Search results for "ThT"

showing 10 items of 13 documents

Protective Effects of L- and D-Carnosine on R-Crystallin Amyloid Fibril Formation: Implications for Cataract Disease

2009

Mildly denaturing conditions induce bovine ?-crystallin, the major structural lens protein, to self-assemble into fibrillar structures in vitro. The natural dipeptide L-carnosine has been shown to have potential protective and therapeutic significance in many diseases. Carnosine derivatives have been proposed as potent agents for ophthalmic therapies of senile cataracts and diabetic ocular complications. Here we report the inhibitory effect induced by the peptide (L- and D-enantiomeric form) on ?-crystallin fibrillation and the almost complete restoration of the chaperone activity lost after denaturant and/or heat stress. Scanning force microscopy (SFM), thioflavin T, and a turbidimetry ass…

CrystallinCircular dichroismAmyloidCarnosinePeptideMicroscopy Atomic ForceBiochemistryCataractLens proteinRats Sprague-Dawleychemistry.chemical_compoundOrgan Culture TechniquesCrystallinChaperone activityAnimalsalpha-CrystallinsSFM Scanning Force Microscopychemistry.chemical_classificationDipeptideCD Circular DichroismThT Thioflavin TCalorimetry Differential ScanningDSC Differential Scanning CalorimetryCircular DichroismCarnosineStereoisomerismIn vitroeye diseasesRatsSpectrometry FluorescencechemistryBiochemistryHEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidThioflavinCattleFemaleSpectrophotometry Ultravioletsense organsAmyloid fibrilMolecular Chaperones
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Artesanado sedero y capital comercial en la Valencia del siglo XVIII

1997

The intense development of the «Verlagssystem» in the XVIII century silk industry in Valencia showed the difficulties of the traditional craftsmen to keep their economic independence. In order to fighy against it, the craftsmen adopted several initiatives, which dealt with the constitution of a share-holding company, as much as with the creation of a communal store to favour the suppley of raw materials to the factories. The most important project was the constitution of the «Compañía de Nuestra Señora de los Desamparados» in 1772. But the requirement of the General Board of Commerce to allow all the social classes to take part in shareholders, as it was not accompanied by the modification …

HistorySedaSpain; Silk; Craftsman; industry; Valencia; Verlagssystem; eigthteenth century.media_common.quotation_subjectEspañaSilkSocial SciencesEconomic independenceindustrialcsh:Social SciencesHH.ª ModernaShareholderPolitical scienceVerlagssystemEconomic historyCraftsmanmedia_commonindustryConstitutionReservationEspaña; Valencia; H.ª Moderna; Seda; artesano; industria; Verlagssystem; siglo XVIII.eigthteenth century.lcsh:Hsiglo XVIII.Order (business)SpainValenciaartesanoHispania : Revista española de historia
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Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq

2015

Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to…

IDP intrinsically-disordered proteinslcsh:Lifelcsh:QR1-502sub-membrane macromolecular assemblyPlasma protein bindingsRNA small non-coding RNABiochemistrylcsh:Microbiologyamyloid fibrilsProtein biosynthesis0303 health sciences[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Escherichia coli Proteins030302 biochemistry & molecular biologyHfqCTRp Hfq C-terminal peptideFTIR Fourier transform infrared spectroscopyNTR N-terminal regionCompartmentalization (psychology)Cell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsRNA Bacterialsmall non-coding ribonucleic acid (RNA)BiochemistryFSD Fourier self-deconvolutionTransfer RNAAmyloid fibrilProtein BindingBiophysicsBiologyHost Factor 1 Protein03 medical and health sciencesEscherichia coliThT thioflavin T[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein Structure QuaternaryncRNA regulatory non-coding RNAPost-transcriptional regulationMolecular Biology030304 developmental biologyOriginal PaperC-terminusRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyCell Biologycellular compartmentalizationWT wild-typeProtein Structure Tertiarylcsh:QH501-531Host Factor 1 ProteinCTR Hfq C-terminal regionribonucleic acid (RNA) processing and degradationBiophysicpost-transcriptional regulationBioscience Reports
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Self-Organization Pathways and Spatial Heterogeneity in Insulin Amyloid Fibril Formation

