Search results for "BM"

showing 10 items of 1459 documents

Highlighting curcumin-induced crosstalk between autophagy and apoptosis: A biochemical approach coupling impedancemetry, imaging, and flow cytometry

2019

Curcumin, a major active component of turmeric (Curcuma longa, L.), is known to have various effects on both healthy and cancerous tissues. In vitro studies suggest that curcumin inhibits cancer cell growth by activating apoptosis, but the mechanism underlying the anticancer effects of curcumin is still unclear. Since there is a consensus about endoplasmic reticulum (ER) stress being involved in the cytotoxicity of many natural compounds, we investigated by Amnis ® Imaging flow cytome-try the mechanistic aspects of curcumin's destabilization of the ER, but also the status of the lysosomal compartment involved in curcumin-associated apoptosis. Curcumin induces ER stress thereby causing an un…

Programmed cell death[SDV]Life Sciences [q-bio][SDV.TOX.TVM]Life Sciences [q-bio]/Toxicology/Vegetal toxicology and mycotoxicology[SDV.CAN]Life Sciences [q-bio]/Cancer[SDV.BC]Life Sciences [q-bio]/Cellular Biology[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Mitochondrion03 medical and health scienceschemistry.chemical_compound0302 clinical medicine[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology030304 developmental biology0303 health sciencesChemistryAutophagy[SDV.BBM.MN]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular Networks [q-bio.MN]Cell cycle3. Good healthCell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsApoptosis030220 oncology & carcinogenesis[SDV.TOX]Life Sciences [q-bio]/ToxicologyCancer cellUnfolded protein responseCurcumin
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TRAIL-R4 promotes tumor growth and resistance to apoptosis in cervical carcinoma HeLa cells through AKT.

2011

International audience; BACKGROUND: TRAIL/Apo2L is a pro-apoptotic ligand of the TNF family that engages the apoptotic machinery through two pro-apoptotic receptors, TRAIL-R1 and TRAIL-R2. This cell death program is tightly controlled by two antagonistic receptors, TRAIL-R3 and TRAIL-R4, both devoid of a functional death domain, an intracellular region of the receptor, required for the recruitment and the activation of initiator caspases. Upon TRAIL-binding, TRAIL-R4 forms a heteromeric complex with the agonistic receptor TRAIL-R2 leading to reduced caspase-8 activation and apoptosis. METHODOLOGY/PRINCIPAL FINDINGS: We provide evidence that TRAIL-R4 can also exhibit, in a ligand independent…

Proliferation indexlcsh:MedicineTNF-Related Apoptosis-Inducing LigandHeLaMicePhosphatidylinositol 3-Kinases0302 clinical medicineMolecular Cell BiologyBasic Cancer ResearchMembrane Receptor SignalingEnzyme Inhibitorslcsh:SciencePhosphoinositide-3 Kinase Inhibitors0303 health sciencesMultidisciplinaryCell Deathbiologyapoptosis3. Good healthCell biologyOncology030220 oncology & carcinogenesisMedicineFemaleSignal transductionResearch ArticleSignal TransductionProgrammed cell deathMorpholinesproliferationBlotting WesternMice Nude03 medical and health sciencesTRAIL-R4[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimalsHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyBiology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein kinase BPI3K/AKT/mTOR pathwayCell Proliferation030304 developmental biologyCell growthAktCell Membranelcsh:RPTEN PhosphohydrolaseNeoplasms Experimentalbiology.organism_classificationTumor Necrosis Factor Decoy ReceptorsChromonesApoptosislcsh:QProto-Oncogene Proteins c-aktHeLa Cells
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Astringency and the interactions between a human salivary proline-rich protein and tannins

2015

International audience

Proline-rich protein[CHIM.ANAL] Chemical Sciences/Analytical chemistrySRMS2Mass spectrometryNoncovalent complexesNoncovalent interactions[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM][SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]synchrotron radiation[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsVUVSAXSSalivary Proline-Rich Proteins[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics[SDV.AEN] Life Sciences [q-bio]/Food and Nutrition[CHIM.ANAL]Chemical Sciences/Analytical chemistry[CHIM] Chemical Sciences[CHIM]Chemical Sciences[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM][SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM][SDV.AEN]Life Sciences [q-bio]/Food and NutritionComputingMilieux_MISCELLANEOUS
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High risk Gleason patterns at prostate biopsy and body mass index.

