Search results for "Cromo"

showing 10 items of 1298 documents

Anti-vimentin staining in muscle pathology

1993

The intermediate filaments of immature muscle fibres contain desmin and vimentin; vimentin is lacking in mature fibres. Regenerating fibres react with anti-vimentin antibodies and more intensely for desmin than mature fibres. The aim of the present study was to evaluate anti-vimentin staining for muscle pathology. Anti-vimentin-reactive fibres were found in 40 of 89 biopsies assessed. Fifteen patients with progressive destructive myopathy, infantile spinal muscular atrophy, clinically suspected Leigh's disease or unclassifiable congenital myopathy had between 1% and 95% vimentin-positive fibres. Less than 1% positive fibres were found in 25 patients with neuropathy with secondary myopathy o…

Adultmedicine.medical_specialtyPathologyHistologyAdolescentBiopsyIntermediate FilamentsMuscle ProteinsVimentinmacromolecular substancesPathology and Forensic MedicineImmunoenzyme TechniquesPhysiology (medical)BiopsyHumansVimentinMedicineChildMyopathyIntermediate filamentAgedStaining and Labelingbiologymedicine.diagnostic_testbusiness.industryMusclesInfant NewbornInfantNeuromuscular DiseasesMiddle Agedmedicine.diseaseCongenital myopathyNeurologyChild Preschoolbiology.proteinImmunohistochemistryHistopathologyDesminNeurology (clinical)medicine.symptombusinessNeuropathology and Applied Neurobiology
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Structural Mechanism of N-Methyl-D-Aspartate Receptor Type 1 Partial Agonism

2012

N-methyl-D-aspartate (NMDA) receptors belong to a family of ionotropic glutamate receptors that contribute to the signal transmission in the central nervous system. NMDA receptors are heterotetramers that usually consist of two GluN1 and GluN2 monomers. The extracellular ligand-binding domain (LBD) of a monomer is comprised of discontinuous segments that form the functional domains D1 and D2. While the binding of a full agonist glycine to LBD of GluN1 is linked to cleft closure and subsequent ion-channel opening, partial agonists are known to activate the receptor only sub-maximally. Although the crystal structures of the LBD of related GluA2 receptor explain the mechanism for the partial a…

AgonistProtein Structuremedicine.drug_classGlycineMolecular ConformationBiophysicslcsh:MedicineMolecular Dynamics SimulationLigandsta3111Receptors N-Methyl-D-AspartateBiochemistryBiophysics Simulationsta3112Partial agonistIon ChannelsChemical BiologyMacromolecular Structure AnalysismedicineBiomacromolecule-Ligand Interactionslcsh:ScienceReceptorBiologyta116Ion channelCrystallographyMultidisciplinaryChemistrylcsh:Rta1182Glutamate receptorProteinsComputational BiologyNeurotransmittersProtein Structure TertiaryTransmembrane ProteinsBiochemistryCycloserineBiophysicsNMDA receptorLigand-gated ion channellcsh:Qhormones hormone substitutes and hormone antagonistsProtein BindingResearch ArticleNeuroscienceIonotropic effectPLoS ONE
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Homodimeric murine interleukin-3 agonists indicate that ligand dimerization is important for high-affinity receptor complex formation.

1994

Homodimeric murine interleukin 3 (mIL-3) agonists were generated by intermolecular cystine-bonding. Steady-state binding assays and association kinetics performed at 4 degrees C using these agonists revealed specific binding to both the high- and low-affinity receptor. DSS-mediated crosslinking studies performed at 4 degrees C with agonist concentrations compatible with high-affinity receptor complex formation allowed to detect protein complexes of the alpha chain, the beta chain(s) and the high-affinity receptor complex migrating with apparent molecular weights of 90 kDa, 140 kDa, and above 180 kDa, respectively. In contrast, monomeric mIL-3 was crosslinked to the alpha chain receptor only…

AgonistReceptor complexmedicine.drug_classMacromolecular SubstancesClinical BiochemistryInterleukin-17 receptorLigandsProtein Structure SecondaryCell LineMiceEndocrinologymedicineAnimalsReceptorProtease-activated receptor 2Interleukin 3Cell Line TransformedMolecular massChemistryGranulocyte-Macrophage Colony-Stimulating FactorCell BiologyLigand (biochemistry)Receptors Interleukin-3Recombinant ProteinsKineticsBiochemistryCystineBiological AssayElectrophoresis Polyacrylamide GelInterleukin-3Interleukin-5Cell DivisionThymidineGrowth factors (Chur, Switzerland)
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Shared midgut binding sites for Cry1A.105, Cry1Aa, Cry1Ab, Cry1Ac and Cry1Fa proteins from Bacillus thuringiensis in two important corn pests, Ostrin…

