X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (11300) 11300
Book Review (1414) 1414
Publication (841) 841
Book Chapter (82) 82
Conference Proceeding (38) 38
Book / eBook (35) 35
Government Document (11) 11
Web Resource (6) 6
Magazine Article (5) 5
Dissertation (3) 3
Data Set (1) 1
Paper (1) 1
Streaming Video (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (10913) 10913
animals (9236) 9236
rats (4476) 4476
neurosciences (4170) 4170
humans (3205) 3205
male (3199) 3199
neurotoxins - toxicity (2701) 2701
neurotoxins - pharmacology (2564) 2564
mice (2550) 2550
biochemistry & molecular biology (2271) 2271
neurons - drug effects (2035) 2035
neurotoxins - metabolism (1723) 1723
neurotoxins (1708) 1708
neurons - metabolism (1602) 1602
cells, cultured (1530) 1530
female (1405) 1405
neurons (1390) 1390
rats, sprague-dawley (1347) 1347
pharmacology & pharmacy (1206) 1206
brain (1190) 1190
neurotoxicity (1126) 1126
toxicology (1126) 1126
neurotoxin (1057) 1057
amino acid sequence (1049) 1049
dose-response relationship, drug (1045) 1045
molecular sequence data (1009) 1009
rats, wistar (983) 983
brain - metabolism (949) 949
oxidative stress (892) 892
parkinson's disease (824) 824
proteins (794) 794
disease models, animal (792) 792
dopamine - metabolism (790) 790
apoptosis (783) 783
analysis (775) 775
time factors (758) 758
neurology (754) 754
parkinsons-disease (740) 740
cell biology (735) 735
brain - drug effects (726) 726
kinetics (725) 725
glutamate (713) 713
neuroprotective agents - pharmacology (708) 708
calcium - metabolism (686) 686
toxins (674) 674
excitotoxicity (644) 644
mice, inbred c57bl (644) 644
rat-brain (643) 643
neurons - pathology (632) 632
expression (620) 620
in vitro techniques (613) 613
neurotoxins - chemistry (612) 612
cell survival - drug effects (607) 607
dopamine (605) 605
neurons - cytology (574) 574
toxicity (571) 571
cell death - drug effects (551) 551
article (540) 540
rat (532) 532
hippocampus - drug effects (531) 531
immunohistochemistry (520) 520
apoptosis - drug effects (515) 515
binding sites (514) 514
research (507) 507
alzheimers-disease (506) 506
neurodegeneration (490) 490
multidisciplinary sciences (480) 480
neuroprotection (478) 478
cell line (471) 471
binding (470) 470
corpus striatum - drug effects (470) 470
neurons - physiology (470) 470
clinical neurology (462) 462
hippocampus - metabolism (458) 458
in-vitro (449) 449
venom (447) 447
cells (445) 445
protein binding (442) 442
corpus striatum - metabolism (433) 433
mptp (422) 422
nervous system (419) 419
neurotoxins - antagonists & inhibitors (419) 419
glutamic acid - metabolism (417) 417
nerve tissue proteins - metabolism (417) 417
hippocampus (410) 410
animals, newborn (409) 409
rats, inbred strains (404) 404
activation (401) 401
physiological aspects (401) 401
inhibition (394) 394
central-nervous-system (385) 385
models, molecular (385) 385
biophysics (384) 384
toxin (382) 382
botulinum neurotoxin (381) 381
protein (379) 379
pc12 cells (357) 357
cell death (356) 356
biomedicine (350) 350
immunology (350) 350
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (11227) 11227
Russian (43) 43
Chinese (28) 28
French (26) 26
Japanese (25) 25
German (14) 14
Spanish (14) 14
Hungarian (4) 4
Italian (3) 3
Polish (3) 3
Ukrainian (2) 2
Bosnian (1) 1
Croatian (1) 1
Czech (1) 1
Finnish (1) 1
Portuguese (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


PLoS ONE, ISSN 1932-6203, 10/2012, Volume 7, Issue 10, pp. e47977 - e47977
In recent years a growing debate is about whether botulinum neurotoxins are retrogradely transported from the site of injection. Immunodetection of cleaved... 
