Search results for " SPECT"

showing 10 items of 11464 documents

Analgesic Activity, Chemical Profiling and Computational Study on Chrysopogon aciculatus

2018

Present study was undertaken to evaluate the analgesic activity of the ethanol extract of Chrysopogon aciculatus. In addition to bioassays in mice, chemical profiling was done by LC-MS and GC-MS to identify phytochemicals, which were further docked on the catalytic site of COX-2 enzymes with a view to suggest the possible role of such phytoconstituents in the observed analgesic activity. Analgesic activity of C. aciculatus was evaluated by acetic acid induced writhing reflex method and hot plate technique. Phytochemical profiling was conducted using liquid chromatography mass spectrometry (LC-MS) and gas chromatography mass spectrometry (GC-MS). In docking studies, homology model of human C…

0301 basic medicineRMliquid chromatography mass spectrometrygas chromatography mass spectrometryChrysopogon aciculatushot plate test03 medical and health sciencesAcetic acidchemistry.chemical_compound0302 clinical medicineLiquid chromatography–mass spectrometryPharmacology (medical)Hot plate testPharmacologyChromatographybiologyChrysopogon aciculatuspoaceaelcsh:RM1-950analgesicbiology.organism_classification030104 developmental biologylcsh:Therapeutics. PharmacologychemistryPhytochemicalDocking (molecular)030220 oncology & carcinogenesisTricinGas chromatography–mass spectrometryFrontiers in Pharmacology
researchProduct

MODOMICS: a database of RNA modification pathways. 2017 update

2017

Abstract MODOMICS is a database of RNA modifications that provides comprehensive information concerning the chemical structures of modified ribonucleosides, their biosynthetic pathways, the location of modified residues in RNA sequences, and RNA-modifying enzymes. In the current database version, we included the following new features and data: extended mass spectrometry and liquid chromatography data for modified nucleosides; links between human tRNA sequences and MINTbase - a framework for the interactive exploration of mitochondrial and nuclear tRNA fragments; new, machine-friendly system of unified abbreviations for modified nucleoside names; sets of modified tRNA sequences for two bact…

0301 basic medicineRNA methylationBiologycomputer.software_genreMass Spectrometry03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferEpitranscriptomicsTerminology as TopicRNA modificationDatabases GeneticGeneticsDatabase IssueHumanschemistry.chemical_classificationDatabase2'-O-methylationRNA030104 developmental biologyEnzymechemistry030220 oncology & carcinogenesisTransfer RNARNARibonucleosidesN6-MethyladenosinecomputerChromatography LiquidNucleic Acids Research
researchProduct

Zero-field nuclear magnetic resonance of chemically exchanging systems.

2019

Zero- to ultralow-field (ZULF) nuclear magnetic resonance (NMR) is an emerging tool for precision chemical analysis. In this work, we study dynamic processes and investigate the influence of chemical exchange on ZULF NMR J-spectra. We develop a computational approach that allows quantitative calculation of J-spectra in the presence of chemical exchange and apply it to study aqueous solutions of [15N]ammonium (15N\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$${\mathrm{H}}_4^ +$$\end{document}H4+) as a model syst…

0301 basic medicineReaction kinetics and dynamicsSciencePhysics::Medical PhysicsGeneral Physics and AstronomyModel system02 engineering and technologyGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesNuclear magnetic resonanceZero fieldHyperpolarization (physics)lcsh:ScienceDissolutionQuantitative Biology::Biomolecules3403 Macromolecular and Materials ChemistryMultidisciplinaryAqueous solution34 Chemical SciencesChemical exchangeQ500Diagnostic markersGeneral ChemistryNuclear magnetic resonance spectroscopy021001 nanoscience & nanotechnologyequipment and supplies030104 developmental biologylcsh:Qddc:5000210 nano-technologyhuman activitiesSolution-state NMR51 Physical Sciences
researchProduct

Nuclear inclusions of pathogenic ataxin-1 induce oxidative stress and perturb the protein synthesis machinery

