I. Gómez

发表

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

Isabel Gómez, Aleksandar Popadic, Shogo Matsumoto, 2011, Journal of insect physiology.

Identification of Bacillus thuringiensis Cry1AbMod binding-proteins from Spodoptera frugiperda

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

Identification of Bacillus thuringiensis Cry3Aa toxin domain II loop 1 as the binding site of Tenebrio molitor cadherin repeat CR12.

M. Soberón, A. Bravo, I. Gómez, 2015, Insect biochemistry and molecular biology.

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.

Pore formation by Cry toxins.

M. Soberón, A. Bravo, C. Muñoz-Garay, 2010, Advances in experimental medicine and biology.

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.

Role of Tryptophan Residues in Toxicity of Cry1Ab Toxin from Bacillus thuringiensis

G. A. de la Riva, M. Soberón, A. Bravo, 2006, Applied and Environmental Microbiology.

Structural and functional analysis of the pre-pore and membrane-inserted pore of Cry1Ab toxin.

M. Soberón, A. Bravo, L. Pardo-López, 2006, Journal of invertebrate pathology.

Specific Epitopes of Domains II and III of Bacillus thuringiensis Cry1Ab Toxin Involved in the Sequential Interaction with Cadherin and Aminopeptidase-N Receptors in Manduca sexta*

J. C. Almagro, J. Miranda-Ríos, R. Grande, 2006, Journal of Biological Chemistry.

Structural changes of the Cry1Ac oligomeric pre-pore from bacillus thuringiensis induced by N-acetylgalactosamine facilitates toxin membrane insertion.

M. Soberón, A. Bravo, L. Pardo-López, 2006, Biochemistry.

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

M. Soberón, A. Bravo, Oscar, 2005 .

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

S. Gill, M. Soberón, A. Bravo, 2004, Biochimica et biophysica acta.

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

M. Soberón, A. Bravo, Joaquín Sánchez, 2002, FEBS letters.

Hydropathic Complementarity Determines Interaction of Epitope 869HITDTNNK876 in Manduca sexta Bt-R1 Receptor with Loop 2 of Domain II ofBacillus thuringiensis Cry1A Toxins*

Mario Soberón, Alejandra Bravo, E. Rudiño-Piñera, 2002, The Journal of Biological Chemistry.

Mapping the Epitope in Cadherin-like Receptors Involved inBacillus thuringiensis Cry1A Toxin Interaction Using Phage Display*

S. Gill, M. Soberón, A. Bravo, 2001, The Journal of Biological Chemistry.

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.

Bacillus thuringiensis Cry1AbMod toxin counters tolerance associated with low cadherin expression but not that associated with low alkaline phosphatase expression in Manduca sexta

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

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

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

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.

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.

Pore formation activity of Cry1Ab toxin from Bacillus thuringiensis in an improved membrane vesicle preparation from Manduca sexta midgut cell microvilli.

M. Soberón, A. Bravo, I. Gómez, 2002, Biochimica et biophysica acta.

Characterization of the mechanism of action of the genetically modified Cry1AbMod toxin that is active against Cry1Ab-resistant insects.

A. Holzenburg, M. Soberón, A. Bravo, 2009, Biochimica et biophysica acta.

A Tenebrio molitor GPI-anchored alkaline phosphatase is involved in binding of Bacillus thuringiensis Cry3Aa to brush border membrane vesicles

M. Soberón, A. Bravo, I. Gómez, 2013, Peptides.

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.

Cadherin binding is not a limiting step for Bacillus thuringiensis subsp. israelensis Cry4Ba toxicity to Aedes aegypti larvae.

S. Gill, M. Soberón, A. Bravo, 2012, The Biochemical journal.

Role of GPI-Anchored Membrane Receptors in the Mode of Action of Bacillus thuringiensis Cry Toxins

M. Soberón, A. Bravo, I. Gómez, 2012 .

Role of Alkaline Phosphatase from Manduca sexta in the Mechanism of Action of Bacillus thuringiensis Cry1Ab Toxin*

M. Soberón, A. Bravo, I. Gómez, 2010, The Journal of Biological Chemistry.

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.

Molecular basis for Bacillus thuringiensis Cry1Ab toxin specificity: two structural determinants in the Manduca sexta Bt-R1 receptor interact with loops alpha-8 and 2 in domain II of Cy1Ab toxin.