2009

At high temperature and low pH, the protein hormone insulin is highly prone to form amyloid fibrils, and for this reason it is widely used as a model system to study fibril formation mechanisms. In this work, we focused on insulin aggregation mechanisms occurring in HCl solutions (pH 1.6) at 60 degrees C. By means of in situ Thioflavin T (ThT) staining, the kinetics profiles were characterized as a function of the protein concentration, and two concurrent aggregation pathways were pointed out, being concentration dependent. In correspondence to these pathways, different morphologies of self-assembled protein molecules were detected by atomic force microscopy images also evidencing the prese…

In situAmyloidHot Temperaturemedicine.medical_treatmentKineticsNucleationMicroscopy Atomic ForceFibrilchemistry.chemical_compoundMicroscopyMaterials ChemistrymedicineAnimalsInsulinBenzothiazolesPhysical and Theoretical ChemistryInsulin Amyloid Fibrils Secondary Nucleation Thioflavin T (ThT) Scanning Force Microscopy (SFM) Spatial HeterogeneityChemistryInsulinfluorescence spectroscopyFluorescenceSurfaces Coatings and FilmsThiazolesBiochemistryBiophysicsCattleThioflavinHydrochloric AcidProtein aggregation
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Kaurane diterpenoids from three Sideritis species

2005

Some kaurane diterpenoids were isolated from 3 species of the genus Sideritis (Lamiaceae) growing in the Eastern Mediterranean region. Sideritis libanotica subsp. libanotica contained siderol 2 and sideridiol 3. Sideritis erythrantha var. erythrantha yielded sideridiol 3. Sideritis perfoliata gave siderol 2, sideridiol 3 and sideritriol 4. The products are known as they occur in another species of Sideritis growing in Italy and in other species growing also in Turkey. The products are isolated for the first time from these 3 species. The taxonomic significance of these results is discussed.

LamiaceaeSideritis erythtrantha var. erythranthakauranediterpenoidSideritis libanotica subsp libanoticaSideritis perfoliata
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Exporting a Google Earth™ aided earthflow susceptibility model: a test in central Sicily

2012

Abstract In the framework of a regional landslide susceptibility study in southern Sicily, a test has been carried out in the Tumarrano river basin (about 80 km2) aimed at characterizing its landslide susceptibility conditions by exporting a ‘‘source model’’, defined and trained inside a limited (about 20 km2) representative sector (the ‘‘source area’’). Also, the possibility of exploiting Google Earth TM software and photo-images databank to produce the landslide archives has been checked. The susceptibility model was defined, according to a multivariate geostatistic approach based on the conditional analysis, using unique condition units (UCUs), which were obtained by combining four selec…

Landslide susceptibility Exportation of models Google EarthTM ValidationSettore GEO/04 - Geografia Fisica E GeomorfologiaSettore GEO/05 - Geologia Applicata
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Carnosine inhibits amyloid fibril formation of alpha crystallin under destabilizing conditions

2008

SFM Scanning Force MicroscopyCD Circular DichroismThT Thioflavin THEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidDSC Differential Scanning Calorimetry
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Inhibition of α-crystallin amyloid fibrils formation by carnosine

2008

SFM Scanning Force MicroscopyCD Circular DichroismThT Thioflavin THEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidDSC Differential Scanning Calorimetry
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Effect of the heat treatment on α-crystallin : characterisation of amyloid fibrils formation and inhibitory effect of carnosine

2009

SFM Scanning Force MicroscopyCD Circular DichroismThT Thioflavin THEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidDSC Differential Scanning Calorimetry
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CCDC 645089: Experimental Crystal Structure Determination

2007

Related Article: M.Cametti, M.Nissinen, A.D.Cort, L.Mandolini, K.Rissanen|2007|J.Am.Chem.Soc.|129|3641|doi:10.1021/ja068561z

Space GroupCrystallographyCrystal SystemCrystal StructureAcetonitrile-(33'-bis(2-naphththylmethoxy)-NN'-phenylene-bis(salicylideneaminato))-dioxo-uranium acetonitrile solvateCell ParametersExperimental 3D Coordinates
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