacterial Proteins--chemistry
Bacterial Toxins--chemistry
Binding Sites--genetics
Carrier Proteins--chemistry
Cell Membrane--enzymology
Coleoptera
Electrophoresis, Gel, Two-Dimensional
Endotoxins--chemistry
Fluorescent Dyes--chemistry
Hemolysin Proteins--chemistry
Insect Proteins--chemistry
Microvilli--enzymology
Models, Molecular
Molecular Sequence Data
Oligopeptides--chemistry
Protein Binding
Protein Structure, Tertiary
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Substrate Specificity
An ADAM metalloprotease is a Cry3Aa Bacillus thuringiensis toxin receptor. [electronic resource] - Biochemical and biophysical research communications Oct 2007 - 437-42 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0006-291X
10.1016/j.bbrc.2007.07.197 doi
ADAM Proteins--chemistry
Amino Acid Sequence
Animals
Bacillus thuringiensis Toxins
Bacterial Proteins--chemistry
Bacterial Toxins--chemistry
Binding Sites--genetics
Carrier Proteins--chemistry
Cell Membrane--enzymology
Coleoptera
Electrophoresis, Gel, Two-Dimensional
Endotoxins--chemistry
Fluorescent Dyes--chemistry
Hemolysin Proteins--chemistry
Insect Proteins--chemistry
Microvilli--enzymology
Models, Molecular
Molecular Sequence Data
Oligopeptides--chemistry
Protein Binding
Protein Structure, Tertiary
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Substrate Specificity