Sabino Pacheco

发表

Transcriptional Profiling of Type II Toxin–Antitoxin Genes of Helicobacter pylori under Different Environmental Conditions: Identification of HP0967–HP0968 System

M. A. De la Cruz, J. Torres, J. Girón, 2016, Front. Microbiol..

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.

Enhancement of insecticidal activity of Bacillus thuringiensis Cry1A toxins by fragments of a toxin-binding cadherin correlates with oligomer formation

S. Gill, M. Soberón, A. Bravo, 2009, Peptides.

Employing phage display to study the mode of action of Bacillus thuringiensis Cry toxins

M. Soberón, A. Bravo, I. Gómez, 2008, Peptides.

The mitogen-activated protein kinase p38 is involved in insect defense against Cry toxins from Bacillus thuringiensis.

S. Gill, Roberto Villaseñor, M. Soberón, 2010, Insect biochemistry and molecular biology.

Mechanism of action of Bacillus thuringiensis insecticidal toxins and their use in the control of insect pests

M. Soberón, A. Bravo, I. Gómez, 2015 .

New Insights into the Mode of Action of Cry1Ab Toxin used in Transgenic Insect-Resistant Crops

M. Soberón, A. Bravo, I. Gómez, 2010 .

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.

The expression of Longus type 4 pilus of enterotoxigenic Escherichia coli is regulated by LngR and LngS and by H‐NS, CpxR and CRP global regulators

M. A. De la Cruz, J. Torres, J. Girón, 2017, Environmental microbiology.

Dominant Negative Mutants of Bacillus thuringiensis Cry1Ab Toxin Function as Anti-Toxins: Demonstration of the Role of Oligomerization in Toxicity

L. Masson, M. Soberón, A. Bravo, 2009, PloS one.

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.

Domain II Loop 3 of Bacillus thuringiensis Cry1Ab Toxin Is Involved in a “Ping Pong” Binding Mechanism with Manduca sexta Aminopeptidase-N and Cadherin Receptors*

G. Saab-Rincón, S. Gill, M. Soberón, 2009, The Journal of Biological Chemistry.

Functional display of Bacillus thuringiensis Cry1Ac toxin on T7 phage.

R. Sato, M. Soberón, A. Bravo, 2006, Journal of invertebrate pathology.

The Cyt1Aa toxin from Bacillus thuringiensis inserts into target membranes via different mechanisms in insects, red blood cells, and lipid liposomes

S. Gill, M. Soberón, A. Bravo, 2020, The Journal of Biological Chemistry.

Antibiotic Resistance of Gram-Negative Bacilli Isolated from Pediatric Patients with Nosocomial Bloodstream Infections in a Mexican Tertiary Care Hospital

M. A. De la Cruz, M. Ares, Sabino Pacheco, 2014, Chemotherapy.

Functional Bacillus thuringiensis Cyt1Aa Is Necessary To Synergize Lysinibacillus sphaericus Binary Toxin (Bin) against Bin-Resistant and -Refractory Mosquito Species

M. Soberón, A. Bravo, A. Pereira-Neves, 2020, Applied and Environmental Microbiology.

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.

Additional regulatory activities of MrkH for the transcriptional expression of the Klebsiella pneumoniae mrk genes: Antagonist of H-NS and repressor

M. A. De la Cruz, J. Gonzalez-Y-Merchand, M. Ares, 2017, PloS one.

Identification of Aminopeptidase-N2 as a Cry2Ab binding protein in Manduca sexta

M. Soberón, A. Bravo, I. Gómez, 2017, Peptides.

Specific binding between Bacillus thuringiensis Cry9Aa and Vip3Aa toxins synergizes their toxicity against Asiatic rice borer (Chilo suppressalis)

M. Soberón, A. Bravo, Longfa Fang, 2018, The Journal of Biological Chemistry.

Insecticidal Proteins from Bacillus thuringiensis and Their Mechanism of Action

M. Soberón, A. Bravo, I. Gómez, 2017 .

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.

Switching an anti-IgG binding site between archaeal extremophilic proteins results in Affitins with enhanced pH stability.

F. Pecorari, G. Béhar, Sabino Pacheco, 2014, Journal of biotechnology.

Helix α-3 inter-molecular salt bridges and conformational changes are essential for toxicity of Bacillus thuringiensis 3D-Cry toxin family

D. Czajkowsky, M. Soberón, A. Bravo, 2018, Scientific Reports.

Engineering Bacillus thuringiensis Cyt1Aa toxin specificity from dipteran to lepidopteran toxicity

M. Soberón, A. Bravo, J. Osuna, 2018, Scientific Reports.

Potent and Specific Inhibition of Glycosidases by Small Artificial Binding Proteins (Affitins)

Pedro M. Alzari, Frédéric Pecorari, P. Alzari, 2014, PloS one.

Molecular Characterization of SehB, a Type II Antitoxin of Salmonella enterica Serotype Typhimurium: Amino Acid Residues Involved in DNA-Binding, Homodimerization, Toxin Interaction, and Virulence

J. Gorvel, S. Méresse, M. A. De la Cruz, 2020, Frontiers in Microbiology.

A Single Point Mutation Resulting in Cadherin Mislocalization Underpins Resistance against Bacillus thuringiensis Toxin in Cotton Bollworm*

Yongbo Yang, Kaiyu Liu, M. Soberón, 2017, The Journal of Biological Chemistry.

Improvement and efficient display of Bacillus thuringiensis toxins on M13 phages and ribosomes

F. Pecorari, M. Soberón, A. Bravo, 2015, AMB Express.

A major conformational change of N‐terminal helices of Bacillus thuringiensis Cry1Ab insecticidal protein is necessary for membrane insertion and toxicity

M. Soberón, A. Bravo, I. Gómez, 2022, The FEBS Journal.

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.

Structural changes upon membrane insertion of the insecticidal pore-forming toxins produced by Bacillus thuringiensis

R. García-Suárez, M. Soberón, A. Bravo, 2023, Frontiers in Insect Science.

Corrigendum to “The mitogen-activated protein kinase p38 is involved in insect defense against Cry toxins from Bacillus thuringiensis” [Insect Biochem. Mol. Biol. 40 (1) (2010) 58–63]

S. Gill, Roberto Villaseñor, M. Soberón, 2013 .

The sigma factor SigD of Mycobacterium tuberculosis putatively enhances gene expression of the septum site determining protein under stressful environments.

M. A. De la Cruz, J. Gonzalez-Y-Merchand, S. Rivera-Gutiérrez, 2017, The new microbiologica.

Helix α-3 inter-molecular salt bridges and conformational changes are essential for toxicity of Bacillus thuringiensis 3D-Cry toxin family

D. Czajkowsky, M. Soberón, A. Bravo, 2018, Scientific Reports.

Affinity transfer to the archaeal extremophilic Sac7d protein by insertion of a CDR.

F. Pecorari, G. Béhar, Sabino Pacheco, 2014, Protein engineering, design & selection : PEDS.

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.