2014

Prostate cancer BMI Gleason scoreSettore MED/24 - Urologia
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Extracellular loop 2 of G protein-coupled olfactory receptors is critical for odorant recognition

2021

International audience; G protein-coupled olfactory receptors (ORs) enable us to detect innumerous odorants. They are also ectopically expressed in non-olfactory tissues and emerging as attractive drug targets. ORs can be promiscuous or highly specific, which is part of a larger mechanism for odor discrimination. Here, we demonstrate that the OR extracellular loop 2 (ECL2) plays critical roles in OR promiscuity and specificity. Using site-directed mutagenesis and molecular modeling, we constructed 3D OR models in which ECL2 forms a lid over the orthosteric pocket. We demonstrate using molecular dynamics simulations that ECL2 controls the shape and the volume of the odorant-binding pocket, m…

Protein Conformation alpha-HelicalOdorant bindingG protein[SDV]Life Sciences [q-bio]Mutagenesis (molecular biology technique)Molecular Dynamics SimulationLigandsReceptors OdorantBiochemistryMice[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyExtracellularOlfactory receptorAnimalsHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyReceptorMolecular BiologyG protein-coupled receptorVirtual screeningmolecular modelingChemistryCell Biologyvirtual screeningLigand (biochemistry)Cell biology[SDV] Life Sciences [q-bio]Smell[SDV.AEN] Life Sciences [q-bio]/Food and NutritionOdorantsMutagenesis Site-Directedsite-directed mutagenesis[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
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Disentangling the complexity of low complexity proteins

2020

Abstract There are multiple definitions for low complexity regions (LCRs) in protein sequences, with all of them broadly considering LCRs as regions with fewer amino acid types compared to an average composition. Following this view, LCRs can also be defined as regions showing composition bias. In this critical review, we focus on the definition of sequence complexity of LCRs and their connection with structure. We present statistics and methodological approaches that measure low complexity (LC) and related sequence properties. Composition bias is often associated with LC and disorder, but repeats, while compositionally biased, might also induce ordered structures. We illustrate this dichot…

Protein ConformationComputer scienceReview ArticleComputational biologyMeasure (mathematics)Evolution MolecularLow complexity03 medical and health sciencesProtein DomainsAmino Acid Sequencestructure[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Databases ProteinMolecular Biology030304 developmental biologyStructure (mathematical logic)0303 health sciencesSequence[SCCO.NEUR]Cognitive science/Neurosciencecomposition bias030302 biochemistry & molecular biologyProteinsdisorderlow complexity regionsStructure and function[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]AlgorithmsInformation SystemsBriefings in Bioinformatics
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Sequence Determines Degree of Knottedness in a Coarse-Grained Protein Model

2015

Knots are abundant in globular homopolymers but rare in globular proteins. To shed new light on this long-standing conundrum, we study the influence of sequence on the formation of knots in proteins under native conditions within the framework of the hydrophobic-polar (HP) lattice protein model. By employing large scale Wang-Landau simulations combined with suitable Monte Carlo trial moves we show that, even though knots are still abundant on average, sequence introduces large variability in the degree of self-entanglements. Moreover, we are able to design sequences which are either almost always or almost never knotted. Our findings serve as proof of concept that the introduction of just o…

Protein ConformationFOS: Physical sciencesGeneral Physics and AstronomyCondensed Matter - Soft Condensed Matterstomatognathic systemComputer SimulationMathematicsSequence (medicine)chemistry.chemical_classificationQuantitative Biology::BiomoleculesDegree (graph theory)Proteinsfood and beveragesBiomolecules (q-bio.BM)Knot theoryAmino acidsurgical procedures operativeModels ChemicalQuantitative Biology - BiomoleculeschemistryFOS: Biological sciencesProtein modelSoft Condensed Matter (cond-mat.soft)Biological systemHydrophobic and Hydrophilic InteractionsMonte Carlo MethodPhysical Review Letters
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The impact of high hydrostatic pressure on structure and dynamics of beta-lactoglobulin

