نتائج البحث - "Coleoptera"

1

A beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite

المؤلفون: Michael Reichelt, Lingfei Hu, Peter Rahfeld, Zoe Bont, Thomas Roder, Meret Huber, Christelle Am Robert, Nicole Liechti, Saskia Gablenz, Ye Meng, Jonathan Gershenzon, Wei Huang, Christian Paetz, Sandra Irmisch, Matthias Erb, Alexander Riedel, Julia Fricke

المصدر: eLife
Huber, Meret; Roder, Thomas; Irmisch, Sandra; Riedel, Alexander; Gablenz, Saskia; Fricke, Julia; Rahfeld, Peter; Reichelt, Michael; Paetz, Christian; Liechti, Nicole; Hu, Lingfei; Bont, Zoe; Ye, Meng; Huang, Wei; Robert, Christelle A. M.; Gershenzon, Jonathan; Erb, Matthias (2021). A beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite. eLife, 10(68642) eLife Sciences Publications 10.7554/eLife.68642 <http://dx.doi.org/10.7554/eLife.68642>
eLife, Vol 10 (2021)

مصطلحات موضوعية: 0106 biological sciences, Taraxacum, Metabolite, Secondary Metabolism, Insect, 580 Plants (Botany), Sesquiterpene lactone, root herbivore, 01 natural sciences, Melolontha melolontha, chemistry.chemical_compound, Lactones, Glucosides, Plant defense against herbivory, Biology (General), media_common, chemistry.chemical_classification, 2. Zero hunger, 0303 health sciences, Ecology, biology, Hydrolysis, General Neuroscience, General Medicine, Glutathione, Coleoptera, Biochemistry, Taraxacum officinale, β-glucosidase, Larva, Inactivation, Metabolic, Medicine, Insect Proteins, Digestion, Sesquiterpenes, Research Article, QH301-705.5, Science, media_common.quotation_subject, Melolontha, Dandelion, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, plant defense, Botany, sesquiterpene lactone, Animals, Herbivory, Sugar, 030304 developmental biology, Herbivore, General Immunology and Microbiology, business.industry, fungi, Pest control, biology.organism_classification, beta-Galactosidase, chemistry, Digestive enzyme, biology.protein, Other, PEST analysis, business, 010606 plant biology & botany

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URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68c9fd5e05616c28a01a53b9faaee0ba
https://hdl.handle.net/21.11116/0000-0009-5C30-A21.11116/0000-0009-5C32-8

2

Effect of endogenous phenoloxidase on protein solubility and digestibility after processing of Tenebrio molitor, Alphitobius diaperinus and Hermetia illucens

المؤلفون: Vincenzo Fogliano, Jean-Paul Vincken, Nathalie J.G. Arts, Catriona M.M. Lakemond, Renske H. Janssen

المصدر: Food Research International 121 (2019)
Food Research International, 121, 684-690

مصطلحات موضوعية: Black soldier fly, Hermetia illucens, Food Handling, 030309 nutrition & dietetics, Blanching, medicine.medical_treatment, Alphitobius diaperinus, Yellow mealworm, 03 medical and health sciences, chemistry.chemical_compound, 0404 agricultural biotechnology, Sulfite, Levensmiddelenchemie, Protein purification, medicine, Animals, Protein extraction, Food science, Amino Acids, Tenebrio, VLAG, Enzymatic browning, 0303 health sciences, Protease, Food Chemistry, biology, Monophenol Monooxygenase, Chemistry, Diptera, Hydrolysis, 04 agricultural and veterinary sciences, biology.organism_classification, Trypsin, 040401 food science, Pepsin A, Coleoptera, Food Quality and Design, Solubility, Larva, Phenoloxidase, Lesser mealworm, Insect Proteins, Digestion, Tyrosinase, Edible insects, Food Science, medicine.drug

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URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21e7a6249497deada03396d9560475a3
https://doi.org/10.1016/j.foodres.2018.12.038

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3

Biochemical and histological alterations induced by nickel oxide nanoparticles in the ground beetle Blaps polychresta (Forskl, 1775) (Coleoptera: Tenebrionidae)

المؤلفون: Awatef Ali, Saeed El-Ashram, Salah Eldein Osman, Amal Mohamed Shouman, Shujian Huang, Dalia A. Kheirallah

