Search results for "nerve"

showing 10 items of 1683 documents

Landmarks for vertebral artery repositioning in bulbar compression syndrome: anatomic and microsurgical nuances

2004

Abstract OBJECTIVE: The purpose of this study was to better elucidate the anatomic relationship between the vertebral artery (VA) along with its perforating vessels and the brainstem to develop anatomic guidelines that would be helpful when decompressing medulla oblongata compressed by the VA. METHODS: Microanatomy dissection was performed in six formalin-fixed cadaveric heads. The VA, posteroinferior cerebellar artery (PICA), anteroinferior cerebellar artery (AICA), and lower brainstem perforators were examined under magnification using a surgical microscope. The outer diameters of the VA, PICA, and AICA were measured. The distance between the VA, lying within the lateral cerebellomedullar…

Microsurgerymedicine.medical_treatmentVertebral arteryDissection (medical)Cisterna magnaMicrovascular anatomyMedulla oblongatamedicine.arterymedicineHumansVertebral arteryVascular compressionmedulla oblongata; microvascular anatomy; vascular compression; vertebral arterybusiness.industrySyndromeAnatomyMicrosurgerymedicine.diseasemedicine.anatomical_structurePractice Guidelines as TopicMedulla oblongataOccipital nerve stimulationSurgeryBrainstemNeurology (clinical)Cerebellar arterybusinessBrain Stem
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Lack of GDAP1 induces neuronal calcium and mitochondrial defects in a knockout mouse model of Charcot-Marie-tooth neuropathy

2015

27 páginas, 9 figuras.

Mitochondrial proteinCancer Researchlcsh:QH426-470Nerve Tissue ProteinsBiologyMitochondrionCharcot-Marie-Tooth diseaseGDAP1 geneMiceGeneticsAutophagyAnimalsCalcium SignalingMolecular BiologyGenetics (clinical)Ecology Evolution Behavior and SystematicsCytoskeletonCalcium signalingGeneticsVoltage-dependent calcium channelEndoplasmic reticulumAutophagyBiología y Biomedicina / BiologíaAxonsCell biologyMitochondriaMitochondrialMice Inbred C57BLAlpha tubulinlcsh:Geneticsmitochondrial fusionKnockout mouseMitochondrial fissionCalcium ChannelsAnimal cellGene DeletionResearch Article
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Gyrification from constrained cortical expansion

2014

The exterior of the mammalian brain - the cerebral cortex - has a conserved layered structure whose thickness varies little across species. However, selection pressures over evolutionary time scales have led to cortices that have a large surface area to volume ratio in some organisms, with the result that the brain is strongly convoluted into sulci and gyri. Here we show that the gyrification can arise as a nonlinear consequence of a simple mechanical instability driven by tangential expansion of the gray matter constrained by the white matter. A physical mimic of the process using a layered swelling gel captures the essence of the mechanism, and numerical simulations of the brain treated a…

Models AnatomicCompressive StrengthModels NeurologicalLissencephalyFOS: Physical sciencesGeometryPattern Formation and Solitons (nlin.PS)Condensed Matter - Soft Condensed MatterNerve Fibers MyelinatedWhite matterNeural PathwaysPolymicrogyriamedicineHumansDimethylpolysiloxanesPhysics - Biological PhysicsTissues and Organs (q-bio.TO)GyrificationCell ProliferationPhysicsCerebral CortexNeuronsMultidisciplinaryta114PachygyriaQuantitative Biology - Tissues and OrgansAnatomymedicine.diseaseNonlinear Sciences - Pattern Formation and SolitonsElasticitymedicine.anatomical_structureCerebral cortexBiological Physics (physics.bio-ph)FOS: Biological sciencesBrain sizePhysical SciencesSoft Condensed Matter (cond-mat.soft)Stress MechanicalBrain morphogenesisGels
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The Protein Structure Context of PolyQ Regions.