TOXIN-A | ACIDIC PROTEIN GFAP | RAT | MULTIDISCIPLINARY SCIENCES | ANIMAL-MODELS | CULTURED ASTROCYTES | SPINAL-CORD | AXONAL-TRANSPORT | NERVE CONSTRICTION | GLIAL-CELLS | SNAP-25 | Immunohistochemistry | Analgesics - pharmacology | Sciatic Nerve - injuries | Spinal Cord - drug effects | Spinal Cord - metabolism | Neuralgia - metabolism | Analgesics - metabolism | Male | Acetylcholine - metabolism | Glial Fibrillary Acidic Protein - metabolism | Botulinum Toxins, Type A - pharmacology | Hindlimb - physiopathology | Sciatic Nerve - metabolism | Biological Transport | Neuralgia - prevention & control | Neuromuscular Agents - pharmacology | Peripheral Nerves - metabolism | Schwann Cells - drug effects | Neuromuscular Agents - metabolism | Cells, Cultured | Nuclear Proteins - metabolism | Schwann Cells - metabolism | Nerve Tissue Proteins - metabolism | Microscopy, Confocal | Animals | Hindlimb - drug effects | Cell Proliferation - drug effects | Mice | Synaptosomal-Associated Protein 25 - metabolism | Botulinum Toxins, Type A - metabolism | CD11b Antigen - metabolism | Hindlimb - metabolism | Astrocytes - metabolism | Ganglia, Spinal - metabolism | Care and treatment | Analysis | Pain | Cell proliferation | Spinal cord | Neurosciences | Complement receptor 3 | Neurobiology | SNAP receptors | Biology | Neuropathy | Proteins | Biological effects | Dorsal root ganglia | Analgesics | Animal tissues | Fibroblasts | Neurotoxin A | Horns | Growth factors | Nerve endings | CD11b antigen | Neurotoxins | Pain perception | Astrocytes | Glial fibrillary acidic protein | Schwann cells | Injection | Retrograde transport | Botulinum toxin | Ganglia | Quality of life | Councils | SNAP-25 protein | Acetylcholine | Toxins | Transport | Immunofluorescence | Sciatic nerve | Combinatorial analysis | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 04/2016, Volume 11, Issue 4, pp. e0153401 - e0153401
Botulinum neurotoxin A (BoNT/A) is composed of three domains: a catalytic domain (LC), a translocation domain (H-N) and a receptor-binding domain (H-C). Like... 
INHIBITION | CHANNEL | SPECTROSCOPIC ANALYSIS | TOXIN T-DOMAIN | LIGHT-CHAIN PROTEASE | TETANUS | BEHAVIOR | MULTIDISCIPLINARY SCIENCES | IDENTIFICATION | PROTEINS | DIPHTHERIA-TOXIN | Protein Structure, Tertiary | Molecular Chaperones - metabolism | Protein Structure, Secondary | Protein Transport - physiology | Permeability | Catalytic Domain - physiology | Protein Folding | Endocytosis - physiology | Membranes - metabolism | Cytosol - metabolism | Neurotoxins - metabolism | Botulinum Toxins, Type A - metabolism | Lipid Bilayers - metabolism | Hydrogen-Ion Concentration | Protein Binding - physiology | Physiological aspects | Genetic aspects | Research | Structure | Botulinum toxin | Protein binding | Translocation | Membranes | Stability | Denaturation | Cloning | Acidification | Biochemistry | Diphtheria | pH effects | Cytosol | Lipid bilayers | Proteins | Endocytosis | Botulism | Mutagenesis | Hydrogen ions | Plasmids | Neurotoxin A | Bacteria | Toxins | Intoxication | Catalysis | Index Medicus | Botulinum Toxins, Type A/metabolism | Lipid Bilayers/metabolism | Membranes/metabolism | Biochemistry, Molecular Biology | Protein Binding/physiology | Catalytic Domain/physiology | Protein Transport/physiology | Neurotoxins/metabolism | Life Sciences | Molecular Chaperones/metabolism | Cytosol/metabolism | Endocytosis/physiology
Journal Article
Neurobiology of Disease, ISSN 0969-9961, 2006, Volume 23, Issue 3, pp. 669 - 678
Prion (PrP) and amyloid-β (Aβ) peptides are involved in the neuronal loss that occurs in Prion disorders (PrD) and Alzheimer's disease (AD), respectively,... 
