S
Sabino Pacheco
Researcher at National Autonomous University of Mexico
Publications - 36
Citations - 796
Sabino Pacheco is an academic researcher from National Autonomous University of Mexico. The author has contributed to research in topics: Bacillus thuringiensis & Cadherin. The author has an hindex of 15, co-authored 34 publications receiving 661 citations. Previous affiliations of Sabino Pacheco include French Institute of Health and Medical Research & University of Nantes.
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Journal ArticleDOI
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
Sabino Pacheco,Isabel Gómez,Iván Arenas,Gloria Saab-Rincón,Claudia Rodríguez-Almazán,Sarjeet S. Gill,Alejandra Bravo,Mario Soberón +7 more
TL;DR: Cry1Ab mutants located in domain II loop 3 are affected in binding to both receptors and toxicity against Manduca sexta larvae, suggesting that loop 3 is differentially involved in the binding with both receptor molecules, depending on the oligomeric state of the toxin.
Journal ArticleDOI
The mitogen-activated protein kinase p38 is involved in insect defense against Cry toxins from Bacillus thuringiensis.
Angeles Cancino-Rodezno,Cynthia Alexander,Roberto Villaseñor,Sabino Pacheco,Helena Porta,Yannick Pauchet,Mario Soberón,Sarjeet S. Gill,Alejandra Bravo +8 more
TL;DR: It is found that both insects respond to Cry toxin action but M. sexta responses more strongly than A. aegypti, suggesting that the MAPK p38 pathway is involved in insect defense against Bt Cry toxins.
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Enhancement of insecticidal activity of Bacillus thuringiensis Cry1A toxins by fragments of a toxin-binding cadherin correlates with oligomer formation.
TL;DR: Cry1A toxin oligomer is in part responsible for the enhancement of Cry1A toxicity by cadherin fragments that is observed in vivo, and analysis of in vitro Cry1Ab in vitro oligomer formation showed a correlation between enhancement ofcry1A toxins activity in bioassays and in vitroCry1Ab-oligomer formation.
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Dominant Negative Mutants of Bacillus thuringiensis Cry1Ab Toxin Function as Anti-Toxins: Demonstration of the Role of Oligomerization in Toxicity
Claudia Rodríguez-Almazán,Luis Enrique Zavala,Carlos Muñoz-Garay,Nuria Jiménez-Juárez,Sabino Pacheco,Luke Masson,Mario Soberón,Alejandra Bravo +7 more
TL;DR: It is demonstrated that oligomerization is a fundamental step in Cry toxin action and represent a potential mechanism to protect special ecosystems from the possible effect of Cry toxins on non-target organisms.
Journal ArticleDOI
Potent and specific inhibition of glycosidases by small artificial binding proteins (affitins).
Agustín Correa,Sabino Pacheco,Ariel E. Mechaly,Gonzalo Obal,Ghislaine Béhar,Barbara Mouratou,Barbara Mouratou,Barbara Mouratou,Pablo Oppezzo,Pedro M. Alzari,Frédéric Pecorari,Frédéric Pecorari,Frédéric Pecorari +12 more
TL;DR: The design and characterization of proteinaceous inhibitors that specifically target endoglycosidase representative of the two major mechanistic classes; retaining and inverting glycosidases are reported here.