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Comparative Biochemistry and Physiology, Part A, ISSN 1095-6433, 01/2017, Volume 203, pp. 167 - 178
Gonad inhibiting hormone (GIH), type II class of the CHH family neuropeptides, is released by the neurohaemal XO-SG complex of the eyestalk. The inhibitory... 
Thioredoxin-fused protein | GIH polyclonal antisera | CHH family hormone | Penaeus monodon | Gonad-inhibiting hormone (GIH) | XO-SG complex | Fusion/chimeric protein | WILD-TYPE | PHYSIOLOGY | CRUSTACEAN-HYPERGLYCEMIC-HORMONE | KURUMA PRAWN | BIOCHEMISTRY & MOLECULAR BIOLOGY | LITOPENAEUS-VANNAMEI | ZOOLOGY | AMINO-ACID-SEQUENCES | HOMARUS-AMERICANUS | EYESTALK | MARSUPENAEUS-JAPONICUS | CDNA CLONING | EXPRESSION | Recombinant Fusion Proteins - pharmacology | Vitellogenesis - drug effects | Penaeidae - cytology | Penaeidae - physiology | Eye | Thioredoxins - genetics | Neurosecretory Systems - physiology | Vitellins - antagonists & inhibitors | Biological Assay | Thioredoxins - metabolism | Invertebrate Hormones - genetics | Vitellins - metabolism | Reproductive Control Agents - pharmacology | Amino Acid Sequence | Vitellogenins - metabolism | Models, Molecular | Arthropod Proteins - genetics | Recombinant Fusion Proteins - chemistry | Arthropod Proteins - chemistry | Arthropod Proteins - pharmacology | Protein Conformation | Escherichia coli Proteins - chemistry | Aquaculture | Vitellins - genetics | Neurosecretory Systems - cytology | Invertebrate Hormones - chemistry | Penaeidae - drug effects | Recombinant Fusion Proteins - metabolism | Thioredoxins - pharmacology | Invertebrate Hormones - pharmacology | Carrier Proteins - pharmacology | Escherichia coli Proteins - pharmacology | Drug Design | Conserved Sequence | Carrier Proteins - chemistry | Female | Invertebrate Hormones - metabolism | Thioredoxins - chemistry | Vitellogenins - genetics | Antibodies, Neutralizing - pharmacology | Escherichia coli Proteins - metabolism | Reproductive Control Agents - metabolism | Reproductive Control Agents - antagonists & inhibitors | Carrier Proteins - genetics | Sequence Alignment | Animals | Carrier Proteins - metabolism | Reproductive Control Agents - chemistry | Arthropod Proteins - metabolism | Escherichia coli Proteins - genetics | Neurosecretory Systems - drug effects | Structural Homology, Protein | Vitellogenins - antagonists & inhibitors | Thioredoxin | Analysis | Genetic engineering
Journal Article
Protein Science, ISSN 0961-8368, 05/2010, Volume 19, Issue 5, pp. 901 - 913
Protein crystallographers are often confronted with recalcitrant proteins not readily crystallizable, or which crystallize in problematic forms. A variety of... 
protein crystallography | rescue strategy | MBP | fixed‐arm | carrier‐driven crystallization | surface entropy reduction | Rescue strategy | Surface entropy reduction | Carrier-driven crystallization | Protein crystallography | Fixed-arm | ANGSTROM CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | F-V FRAGMENT | IN-SITU PROTEOLYSIS | carrier-driven crystallization | MALTOSE-BINDING-PROTEIN | CYTOCHROME-C-OXIDASE | PARACOCCUS-DENITRIFICANS | DRIVEN CRYSTALLIZATION | fixed-arm | FUSION PROTEIN | COUPLED-RECEPTOR | Periplasmic Binding Proteins - biosynthesis | Molecular Sequence Data | Crystallography, X-Ray | Entropy | Arthropod Proteins | Arabidopsis Proteins - biosynthesis | Base Sequence | Receptors for Activated C Kinase | Sulfotransferases - biosynthesis | Receptors, Cell Surface - chemistry | Receptors, Cell Surface - biosynthesis | Maltose-Binding Proteins | Periplasmic Binding Proteins - genetics | Periplasmic Binding Proteins - chemistry | Recombinant Fusion Proteins - biosynthesis | Sulfotransferases - genetics | Amino Acid Sequence | Arabidopsis Proteins - genetics | Antigens, Dermatophagoides - biosynthesis | Arabidopsis | Models, Molecular | Antigens, Dermatophagoides - genetics | Recombinant Fusion Proteins - chemistry | Dermatophagoides pteronyssinus | Animals | Arabidopsis Proteins - chemistry | Chickens | Recombinant Fusion Proteins - genetics | Protein Conformation | Antigens, Dermatophagoides - chemistry | Crystallization - methods | Sulfotransferases - chemistry | Receptors, Cell Surface - genetics | Proteins | Crystallization | Review
Journal Article
Development Genes and Evolution, ISSN 0949-944X, 9/2017, Volume 227, Issue 5, pp. 339 - 353
The Notch signaling pathway is highly conserved in all animal metazoa: upon Notch receptor activation, transcription of Notch target genes is turned on by an... 