Oxidative stress | Prion peptide | Ca 2+ homeostasis | Prion disorders | Amyloid-β peptide | Alzheimer's disease | Endoplasmic reticulum | Apoptosis | homeostasis | prion peptide | peptide | ACTIVATION | CA2+ STORES | prion disorders | ALZHEIMERS-DISEASE | CALCIUM HOMEOSTASIS | ER STRESS | apoptosis | NEUROBLASTOMA-CELLS | NEUROSCIENCES | amyloid-beta | Ca2+ homeostasis | UNFOLDED PROTEIN RESPONSE | A-BETA | endoplasmic reticulum | oxidative stress | CASPASE-12 | Neurons - pathology | Prion Diseases - physiopathology | Reactive Oxygen Species - metabolism | Calcium Channels - metabolism | Rats, Wistar | Apoptosis - drug effects | Calcium - metabolism | Peptide Fragments - toxicity | Calcium Signaling - physiology | Oxidative Stress - physiology | Endoplasmic Reticulum - metabolism | Ryanodine Receptor Calcium Release Channel - metabolism | Cerebral Cortex - metabolism | Cerebral Cortex - physiopathology | Electron Transport Complex IV - metabolism | Caspases - metabolism | Peptides - metabolism | Peptides - toxicity | Endoplasmic Reticulum - drug effects | Amyloid beta-Peptides - metabolism | Inositol 1,4,5-Trisphosphate Receptors | Cerebral Cortex - drug effects | Homeostasis - drug effects | Neurons - drug effects | Calcium Channels - drug effects | Prions - metabolism | Alzheimer Disease - physiopathology | Peptide Fragments - metabolism | Amyloid beta-Peptides - toxicity | Receptors, Cytoplasmic and Nuclear - drug effects | Cells, Cultured | Rats | Neurotoxins - toxicity | Ryanodine Receptor Calcium Release Channel - drug effects | Prions - toxicity | Animals | Calcium Signaling - drug effects | Homeostasis - physiology | Alzheimer Disease - metabolism | Neurotoxins - metabolism | Apoptosis - physiology | Oxidative Stress - drug effects | Prion Diseases - metabolism | Receptors, Cytoplasmic and Nuclear - metabolism | Cytochrome c | Inositol | Neurosciences | Corticosteroids | Synthesis | Peptides | Analysis | Lipids | Target marketing | Index Medicus
Journal Article
Molecular Neurobiology, ISSN 0893-7648, 11/2016, Volume 53, Issue 9, pp. 6426 - 6443
Artemether, a lipid-soluble derivative of artemisinin has been reported to possess anti-inflammatory properties. In this study, we have investigated the... 