2020

Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. These expansions are responsible for protein misfolding and self-assembly into intranuclear inclusion bodies (IIBs) that are somehow linked to neuronal death. However, owing to lack of a suitable cellular model, the downstream consequences of IIB formation are yet to be resolved. Here, we describe a nuclear protein aggregation model of pathogenic human ataxin-1 and characterize IIB effects. Using an inducible Sleeping Beauty transposon system, we overexpressed the ATXN1(Q82) gene in human mesenchymal stem cells that are resistant to the early cytotoxic effects caused by the expr…

0301 basic medicineSCA1 Spinocerebellar ataxia type-1Intranuclear Inclusion BodiesClinical BiochemistryMSC mesenchymal stem cellProtein aggregationBiochemistry0302 clinical medicineMutant proteinProtein biosynthesisDE differentially expressed genesNuclear proteinlcsh:QH301-705.5FTIR Fourier-transform infrared spectroscopyAtaxin-1lcsh:R5-920biologyChemistryNuclear ProteinspolyQ polyglutamineRibosomeCell biologySB Sleeping BeautyRibosome ; Polyglutamine ; Ataxin-1 ; Oxidative stress ; Transposon ; Sleeping beauty transposon ; Protein networkSpinocerebellar ataxiaProtein foldingCellular modelFunction and Dysfunction of the Nervous Systemlcsh:Medicine (General)Research PaperiPSC induced pluripotent stem cellAtaxin 1Nerve Tissue ProteinsPPI protein-protein interaction03 medical and health sciencesROS reactive oxygen speciesProtein networkSleeping beauty transposonGSEA Gene Set Enrichment AnalysismedicineHumansNPC neural progenitor cellOrganic Chemistrymedicine.diseaseAFM atomic force microscopyOxidative Stress030104 developmental biologylcsh:Biology (General)IIBs intranuclear inclusion bodiesMS mass spectrometryCardiovascular and Metabolic Diseasesbiology.proteinPolyglutamine030217 neurology & neurosurgery
researchProduct

SPEN haploinsufficiency causes a neurodevelopmental disorder overlapping proximal 1p36 deletion syndrome with an episignature of X chromosomes in fem…

2021

Contains fulltext : 231702.pdf (Publisher’s version ) (Closed access) Deletion 1p36 (del1p36) syndrome is the most common human disorder resulting from a terminal autosomal deletion. This condition is molecularly and clinically heterogeneous. Deletions involving two non-overlapping regions, known as the distal (telomeric) and proximal (centromeric) critical regions, are sufficient to cause the majority of the recurrent clinical features, although with different facial features and dysmorphisms. SPEN encodes a transcriptional repressor commonly deleted in proximal del1p36 syndrome and is located centromeric to the proximal 1p36 critical region. Here, we used clinical data from 34 individuals…

