Search results for "Intrinsic"

showing 10 items of 386 documents

A Pathology-Based Combined Model to Identify PAM50 Non-luminal Intrinsic Disease in Hormone Receptor-Positive HER2-Negative Breast Cancer

2019

No luminal; Subtipus intrínsec; Càncer de mama No luminal; Subtipo intrínseco; Cáncer de mama Non-luminal; Intrinsic subtype, Breast cancer Background: In hormone receptor-positive (HR+)/HER2-negative breast cancer, the HER2-enriched and Basal-like intrinsic subtypes are associated with poor outcome, low response to anti-estrogen therapy and high response to chemotherapy. To date, no validated biomarker exists to identify both molecular entities other than gene expression. Methods: PAM50 subtyping and immunohistochemical data were obtained from 8 independent studies of 1,416 HR+/HER2-negative early breast tumors. A non-luminal disease score (NOLUS) from 0 to 100, based on percentage of estr…

0301 basic medicineCancer Researchmedicine.medical_specialtyintrinsic subtype:Neoplasms::Neoplasms by Site::Breast Neoplasms [DISEASES]:Genetic Phenomena::Gene Expression Regulation::Gene Expression Regulation Neoplastic [PHENOMENA AND PROCESSES]medicine.medical_treatmentEstrogen receptor:fenómenos genéticos::regulación de la expresión génica::regulación de la expresión génica neoplásica [FENÓMENOS Y PROCESOS]:aminoácidos péptidos y proteínas::proteínas::receptores citoplásmicos y nucleares::receptores de esteroides::receptores de estrógenos [COMPUESTOS QUÍMICOS Y DROGAS]lcsh:RC254-282Gastroenterology03 medical and health sciencesbreast cancer0302 clinical medicineBreast cancerMama - CàncerInternal medicineRegulació genèticaProgesterone receptorMedicinePAM50Original Research:neoplasias::neoplasias por localización::neoplasias de la mama [ENFERMEDADES]Chemotherapynon-luminalbusiness.industry:Amino Acids Peptides and Proteins::Proteins::Receptors Cytoplasmic and Nuclear::Receptors Steroid::Receptors Estrogen [CHEMICALS AND DRUGS]lcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensmedicine.disease030104 developmental biologyEstrògens - ReceptorsOncologyHormone receptor030220 oncology & carcinogenesisCohortgene expressionBiomarker (medicine)ImmunohistochemistrybusinessFrontiers in Oncology
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Secondary structure and dynamics study of the intrinsically disordered silica-mineralizing peptide P5S3during silicic acid condensation and silica de…

2017

The silica forming repeat R5 of sil1 from Cylindrotheca fusiformis was the blueprint for the design of P5 S3 , a 50-residue peptide which can be produced in large amounts by recombinant bacterial expression. It contains 5 protein kinase A target sites and is highly cationic due to 10 lysine and 10 arginine residues. In the presence of supersaturated orthosilicic acid P5 S3 enhances silica-formation whereas it retards the dissolution of amorphous silica (SiO2 ) at globally undersaturated concentrations. The secondary structure of P5 S3 during these 2 processes was studied by circular dichroism (CD) spectroscopy, complemented by nuclear magnetic resonance (NMR) spectroscopy of the peptide in …

0301 basic medicineCircular dichroismProtein ConformationSilicic AcidPeptideMolecular Dynamics SimulationSodium Chloride010402 general chemistry01 natural sciencesBiochemistryArticle03 medical and health scienceschemistry.chemical_compoundStructural BiologyPolymer chemistryOrganic chemistrySilicic acidNuclear Magnetic Resonance BiomolecularMolecular BiologyDissolutionProtein secondary structurePolyproline helixchemistry.chemical_classificationNuclear magnetic resonance spectroscopySilicon Dioxide0104 chemical sciencesIntrinsically Disordered Proteins030104 developmental biologychemistryPolymerizationPeptidesProteins: Structure, Function, and Bioinformatics
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Providing choice and/or variety during a meal: Impact on vegetable liking and intake