NF-κB | Neurology | Neurosciences | Biomedicine | HT22 hippocampal neurons | Nrf2 | BV2 microglia | Neurobiology | Neuroinflammation | Artemether | Cell Biology | ALZHEIMERS-DISEASE | INFLAMMATORY REACTIONS | NEUROSCIENCES | BV-2 CELLS | PROTECTS | STAT3 ACTIVATION | NF-kappa B | CULTURED ASTROCYTES | HEME OXYGENASE-1 | NF-KAPPA-B | ARTEMISININ | Neuroprotective Agents - therapeutic use | Inflammation - pathology | Microglia - metabolism | Heme Oxygenase-1 - metabolism | Transcriptional Activation - genetics | Antioxidants - metabolism | Transcriptional Activation - drug effects | NF-kappa B - metabolism | Lipopolysaccharides | Artemisinins - pharmacology | Cell Nucleus - metabolism | Neuroprotective Agents - pharmacology | Inflammation - drug therapy | Amyloid beta-Peptides - metabolism | Microglia - pathology | NF-E2-Related Factor 2 - genetics | p38 Mitogen-Activated Protein Kinases - metabolism | Artemisinins - chemistry | Cell Line | Cell Survival - drug effects | Microglia - drug effects | Prostaglandin-E Synthases - metabolism | Neurotoxins - toxicity | Antimalarials - therapeutic use | Antimalarials - pharmacology | Dinoprostone - metabolism | Amyloid Precursor Protein Secretases - metabolism | Animals | Artemisinins - therapeutic use | MAP Kinase Signaling System - drug effects | Aspartic Acid Endopeptidases - metabolism | NF-E2-Related Factor 2 - metabolism | Antimalarials - chemistry | Cyclooxygenase 2 - metabolism | Interleukin-6 - biosynthesis | NAD(P)H Dehydrogenase (Quinone) - metabolism | Mice | Cell Nucleus - drug effects | Nitric Oxide - metabolism | Tumor Necrosis Factor-alpha - biosynthesis | Nitric Oxide Synthase Type II - metabolism | Nervous system diseases | Neurons | Nitric oxide | Heme | Amyloid beta-protein | Synthetic prostaglandins E | Mitogens | Protein kinases | Proteins | Enzymes | Inflammation | Kinases | Index Medicus
Journal Article
Journal of Neuroscience, ISSN 0270-6474, 01/2009, Volume 29, Issue 2, pp. 529 - 542
Aging may be determined by a genetic program and/or by the accumulation rate of molecular damages. Reactive oxygen species (ROS) generated by the mitochondrial... 
Aging | Antioxidant | Bmi1 | Neuronal cell death | ROS | p53 | antioxidant | OXIDATIVE-STRESS | STEM-CELLS | ACTIVATION | ALZHEIMERS-DISEASE | EXTENDS LIFE-SPAN | CELLULAR SENESCENCE | NEUROSCIENCES | neuronal cell death | IN-VIVO | INTRACELLULAR AMYLOID-BETA | aging | EXPRESSION | PARKINSONS-DISEASE | Cell Proliferation | Reactive Oxygen Species - metabolism | Age Factors | Embryo, Mammalian | Microtubule-Associated Proteins - metabolism | Homeodomain Proteins - metabolism | Peroxiredoxins - metabolism | Cell Survival - genetics | Apoptosis - genetics | Phosphopyruvate Hydratase - metabolism | Glial Fibrillary Acidic Protein - metabolism | Cerebral Cortex - cytology | Tumor Suppressor Protein p53 - genetics | Peroxiredoxins - genetics | Nuclear Proteins - deficiency | beta-Galactosidase - metabolism | Neurons - metabolism | Neurons - drug effects | Repressor Proteins - metabolism | Proto-Oncogene Proteins - metabolism | Gene Expression Regulation - genetics | Mice, Inbred C57BL | Cells, Cultured | Hydrogen Peroxide - pharmacology | Tumor Suppressor Protein p53 - metabolism | Nuclear Proteins - metabolism | PAX6 Transcription Factor | Proto-Oncogene Proteins - deficiency | Mice, Knockout | Neurotoxins - pharmacology | Animals | Polycomb Repressive Complex 1 | Analysis of Variance | Eye Proteins - metabolism | Mice | Histones - metabolism | Lipid Peroxidation - genetics | Paired Box Transcription Factors - metabolism | Index Medicus
Journal Article
Brain Pathology, ISSN 1015-6305, 01/2008, Volume 18, Issue 1, pp. 52 - 61
Journal Article
Experimental Neurology, ISSN 0014-4886, 2009, Volume 217, Issue 2, pp. 429 - 433
β- -methylamino- -alanine (BMAA) is a non-protein amino acid implicated in the neurodegenerative disease amyotrophic lateral sclerosis/Parkinson–dementia... 
