A. Bravo | Semantic Scholar

Publications
Influence

Characterization of cry Genes in a Mexican Bacillus thuringiensis Strain Collection

A. Bravo, Sergio Sarabia, R. Quintero
Medicine, Biology
Applied and Environmental Microbiology
1 December 1998

The results indicate the presence of strains that may harbor potentially novel Cry proteins as well as strains with combinations of less frequently observed cry genes, which could lead to novel bioinsecticidal products.

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Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect control.

A. Bravo, S. Gill, M. Soberón
Biology
Toxicon : official journal of the International…
15 March 2007

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Bacillus thuringiensis: A story of a successful bioinsecticide.

A. Bravo, Supaporn Likitvivatanavong, S. Gill, M. Soberón
Biology
Insect biochemistry and molecular biology
1 July 2011

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RNA interference in Lepidoptera: an overview of successful and unsuccessful studies and implications for experimental design.

O. Terenius, A. Papanicolaou, G. Smagghe
Biology
Journal of insect physiology
1 February 2011

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Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains.

A. Bravo, I. Gómez, M. Soberón
Biology, Chemistry
Biochimica et biophysica acta
17 November 2004

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How Bacillus thuringiensis has evolved specific toxins to colonize the insect world.

R. D. de Maagd, A. Bravo, N. Crickmore
Biology
Trends in genetics : TIG
1 April 2001

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Structure, diversity, and evolution of protein toxins from spore-forming entomopathogenic bacteria.

R. D. de Maagd, A. Bravo, C. Berry, N. Crickmore, H. E. Schnepf
Biology
Annual review of genetics
28 November 2003

Most of the toxins used by Gram-positive spore-forming entomopathogenic bacteria are produced in large amounts during sporulation and have the remarkable feature that they are localized in parasporal crystals.

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Cadherin‐like receptor binding facilitates proteolytic cleavage of helix α‐1 in domain I and oligomer pre‐pore formation of Bacillus thuringiensis Cry1Ab toxin

I. Gómez, Joaquín Sánchez, R. Miranda, A. Bravo, M. Soberón
Biology, Chemistry
FEBS letters
27 February 2002

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Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection.

L. Pardo-López, M. Soberón, A. Bravo
Biology
FEMS microbiology reviews
2013

Activity of Cry1AMod toxins, which are able to form toxin oligomers in the absence of receptors, against different resistant populations, supports the hypothesis that toxin oligomerization is a limiting step in the Cry insecticidal activity.

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Bacillus thuringiensis subsp. israelensis Cyt1Aa synergizes Cry11Aa toxin by functioning as a membrane-bound receptor.

C. Perez, L. E. Fernández, A. Bravo
Biology
Proceedings of the National Academy of Sciences…
20 December 2005

Evidence is provided that Cyt1Aa functions as a receptor of Cry11Aa, a highly effective pathogenic bacterium that produces a toxin and also its functional receptor, promoting toxin binding to the target membrane and causing toxicity.

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