2016

Food choice is defined as providing the opportunity for an individual to select the food he or she wants to consume while food variety is defined as providing an individual with foods that differ on at least one sensory characteristic. Literature shows that providing food choice or providing food variety may increase meal enjoyment and food intake. However, these two factors have been mainly investigated separately, while they may actually co-occur in real-life settings. In fact, in many out-of-home catering situations, individuals have the possibility to choose as many dishes as they desire from among different proposals for their meal. The aim of the present study was to assess the impact…

0301 basic medicineMaleFood intakerepas[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionFood choiceFood likingmealFood varietyChoice BehaviorBody Mass IndexToxicologyEatingFood intakeSurveys and QuestionnairesFood choiceVegetablesPlate clearersIntrinsic motivationchildrens likingPalatabilityMealsintrinsic motivationGeneral Psychologychoice2. Zero hungerMealNutrition and Dieteticsdigestive oral and skin physiologyfood-intakevarietyrandomized controlled-trialFemalePsychologyeffective strategyAdultpleasureplaisirnormal-weight03 medical and health sciencesFood PreferencesYoung AdultacceptabilityLunch timeHumansEating behaviorconsumption030109 nutrition & dieteticsfoodBody WeightplateVariety (linguistics)Diet[SDV.AEN] Life Sciences [q-bio]/Food and Nutritionpalatability[SDV.AEN]Life Sciences [q-bio]/Food and NutritionOlive oil
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Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRET

2018

Abstract Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex. They are highly dynamic under physiological conditions and studying their interaction with nuclear transport receptors (NTRs) is key to understanding the molecular mechanism of nucleocytoplasmic transport. Distinct conformational features of FG-Nups interacting with diverse NTRs can be detected by multiparameter single-molecule fluorescence energy transfer (smFRET), which is a powerful technique for studying the dynamics and interactions of biomolecules in solution. Here we provide a detailed protocol utilizing smFRET to reveal dif…

0301 basic medicineModels MolecularGlycosylationProtein ConformationPhenylalanineGlycineIntrinsically disordered proteinsArticle03 medical and health scienceschemistry.chemical_compoundFluorescence Resonance Energy TransferAnimalsHumansNuclear porechemistry.chemical_classificationBiomoleculeSingle-molecule FRETEquipment DesignIntrinsically Disordered ProteinsNuclear Pore Complex Proteins030104 developmental biologychemistryNucleocytoplasmic TransportBiophysicsNucleoporinNuclear transportProtein BindingIntrinsically Disordered Proteins
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Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors

2018

Summary Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex (NPC). Previous studies showed that nuclear transport receptors (NTRs) were found to interact with FG-Nups by forming an “archetypal-fuzzy” complex through the rapid formation and breakage of interactions with many individual FG motifs. Here, we use single-molecule studies combined with atomistic simulations to show that, in sharp contrast, FG-Nup214 undergoes a coupled reconfiguration-binding mechanism when interacting with the export receptor CRM1. Association and dissociation rate constants are more than an order of magnitude lowe…

0301 basic medicineModels MolecularGlycosylationglycosylationProtein ConformationPhenylalanineGlycineSequence (biology)Intrinsically disordered proteinsnuclear transport receptorssingle-molecule FRETGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicineEscherichia coliFluorescence Resonance Energy TransferHumansNuclear poreReceptorlcsh:QH301-705.5Single-molecule FRETmolecular dynamics simulationsbinding mechanismintrinsically disordered proteinFG-Nup3. Good healthNuclear Pore Complex Proteins030104 developmental biologychemistrylcsh:Biology (General)BiophysicsNuclear PoreNucleoporinNuclear transport030217 neurology & neurosurgeryProtein BindingCell Reports
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Evolving Notch polyQ tracts reveal possible solenoid interference elements.

