Search results for "TERT"

showing 10 items of 1210 documents

Exploring alternative approaches in service industries: the role of entrepreneurship

2008

Today, it is widely recognised that the success and vitality of the service sector are essential factors in measuring an economy’s progress, its quality, and its future expectations. It not only im...

Professional servicesEntrepreneurshipbusiness.industryStrategy and Managementmedia_common.quotation_subjectVitalityHospitality industryManagement of Technology and InnovationQuality (business)Catering industryMarketingbusinessTertiary sector of the economymedia_commonThe Service Industries Journal
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Comparative analysis of stress responses of H9c2 rat cardiomyoblasts following treatment with doxorubicin and tBOOH

2011

Abstract Cardiotoxicity is the major dose-limiting adverse effect of anthracyclines and is hypothesized to result from damage induced by reactive oxygen species (ROS) or inhibition of topoisomerase II. Here, we comparatively analyzed the effect of doxorubicin and the organic peroxide tertiary-butylhydroperoxide (tBOOH) on stress responses of rat cardiomyblast cells (H9c2). Moreover, we investigated the impact of serum factors and the novel prototypical protein kinase CK2 inhibitor resorufin on the sensentivity of H9c2 cells exposed to doxorubicin or tBOOH. Measuring cell viability by use of the WST assay as well as cell cycle progression and apoptotic death by FACS-based methods, we found t…

Programmed cell deathDNA damageCell SurvivalAntineoplastic AgentsApoptosisBiologyPharmacologyAntioxidantsCell Linetert-ButylhydroperoxidemedicineAnimalsDoxorubicinViability assayCytotoxicitychemistry.chemical_classificationReactive oxygen speciesCardiotoxicityDose-Response Relationship DrugKinaseCell BiologyMolecular biologyAcetylcysteineRatsOxidative StresschemistryDoxorubicinReactive Oxygen SpeciesMyoblasts Cardiacmedicine.drug
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Properzio e Cornelio Gallo: il modello 'cogente', il modello 'sfuggente'

2014

Se la scoperta del papiro di Qaṣr Ibrîm ha ampliato le nostre conoscenze sulla produzione di Cornelio Gallo, la fisionomia di questi distici ha consentito di retrodatare l’apparizione del servitium amoris e delle lamentele sulla nequitia puellae restituendo a Gallo la paternità di entrambi e alla sua poesia un ruolo paradigmatico. Viceversa, per quel che concerne il fr. 4, il complesso legame che intercorre fra le Muse, Licoride e l’autore non permette di ipotizzare diretti influssi sulla creazione della figura della puella carminum iudex compiuta da Properzio soprattutto nel secondo libro delle Elegie. Un modello soggetto a continui riadattamenti appare viceversa il fr. 3, dedicato alla ma…

Properzio Cornelio Gallo intertestualità.Settore L-FIL-LET/04 - Lingua E Letteratura Latina
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Development of Novel Selective Peptidomimetics Containing a Boronic Acid Moiety, Targeting the 20S Proteasome as Anticancer Agents

2014

This paper describes the design, synthesis, and biological evaluation of peptidomimetic boronates as inhibitors of the 20S proteasome, a validated target in the treatment of multiple myeloma. The synthesized compounds showed a good inhibitory profile against the ChT-L activity of 20S proteasome. Compounds bearing a β-alanine residue at the P2 position were the most active, that is, 3-ethylphenylamino and 4-methoxyphenylamino (R)-1-{3-[4-(substituted)-2-oxopyridin-1(2H)-yl]propanamido}-3-methylbutylboronic acids (3 c and 3 d, respectively), and these derivatives showed inhibition constants (Ki ) of 17 and 20 nM, respectively. In addition, they co-inhibited post glutamyl peptide hydrolase act…

