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Spider-Venom Peptides: Structure, Pharmacology, and Potential for Control of Insect Pests
Annual Review of Entomology, ISSN 0066-4170, 1/2013, Volume 58, Issue 1, pp. 475 - 496
Spider venoms are an incredibly rich source of disulfide-rich insecticidal peptides that have been tuned over millions of years to target a wide range of...
inhibitor cystine knot | insecticidal peptide | entomopathogen | bioinsecticide | insect nervous system | transgenic plant | MANAGEMENT | TOXINS | ENTOMOLOGY | VECTOR | SCORPION | ALPHA-LATROTOXIN | EVOLUTION | NEUROTOXINS | SNOWDROP LECTIN | BIOLOGY | WEB SPIDERS | Insecticides - pharmacology | Insecticides - chemistry | Animals | Peptides - chemistry | Insecta | Spider Venoms - pharmacology | Insect Control - methods | Spider Venoms - chemistry | Spiders - chemistry | Peptides - pharmacology | Peptides | Biological control | Physiological aspects | Spider venom | Pharmacology | Research | Pests | Health aspects
inhibitor cystine knot | insecticidal peptide | entomopathogen | bioinsecticide | insect nervous system | transgenic plant | MANAGEMENT | TOXINS | ENTOMOLOGY | VECTOR | SCORPION | ALPHA-LATROTOXIN | EVOLUTION | NEUROTOXINS | SNOWDROP LECTIN | BIOLOGY | WEB SPIDERS | Insecticides - pharmacology | Insecticides - chemistry | Animals | Peptides - chemistry | Insecta | Spider Venoms - pharmacology | Insect Control - methods | Spider Venoms - chemistry | Spiders - chemistry | Peptides - pharmacology | Peptides | Biological control | Physiological aspects | Spider venom | Pharmacology | Research | Pests | Health aspects
Journal Article
Cell, ISSN 0092-8674, 11/2017, Volume 171, Issue 4, pp. 745 - 769
Synapses are specialized junctions between neurons in brain that transmit and compute information, thereby connecting neurons into millions of overlapping and...
REPEAT TRANSMEMBRANE PROTEINS | CELL-ADHESION MOLECULE | ATTENTION-DEFICIT/HYPERACTIVITY DISORDER | INHIBITORY SYNAPSES | PRESYNAPTIC NEUREXIN-3 | BIOCHEMISTRY & MOLECULAR BIOLOGY | LONG-TERM DEPRESSION | FAMILY MESSENGER-RNAS | CBLN FAMILY | ALPHA-LATROTOXIN RECEPTOR | GLUTAMATE-RECEPTOR DELTA-2 | CELL BIOLOGY | Autistic Disorder - pathology | Schizophrenia - metabolism | Cell Adhesion Molecules, Neuronal - chemistry | Alternative Splicing | Autistic Disorder - metabolism | Membrane Glycoproteins - metabolism | Signal Transduction | Tourette Syndrome - pathology | Humans | Tourette Syndrome - metabolism | Schizophrenia - pathology | Neural Pathways | Cell Adhesion Molecules, Neuronal - genetics | Animals | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Cell Adhesion Molecules, Neuronal - metabolism | Synapses | Protein Isoforms - genetics | Nervous system diseases | Disease susceptibility | Neural circuitry | Tourette's syndrome | Autism | Neurons
REPEAT TRANSMEMBRANE PROTEINS | CELL-ADHESION MOLECULE | ATTENTION-DEFICIT/HYPERACTIVITY DISORDER | INHIBITORY SYNAPSES | PRESYNAPTIC NEUREXIN-3 | BIOCHEMISTRY & MOLECULAR BIOLOGY | LONG-TERM DEPRESSION | FAMILY MESSENGER-RNAS | CBLN FAMILY | ALPHA-LATROTOXIN RECEPTOR | GLUTAMATE-RECEPTOR DELTA-2 | CELL BIOLOGY | Autistic Disorder - pathology | Schizophrenia - metabolism | Cell Adhesion Molecules, Neuronal - chemistry | Alternative Splicing | Autistic Disorder - metabolism | Membrane Glycoproteins - metabolism | Signal Transduction | Tourette Syndrome - pathology | Humans | Tourette Syndrome - metabolism | Schizophrenia - pathology | Neural Pathways | Cell Adhesion Molecules, Neuronal - genetics | Animals | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Cell Adhesion Molecules, Neuronal - metabolism | Synapses | Protein Isoforms - genetics | Nervous system diseases | Disease susceptibility | Neural circuitry | Tourette's syndrome | Autism | Neurons
Journal Article
Science Signaling, ISSN 1945-0877, 05/2013, Volume 6, Issue 276, pp. re3 - re3
Adhesion-type heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (Adhesion-GPCRs) comprise a class of widely distributed...