NMDA | Oxidative stress | BMAA | Glutamate | Alzheimer's disease | Cystine | NEURODEGENERATIVE DISEASE | NEUROTOXIC AMINO-ACID | X(C)(-) | AMYOTROPHIC-LATERAL-SCLEROSIS | NEUROSCIENCES | CYANOBACTERIAL NEUROTOXINS | CORTICAL-NEURONS | GLUTATHIONE | GUAM | PARKINSONISM-DEMENTIA | Amino Acids, Diamino - toxicity | Receptors, Metabotropic Glutamate - drug effects | Central Nervous System - metabolism | Amyotrophic Lateral Sclerosis - physiopathology | Glutathione - metabolism | Coculture Techniques | Oxidative Stress - physiology | Extracellular Space - drug effects | Receptors, Metabotropic Glutamate - metabolism | Extracellular Space - metabolism | Amino Acid Transport System y+ - metabolism | Receptor, Metabotropic Glutamate 5 | Glutamic Acid - secretion | Neurons - metabolism | Neurons - drug effects | Amino Acids, Diamino - metabolism | Excitatory Amino Acid Agonists - metabolism | Cells, Cultured | Glutathione - antagonists & inhibitors | Neurotoxins - toxicity | Neurodegenerative Diseases - metabolism | Animals | Excitatory Amino Acid Agonists - toxicity | Neurodegenerative Diseases - chemically induced | Neurodegenerative Diseases - physiopathology | Cystine - metabolism | Amyotrophic Lateral Sclerosis - metabolism | Central Nervous System - drug effects | Neurotoxins - metabolism | Glutamic Acid - metabolism | Mice | Amyotrophic Lateral Sclerosis - chemically induced | Central Nervous System - physiopathology | Oxidative Stress - drug effects | Amino Acid Transport System y+ - drug effects | Index Medicus
Journal Article
Biochemical Journal, ISSN 0264-6021, 09/2013, Volume 454, Issue 2, pp. 303 - 310
To identify high-affinity interactions between long-chain α-neurotoxins and nicotinic receptors, we determined the crystal structure of the complex between... 
Molecular recognition | Neurotoxin | Nicotinic acetylcholine receptor | Crystal structure | Reptilian Proteins - chemistry | Nicotinic Agonists - metabolism | Cobra Neurotoxin Proteins - metabolism | Pyridines - chemistry | Humans | Recombinant Fusion Proteins - metabolism | Nicotinic Agonists - chemistry | Receptors, Nicotinic - chemistry | Carrier Proteins - chemistry | Protein Interaction Domains and Motifs | Binding Sites | Peptide Fragments - genetics | Bridged Bicyclo Compounds, Heterocyclic - metabolism | Bungarotoxins - metabolism | Neurotoxins - chemistry | Peptide Fragments - metabolism | Receptors, Nicotinic - metabolism | Bridged Bicyclo Compounds, Heterocyclic - chemistry | Bungarotoxins - chemistry | Lymnaea | Models, Molecular | Mutant Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Cobra Neurotoxin Proteins - chemistry | Bungarus | Carrier Proteins - genetics | Peptide Fragments - chemistry | Animals | Carrier Proteins - metabolism | Pyridines - metabolism | Mutant Proteins - chemistry | Ligands | Neurotoxins - metabolism | Protein Conformation | Receptors, Nicotinic - genetics | Amino Acid Substitution | Reptilian Proteins - metabolism | alpha7 Nicotinic Acetylcholine Receptor | Index Medicus | BASIC BIOLOGICAL SCIENCES | crystal structure | neurotoxin | molecular recognition | nicotinic acetylcholine receptor
Journal Article
Neuroscience Letters, ISSN 0304-3940, 2009, Volume 455, Issue 3, pp. 187 - 190
Journal Article