Proteasome Endopeptidase ComplexPeptidomimeticStereochemistryCell Survivalanticancer agents; boronates; bortemib; Docking studies; Peptidomimetics; inhibitor; proteasomesAntineoplastic AgentsSaccharomyces cerevisiaedocking studieBiochemistrySubstrate Specificitychemistry.chemical_compoundCell Line TumorDrug DiscoverymedicineMoietyHumansGeneral Pharmacology Toxicology and PharmaceuticsPharmacologychemistry.chemical_classificationBinding SitesproteasomesBortezomibOrganic ChemistrybortezomibboronateBoronic AcidspeptidomimeticProtein Structure Tertiaryanticancer agentMolecular Docking SimulationinhibitorEnzymechemistryProteasomeBiochemistryDocking (molecular)Molecular MedicinePeptidomimeticsGrowth inhibitionDrug Screening Assays AntitumorProteasome InhibitorsBoronic acidmedicine.drug
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Insights into functional aspects of centrins from the structure of N-terminally extended mouse centrin 1

2006

AbstractCentrins are members of the family of Ca2+-binding EF-hand proteins. In photoreceptor cells, centrin isoform 1 is specifically localized in the non-motile cilium. This connecting cilium links the light-sensitive outer segment with the biosynthetic active inner segment of the photoreceptor cell. All intracellular exchanges between these compartments have to occur through this cilium. Three-dimensional structures of centrins from diverse organisms are known, showing that the EF-hand motifs of the N-terminal domains adopt closed conformations, while the C-terminal EF-hand motifs have open conformations. The crystal structure of an N-terminally extended mouse centrin 1 (MmCen1-L) resemb…

Protein ConformationAmino Acid MotifsSequence HomologyPlasma protein bindingEF-handTroponin CMiceStructure-Activity RelationshipProtein structureCalcium-binding proteinConnecting ciliumCentrinAnimalsHumansPhotoreceptor CellsCiliaEF Hand MotifsProtein Structure QuaternaryChemistryEF handCiliumCalcium-Binding ProteinsTerminal Repeat SequencesCalcium-binding proteinSensory SystemsProtein Structure TertiaryCell biologyOphthalmologyCentrinCalciumTransducinsense organsX-ray structureProtein BindingVision Research
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Aggregation Kinetics of Bovine Serum Albumin Studied by FTIR Spectroscopy and Light Scattering

2003

To investigate which type of structural and conformational changes is involved in the aggregation processes of bovine serum albumin (BSA), we have performed thermal aggregation kinetics in D(2)O solutions of this protein. The tertiary conformational changes are followed by Amide II band, the secondary structural changes and the formation of beta-aggregates by the Amide I' band and, finally, the hydrodynamic radius of aggregates by dynamic light scattering. The results show, as a function of pD, that: tertiary conformational changes are more rapid as pD increases; the aggregation proceeds through formation of ordered aggregates (oligomers) at pD far from the isoelectric point of the protein;…

Protein ConformationKineticsBiophysicsProtein aggregationBiochemistryProtein Structure SecondaryProtein structureDynamic light scatteringSpectroscopy Fourier Transform InfraredAnimalsScattering RadiationStatic light scatteringDeuterium OxideBovine serum albuminInfrared spectroscopyStatic light scatteringbiologyChemistryOrganic ChemistryTemperatureSerum Albumin BovineConformational changeRandom coilProtein tertiary structureKineticsCrystallographyBovine serum albuminbiology.proteinDynamic light scatteringCattleProtein aggregation
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Human Brain Neuroglobin Structure Reveals a Distinct Mode of Controlling Oxygen Affinity

2003

Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O(2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a hexacoordinated heme. O(2) and CO bind to the heme iron, displacing the endogenous HisE7 heme distal ligand. Hexacoordinated human neuroglobin displays a classical globin fold adapted to host the reversible bis-histidyl heme complex and an elongated protein matrix cavity, held to facilitate O(2) diffusion to the heme. The neuroglobin structure suggests that the classical globin fold is endowed …