ALPHA-LATROTOXIN CIRL | QUANTITATIVE PHOSPHOPROTEOMICS | ACTIVATION ANTIGEN CD97 | CALCIUM-INDEPENDENT RECEPTOR | ANKLE-LINK COMPLEX | TISSUE POLARITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLANAR CELL POLARITY | 7-PASS TRANSMEMBRANE CADHERIN | BRAIN ANGIOGENESIS INHIBITOR-1 | GENOME-WIDE ASSOCIATION | CELL BIOLOGY | Biological Evolution | Animals | Receptors, G-Protein-Coupled - metabolism | Signal Transduction | Proteolysis | Humans | Protein Binding | Ligands | Receptors, G-Protein-Coupled - genetics
ALPHA-LATROTOXIN CIRL | QUANTITATIVE PHOSPHOPROTEOMICS | ACTIVATION ANTIGEN CD97 | CALCIUM-INDEPENDENT RECEPTOR | ANKLE-LINK COMPLEX | TISSUE POLARITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLANAR CELL POLARITY | 7-PASS TRANSMEMBRANE CADHERIN | BRAIN ANGIOGENESIS INHIBITOR-1 | GENOME-WIDE ASSOCIATION | CELL BIOLOGY | Biological Evolution | Animals | Receptors, G-Protein-Coupled - metabolism | Signal Transduction | Proteolysis | Humans | Protein Binding | Ligands | Receptors, G-Protein-Coupled - genetics
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Structural diversity of G protein-coupled receptors and significance for drug discovery
Nature Reviews Drug Discovery, ISSN 1474-1776, 04/2008, Volume 7, Issue 4, pp. 339 - 357
G protein-coupled receptors (GPCRs) are the largest family of membrane-bound receptors and also the targets of many drugs. Understanding of the functional...
EXTRACELLULAR CA2+-SENSING RECEPTOR | CYSTEINE-RICH DOMAIN | CALCIUM-SENSING RECEPTOR | GLUCAGON-LIKE PEPTIDE-1 | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | BETA-ADRENERGIC-RECEPTOR | MAMMALIAN TASTE RECEPTORS | POSITIVE ALLOSTERIC MODULATORS | PHARMACOLOGY & PHARMACY | METABOTROPIC GLUTAMATE RECEPTORS | AUTOSOMAL-DOMINANT HYPOCALCEMIA | ALPHA-LATROTOXIN RECEPTOR | Animals | Receptors, G-Protein-Coupled - metabolism | Humans | Drug Design | Models, Molecular | Ligands | Protein Conformation | Receptors, G-Protein-Coupled - genetics | Binding Sites | Receptors, G-Protein-Coupled - chemistry | Receptors, G-Protein-Coupled - physiology | Cell receptors | Rhodopsin | Research | Structure | Health aspects | Medical and Health Sciences | MEDICINE | Medicin och hälsovetenskap | MEDICIN
EXTRACELLULAR CA2+-SENSING RECEPTOR | CYSTEINE-RICH DOMAIN | CALCIUM-SENSING RECEPTOR | GLUCAGON-LIKE PEPTIDE-1 | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | BETA-ADRENERGIC-RECEPTOR | MAMMALIAN TASTE RECEPTORS | POSITIVE ALLOSTERIC MODULATORS | PHARMACOLOGY & PHARMACY | METABOTROPIC GLUTAMATE RECEPTORS | AUTOSOMAL-DOMINANT HYPOCALCEMIA | ALPHA-LATROTOXIN RECEPTOR | Animals | Receptors, G-Protein-Coupled - metabolism | Humans | Drug Design | Models, Molecular | Ligands | Protein Conformation | Receptors, G-Protein-Coupled - genetics | Binding Sites | Receptors, G-Protein-Coupled - chemistry | Receptors, G-Protein-Coupled - physiology | Cell receptors | Rhodopsin | Research | Structure | Health aspects | Medical and Health Sciences | MEDICINE | Medicin och hälsovetenskap | MEDICIN
