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1. Some structural and functional aspects of presynaptic neurotoxins from elapid snakes
by Lind, Peter
1981, ISBN 9155411975, 37
Book
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2. Fundamental neuropathology for pathologists and toxicologists
: principles and techniques
by Bolon, Brad and Butt, Mark T
2011, 1. Aufl., ISBN 9780470939956, xx, 590
This book offers pathologists, toxicologists, other medical professionals, and students an introduction to the discipline and techniques of neuropathology –... 
Nervous system | Neurotoxicology | Diseases | Science | Chemistry | Industrial & Technical
Book
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3. Neurotoxicity research
Neurotoxicity Society
Neurotoxicity research, ISSN 1029-8428, 1999
Regeneration | Nervous system | Degeneration | Neurotoxicology | Apoptosis | Neurotoxic agents
Journal
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4. Clinical neurotoxicology
: syndromes, substances, environments
by Dobbs, Michael R
2009, ISBN 0323052606, xxii, 691 p., [16] p. of plates
Clinical Neurotoxicology offers accurate, relevant, and comprehensive coverage of a field that has grown tremendously in the last 20 years. You'll get a... 
Neurotoxicology
Book
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5. Full Text Investigation of the relationship between the structure and function of Ts2, a neurotoxin from Tityus serrulatus venom
by Cologna, Camila T and Peigneur, Steve and Rustiguel, Joane K and Nonato, M. Cristina and Tytgat, Jan and Arantes, Eliane C
FEBS Journal, ISSN 1742-464X, 04/2012, Volume 279, Issue 8, pp. 1495 - 1504
Scorpion toxins targeting voltage‐gated sodium (Na V ) channels are peptides that comprise 60–76 amino acid residues cross‐linked by four disulfide bridges.... 
Tityus serrulatus | β‐neurotoxin | Ts2 three‐dimensional structure | α‐neurotoxin | sodium channel | Ts2 three-dimensional structure | α-neurotoxin | β-neurotoxin | Tityus serrulatus | CATION-PI INTERACTIONS | RECEPTOR-SITES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GATED SODIUM-CHANNELS | INSECT | ss-neurotoxin | a-neurotoxin | DOMAIN-II | BETA-TOXINS | SCORPION ALPHA-TOXINS | NA+-CHANNELS | MOLECULAR-GRAPHICS PROJECT | Electrophysiology | Molecular Sequence Data | Scorpions - metabolism | Oocytes - cytology | Scorpion Venoms - toxicity | Sodium Channels - metabolism | Oocytes - drug effects | Female | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Sodium Channel Blockers - toxicity | Amino Acid Sequence | Neurotoxins - chemistry | Oocytes - metabolism | Cells, Cultured | Models, Molecular | Rats | Neurotoxins - toxicity | Sodium Channels - drug effects | Sequence Homology, Amino Acid | Animals | Scorpion Venoms - chemistry | Xenopus laevis - metabolism | Mice | Sodium Channel Blockers - chemistry | Ion Channel Gating - drug effects | RNA | Peptides | Analysis | Venom | Investigations | Index Medicus
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6. Full Text Short-chain consensus alpha-neurotoxin: a synthetic 60-mer peptide with generic traits and enhanced immunogenic properties
by de la Rosa, Guillermo and Corrales-García, Ligia L and Rodriguez-Ruiz, Ximena and López-Vera, Estuardo and Corzo, Gerardo
Amino Acids, ISSN 0939-4451, 7/2018, Volume 50, Issue 7, pp. 885 - 895
The three-fingered toxin family and more precisely short-chain α-neurotoxins (also known as Type I α-neurotoxins) are crucial in defining the elapid... 
Biochemistry, general | α-Neurotoxin | Neurobiology | Antisera | Synthetic gene | Elapid | Life Sciences | Analytical Chemistry | Micrurus | Life Sciences, general | Biochemical Engineering | Proteomics | Three finger toxins | Recombinant | 3-FINGER TOXINS | VENOM | MUTAGENESIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CLINICAL-FEATURES | EVOLUTION | alpha-Neurotoxin | INHIBITORS | PROTEINS | RESIDUES | SNAKE NEUROTOXINS | Elapid Venoms - chemistry | Neurotoxins - chemistry | Rabbits | Peptides - chemistry | Elapidae | Peptides - immunology | Peptides - genetics | Elapid Venoms - immunology | Recombinant Proteins - chemistry | Recombinant Proteins - biosynthesis | Recombinant Proteins - pharmacology | Peptides - pharmacology | Animals | Peptide Biosynthesis | Neurotoxins - biosynthesis | Recombinant Proteins - immunology | Neurotoxins - pharmacokinetics | Mice | Neurotoxins - immunology | Biological products | Peptides | Venom | Escherichia coli | Amino acids | Genetic engineering | Health aspects | Snakes | Cell culture | Neurotoxins | Immunization | Nucleotide sequence | Chains | Gene expression | Receptors | Conserved sequence | Immunogenicity | Proteolysis | Acetylcholine receptors (nicotinic) | Toxins | Acetylcholine | Index Medicus
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7. Full Text Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake α-neurotoxins and nicotinic receptors
by Hansen, Scott B and Bourne, Yves and Talley, Todd T and Taylor, Palmer and Marchot, Pascale
The EMBO Journal, ISSN 0261-4189, 04/2005, Volume 24, Issue 8, pp. 1512 - 1522
The crystal structure of the snake long α‐neurotoxin, α‐cobratoxin, bound to the pentameric acetylcholine‐binding protein (AChBP) from Lymnaea stagnalis , was... 