0301 basic medicineSHARPMaleobesitygenotype-phenotype correlationsAutism Spectrum DisorderPROTEINChromosome DisordersHaploinsufficiencyRNA-Binding ProteinPHENOTYPE CORRELATIONS1p36; distal 1p36 deletion syndrome; DNA methylome analysis; episignature; genotype-phenotype correlations; neurodevelopmental disorder; obesity; proximal 1p36 deletion syndrome; SPEN; X chromosome; Adolescent; Autism Spectrum Disorder; Child; Child Preschool; Chromosome Deletion; Chromosome Disorders; Chromosomes Human Pair 1; Chromosomes Human X; DNA Methylation; DNA-Binding Proteins; Epigenesis Genetic; Female; Haploinsufficiency; Humans; Intellectual Disability; Male; Neurodevelopmental Disorders; Phenotype; RNA-Binding Proteins; Young AdultEpigenesis GeneticX chromosome0302 clinical medicineNeurodevelopmental disorderNeurodevelopmental DisorderIntellectual disabilityMOLECULAR CHARACTERIZATIONdistal 1p36 deletion syndromeChildGenetics (clinical)X chromosomeGeneticsXDNA methylome analysiRNA-Binding ProteinsSPLIT-ENDSHypotoniaDNA-Binding ProteinsPhenotypeAutism spectrum disorderChromosomes Human Pair 1Child PreschoolDNA methylome analysisMONOSOMY 1P36Pair 1SPENFemalemedicine.symptomChromosome DeletionHaploinsufficiencyRare cancers Radboud Institute for Health Sciences [Radboudumc 9]HumanAdolescentDNA-Binding ProteinBiologygenotype-phenotype correlationChromosomes03 medical and health sciencesYoung AdultGeneticSDG 3 - Good Health and Well-beingReportIntellectual DisabilityREVEALSGeneticsmedicineHumansEpigeneticsPreschoolChromosomes Human XNeurodevelopmental disorders Donders Center for Medical Neuroscience [Radboudumc 7]1p361p36 deletion syndromeIDENTIFICATIONMUTATIONSproximal 1p36 deletion syndromeDNA Methylationmedicine.diseaseneurodevelopmental disorderGENEepisignature030104 developmental biologyChromosome DisorderNeurodevelopmental Disorders030217 neurology & neurosurgeryEpigenesis
researchProduct

Quantitative and Qualitative in vivo Analysis of Metal Residuals in the Saliva of Subjects with and without Fixed Orthodontic Appliances

2020

Aim of the Work: The aim of this work was to evaluate Ni e Cr ions in the saliva of subjects with and without fixed orthodontic appliances. Materials and Methods: This was a prospective, non-randomized study of 100 patients, so selected: 50 have undergone fixed orthodontic appliance at least from 24 months; others 50 subjects as control-group, without any fixed and/or removable orthodontic appliance It was conducted according to the Declaration of the World Medical Association of Helsinki. The two selected groups were compatible for age, sex, absence of restoration in amalgam or other metals in the oral cavity. The saliva of all the subjects was collected with standardized sterile methods. …

0301 basic medicineSalivaMaterials scienceMetal ions in aqueous solutionfungiMetallurgytechnology industry and agriculture030206 dentistryGeneral MedicineBiocompatible materialCorrosionMetal03 medical and health sciences030104 developmental biology0302 clinical medicineNickel titaniumFixed Orthodontic Appliancevisual_artGalvanic cellvisual_art.visual_art_mediumNickel ionsAtomic Absorption SpectrophotometryMetal IonSaliva
researchProduct

2017

Disruption of the human SHANK3 gene can cause several neuropsychiatric disease entities including Phelan-McDermid syndrome, autism spectrum disorder (ASD), and intellectual disability. Although, a wide array of neurobiological studies strongly supports a major role for SHANK3 in organizing the post-synaptic protein scaffold, the molecular processes at synapses of individuals harboring SHANK3 mutations are still far from being understood. In this study, we biochemically isolated the post-synaptic density (PSD) fraction from striatum and hippocampus of adult Shank3Δ11-/- mutant mice and performed ion-mobility enhanced data-independent label-free LC-MS/MS to obtain the corresponding PSD proteo…

0301 basic medicineScaffold proteinMutantHOMER1CDKL5Biologymedicine.diseaseSHANK3 GeneSynapse03 medical and health sciencesCellular and Molecular Neuroscience030104 developmental biology0302 clinical medicineAutism spectrum disordermedicineMolecular BiologyNeurosciencePostsynaptic density030217 neurology & neurosurgeryFrontiers in Molecular Neuroscience
researchProduct

Heat- and pH-induced BSA conformational changes, hydrogel formation and application as 3D cell scaffold

2016

Aggregation and gelation of globular proteins can be an advantage to generate new forms of nanoscale biomaterials based on the fibrillar architecture. Here, we report results obtained by exploiting the proteins' natural tendency to self-organize in 3D network, for the production of new material based on BSA for medical application. In particular, at five different pH values the conformational and structural changes of the BSA during all the steps of the thermal aggregation and gelation have been analyzed by FTIR spectroscopy. The macroscopic mechanical properties of these hydrogels have been obtained by rheological measurements. The microscopic structure of the gels have been studied by AFM…