2013

First generation of insect-protected transgenic corn (Bt-corn) was based on the expression of Cry1Ab or Cry1Fa proteins. Currently, the trend is the combination of two or more genes expressing proteins that bind to different targets. In addition to broadening the spectrum of action, this strategy helps to delay the evolution of resistance in exposed insect populations. One of such examples is the combination of Cry1A.105 with Cry1Fa and Cry2Ab to control O. nubilalis and S. frugiperda. Cry1A.105 is a chimeric protein with domains I and II and the C-terminal half of the protein from Cry1Ac, and domain III almost identical to Cry1Fa. The aim of the present study was to determine whether the c…

Agricultural BiotechnologyApplied MicrobiologyCoated vesiclePlant SciencePlasma protein bindingMothsBiochemistryOstriniaPlagues ControlBacillus thuringiensisBiomacromolecule-Ligand InteractionsPlant PestsMultidisciplinaryMicrovillibiologyGenetically Modified OrganismsQRAgricultureRecombinant ProteinsBiochemistryLarvaMedicineDisease SusceptibilityAgrochemicalsResearch ArticleBiotechnologyProtein BindingScienceProtein domainBiotecnologia agrícolaBacillus thuringiensisCoated VesiclesCerealsCropsSpodopteraSpodopteraMicrobiologyBinding CompetitiveZea maysBacterial ProteinsBotanyAnimalsPesticidesBinding siteProtein InteractionsBiologyTransgenic PlantsfungiProteinsPlant Pathologybiology.organism_classificationFusion proteinMaizeGastrointestinal TractKineticsPlant BiotechnologyPest ControlProteïnes
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Current therapeutical strategies for allergic rhinitis

2018

Allergic rhinitis is a common condition with increasing prevalence and is associated with several comorbid disorders such as bronchial asthma and atopic dermatitis. If allergen avoidance is not possible, allergen-specific immunotherapy is the only causal treatment option.This review focuses on current treatments and the future outlook for allergic rhinitis. Pharmacotherapy includes mast cell stabilizers, antihistamines, glucocorticosteroids (GCSs), leukotriene receptor antagonists, and nasal decongestants. Nasal GCSs are currently regarded as the most effective treatment and are considered first-line therapy together with non-sedating antihistamines. The new formulation MP29-02 combines the…

Allergen immunotherapyRhinitis allergicTreatment outcomeHistamine Antagonistsmacromolecular substancesmedicine.disease_cause03 medical and health sciences0302 clinical medicineAllergenimmune system diseasesmedicineHumansPharmacology (medical)AsthmaPharmacologybusiness.industryHistamine antagonistsGeneral MedicineAtopic dermatitisrespiratory systemmedicine.diseaseRhinitis Allergicrespiratory tract diseasesbody regionsTreatment OutcomeDesensitization Immunologic030220 oncology & carcinogenesisImmunologybusiness030217 neurology & neurosurgeryExpert Opinion on Pharmacotherapy
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Negative Staining and Cryo-negative Staining: Applications in Biology and Medicine

2013

Negative staining is widely applicable to isolated viruses, protein molecules, macromolecular assemblies and fibrils, subcellular membrane fractions, liposomes and artificial membranes, synthetic DNA arrays, and also to polymer solutions and a variety of nanotechnology samples. Techniques are provided for the preparation of the necessary support films (continuous carbon and holey/perforated carbon). The range of suitable negative stains is presented, with some emphasis on the benefit of using ammonium molybdate and of negative stain-trehalose combinations. Protocols are provided for the single droplet negative staining technique (on continuous and holey carbon support films), the floating a…

Ammonium molybdatechemistry.chemical_compoundMembraneCarbon filmchemistryBiophysicsUranyl formateUranyl acetateNegative stainStainingMacromolecule
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Decoding vibrational states of Concanavalin A amyloid fibrils.