2016

Proteins containing glutamine repeats (polyQ) are known to be structurally unstable. Abnormal expansion of polyQ in some proteins exceeding a certain threshold leads to neurodegenerative disease, a symptom of which are protein aggregates. This has led to extensive research of the structure of polyQ stretches. However, the accumulation of contradictory results suggests that protein context might be of importance. Here we aimed to evaluate the structural context of polyQ regions in proteins by analysing the secondary structure of polyQ proteins and their homologs. The results revealed that the secondary structure in polyQ vicinity is predominantly random coil or helix. Importantly, the region…

Models MolecularProtein Conformation alpha-HelicalProtein Structure ComparisonProtein StructureSaccharomyces cerevisiae ProteinsGlutaminelcsh:MedicineNerve Tissue ProteinsSaccharomyces cerevisiaePlant ScienceResearch and Analysis MethodsBiochemistryPlant Roots570 Life sciencesDatabase and Informatics MethodsProtein Structure DatabasesMacromolecular Structure AnalysisHumansProtein Interaction Domains and MotifsAmino AcidsDatabases ProteinProtein Interactionslcsh:ScienceMolecular BiologyMediator ComplexOrganic CompoundsPlant AnatomyAcidic Amino AcidsOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesProteinsRoot StructureChemistryBiological DatabasesProtein-Protein InteractionsPhysical Scienceslcsh:QStructural ProteinsProtein Structure DeterminationPeptidesResearch Article570 BiowissenschaftenPLoS ONE
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Reversed Enantioselectivity of Diisopropyl Fluorophosphatase against Organophosphorus Nerve Agents by Rational Design

2009

Diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris is an efficient and robust biocatalyst for the hydrolysis of a range of highly toxic organophosphorus compounds including the nerve agents sarin, soman, and cyclosarin. In contrast to the substrate diisopropyl fluorophosphate (DFP) the nerve agents possess an asymmetric phosphorus atom, which leads to pairs of enantiomers that display markedly different toxicities. Wild-type DFPase prefers the less toxic stereoisomers of the substrates which leads to slower detoxification despite rapid hydrolysis. Enzyme engineering efforts based on rational design yielded two quadruple enzyme mutants with reversed enantioselectivity and overall en…

Models MolecularSarinStereochemistryRational designCyclosarinStereoisomerismGeneral ChemistryNervous SystemBiochemistryCatalysisKineticschemistry.chemical_compoundOrganophosphorus CompoundsPhosphoric Triester HydrolasesColloid and Surface ChemistrychemistrySomanHydrolasemedicineDiisopropyl fluorophosphateChemical Warfare AgentsCrystallizationDiisopropyl-fluorophosphatasemedicine.drugNerve agentJournal of the American Chemical Society
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The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin.

2003

Neuroglobin and cytoglobin reversibly bind oxygen in competition with the distal histidine, and the observed oxygen affinity therefore depends on the properties of both ligands. In the absence of an external ligand, the iron atom of these globins is hexacoordinated. There are three cysteine residues in human neuroglobin; those at positions CD7 and D5 are sufficiently close to form an internal disulfide bond. Both cysteine residues in cytoglobin, although localized in other positions than in human neuroglobin, may form a disulfide bond as well. The existence and position of these disulfide bonds was demonstrated by mass spectrometry and thiol accessibility studies. Mutation of the cysteines …

Models MolecularSpectrometry Mass Electrospray IonizationStereochemistryNeuroglobinNerve Tissue ProteinsLigandsBiochemistryRedoxHumansHistidineCysteineDisulfidesGlobinMolecular BiologyHistidineChemistryCytoglobinCytoglobinCell BiologyLigand (biochemistry)Recombinant ProteinsGlobinsOxygenKineticsNeuroglobinOxidation-ReductionOxygen bindingProtein BindingCysteine
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High Pressure Enhances Hexacoordination in Neuroglobin and Other Globins

2005

The techniques of high applied pressure and flash photolysis have been combined to study ligand rebinding to neuroglobin (Ngb) and tomato Hb, globins that may display a His-Fe-His hexacoordination in the absence of external ligands. High pressure induces a moderate decrease in the His association rate and a large decrease in His dissociation rate, thus leading to an enhancement of the overall His affinity. The overall structural difference between penta- and hexacoordinated globins may be rather small and can be overcome by external modifications such as high pressure. Over the pressure range 0.1-700 MPa (7 kbar), the globins may show a loss of over a factor of 100 in the amplitude of the b…