Life Sciences | Biochemistry, general | Neurosciences | Notch signaling | Notch antagonist Hairless | Daphnia pulex | Developmental Biology | Drosophila melanogaster | Cell Biology | Animal Genetics and Genomics | SUPPRESSOR | COMPLEX | PROTEIN | DEVELOPMENTAL BIOLOGY | CELL BIOLOGY | NEURAL DEVELOPMENT | COREPRESSORS | GROUCHO | EVOLUTIONARY BIOLOGY | EVOLUTION | REPRESSION | CELL FATES | EXPRESSION | Transcription Factors - chemistry | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Drosophila melanogaster - metabolism | Sequence Homology | Receptors, Notch - antagonists & inhibitors | Protein Interaction Domains and Motifs | Daphnia - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Daphnia - growth & development | Repressor Proteins - chemistry | Signal Transduction | Repressor Proteins - genetics | Arthropod Proteins - genetics | Drosophila Proteins - chemistry | Transcription Factors - genetics | Daphnia - metabolism | Transcription Factors - metabolism | Arthropod Proteins - chemistry | Animals | Arthropod Proteins - metabolism | Protein Binding | Drosophila melanogaster - growth & development | Structural Homology, Protein | Drosophila Proteins - genetics | Genetic research | Wildlife conservation | Genetic transcription | Analysis | Genes | Protein binding | Hairless protein | Amino acids | Hairless | Kinases | Proteins | Gene silencing | Signal transduction | Repressors | Insects | Transcription activation | Suppressor of Hairless protein | Notch protein | Receptor mechanisms | Protein interaction
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 08/2016, Volume 11, Issue 8, p. e0160641
Background The house dust mite (HDM) allergen Der p 18 belongs to the glycoside hydrolase family 18 chitinases. The relevance of Der p 18 for house dust mite... 
PROTEIN | SENSITIZATION | RECOMBINANT | CLONING | INFLAMMATION | MULTIDISCIPLINARY SCIENCES | ASTHMA | DERMATOPHAGOIDES-PTERONYSSINUS | IGE-BINDING | IDENTIFICATION | PERITROPHIC MATRIX | Immune Sera - chemistry | Antibodies - chemistry | Humans | Pyroglyphidae - ultrastructure | Male | Antigens, Dermatophagoides - immunology | Basophils - immunology | Cloning, Molecular | Escherichia coli - metabolism | Respiratory Hypersensitivity - physiopathology | Female | Protein Interaction Domains and Motifs | Basophils - drug effects | Amino Acid Sequence | Protein Conformation, alpha-Helical | Rabbits | Gene Expression | Pyroglyphidae - chemistry | Respiratory Hypersensitivity - chemically induced | Recombinant Proteins - chemistry | Chitin - chemistry | Antigens, Dermatophagoides - genetics | Arthropod Proteins - genetics | Recombinant Proteins - genetics | Arthropod Proteins - immunology | Respiratory Hypersensitivity - immunology | Protein Folding | Basophils - cytology | Sequence Homology, Amino Acid | Arthropod Proteins - chemistry | Sequence Alignment | Animals | Protein Conformation, beta-Strand | Recombinant Proteins - immunology | Escherichia coli - genetics | Protein Binding | Antibodies - blood | Antigens, Dermatophagoides - chemistry | Chitin - immunology | Antibodies - isolation & purification | Allergens | House-dust mite | Control | Care and treatment | Respiratory allergy | Chitin | Research | Health aspects | Risk factors | Chitinase | Immunoglobulin G | Mites | Immunoglobulin E | Antibodies | Proteins | Immunology | E coli | Dichroism | Localization | Recombinant | Binding | Enzymes | Hydrolase | Cross-reactivity | Hypersensitivity | House dust | Inflammation | Electron microscopy | Secondary structure | Patients | Chromatography | Biological activity | Allergies | Circular dichroism | Asthma | Dust | Insects | Homogeneity | Diagnostic systems | Protein structure | Glycoside hydrolase | Structural analysis
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2018, Volume 13, Issue 7, p. e0200153
Embryos of the crustacean, Artemia franciscana, may undergo oviparous development, forming encysted embryos (cysts) that are released from females and enter... 