2013

Abstract Methods Combining small-angle X-ray and neutron scattering measurements with inelastic neutron scattering experiments, we investigated the impact of high hydrostatic pressure on the structure and dynamics of β-lactoglobulin (βLG) in aqueous solution. Background βLG is a relatively small protein, which is predominantly dimeric in physiological conditions, but dissociates to monomer below about pH 3. Results High-pressure structural results show that the dimer–monomer equilibrium, as well as the protein–protein interactions, are only slightly perturbed by pressure, and βLG unfolding is observed above a threshold value of 3000 bar. In the same range of pressure, dynamical results put …

Protein ConformationHydrostatic pressureBiophysics02 engineering and technologyLactoglobulinsProtein dynamicsNeutron scatteringNeutron scattering010402 general chemistry01 natural sciencesBiochemistryInelastic neutron scatteringchemistry.chemical_compound[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein foldingMolecular BiologyHydrostatic pressureQuantitative Biology::BiomoleculesAqueous solutionSmall angle X-ray and neutron scatteringProtein dynamics021001 nanoscience & nanotechnology0104 chemical sciencesCrystallographyMonomerchemistryChemical physicsCompressibilityProtein folding0210 nano-technology
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Reconstructing the free-energy landscape of Met-enkephalin using dihedral principal component analysis and well-tempered metadynamics

2013

Well-Tempered Metadynamics (WTmetaD) is an efficient method to enhance the reconstruction of the free-energy surface of proteins. WTmetaD guarantees a faster convergence in the long time limit in comparison with the standard metadynamics. It still suffers however from the same limitation, i.e. the non trivial choice of pertinent collective variables (CVs). To circumvent this problem, we couple WTmetaD with a set of CVs generated from a dihedral Principal Component Analysis (dPCA) on the Ramachadran dihedral angles describing the backbone structure of the protein. The dPCA provides a generic method to extract relevant CVs built from internal coordinates. We illustrate the robustness of this …

Protein ConformationSurface PropertiesEnkephalin MethionineFOS: Physical sciencesGeneral Physics and AstronomyDihedral angle01 natural scienceslaw.invention03 medical and health scienceslaw0103 physical sciencesComputer SimulationCartesian coordinate systemPhysics - Biological PhysicsStatistical physicsPhysical and Theoretical ChemistryProtein secondary structureReference modelComputingMilieux_MISCELLANEOUS030304 developmental biologyMathematicsPrincipal Component AnalysisQuantitative Biology::Biomolecules0303 health sciences010304 chemical physicsMetadynamicsEnergy landscapeBiomolecules (q-bio.BM)Condensed Matter - Other Condensed Matter[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryQuantitative Biology - BiomoleculesBiological Physics (physics.bio-ph)FOS: Biological sciencesPrincipal component analysis[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistryPhysics::Accelerator PhysicsThermodynamicsEnergy MetabolismAlgorithmsOther Condensed Matter (cond-mat.other)Ramachandran plot
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CandidaDB: a genome database for Candida albicans pathogenomics.

2004

CandidaDB is accessible at http://genolist.pasteur.fr/CandidaDB.; International audience; CandidaDB is a database dedicated to the genome of the most prevalent systemic fungal pathogen of humans, Candida albicans. CandidaDB is based on an annotation of the Stanford Genome Technology Center C.albicans genome sequence data by the European Galar Fungail Consortium. CandidaDB Release 2.0 (June 2004) contains information pertaining to Assembly 19 of the genome of C.albicans strain SC5314. The current release contains 6244 annotated entries corresponding to 130 tRNA genes and 5917 protein-coding genes. For these, it provides tentative functional assignments along with numerous pre-run analyses th…

Protein familyGenomicsComputational biologyBiologyGenomeANNOTATIONFUNCTIONNAL ASSIGNEMENTFungal ProteinsUser-Computer Interface03 medical and health sciencesAnnotationPathogenomicsCandida albicansDatabases GeneticGeneticsGENOME DATABASE[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]GeneComputingMilieux_MISCELLANEOUS030304 developmental biologyWhole genome sequencingGeneticsInternet0303 health sciencesFungal protein030306 microbiologygénomeEUROPEAN CONSORTIUMGENOME SEQUENCEGenomicsArticlesGENOME DATABASE;CANDIDA DB;ANNOTATION;GENOME SEQUENCE;GENE FUNCTION;EUROPEAN CONSORTIUM;FUNCTIONNAL ASSIGNEMENTGENE FUNCTIONCANDIDA DB[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyGenome FungalNucleic Acids Research
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