Jorge Sánchez

发表

An Intramolecular Salt Bridge in Bacillus thuringiensis Cry4Ba Toxin Is Involved in the Stability of Helix α-3, Which Is Needed for Oligomerization and Insecticidal Activity

M. Soberón, A. Bravo, I. Gómez, 2017, Applied and Environmental Microbiology.

Bacillus thuringiensis Cry 1 Ab Toxin from Role of Tryptophan Residues in Toxicity of

M. Soberón, A. Bravo, Oscar, 2005 .

Identification of a calmodulin-binding site within the domain I of Bacillus thuringiensis Cry3Aa toxin.

I. García-Robles, M. Real, C. Rausell, 2012, Archives of insect biochemistry and physiology.

Bacillus thuringiensis Cry1A toxins are versatile proteins with multiple modes of action: two distinct pre-pores are involved in toxicity

S. Gill, M. Soberón, A. Bravo, 2014, The Biochemical journal.

Whole Genome Sequencing Analysis of Bacillus thuringiensis GR007 Reveals Multiple Pesticidal Protein Genes

M. Soberón, A. Bravo, I. Gómez, 2021, Frontiers in Microbiology.

Cell lines as models for the study of Cry toxins from Bacillus thuringiensis.

M. Soberón, A. Bravo, I. Gómez, 2018, Insect biochemistry and molecular biology.

Functional significance of membrane associated proteolysis in the toxicity of Bacillus thuringiensis Cry3Aa toxin against Colorado potato beetle.

I. García-Robles, M. Real, C. Rausell, 2012, Toxicon : official journal of the International Society on Toxinology.

Bacillus thuringiensis Cry1Ab Domain III β-22 Mutants with Enhanced Toxicity to Spodoptera frugiperda (J. E. Smith)

M. Soberón, A. Bravo, I. Gómez, 2020, Applied and Environmental Microbiology.

Enhancement of Bacillus thuringiensis Cry1Ab and Cry1Fa Toxicity to Spodoptera frugiperda by Domain III Mutations Indicates There Are Two Limiting Steps in Toxicity as Defined by Receptor Binding and Protein Stability

M. Soberón, A. Bravo, A. Abad, 2018, Applied and Environmental Microbiology.

Spodoptera frugiperda (J. E. Smith) Aminopeptidase N1 Is a Functional Receptor of the Bacillus thuringiensis Cry1Ca Toxin

R. Grande, M. Soberón, A. Bravo, 2018, Applied and Environmental Microbiology.

The C-terminal protoxin region of Bacillus thuringiensis Cry1Ab toxin has a functional role in binding to GPI-anchored receptors in the insect midgut

R. Grande, B. Tabashnik, M. Soberón, 2018, The Journal of Biological Chemistry.

Midgut GPI-anchored proteins with alkaline phosphatase activity from the cotton boll weevil (Anthonomus grandis) are putative receptors for the Cry1B protein of Bacillus thuringiensis.

P. Queiroz, A. Bravo, B. Ribeiro, 2010, Insect biochemistry and molecular biology.

Oligomerization is a key step for Bacillus thuringiensis Cyt1Aa insecticidal activity but not for toxicity against red blood cells.

S. Gill, M. Soberón, A. Bravo, 2020, Insect biochemistry and molecular biology.

Bacillus thuringiensis Cry1Ab Domain III β-16 Is Involved in Binding to Prohibitin, Which Correlates with Toxicity against Helicoverpa armigera (Lepidoptera: Noctuidae)

M. Soberón, A. Bravo, R. Polanczyk, 2020, Applied and Environmental Microbiology.

ABCC2 is associated with Bacillus thuringiensis Cry1Ac toxin oligomerization and membrane insertion in diamondback moth

B. Tabashnik, M. Soberón, A. Bravo, 2017, Scientific Reports.

In vivo nanoscale analysis of the dynamic synergistic interaction of Bacillus thuringiensis Cry11Aa and Cyt1Aa toxins in Aedes aegypti

S. Gill, M. Soberón, A. Bravo, 2021, PLoS pathogens.

Binding and Oligomerization of Modified and Native Bt Toxins in Resistant and Susceptible Pink Bollworm

B. Tabashnik, M. Soberón, A. Bravo, 2015, PloS one.

Cysteine Mutations in the Protoxin Region Promoter and Single cry3Aa Regulation of thuringiensis Cry1AMod Toxins under Efficient Production of Bacillus

A. Bravo, J. Ibarra, Jorge Sánchez, 2013 .

Rearrangement of N-Terminal α-Helices of Bacillus thuringiensis Cry1Ab Toxin Essential for Oligomer Assembly and Toxicity

M. Soberón, A. Bravo, I. Gómez, 2020, Toxins.

Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin

F. Valicente, M. Soberón, A. Bravo, 2018, PloS one.

Mode of action of Bacillus thuringiensis PS86Q3 strain in hymenopteran forest pests.

A. Bravo, A. Gruppe, J. Sánchez, 2001, Insect biochemistry and molecular biology.

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

M. Soberón, A. Bravo, J. Sánchez, 2000, FEMS microbiology letters.

Isolated domain II and III from the Bacillus thuringiensis CrylAb δ‐endotoxin binds to lepidopteran midgut membranes

X. Soberón, A. Bravo, J. Sánchez, 1997, FEBS letters.

Cell lines as models for the study of Cry toxins from Bacillus thuringiensis.

M. Soberón, A. Bravo, I. Gómez, 2018, Insect biochemistry and molecular biology.

Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (Say).

A. Bravo, J. Sánchez, C. Muñoz-Garay, 2004, Biochimica et biophysica acta.