2016

ABSTRACTPolyglutamine (polyQ) tracts in regulatory proteins are extremely polymorphic. As functional elements under selection for length, triplet repeats are prone to DNA replication slippage and indel mutations. Many polyQ tracts are also embedded within intrinsically disordered domains, which are less constrained, fast evolving, and difficult to characterize. To identify structural principles underlying polyQ tracts in disordered regulatory domains, here I analyze deep evolution of metazoan Notch polyQ tracts, which can generate alleles causing developmental and neurogenic defects. I show that Notch features polyQ tract turnover that is restricted to a discrete number of conserved “polyQ …

0301 basic medicineModels MolecularProtein Structure ComparisonProtein FoldingHuntingtinlcsh:MedicineCarboxamideAnkyrin Repeat DomainBiochemistryProtein Structure SecondaryDatabase and Informatics Methods0302 clinical medicineProtein structureMacromolecular Structure AnalysisDrosophila Proteinslcsh:ScienceGeneticsHuntingtin ProteinMultidisciplinaryReceptors NotchChemistryDrosophila MelanogasterAnimal ModelsCell biologyInsectsExperimental Organism SystemsProtein foldingDrosophilaSequence AnalysisResearch ArticleMultiple Alignment CalculationProtein StructureArthropodamedicine.drug_classBioinformaticsProtein domainSequence alignmentBiologyIntrinsically disordered proteinsResearch and Analysis MethodsTerminal loopEvolution Molecular03 medical and health sciencesModel OrganismsProtein DomainsSequence Motif AnalysisComputational TechniquesmedicineHuntingtin ProteinAnimalsIndelMolecular BiologyRepetitive Sequences Nucleic AcidModels GeneticSequence Homology Amino Acidlcsh:RDNA replicationOrganismsBiology and Life SciencesProteinsHydrogen BondingInvertebratesSplit-Decomposition MethodIntrinsically Disordered Proteins030104 developmental biologyAnkyrin repeatlcsh:QPeptidesSequence Alignment030217 neurology & neurosurgeryPLoS ONE
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Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”

2018

Editors at Science requested our input on the above discussion (comment by Best et al . and response by Riback et al .) because both sets of authors use our data from Fuertes et al . (2017) to support their arguments. The topic of discussion pertains to the discrepant inferences drawn from SAXS versus FRET measurements regarding the dimensions of intrinsically disordered proteins (IDPs) in aqueous solvents. Using SAXS measurements on labeled and unlabeled proteins, we ruled out the labels used for FRET measurements as the cause of discrepant inferences between the two methods. Instead, we propose that FRET and SAXS provide complementary readouts because of a decoupling of size and shape fl…

0301 basic medicinePhysicsMultidisciplinarySmall-angle X-ray scatteringScattering010402 general chemistryIntrinsically disordered proteins01 natural sciences0104 chemical sciences03 medical and health sciences030104 developmental biologyFörster resonance energy transferStatistical physicsDecoupling (electronics)Science
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Rapid generation of hydrogen peroxide contributes to the complex cell death induction by the angucycline antibiotic landomycin E

2017

Landomycin E (LE) is an angucycline antibiotic produced by Streptomyces globisporus. Previously, we have shown a broad anticancer activity of LE which is, in contrast to the structurally related and clinically used anthracycline doxorubicin (Dx), only mildly affected by multidrug resistance-mediated drug efflux. In the present study, cellular and molecular mechanisms underlying the anticancer activity of landomycin E towards Jurkat T-cell leukemia cells were dissected focusing on the involvement of radical oxygen species (ROS). LE-induced apoptosis distinctly differed in several aspects from the one induced by Dx. Rapid generation of both extracellular and cell-derived hydrogen peroxide alr…

