نتائج البحث - "Salvador Herrero"

81

Increase in midgut microbiota load induces an apparent immune priming and increases tolerance to Bacillus thuringiensis

المؤلفون: Gloria Navarro-Cerrillo, Salvador Herrero, Bahram Naseri, Juan Ferré, Patricia Hernández-Martínez, Baltasar Escriche

المصدر: Environmental Microbiology.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::4b1092948ca5b7b7454ad114bf6cf472Test
https://doi.org/10.1111/j.1462-2920.2010.02241.xTest

82

Increase in midgut microbiota load induces an apparent immune priming and increases tolerance to Bacillus thuringiensis

المؤلفون: Patricia, Hernández-Martínez, Bahram, Naseri, Gloria, Navarro-Cerrillo, Baltasar, Escriche, Juan, Ferré, Salvador, Herrero

المصدر: Environmental microbiology. 12(10)

مصطلحات موضوعية: Gastrointestinal Tract, Male, Larva, Bacillus thuringiensis, Colony Count, Microbial, Immune Tolerance, Animals, Female, Spodoptera, Bacterial Load, Biomarkers, Gram-Positive Bacterial Infections, Immunity, Innate

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=pmid________::314f4f08f215a96c267f315db885d37bTest
https://pubmed.ncbi.nlm.nih.gov/20482744Test

83

Constitutive Activation of the Midgut Response to Bacillus thuringiensis in Bt-Resistant Spodoptera exigua

المؤلفون: Juan Ferré, William J. Moar, Baltasar Escriche, Salvador Herrero, Ruud A. de Maagd, Silvia Caccia, Patricia Hernández-Martínez, Gloria Navarro-Cerrillo

المساهمون: Hernández Martínez, Patricia, Navarro Cerrillo, Gloria, Caccia, Silvia, de Maagd, Ruud A, Moar, William J, Ferré, Juan, Escriche, Baltasar, Herrero, Salvador

المصدر: PLoS ONE 5 (2010) 9
PLoS ONE
PLoS ONE, 5(9)
PLoS ONE, Vol 5, Iss 9, Pp 3307-3314 (2010)

مصطلحات موضوعية: 0106 biological sciences, Drug Resistance, lcsh:Medicine, Gene Expression, Insect, aminopeptidase n, 01 natural sciences, Aminopeptidases, Hemolysin Proteins, Endotoxin, manduca-sexta, Bacillus thuringiensis, Insect Protein, Biotechnology/Applied Microbiology, lcsh:Science, heliothis-virescens, media_common, 0303 health sciences, Larva, Multidisciplinary, biology, mediated insect resistance, Genetics and Genomics/Gene Expression, Ecology/Population Ecology, bacterial-infection, Noctuidae, Insect Proteins, Research Article, media_common.quotation_subject, Aminopeptidase, Molecular Sequence Data, Bacterial Protein, Spodoptera, stem-cell proliferation, Microbiology, 03 medical and health sciences, Microbiology/Applied Microbiology, Bacterial Proteins, Exigua, Botany, Bacillus thuringiensi, Animals, crystal proteins, BIOS Plant Development Systems, Amino Acid Sequence, kinase pathways, 030304 developmental biology, posterior midgut, Heliothis virescens, Bacillus thuringiensis Toxins, Animal, trichoplusia-ni, lcsh:R, fungi, Midgut, Hemolysin Protein, biology.organism_classification, Endotoxins, Gastrointestinal Tract, 010602 entomology, Plant Biology/Agricultural Biotechnology, lcsh:Q, Sequence Alignment

وصف الملف: application/pdf; application/octet-stream

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9965836f75ea8c117488fbfd8af4b28eTest
https://research.wur.nl/en/publications/constitutive-activation-of-the-midgut-response-to-bacillus-thurinTest

84

Host-range expansion of Spodoptera exigua multiple nucleopolyhedrovirus to Agrotis segetum larvae when the midgut is bypassed

المؤلفون: Salvador Herrero, Agata K. Jakubowska, Dwight E. Lynn, Monique M. van Oers, Just M. Vlak

المصدر: Journal of General Virology 91 (2010) 4
Journal of General Virology, 91(4), 898-906

وصف الملف: application/pdf; application/octet-stream

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afe0cc3570e7db6528e372e04b5fc370Test
https://pubmed.ncbi.nlm.nih.gov/19923260Test

85

Bacillus thuringiensis Cry1Ca-resistant Spodoptera exigua lacks expression of one of four Aminopeptidase N genes

المؤلفون: William J. Moar, Tsanko Gechev, Salvador Herrero, Petra L. Bakker, Ruud A. de Maagd

المصدر: BMC Genomics
BMC Genomics, Vol 6, Iss 1, p 96 (2005)
BMC Genomics 6 (2005)
BMC Genomics, 6, 96-96