Protein ConformationNeuroglobinNerve Tissue ProteinsBiologyProtein Structure Secondarychemistry.chemical_compoundProtein structureStructural BiologyHumansAmino Acid SequenceGlobinHemeMolecular BiologyBrain ChemistryCytoglobinOxygen transportGlobinsProtein Structure TertiaryGlobin foldOxygenMyoglobinchemistryBiochemistryNeuroglobinBiophysicsSequence AlignmentProtein BindingStructure
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Conformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMR

2005

Copyright © by Portland Press. The final version of record is available at http://www.biochemj.org/bj/default.htm

Protein ConformationStereochemistryIntegrinNMR protein dynamics determinationTripeptideBiochemistryHomonuclear moleculeOff-resonance rotating-frame Overhauser enhancement spectroscopy (off-resonance ROESY)Protein structureSide chainAnimalsNuclear Magnetic Resonance BiomolecularMolecular BiologyIntegrin bindingRGD motifchemistry.chemical_classificationBinding Sites:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]ChemistryEchistatin integrinSnakesUNESCO::CIENCIAS DE LA VIDA::BioquímicaCell BiologyRGD disintegrin; Echistatin; Integrin; NMR protein dynamics determination; Off-resonance rotating-frame Overhauser enhancement spectroscopy (off-resonance ROESY)Protein Structure TertiaryAmino acidRGD disintegrinDocking (molecular)EchistatinIntercellular Signaling Peptides and ProteinsPeptidesResearch ArticleProtein Binding
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Conformational changes involved in thermal aggregation processes of bovine serum albumin

2003

We report a kinetic study on thermal aggregation process of the model protein bovine serum albumin (BSA) in low concentration regime. Aim of this study is to provide information on relationship between conformational changes and initial step of aggregation. The experimental approach is based on steady-state fluorescence spectra of the two tryptophans located in two different domains, in way to study conformational changes in the surrounding of these residues. We also follow emission spectra of Fluorescein-5-Maleimide dye bound to the single free cysteine of BSA. Complementary information on the extent of aggregation and on the structural changes is obtained by Rayleigh scattering and circul…

Protein DenaturationCircular dichroismHot TemperatureLightKineticsSerum albuminBiophysicsProtein aggregationCircular dichroismBiochemistryProtein Structure SecondaryProtein structureAnimalsHumansScattering RadiationCysteineBovine serum albuminPhysical and Theoretical ChemistryProtein secondary structurebiologyChemistryOrganic ChemistryTryptophanSerum Albumin BovineFluoresceinsConformational changeProtein Structure TertiaryKineticsCrystallographySpectrometry FluorescenceBovine serum albuminSteady-state fluorescencebiology.proteinCattlesense organsProtein aggregationCysteine
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The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains.

2007

Abstract Procollagen C-proteinase (PCP) removes the C-terminal pro-peptides of procollagens and also processes other matrix proteins. The major splice form of the PCP is termed BMP1 (bone morphogenetic protein 1). Active BMP1 is composed of an astacin-like protease domain, three CUB (complement, sea urchin Uegf, BMP1) domains and one EGF-like domain. Here we compare the recombinant human full-length BMP1 with its isolated proteolytic domain to further unravel the functional influence of the CUB and EGF domains. We show that the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. However, u…

Protein FoldingCollagen Type VIIDNA Complementarymedicine.medical_treatmentClinical BiochemistryAmino Acid MotifsGene ExpressionGlutamic AcidBiochemistryBone morphogenetic protein 1Mass SpectrometryBone Morphogenetic Protein 1Cell LineSubstrate SpecificityProtein structuremedicineEscherichia coliAnimalsHumansCysteineDisulfidesMolecular BiologyInclusion BodiesMetalloproteinaseProteasebiologyChemistryMetalloendopeptidasesRecombinant ProteinsProtein Structure TertiaryFibronectinProcollagen peptidaseDrosophila melanogasterBiochemistryBone Morphogenetic ProteinsMutationbiology.proteinProtein foldingAstacinBiological chemistry
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