about
Potent and specific inhibition of glycosidases by small artificial binding proteins (affitins)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.Employing phage display to study the mode of action of Bacillus thuringiensis Cry toxins.Affinity transfer to the archaeal extremophilic Sac7d protein by insertion of a CDR.Improvement and efficient display of Bacillus thuringiensis toxins on M13 phages and ribosomesAdditional regulatory activities of MrkH for the transcriptional expression of the Klebsiella pneumoniae mrk genes: Antagonist of H-NS and repressor.Dominant negative mutants of Bacillus thuringiensis Cry1Ab toxin function as anti-toxins: demonstration of the role of oligomerization in toxicity.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.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.A Single Point Mutation Resulting in Cadherin Mislocalization Underpins Resistance against Bacillus thuringiensis Toxin in Cotton Bollworm.Transcriptional Profiling of Type II Toxin-Antitoxin Genes of Helicobacter pylori under Different Environmental Conditions: Identification of HP0967-HP0968 System.The mitogen-activated protein kinase p38 is involved in insect defense against Cry toxins from Bacillus thuringiensis.Enhancement of insecticidal activity of Bacillus thuringiensis Cry1A toxins by fragments of a toxin-binding cadherin correlates with oligomer formation.Functional display of Bacillus thuringiensis Cry1Ac toxin on T7 phage.Switching an anti-IgG binding site between archaeal extremophilic proteins results in Affitins with enhanced pH stability.Antibiotic resistance of gram-negative bacilli isolated from pediatric patients with nosocomial bloodstream infections in a Mexican tertiary care hospital.Cell lines as models for the study of Cry toxins from Bacillus thuringiensis.Identification of Aminopeptidase-N2 as a Cry2Ab binding protein in Manduca sexta.Engineering Bacillus thuringiensis Cyt1Aa toxin specificity from dipteran to lepidopteran toxicity.Helix α-3 inter-molecular salt bridges and conformational changes are essential for toxicity of Bacillus thuringiensis 3D-Cry toxin family.New Insights into the Mode of Action of Cry1Ab Toxin used in Transgenic Insect-Resistant CropsSpecific binding between Bacillus thuringiensis Cry9Aa and Vip3Aa toxins synergizes their toxicity against Asiatic rice borer (Chilo suppressalis)Spodoptera frugiperda (J. E. Smith) Aminopeptidase N1 Is a Functional Receptor of the Bacillus thuringiensis Cry1Ca ToxinThe Cyt1Aa toxin from Bacillus thuringiensis inserts into target membranes via different mechanisms in insects, red blood cells, and lipid liposomes
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Sabino Pacheco
@ast
Sabino Pacheco
@en
Sabino Pacheco
@es
Sabino Pacheco
@nl
type
label
Sabino Pacheco
@ast
Sabino Pacheco
@en
Sabino Pacheco
@es
Sabino Pacheco
@nl
prefLabel
Sabino Pacheco
@ast
Sabino Pacheco
@en
Sabino Pacheco
@es
Sabino Pacheco
@nl
P106
P1153
56013563000
P31
P496
0000-0002-0208-0046