ENCYSTED EMBRYOS | DROSOPHILA-MELANOGASTER | PROTEIN GENES | MULTIDISCIPLINARY SCIENCES | APIS-CERANA-CERANA | LEA PROTEINS | INSECT DIAPAUSE | OVERWINTERING DIAPAUSE | MOSQUITO CULEX-PIPIENS | TRANSCRIPTIONAL REGULATION | BRINE SHRIMP | Amino Acid Sequence | Artemia - genetics | Gene Expression | Heat Shock Transcription Factors - metabolism | Heat-Shock Proteins, Small - metabolism | Artemia - metabolism | DNA, Complementary - genetics | Heat Shock Transcription Factors - genetics | Stress, Physiological | Arthropod Proteins - genetics | Gene Knockdown Techniques | Sequence Homology, Amino Acid | Heat-Shock Proteins, Small - genetics | Animals | Diapause - physiology | Base Sequence | Arthropod Proteins - metabolism | Protein Domains | Artemia - embryology | Female | Heat Shock Transcription Factors - antagonists & inhibitors | Diapause - genetics | Arthropod Proteins - antagonists & inhibitors | Transcription factors | Genetic aspects | Artemia | Health aspects | Diapause | Genomics | Ferritin | Homology | Chaperones | Small heat shock proteins | Heat shock factors | Proteins | Crustaceans | Synthesis | Dependence | HSF1 protein | Deoxyribonucleic acid--DNA | Stresses | RNA-mediated interference | Cloning | Heat shock proteins | Gene expression | Metabolism | Embryos | Survival | Stress | Molecular chains | Heat | Mosquitoes | Cysts | Ribonucleic acids | Insects | Females | Heat shock | Deoxyribonucleic acid | DNA
Journal Article
PLoS ONE, ISSN 1932-6203, 01/2013, Volume 8, Issue 1, p. e54053
Invertebrates rely solely on the innate immune system for defense against pathogens and other stimuli. Fatty acid binding proteins (FABP), members of the lipid... 
SHRIMP | CELLS | C-TYPE LECTIN | SUPPRESSION SUBTRACTIVE HYBRIDIZATION | RECOGNITION | MULTIDISCIPLINARY SCIENCES | LIVER | INNATE IMMUNE-RESPONSE | DIFFERENTIALLY EXPRESSED GENES | SPOT SYNDROME VIRUS | INVERTEBRATES | Escherichia coli - drug effects | Hemocytes - immunology | Fatty Acid-Binding Proteins - immunology | Gills - immunology | Phylogeny | RNA, Messenger - biosynthesis | Brachyura - metabolism | Hepatopancreas - metabolism | Lipid Metabolism - genetics | Fatty Acids - metabolism | Brachyura - immunology | Brachyura - microbiology | Fatty Acid-Binding Proteins - pharmacology | Vibrio parahaemolyticus - drug effects | RNA, Messenger - genetics | Phagocytosis - immunology | Gills - metabolism | Arthropod Proteins - genetics | Recombinant Proteins - genetics | Recombinant Proteins - pharmacology | Arthropod Proteins - immunology | Immunity, Innate | Fatty Acid-Binding Proteins - genetics | Hemocytes - metabolism | Brachyura - genetics | Gene Expression Regulation - drug effects | Protein Isoforms - pharmacology | Arthropod Proteins - pharmacology | Animals | Recombinant Proteins - immunology | Escherichia coli - genetics | Lipopolysaccharides - pharmacology | Protein Isoforms - immunology | Staphylococcus aureus - drug effects | Aeromonas hydrophila - drug effects | Bacillus subtilis - drug effects | Hepatopancreas - immunology | Protein Isoforms - genetics | Lipid metabolism | Binding proteins | Fatty acids | Analysis | Water-borne diseases | Infections | Adipocytes | Lipopolysaccharides | Proteins | Receptors | E coli | Hepatopancreas | Bacteria | Peroxidase | Inhibition | Agglutination | Immune system | Recombinant | Antigens | Bacterial infections | Crabs | Gills | Metabolism | Gene expression | Fatty acid-binding protein | Lectins | Invertebrates | Beads | Hemocytes | Vibrio
Journal Article