crystal structure | high‐affinity toxin–receptor complex | snake three‐fingered α‐neurotoxin | acetylcholine‐binding protein | nicotinic acetylcholine receptor | Acetylcholine-binding protein | Snake three-fingered α-neurotoxin | Nicotinic acetylcholine receptor | Crystal structure | High-affinity toxin-receptor complex | VENOM | SITE | high-affinity toxin-receptor complex | BUNGAROTOXIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | CONFORMATION | ACETYLCHOLINE-BINDING-PROTEIN | CELL BIOLOGY | NMR | snake three-fingered alpha-neurotoxin | CALIFORNICA | ION-CHANNEL | acetylcholine-binding protein | SUBUNIT | Models, Theoretical | Amino Acid Sequence | Receptors, Nicotinic - metabolism | Cobra Neurotoxin Proteins - metabolism | Humans | Multiprotein Complexes | Models, Molecular | Molecular Sequence Data | Cobra Neurotoxin Proteins - chemistry | Carrier Proteins - genetics | Sequence Alignment | Animals | Carrier Proteins - metabolism | Cobra Neurotoxin Proteins - genetics | Receptors, Nicotinic - chemistry | Protein Binding | Carrier Proteins - chemistry | Protein Conformation | Receptors, Nicotinic - genetics | Index Medicus | high-affinity toxin–receptor complex | snake three-fingered α-neurotoxin
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8. Chemo fog
: cancer chemotherapy-related cognitive impairment
by Raffa, Robert B and Tallarida, Ronald J
2010, Advances in experimental medicine and biology, ISBN 1441963057, Volume 678., xxi, 216
This resource has been compiled by editors who are professors researching factors that compromise the total healing of body and mind in this patient... 
toxicity | chemically induced | Complications | Drug Therapy | Cognition disorders | Antineoplastic agents | Chemotherapy | Side effects | Neurotoxicity Syndromes | pharmacokinetics | adverse effects | Models, Animal | Cancer | Neurotoxic agents | Cancer Research | Biomedicine general | Biomedicine
Book
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9. Production of a purified marine neurotoxin and demonstration of its binding affinity to ion channel receptors
: final report
by Balthrop, J.E and Babinchak, J.A and Travis, P.B and Herring, T.L and Brown-Eyo, P.Y
1988, 18
neurotoxins | ciguatoxins
Book
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10. Full Text Neurotoxicity of Micrurus lemniscatus lemniscatus (South American coralsnake) venom in vertebrate neuromuscular preparations in vitro and neutralization by antivenom
by Floriano, Rafael S and Schezaro-Ramos, Raphael and Silva Jr, Nelson J and Bucaretchi, Fábio and Rowan, Edward G and Hyslop, Stephen
Archives of Toxicology, ISSN 0340-5761, 7/2019, Volume 93, Issue 7, pp. 2065 - 2086
We investigated the effect of South American coralsnake (Micrurus lemniscatus lemniscatus) venom on neurotransmission in vertebrate nerve–muscle preparations... 