0301 basic medicinePoly (ADP-Ribose) Polymerase-1ApoptosisBiochemistryLandomycin EJurkat Cellschemistry.chemical_compoundSuperoxidesCaspaseCaspase-9chemistry.chemical_classificationCaspase 7Antibiotics AntineoplasticLeukemiabiologySuperoxideStreptomycesCaspase 9Respiratory burstMitochondriaBiochemistrySettore CHIM/03 - Chimica Generale E InorganicaReactive oxygen specieHumanJurkat CellCaspase 7Article03 medical and health sciencesPhysiology (medical)HumansReactive oxygen speciesAminoglycosideIntrinsic apoptosisApoptosiOxidative StreAnticancer drugHydrogen PeroxideMolecular biologyN-acetylcysteineSuperoxide radicalAcetylcysteineMulti-drug resistanceOxidative StressAminoglycosides030104 developmental biologychemistryStreptomyceApoptosisDoxorubicinbiology.proteinReactive Oxygen Species
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Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions.

2016

Lunasin is a 43 amino acid peptide with anti-cancer, antioxidant, anti-inflammatory and cholesterol-lowering properties. Although the mechanism of action of lunasin has been characterized to some extent, its exact three-dimensional structure as well as the function of the N-terminal sequence remains unknown. We established a novel method for the production of recombinant lunasin that allows efficient isotope labeling for NMR studies. Initial studies showed that lunasin can exist in a reduced or oxidized state with an intramolecular disulfide bond depending on solution conditions. The structure of both forms of the peptide at pH 3.5 and 6.5 was characterized by CD spectroscopy and multidimen…

0301 basic medicineProtein Conformation alpha-HelicalCircular dichroismPhysiologyBeta sheetPeptideIntrinsically disordered proteinsBiochemistryLunasinAntioxidantsHistones03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineEndocrinologyNeoplasmsAnticarcinogenic AgentsHumansAmino Acid SequenceDisulfidesProtein secondary structureNuclear Magnetic Resonance BiomolecularPlant Proteinschemistry.chemical_classificationChemistryAcetylationNuclear magnetic resonance spectroscopyIntrinsically Disordered Proteins030104 developmental biologyBiochemistry030220 oncology & carcinogenesisBiophysicsSoybean ProteinsPeptidesOxidation-ReductionFunction (biology)Peptides
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Rev-Erb modulates retinal visual processing and behavioral responses to light

2016

International audience; The circadian clock is thought to adjust retinal sensitivity to ambient light levels, yet the involvement of specific clock genes is poorly understood. We explored the potential role of the nuclear receptor subfamily 1, group D, member 1 (REV-ERB; or NR1D1) in this respect. In light-evoked behavioral tests, compared with wild-type littermates, Rev-Erb(-/-) mice showed enhanced negative masking at low light levels (0.1 lx). Rev-Erb(-/-) mouse retinas displayed significantly higher numbers of intrinsically photosensitive retinal ganglion cells (ipRGCs; 62% more compared with wild-type) and more intense melanopsin immunostaining of individual ipRGCs. In agreement with a…

0301 basic medicineRetinal Ganglion CellsLight[SDV]Life Sciences [q-bio]Circadian clockelectroretinogramBiochemistrychemistry.chemical_compound0302 clinical medicinecircadian clockskin and connective tissue diseasesComputingMilieux_MISCELLANEOUSMice KnockoutipRGCsBehavior AnimalphotoreceptorsorganizationCircadian Rhythmmedicine.anatomical_structurerodtranscriptionBiotechnologyPhotopic visionMelanopsinnegative maskingrat retinaBiologyRetina03 medical and health sciences[ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathologyCircadian ClocksGeneticsmedicineAnimalsCircadian rhythmScotopic visionmelanopsin-knockout miceMolecular BiologymouseRetinaIntrinsically photosensitive retinal ganglion cellsRod OpsinsRetinalganglion-cellsbody regionsmammalian retina030104 developmental biologychemistryNuclear Receptor Subfamily 1 Group D Member 1sense organsNeuroscience030217 neurology & neurosurgeryPhotic Stimulation[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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