Models MolecularSteric effectsProtein ConformationStereochemistryIronNeuroglobinchemistry.chemical_elementNerve Tissue ProteinsHemeLigandsBiochemistryOxygenHemoglobinschemistry.chemical_compoundSolanum lycopersicumPressureAnimalsHumansHistidineHorsesGlobinMolecular BiologyHemeBinding SitesPhotolysisMyoglobinChemistryPhotodissociationHeartCell BiologyLigand (biochemistry)GlobinsOxygenKineticsNeuroglobinBiophysicsFlash photolysisProtein BindingJournal of Biological Chemistry
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Magnesium Exchanged Zirconium Metal−Organic Frameworks with Improved Detoxification Properties of Nerve Agents

2019

UiO-66, MOF-808 and NU-1000 metal-organic frameworks exhibit a differentiated reactivity toward [Mg(OMe)2(MeOH)2]4 related to their pore accessibility. Microporous UiO-66 remains unchanged while mesoporous MOF-808 and hierarchical micro/mesoporous NU-1000 materials yield doped systems containing exposed MgZr5O2(OH)6 clusters in the mesoporous cavities. This modification is responsible for a remarkable enhancement of the catalytic activity toward the hydrolytic degradation of P-F and P-S bonds of toxic nerve agents, at room temperature, in unbuffered aqueous solutions.

Models MolecularSurface PropertiesQuímica organometàl·licachemistry.chemical_element010402 general chemistry01 natural sciencesBiochemistryCatalysisCatalysisColloid and Surface ChemistryPolymer chemistryReactivity (chemistry)MagnesiumParticle SizeMaterialsMetal-Organic FrameworksZirconiumAqueous solutionMagnesiumHydrolysisTemperatureGeneral ChemistryMicroporous material0104 chemical scienceschemistryMetal-organic frameworkZirconiumMesoporous materialNerve AgentsOxidation-ReductionPorosity
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Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family.

2001

Neuroglobin is a recently discovered member of the globin superfamily that is suggested to enhance the O(2) supply of the vertebrate brain. Spectral measurements with human and mouse recombinant neuroglobin provide evidence for a hexacoordinated deoxy ferrous (Fe(2+)) form, indicating a His-Fe(2+)-His binding scheme. O(2) or CO can displace the endogenous protein ligand, which is identified as the distal histidine by mutagenesis. The ferric (Fe(3+)) form of neuroglobin is also hexacoordinated with the protein ligand E7-His and does not exhibit pH dependence. Flash photolysis studies show a high recombination rate (k(on)) and a slow dissociation rate (k(off)) for both O(2) and CO, indicating…

Models MolecularTime FactorsLightStereochemistryIronNeuroglobinNerve Tissue ProteinsPlasma protein bindingLigandsBiochemistryMiceAnimalsHumansHistidineGlobinCloning MolecularMolecular BiologyHistidineChromatography High Pressure LiquidCarbon MonoxideChemistryCytoglobinTemperatureCell BiologyHydrogen-Ion ConcentrationLigand (biochemistry)Recombinant ProteinsGlobin foldGlobinsOxygenKineticsNeuroglobinOxidation-ReductionUltracentrifugationProtein ligandProtein BindingThe Journal of biological chemistry
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Redistribution of aquaporin-4 in human glioblastoma correlates with loss of agrin immunoreactivity from brain capillary basal laminae

2003

Vasogenic edema is one of the most serious clinical problems in brain tumors and tightly connected to water shifts between the different fluid compartments in the brain. Aquaporin water channels have been recognized to have an important impact on the development of edematous swelling in the brain. Astrocytes, which are believed to induce or at least maintain the blood-brain barrier in the brain capillary endothelial cells, express the aquaporin isoform AQP4. Normally, AQP4 is highly concentrated in the glial membrane where astrocytes contact mesenchymal space, such as perivascular or brain superficial regions. Parenchymal membranes do not show any immunocytochemical AQP4-specific signal. We…

Models NeurologicalSynucleinsAquaporinNerve Tissue ProteinsBiologyAquaporinsBlood–brain barrierBasement MembranePathology and Forensic MedicineCellular and Molecular NeuroscienceGliomaUtrophinmedicineExtracellularAnimalsHumansAgrinDystroglycansAquaporin 4Membrane GlycoproteinsAgrinBrain NeoplasmsEndothelial Cellsmedicine.diseaseImmunohistochemistryRatsCell biologyCytoskeletal Proteinsmedicine.anatomical_structureAquaporin 4Immunologysense organsNeurology (clinical)GlioblastomaAstrocyteActa Neuropathologica
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