Biomedicine, general | Biomedicine | Environmental Health | Antivenom | α-Neurotoxin | Occupational Medicine/Industrial Medicine | Phospholipase A 2 (β-neurotoxin) | Neuromuscular blockade | Pharmacology/Toxicology | Coralsnake venom | Neutralization | β-neurotoxin | Phospholipase A | MYONECROSIS | ASP49 PHOSPHOLIPASE A | FOREST VIPER VENOM | TAIPOXIN | Phospholipase A (beta-neurotoxin) | SNAKE-VENOMS | CROSS-REACTIVITY | FULVIUS | alpha-Neurotoxin | TOXICOLOGY | RECEPTORS | PRESYNAPTIC TOXICITY | BITES | Venom | Acetylcholine | Biological products | Neurotoxins | Amplitudes | Phospholipase A2 | Calcium | Incubation | Muscles | End plates | Potassium chloride | Depolarization | Vertebrates | Neurotoxicity | Phrenic nerve | Carbachol | Neuromuscular junctions | Toxins | Myonecrosis | Diaphragm | Neurotransmission | Sciatic nerve | Calcium ions
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11. Full Text Diverse Taxa of Cyanobacteria Produce β-N-Methylamino-L-Alanine, a Neurotoxic Amino Acid
by Paul Alan Cox and Sandra Anne Banack and Susan J. Murch and Ulla Rasmussen and Georgia Tien and Robert Richard Bidigare and James S. Metcalf and Louise F. Morrison and Geoffrey A. Codd and Birgitta Bergman and William S. Bowers
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2005, Volume 102, Issue 14, pp. 5074 - 5078
Cyanobacteria can generate molecules hazardous to human health, but production of the known cyanotoxins is taxonomically sporadic. For example, members of a... 
Symbiosis | Symbionts | Biological Sciences | Neurotoxins | Seas | Cyanobacteria | Fresh water | Flowering plants | Amino acids | Genera | Microcystins | Amyotrophic lateral sclerosis/parkinsonism-dementia complex | Neurotoxin | Biomagnification | NEURODEGENERATIVE DISEASE | ALS-PDC | MULTIDISCIPLINARY SCIENCES | amyotrophic lateral sclerosis/parkinsonism-dementia complex | AMYOTROPHIC-LATERAL-SCLEROSIS | TRICHODESMIUM | BMAA | symbiosis | neurotoxin | FLYING FOXES | biomagnification | GUAM | PARKINSONISM-DEMENTIA | CYCAD NEUROTOXINS | Amino Acids, Diamino - toxicity | Species Specificity | Cyanobacteria - classification | Humans | Cyanobacteria - metabolism | Cyanobacteria - pathogenicity | Neurotoxins - toxicity | Plants - microbiology | Chromatography, High Pressure Liquid | Amino Acids, Diamino - isolation & purification | Neurotoxins - isolation & purification | Water Pollutants, Chemical - isolation & purification | Water Pollutants, Chemical - toxicity | Neurotoxins - biosynthesis | Ecosystem | Water Microbiology | Amino Acids, Diamino - biosynthesis | Bacteria | Toxins | Index Medicus | parkinsonism–dementia complex | amyotrophic lateral sclerosis
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12. Full Text Enhancing toxin-based vaccines against botulism
by Przedpelski, Amanda and Tepp, William H and Zuverink, Madison and Johnson, Eric A and Pellet, Sabine and Barbieri, Joseph T
Vaccine, ISSN 0264-410X, 02/2018, Volume 36, Issue 6, pp. 827 - 832
Botulinum neurotoxins (BoNT) are the most toxic proteins for humans. BoNTs are single chain proteins with an N-terminal light chain (LC) and a C-terminal heavy... 
Botulinum neurotoxin A1 | Botulinum neurotoxin A2 | Botulinum neurotoxin | Vaccine | Botulism | ELISA | MEDICINE, RESEARCH & EXPERIMENTAL | IMMUNE-RESPONSE | DOMAIN | ASSAY | SUBTYPES | CERVICAL DYSTONIA PATIENTS | Botulinum neurotoxin Al | NEUROTOXIN TYPE-A | IMMUNOLOGY | HEAVY-CHAIN | SEROTYPE | MONOCLONAL-ANTIBODIES | BINDING | Immunization | Enzyme-Linked Immunosorbent Assay | Humans | Antigens, Bacterial - immunology | Neurons - immunology | Recombinant Proteins | Epitopes - immunology | Botulinum Toxins - immunology | Antibodies, Neutralizing - immunology | Animals | Bacterial Vaccines - immunology | Antibodies, Bacterial - immunology | Botulism - immunology | Mice | Neurons - metabolism | Botulism - prevention & control | Clostridium botulinum - immunology | Disease Models, Animal | Proteins | Medical research | Analysis | Vaccination | Medicine, Experimental | Vaccines | Catalysis | Contamination | Antigenic determinants | Water-borne diseases | Laboratories | Toxicity | Food contamination | Antibodies | Amino acids | Chains | Catalytic activity | Experiments | E coli | Safety engineering | Recombinant | Binding | Translocation | Neurotoxins | Immunoglobulins | Immune response | Glycerol | Biological assays | Botulinum toxin | Immune systems | Studies | Neutralizing | Toxins | Mutation | Index Medicus | vaccine
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13. Full Text BoNT/AB hybrid maintains similar duration of paresis as BoNT/A wild-type in murine running wheel assay
by Kutschenko, Anna and Reinert, Marie-Christine and Krez, Nadja and Liebetanz, David and Rummel, Andreas
Neurotoxicology, ISSN 0161-813X, 03/2017, Volume 59, pp. 1 - 8
The highly potent Botulinum neurotoxins (BoNT) are successful drugs to treat neuromuscular disorders. Efforts are being made to further reduce the injected... 