المصدر: PLoS ONE, Vol 16, Iss 9, p e0255623 (2021)
PLoS ONE

مصطلحات موضوعية: Metal Nanoparticles, Insect, Endoplasmic Reticulum, Biochemistry, Ground beetle, Ascorbate Peroxidases, Beetles, Nickel, Morphogenesis, Medicine and Health Sciences, Nanotechnology, Energy-Producing Organelles, media_common, Multidisciplinary, Secretory Pathway, biology, Microvilli, Chemistry, Eukaryota, Alanine Transaminase, Mitochondria, Insects, Coleoptera, Cell Processes, Engineering and Technology, Insect Proteins, Medicine, Cellular Structures and Organelles, Anatomy, Muscle Regeneration, Peroxidase, Research Article, Histology, Arthropoda, media_common.quotation_subject, Science, Bioenergetics, Andrology, Animals, Regeneration, Aspartate Aminotransferases, Vitamin C, Organisms, Biology and Life Sciences, Midgut, Cell Biology, biology.organism_classification, Invertebrates, Gastrointestinal Tract, Nanotoxicology, biology.protein, Ultrastructure, Rough Endoplasmic Reticulum, Nanoparticles, Zoology, Entomology, Organism Development, Developmental Biology

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e65bfa1e0dae8336db7a9d250897db97
https://doaj.org/article/dd534ce14c024446b56b0f32c9d3a39e

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4

A Novel Peptide Antibiotic, Pro10-1D, Designed from Insect Defensin Shows Antibacterial and Anti-Inflammatory Activities in Sepsis Models

المؤلفون: Yangmee Kim, Ahjin Jang, Manigandan Krishnan, Joonhyeok Choi

المصدر: International Journal of Molecular Sciences
Volume 21
Issue 17
International Journal of Molecular Sciences, Vol 21, Iss 6216, p 6216 (2020)

مصطلحات موضوعية: 0301 basic medicine, Acinetobacter baumannii, Lipopolysaccharides, antimicrobial peptide, Antibiotics, Peptide, medicine.disease_cause, Bacterial cell structure, biofilm, lcsh:Chemistry, Defensins, sepsis, Mice, Drug Stability, Drug Resistance, Multiple, Bacterial, Defensin, lcsh:QH301-705.5, Spectroscopy, Escherichia coli Infections, chemistry.chemical_classification, biology, NF-kappa B, Shock, General Medicine, Antimicrobial, gram-negative infection, Computer Science Applications, Coleoptera, Insect Proteins, Female, Antibacterial activity, Signal Transduction, medicine.drug_class, 030106 microbiology, Microbial Sensitivity Tests, Catalysis, Article, Microbiology, Inorganic Chemistry, 03 medical and health sciences, medicine, Escherichia coli, Animals, Physical and Theoretical Chemistry, Molecular Biology, Organic Chemistry, Cell Membrane, biology.organism_classification, Toll-Like Receptor 4, Disease Models, Animal, 030104 developmental biology, RAW 264.7 Cells, chemistry, lcsh:Biology (General), lcsh:QD1-999, peptide antibiotics, Bacteria, Antimicrobial Cationic Peptides

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fa6725afd56dbae3623312f958473e0

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5

Identification and Functional Analysis of a Pseudo-Cysteine Protease from the Midgut Transcriptome of Sphenophorus levis

المؤلفون: Milene Ferro, Bruno Salata Lima, Flávio Henrique-Silva, Fernando Fonseca Pereira de Paula, Priscila Yumi Tanaka Shibao

المصدر: International Journal of Molecular Sciences, Vol 22, Iss 11476, p 11476 (2021)
International Journal of Molecular Sciences
Volume 22
Issue 21

مصطلحات موضوعية: Proteases, coleoptera, QH301-705.5, medicine.medical_treatment, Sequence Homology, Article, Catalysis, protease inhibitor, Inorganic Chemistry, chemistry.chemical_compound, Cysteine Proteases, medicine, Animals, cysteine protease, Amino Acid Sequence, Biology (General), Physical and Theoretical Chemistry, QD1-999, Molecular Biology, Spectroscopy, Serine protease, Protease, biology, Organic Chemistry, Gene Expression Regulation, Developmental, General Medicine, Cysteine protease, Protease inhibitor (biology), Computer Science Applications, Gastrointestinal Tract, insect digestion, Chemistry, Biochemistry, chemistry, Larva, pseudoenzyme, biology.protein, Insect Proteins, Weevils, Cystatin, PMSF, Transcriptome, medicine.drug, Cysteine