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A novel evolutionarily conserved domain of cell‐adhesion GPCRs mediates autoproteolysis
The EMBO Journal, ISSN 0261-4189, 03/2012, Volume 31, Issue 6, pp. 1364 - 1378
The G protein‐coupled receptor (GPCR) Proteolysis Site (GPS) of cell‐adhesion GPCRs and polycystic kidney disease (PKD) proteins constitutes a highly conserved...
polycystic kidney disease‐1 | synapse | adhesion GPCRs | autoproteolysis | latrotoxin | polycystic kidney disease-1 | SECRETIN FAMILY | TISSUE POLARITY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CLEAVAGE | ALPHA-LATROTOXIN RECEPTOR | MEMBER | CELL BIOLOGY | GENE | PROTEIN-COUPLED RECEPTOR | PROTEOLYTIC SITE | NEUREXINS | Polycystic Kidney Diseases - genetics | Receptors, G-Protein-Coupled - metabolism | Humans | Molecular Sequence Data | Receptors, Peptide - genetics | Proteolysis | HEK293 Cells | Conserved Sequence | TRPP Cation Channels - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Polycystic Kidney Diseases - metabolism | Cell Adhesion - genetics | Cells, Cultured | Models, Molecular | Rats | Mutation - genetics | Nerve Tissue Proteins - genetics | Protein Folding | TRPP Cation Channels - genetics | Hydrolysis | Nerve Tissue Proteins - metabolism | Animals | Mice | Receptors, G-Protein-Coupled - genetics | Receptors, G-Protein-Coupled - chemistry | Evolution, Molecular | Receptors, Peptide - metabolism | Proteins | Evolution | Kidney diseases | Molecular biology | Cell adhesion & migration | CHEM
polycystic kidney disease‐1 | synapse | adhesion GPCRs | autoproteolysis | latrotoxin | polycystic kidney disease-1 | SECRETIN FAMILY | TISSUE POLARITY | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CLEAVAGE | ALPHA-LATROTOXIN RECEPTOR | MEMBER | CELL BIOLOGY | GENE | PROTEIN-COUPLED RECEPTOR | PROTEOLYTIC SITE | NEUREXINS | Polycystic Kidney Diseases - genetics | Receptors, G-Protein-Coupled - metabolism | Humans | Molecular Sequence Data | Receptors, Peptide - genetics | Proteolysis | HEK293 Cells | Conserved Sequence | TRPP Cation Channels - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Polycystic Kidney Diseases - metabolism | Cell Adhesion - genetics | Cells, Cultured | Models, Molecular | Rats | Mutation - genetics | Nerve Tissue Proteins - genetics | Protein Folding | TRPP Cation Channels - genetics | Hydrolysis | Nerve Tissue Proteins - metabolism | Animals | Mice | Receptors, G-Protein-Coupled - genetics | Receptors, G-Protein-Coupled - chemistry | Evolution, Molecular | Receptors, Peptide - metabolism | Proteins | Evolution | Kidney diseases | Molecular biology | Cell adhesion & migration | CHEM
Journal Article