BoNT/A | Autonomic nervous system | BoNT/AB hybrid | Neurotoxin potency | Murine running wheel assay | Duration of action | PROTEIN-RECEPTOR | BOTULINUM-NEUROTOXIN-A | NEUROTRANSMITTER RELEASE | B NEUROTOXIN | HIGH-AFFINITY BINDING | NEUROSCIENCES | SYNAPTOTAGMIN-II | IN-VIVO | DOUBLE-BLIND | PHARMACOLOGY & PHARMACY | TOXICOLOGY | CLOSTRIDIAL NEUROTOXINS | TETANUS NEUROTOXIN | Diaphragm - drug effects | Paresis - chemically induced | Male | Botulinum Toxins, Type A - pharmacology | Dose-Response Relationship, Drug | Neurotoxins - pharmacology | Running - physiology | Animals | Phrenic Nerve - drug effects | Analysis of Variance | Muscle, Skeletal - drug effects | Muscle, Skeletal - physiopathology | Mice | Phrenic Nerve - physiology | Disease Models, Animal | Paresis - physiopathology | Paralysis | Neurophysiology | Running | Drugs | Binding | Wheel running | Translocation | Neuromuscular diseases | Neurotoxins | Effectiveness | Medical treatment | Disorders | Muscles | Assaying | Bioactive | Studies | Neurotoxicity | Phrenic nerve | Paresis | Serotypes | Affinity | Toxins | Acetylcholine | Catalysis | Neuromuscular system | Index Medicus
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14. Full Text Defensin‐neurotoxin dyad in a basally branching metazoan sea anemone
by Kim, Chan‐Hee and Lee, Ye Jin and Go, Hye‐Jin and Oh, Hye Young and Lee, Tae Kwan and Park, Ji Been and Park, Nam Gyu
The FEBS Journal, ISSN 1742-464X, 10/2017, Volume 284, Issue 19, pp. 3320 - 3338
Recent studies suggest that vertebrate and invertebrate defensins have evolved from two independent ancestors, and that both defensins could share origins with... 
paralytic activity | neurotoxin‐like antimicrobial peptides | sea anemone | β‐defensin‐fold family | β-defensin-fold family | neurotoxin-like antimicrobial peptides | VENOM | TRANSCRIPTOME | SODIUM-CHANNELS | BIOCHEMISTRY & MOLECULAR BIOLOGY | TOXINS | ANTIMICROBIAL PEPTIDES | MODEL | ANTHOPLEURA-ELEGANTISSIMA | EVOLUTION | PURIFICATION | beta-defensin-fold family | INNATE IMMUNITY | Peptides | Escherichia coli - drug effects | Cnidarian Venoms - isolation & purification | Penaeidae - drug effects | beta-Defensins - isolation & purification | Recombinant Proteins - biosynthesis | beta-Defensins - toxicity | Neurotoxins - isolation & purification | Sea Anemones - pathogenicity | Penaeidae - physiology | Microbial Sensitivity Tests | Recombinant Proteins - isolation & purification | Salmonella enterica - drug effects | Sea Anemones - physiology | Bacillus subtilis - growth & development | Base Sequence | Cloning, Molecular | Escherichia coli - metabolism | Conserved Sequence | Protein Interaction Domains and Motifs | Amino Acid Sequence | Cnidarian Venoms - biosynthesis | Neurotoxins - chemistry | Gene Expression | Protein Structure, Secondary | Models, Molecular | Recombinant Proteins - chemistry | Neurotoxins - toxicity | Salmonella enterica - growth & development | Sea Anemones - chemistry | beta-Defensins - chemistry | Sequence Homology, Amino Acid | Cnidarian Venoms - chemistry | Sequence Alignment | Animals | Neurotoxins - biosynthesis | Escherichia coli - genetics | Recombinant Proteins - toxicity | Cnidarian Venoms - toxicity | beta-Defensins - biosynthesis | Bacillus subtilis - drug effects | Analysis | Escherichia coli | Salmonella | Antimicrobial activity | Similarity | Transcription | Amino acids | Homology | Antiinfectives and antibacterials | Crustaceans | Antimicrobial peptides | Chemical bonds | Bacteria | Gram-negative bacteria | Immune system | Recombinant | Disulfide bonds | Neurotoxins | Nucleotide sequence | AMP | Cloning | Ions | Antimicrobial agents | Pharynx | Molecular modelling | Defensins | Toxins | Three dimensional models | Index Medicus
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