2015

International audience; Amyloid and amyloid-like fibrils are a general class of protein aggregates and represent a central topic in life sciences for their involvement in several neurodegenerative disorders and their unique mechanical and supramolecular morphological properties. Both their biological role and their physical properties, including their high mechanical stability and thermodynamic inertia, are related to the structural arrangement of proteins in the aggregates at molecular level. Significant variations may exist in the supramolecular organization of the commonly termed cross-β structure that constitutes the amyloid core. In this context, a fine knowledge of the structural deta…

AmyloidAbsorption spectroscopy[SDV]Life Sciences [q-bio]BiophysicsSupramolecular chemistry02 engineering and technologymacromolecular substancesProtein aggregationAntiparallel (biochemistry)FibrilSpectrum Analysis RamanBiochemistryVibrationProtein Structure Secondary03 medical and health sciencessymbols.namesakeSpectroscopy Fourier Transform InfraredConcanavalin AHumansFourier transform infrared spectroscopyRaman030304 developmental biology0303 health sciencesChemistryOrganic ChemistryIntermolecular force021001 nanoscience & nanotechnologyAmyloid FTIR RAMAN hydration water THz spectroscopy[SDV] Life Sciences [q-bio]CrystallographyFTIRTerahertz spectroscopysymbolsBiophysicsFibrils0210 nano-technologyRaman spectroscopy
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Cholesterol binding to amyloid-β fibrils: A TEM study

2008

There is increasing interest in the role of brain cholesterol in Alzheimer's disease and the contribution of cholesterol to the formation of amyloid plaques. This paper presents a TEM study showing the binding of soluble approximately 10 nm diameter cholesterol-PEG 600 micelles to amyloid-beta(1-42) (Abeta(1-42)) fibrils formed either in the presence of this cholesterol derivative or to preformed fibrils generated under four different fibrillogenesis conditions. Specimens negatively stained with uranyl acetate revealed that during 24 h fibrillogenesis at 37 degrees C the cholesterol-PEG micelles bound periodically to Abeta(1-42) protofibrils and apparently also formed a thin smooth unbroken…

AmyloidAmyloid beta-PeptidesCholesterolCholesterol bindingGeneral Physics and AstronomyUranyl acetateFibrillogenesismacromolecular substancesCell BiologyFibrilNegative stainMicellePolyethylene GlycolsCrystallographychemistry.chemical_compoundCholesterolMicroscopy Electron TransmissionchemistryStructural BiologyHumanslipids (amino acids peptides and proteins)General Materials ScienceHydrogen peroxideMicellesMicron
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Detection of Amyloid-β Fibrils Using Track-Etched Nanopores: Effect of Geometry and Crowding

2021

Several neurodegenerative diseases have been linked to proteins or peptides that are prone to aggregate in different brain regions. Aggregation of amyloid-β (Aβ) peptides is recognized as the main cause of Alzheimer's disease (AD) progression, leading to the formation of toxic Aβ oligomers and amyloid fibrils. The molecular mechanism of Aβ aggregation is complex and still not fully understood. Nanopore technology provides a new way to obtain kinetic and morphological aspects of Aβ aggregation at a single-molecule scale without labeling by detecting the electrochemical signal of the peptides when they pass through the hole. Here, we investigate the influence of nanoscale geometry (conical an…

AmyloidAmyloidAmyloid βSonicationBioengineeringGeometrymacromolecular substances02 engineering and technologyPolyethylene glycol010402 general chemistryFibril01 natural sciencesNanoporeschemistry.chemical_compoundAlzheimer DiseasePEG ratioHumansInstrumentationNanoscopic scaleFluid Flow and Transfer ProcessesAmyloid beta-PeptidesChemistryProcess Chemistry and Technology021001 nanoscience & nanotechnology0104 chemical sciencesKineticsNanopore0210 nano-technologyACS Sensors
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Polymorphism of amyloid-beta fibrils and its effects on human erythrocyte catalase binding.

2009

The Alzheimer's amyloid-beta (Abeta) peptide exists as a number of naturally occurring forms due to differential proteolytic processing of its precursor molecule. Many of the Abeta peptides of different lengths form fibrils in vitro, which often show polymorphisms in the fibril structure. This study presents a TEM based analysis of fibril formation by eighteen different Abeta peptides ranging in length from 5 to 43 amino acids. Spectrophotometric analysis of Congo red binding to the fibrillar material has been assessed and the binding of human erythrocyte catalase (HEC) to Abeta fibrils has also been investigated by TEM. The results show that a diverse range of Abeta peptides form fibrils a…

AmyloidErythrocytesGeneral Physics and AstronomyPeptidemacromolecular substancesPlasma protein bindingFibrilchemistry.chemical_compoundMicroscopy Electron TransmissionStructural BiologyHumansGeneral Materials Sciencechemistry.chemical_classificationbiologyStaining and LabelingCongo RedCell BiologyCatalaseIn vitroAmino acidCongo redPolymorphism (materials science)BiochemistrychemistryCatalaseSpectrophotometrybiology.proteinProtein BindingMicron (Oxford, England : 1993)
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