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Journal Article
Developmental and Comparative Immunology, ISSN 0145-305X, 11/2018, Volume 88, pp. 152 - 160
The Notch signaling pathway transcriptional regulator, CSL (also called as CBF1, Suppressor of Hairless or Lag-1 in different species, generally designated as... 
Hemocytes proliferation | Immune resistance | Litopenaeus vannamei | LvCSL | PENAEID SHRIMP | DENDRITIC CELLS | NOTCH | IMMUNOLOGY | ADAPTIVE IMMUNITY | NEURAL STEM-CELLS | FISHERIES | ZOOLOGY | DISEASE | VIBRIO-ALGINOLYTICUS | INFECTION | DIFFERENTIATION | NF-KAPPA-B | Vibrio parahaemolyticus - immunology | Hemocytes - immunology | Arthropod Proteins - isolation & purification | Disease Resistance - immunology | Phylogeny | Vibrio Infections - immunology | Protein Domains - genetics | Gene Knockdown Techniques | Host-Pathogen Interactions - immunology | Cloning, Molecular | Fish Diseases - immunology | Protein Domains - immunology | Immunoglobulin J Recombination Signal Sequence-Binding Protein - genetics | Vibrio Infections - veterinary | Gene Expression Regulation - immunology | Penaeidae - genetics | Penaeidae - microbiology | Arthropod Proteins - genetics | Arthropod Proteins - immunology | Sequence Homology, Nucleic Acid | Vibrio Infections - virology | Sequence Alignment | Animals | Fish Diseases - virology | Immunoglobulin J Recombination Signal Sequence-Binding Protein - immunology | Immunoglobulin J Recombination Signal Sequence-Binding Protein - isolation & purification | Aquaculture | Hepatopancreas - immunology | Penaeidae - immunology | Immune response | Analysis | Cloning | Mortality | Genetic aspects | Genetic transcription | Cell differentiation | Health aspects | Mitogens
Journal Article
Immunology Letters, ISSN 0165-2478, 2012, Volume 148, Issue 1, pp. 41 - 48
Highlights ► Shrimp were vaccinated using rVP28 or rVP36B and subsequently challenged with WSSV. ► Complete survival was induced from a higher rVP28 dose and a... 
Allergy and Immunology | Vaccine | Invertebrate immunity | White spot syndrome virus (WSSV) | Shrimp | PROCAMBARUS-CLARKII | IMMUNOLOGY | ENVELOPE PROTEINS | SERINE PROTEINASE | PENAEUS-JAPONICUS | SPOT-SYNDROME-VIRUS | CULTURED KURUMA SHRIMP | ORAL VACCINATION | PROTEOMIC ANALYSIS | MARSUPENAEUS-JAPONICUS | PACIFIC WHITE SHRIMP | Hemolymph - cytology | Superoxide Dismutase - genetics | Cell Count | Hemocytes - immunology | Disease Resistance - immunology | Monophenol Monooxygenase - metabolism | White spot syndrome virus 1 - genetics | Vaccination - methods | Gene Expression - immunology | Viral Envelope Proteins - metabolism | Penaeidae - metabolism | Monophenol Monooxygenase - genetics | Adaptive Immunity - immunology | Superoxide Dismutase - metabolism | White spot syndrome virus 1 - immunology | Recombinant Proteins - metabolism | Penaeidae - virology | Viral Envelope Proteins - genetics | Hemolymph - immunology | Electrophoresis, Polyacrylamide Gel | Hemolymph - metabolism | Immunity - immunology | Reverse Transcriptase Polymerase Chain Reaction | Viral Vaccines - administration & dosage | Immunity, Innate - immunology | Superoxide Dismutase - immunology | White spot syndrome virus 1 - metabolism | Animals | Monophenol Monooxygenase - immunology | Recombinant Proteins - immunology | Viral Envelope Proteins - immunology | Viral Vaccines - immunology | Hemocytes - cytology | Penaeidae - immunology | Virus diseases | Immune response | Messenger RNA | Vaccination
Journal Article
Journal of Allergy and Clinical Immunology: In Practice, ISSN 2213-2198, 2015, Volume 3, Issue 4, pp. 521 - 529.e10
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2012, Volume 287, Issue 13, pp. 10060 - 10069
The prophenoloxidase (proPO) system is activated upon recognition of pathogens by pattern recognition proteins (PRPs), including a lipopolysaccharide-and... 