M. Soberón, A. Bravo, I. Gómez, 2003, Biochemistry.

Heliothis virescens and Manduca sextaLipid Rafts Are Involved in Cry1A Toxin Binding to the Midgut Epithelium and Subsequent Pore Formation*

S. Gill, M. Soberón, A. Bravo, 2002, The Journal of Biological Chemistry.

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.

Differential Role of Manduca sexta Aminopeptidase-N and Alkaline Phosphatase in the Mode of Action of Cry1Aa, Cry1Ab, and Cry1Ac Toxins from Bacillus thuringiensis

M. Soberón, A. Bravo, I. Gómez, 2013, Applied and Environmental Microbiology.

Functional display of Bacillus thuringiensis Cry1Ac toxin on T7 phage.

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

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.

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

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

The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta

S. Gill, M. Soberón, A. Bravo, 2008, Peptides.

Bacillus thuringiensis Cry1Ab Mutants Affecting Oligomer Formation Are Non-toxic to Manduca sexta Larvae*

G. Saab-Rincón, J. Y. Damián-Almazo, S. Gill, 2007, Journal of Biological Chemistry.

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 .

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

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

Role of receptor interaction in the mode of action of insecticidal Cry and Cyt toxins produced by Bacillus thuringiensis

M. Soberón, A. Bravo, J. Sánchez, 2007, Peptides.

Single Amino Acid Mutations in the Cadherin Receptor from Heliothis virescens Affect Its Toxin Binding Ability to Cry1A Toxins*

Alejandra Bravo, Mario Soberon, L. S. Ross, 2005, Journal of Biological Chemistry.

The Cadherin Protein Is Not Involved in Susceptibility to Bacillus thuringiensis Cry1Ab or Cry1Fa Toxins in Spodoptera frugiperda

Yongbo Yang, Kaiyu Liu, M. Jin, 2020, Toxins.

Early expression of the receptor for advanced glycation end products in a toxic model produced by 6-hydroxydopamine in the rat striatum.

N. Pastor, A. Santamaría, R. Pérez-Montfort, 2016, Chemico-biological interactions.

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.

Identification and Characterization of Receptors for Insecticidal Toxins from Bacillus thuringiensis

I. Gómez, Ricardo A. Grande-Cano, 2015 .

Engineering Modified Bt Toxins to Counter Insect Resistance

B. Tabashnik, M. Soberón, A. Bravo, 2007, Science.

Engineering Bacillus thuringiensis Cyt1Aa toxin specificity from dipteran to lepidopteran toxicity

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

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

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

Evolution of Bacillus thuringiensis Cry toxins insecticidal activity

Isabel Gómez, Mario Soberón, Alejandra Bravo, 2013, Microbial biotechnology.

Bacillus thuringiensis Cry1Ab mutants affecting oligomer formation are non-toxic to Manduca sexta larvae.

G. Saab-Rincón, J. Y. Damián-Almazo, S. Gill, 2013, The Journal of Biological Chemistry.

Oligomerization of Cry11Aa from Bacillus thuringiensis Has an Important Role in Toxicity against Aedes aegypti

G. Saab-Rincón, M. Soberón, A. Bravo, 2009, Applied and Environmental Microbiology.

Domains II and III of Bacillus thuringiensis Cry1Ab Toxin Remain Exposed to the Solvent after Insertion of Part of Domain I into the Membrane*

M. Soberón, A. Bravo, L. Pardo-López, 2011, The Journal of Biological Chemistry.

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.

Tryptophan spectroscopy studies and black lipid bilayer analysis indicate that the oligomeric structure of Cry1Ab toxin from Bacillus thuringiensis is the membrane-insertion intermediate.

Isabel Gómez, Mario Soberón, Alejandra Bravo, 2004, Biochemistry.

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.

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.

Sequential Treatment With Bacillus Calmette-Güerin (BCG) and Mitomycin C Administered With Electromotive Drug Administration (EMDA) in Patients With High-Risk Nonmuscle Invasive Bladder Cancer After BCG Failure.

A. Breda, J. Palou, I. Gómez, 2023, Clinical Genitourinary Cancer.

Identification of Bacillus thuringiensis Cry3Aa toxin domain II loop 1 as the binding site of Tenebrio molitor cadherin repeat CR12.

M. Soberón, A. Bravo, I. Gómez, 2015, Insect biochemistry and molecular biology.

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.

Important Interactions with Membrane Receptors in the Mode of Action of Bacillus thuringiensis Cry Toxins

S. Gill, M. Soberón, A. Bravo, 2005 .