0301 basic medicineScaffoldHot TemperatureNanostructureBSACell SurvivalProtein ConformationGlobular proteinBiophysics?-aggregatesBiocompatible Materials02 engineering and technologymacromolecular substancesMicroscopy Atomic ForceBiochemistryMice03 medical and health sciencesProtein structureRheologySpectroscopy Fourier Transform Infraredβ-aggregateAnimalsCell-scaffoldFourier transform infrared spectroscopyMolecular BiologyNanoscopic scalechemistry.chemical_classificationTissue ScaffoldsChemistrySerum Albumin BovineHydrogelsHydrogen-Ion Concentration021001 nanoscience & nanotechnologySettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)NanostructuresHydrogelCrystallography030104 developmental biologyMechanical spectraBiophysicChemical engineeringFTIRSelf-healing hydrogelsMicroscopy Electron ScanningCattleStress MechanicalRheology0210 nano-technology
researchProduct

Resistance against Echinostoma caproni (Trematoda) secondary infections in mice is not dependent on the ileal protein production

2016

Echinostoma caproni (Trematoda: Echinostomatidae) is an intestinal trematode, which has been widely employed to investigate the factors determining the rejection of intestinal helminths. Protein production patterns of intestinal epithelial cells are related to the infection-induced changes that determine the course of E. caproni infections. Herein, we compare the protein production profiles in the ileum of four experimental groups of mice: control; infected; dewormed and reinfected. Worm burdens were significantly lower in secondary infections, confirming the generation of partial resistance to homologous secondary infections in mice. However, quantitative comparison by 2D-DIGE showed that …

0301 basic medicineSecondary infection030231 tropical medicineBiophysicsIleumBiochemistryMass SpectrometryMice03 medical and health sciences0302 clinical medicineIleumEchinostomaProtein biosynthesismedicineAnimalsHelminthsTissue homeostasisCell ProliferationDisease ResistanceEchinostomiasisCell DeathbiologyCoinfectionEpithelial Cellsbiology.organism_classificationPraziquantel030104 developmental biologymedicine.anatomical_structureProtein BiosynthesisImmunologyTrematodaEchinostomamedicine.drugJournal of Proteomics
researchProduct

The O-antigen of Plesiomonas shigelloides serotype O36 containing pseudaminic acid

2016

The structure of the repeating unit of O-antigen of Plesiomonas shigelloides serotype O36 has been investigated by 1H and 13C NMR spectroscopy, matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry and chemical methods. The new structure of trisaccharide has been established: →4)-β-Pse5Ac7(R3Hb)-(2 → 4)-β-D-Galp-(1 → 3)-β-D-GlcpNAc-(1→ These trisaccharide O-antigen units substitute the core undecasaccharide at C-4 of the β-D-GlcpNAc residue. The core oligosaccharide and lipid A are identical with these of the serotype O17 (PCM 2231) (Maciejewska, A., Lukasiewicz, J., Kaszowska, M., Jachymek, W., Man-Kupisinska, A.; Lugowski, C. Mar. Drugs.2013, 11 (2), 440–454; Lukasi…

0301 basic medicineSerotypeMagnetic Resonance SpectroscopyStereochemistryMass spectrometrySerogroupBiochemistryAnalytical ChemistryLipid A03 medical and health sciencesResidue (chemistry)AntigenMALDI-TOF MSTrisaccharidechemistry.chemical_classification030102 biochemistry & molecular biologybiologyChemistryOrganic ChemistryO AntigensGeneral MedicineO-antigenbiology.organism_classificationPlesiomonas shigelloidesNMRMatrix-assisted laser desorption/ionization030104 developmental biologyBiochemistryCarbohydrate SequencePlesiomonas shigelloidesPlesiomonasCarbohydrate Research
researchProduct