BLACK TIGER SHRIMP | MANDUCA-SEXTA | FENNEROPENAEUS-CHINENSIS | GRAM-NEGATIVE BACTERIA | LIPOTEICHOIC ACID | BIOCHEMISTRY & MOLECULAR BIOLOGY | PENAEUS-MONODON | LITOPENAEUS-VANNAMEI | TOBACCO HORNWORM | MOLECULAR-CLONING | INNATE IMMUNITY | Antimicrobial Cationic Peptides - immunology | Catechol Oxidase - immunology | Glucans - immunology | Vibrio - immunology | Enzyme Precursors - genetics | Lipopolysaccharides - metabolism | Antimicrobial Cationic Peptides - metabolism | Lipopolysaccharides - immunology | Vibrio Infections - metabolism | Enzyme Activation - immunology | Vibrio - metabolism | Lectins - metabolism | Vibrio Infections - genetics | Penaeidae - metabolism | Catechol Oxidase - genetics | Glucans - metabolism | Antimicrobial Cationic Peptides - genetics | Lectins - immunology | Vibrio - genetics | Enzyme Precursors - immunology | Penaeidae - microbiology | Glucans - pharmacology | Arthropod Proteins - genetics | Arthropod Proteins - immunology | Enzyme Activation - drug effects | Enzyme Precursors - metabolism | Animals | Catechol Oxidase - metabolism | Lipopolysaccharides - pharmacology | Arthropod Proteins - metabolism | Protein Binding | Lectins - genetics | Enzyme Activation - genetics | Penaeidae - immunology | Pattern Recognition Protein | Phenoloxidase | Carbohydrate-binding Protein | RNA Interference (RNAi) | Pathogen-associated Molecular Pattern (PAMP) | β-Glucan | Enzymology | Shrimp | Lipopolysaccharide (LPS) | Pattern Recognition Receptor
Journal Article
PLoS ONE, ISSN 1932-6203, 11/2014, Volume 9, Issue 11, pp. e111649 - e111649
Designer proteins deprived of its IgE-binding reactivity are being sought as a regimen for allergen-specific immunotherapy. Although shrimp tropomyosin (Met e... 
BIRCH POLLEN ALLERGEN | MOLECULAR CHARACTERIZATION | ANTIBODIES | MURINE MODEL | FOOD ALLERGY | MULTIDISCIPLINARY SCIENCES | MOUSE MODEL | ORAL IMMUNOTHERAPY | IDENTIFICATION | CALCIUM-BINDING PROTEIN | EPITOPES | Tropomyosin - genetics | Immunoglobulin G - blood | Humans | Molecular Sequence Data | Epitopes - immunology | Food Hypersensitivity - immunology | Immunoglobulin E - immunology | Allergens - immunology | Antibody Specificity - immunology | Immunoglobulin G - immunology | Allergens - chemistry | Female | Disease Models, Animal | Amino Acid Sequence | Immunization | Tropomyosin - immunology | Allergens - genetics | Epitopes - genetics | Proteins - immunology | Proteins - genetics | Sequence Alignment | Animals | Recombinant Proteins - immunology | Epitopes - chemistry | Mice | Mutation | Proteins - chemistry | Penaeidae - immunology | Allergens | Allergy | Analysis | Immunoglobulin E | Amino acids | Muscle proteins | Allergic reaction | Enzyme-linked immunosorbent assay | Antigenic determinants | Protein binding | Pediatrics | Animal models | Shellfish | Immunoglobulin G | Antibodies | Construction sites | Mollusks | Allergenicity | Proteins | Reduction | Crustaceans | Anaphylaxis | Clonal deletion | Immunotherapy | Deletion | Life sciences | Mathematical models | Binding | Food allergies | Immunoglobulins | Tropomyosin | Hypersensitivity | Rheumatology | Epitopes | Patients | Medicine | Reactivity | Mutagenesis | Site-directed mutagenesis | Computer applications | Degranulation | Passive cutaneous anaphylaxis | Index Medicus
Journal Article
Journal Article
Clinical & Experimental Allergy, ISSN 0954-7894, 03/2016, Volume 46, Issue 3, pp. 491 - 503
Journal Article