مصطلحات موضوعية: Gene Expression, bombyx-mori, brush-border membrane, Hemolysin Proteins, manduca-sexta, Bacillus thuringiensis, Cluster Analysis, Cloning, Molecular, heliothis-virescens, Phylogeny, biology, Nucleic Acid Hybridization, plutella-xylostella, cry1a toxins, Up-Regulation, PRI Bioscience, toxin receptor, hormones, hormone substitutes, and hormone antagonists, Biotechnology, Delta endotoxin, Research Article, animal structures, DNA, Complementary, lcsh:QH426-470, lcsh:Biotechnology, Bacterial Toxins, Molecular Sequence Data, Down-Regulation, midgut, Spodoptera, CD13 Antigens, Bacterial Proteins, Complementary DNA, lcsh:TP248.13-248.65, Exigua, Genetics, Escherichia coli, Animals, Amino Acid Sequence, RNA, Messenger, Pest Control, Biological, DNA Primers, Gene Library, Bacillus thuringiensis Toxins, Models, Genetic, Sequence Homology, Amino Acid, cDNA library, molecular-cloning, fungi, Midgut, Sequence Analysis, DNA, biology.organism_classification, Blotting, Northern, Molecular biology, Endotoxins, lcsh:Genetics, Gene Expression Regulation, Suppression subtractive hybridization, delta-endotoxin, Software

وصف الملف: application/pdf; application/octet-stream

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98900af212e63c737041a99dd177843dTest
https://pubmed.ncbi.nlm.nih.gov/15978131Test

86

Identification and recombinant expression of a novel chymotrypsin from Spodoptera exigua

المؤلفون: Eliette Combes, Jules Beekwilder, Just M. Vlak, Ruud A. de Maagd, Monique M. van Oers, Salvador Herrero

المصدر: Insect Biochemistry and Molecular Biology, 35(10), 1073-1082
Insect Biochemistry and Molecular Biology 35 (2005) 10

مصطلحات موضوعية: Laboratory of Virology, Biochemistry, law.invention, Serine, chemistry.chemical_compound, law, manduca-sexta, Chymotrypsin, Conserved Sequence, Phylogeny, trypsin-inhibitor, Trypsin, PE&RC, Recombinant Proteins, PRI Bioscience, Recombinant DNA, medicine.drug, Proteases, Molecular Sequence Data, agrotis-ipsilon, proteinase-inhibitors, larvae, midgut, Biology, Spodoptera, bacillus-thuringiensis toxins, Laboratorium voor Virologie, medicine, Animals, Amino Acid Sequence, Molecular Biology, DNA Primers, Base Sequence, Sequence Homology, Amino Acid, fungi, Midgut, sequence, biology.organism_classification, Molecular biology, chemistry, Insect Science, biology.protein, Cattle, proteases, helicoverpa-zea, PMSF

وصف الملف: application/octet-stream; application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ca3d3f7f93b4ac5e881f488d6842c26Test
https://research.wur.nl/en/publications/identification-and-recombinant-expression-of-a-novel-chymotrypsinTest

87

Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae

المؤلفون: Ruud A. de Maagd, Juan Ferré, Joel González-Cabrera, Petra L. Bakker, Salvador Herrero

المصدر: Herrero,S.; González Cabrera, J.; Ferré, J.; Bakker, P.; de Maagd, R.A. Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae. En Biochemical Journal 384, 2004, 507–513
Biochemical Journal 384 (2004) 3
Biochemical Journal, 384(3), 507-513
RODERIC. Repositorio Institucional de la Universitat de Valéncia
instname
BASE-Bielefeld Academic Search Engine

مصطلحات موضوعية: Models, Molecular, Mutant, Laboratory of Virology, aminopeptidase n, medicine.disease_cause, Biochemistry, brush-border membrane, Toxin oligomerization, Substrate Specificity, Bacterial toxin, Manduca sexta, Mode of action, Protoxin activation, Toxin receptor binding, Hemolysin Proteins, manduca-sexta, Bacillus thuringiensis, heliothis-virescens, Alanine, CIENCIAS DE LA VIDA::Bioquímica [UNESCO], Microvilli, biology, PRI Bioscience, Larva, Thermodynamics, Research Article, Protein Binding, Bacterial Toxins, pink-bollworm, Spodoptera, Binding, Competitive, Laboratorium voor Virologie, Bacterial Proteins, Exigua, medicine, irreversible binding, Animals, crystal proteins, Protein Structure, Quaternary, Molecular Biology, Bacillus thuringiensis Toxins, Toxin, insecticidal toxin, pore formation, Cytoplasmic Vesicles, fungi, UNESCO::CIENCIAS DE LA VIDA::Bioquímica, Cell Biology, biology.organism_classification, Protein Structure, Tertiary, Endotoxins, Mutation, cryia delta-endotoxins