Search results for "Protein interaction mapping"

showing 10 items of 44 documents

Revisited BIA-MS combination: Entire "on-a-chip" processing leading to the proteins identification at low femtomole to sub-femtomole levels

2008

International audience; We present the results of a study in which biomolecular interaction analysis (BIA, Biacore 2000) was combined with mass spectrometry (MS) using entire "on-a-chip" procedure. Most BIA-MS studies included an elution step of the analyte prior MS analysis. Here, we report a low-cost approach combining Biacore analysis with homemade chips and MS in situ identification onto the chips without elution step. First experiments have been made with rat serum albumin to determine the sensitivity and validation of the concept has been obtained with an antibody/antigen couple. Our "on-a-chip" procedure allowed complete analysis by MS-MS of the biochip leading to protein identificat…

In situMALDI-TOFAnalyte[ SDV.BBM.BP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsBiomedical EngineeringBiophysicsAnalytical chemistrySPRBiosensing TechniquesMass spectrometry01 natural sciencesSensitivity and Specificity03 medical and health sciencesProtein Interaction MappingElectrochemistryNanotechnologyBIA-MSBiochipChromatography High Pressure Liquid030304 developmental biology0303 health sciencesChromatographyprotein complexesElutionChemistryMicrochemistry010401 analytical chemistryMs analysisReproducibility of ResultsGeneral MedicineEquipment DesignMicrofluidic Analytical Techniques0104 chemical sciencesEquipment Failure Analysis[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMatrix-assisted laser desorption/ionizationSAMSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationBiotechnology
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MMGBSA As a Tool To Understand the Binding Affinities of Filamin–Peptide Interactions

2013

Filamins (FLN) are large dimeric proteins that cross-link actin and work as important scaffolds in human cells. FLNs consist of an N-terminal actin-binding domain followed by 24 immunoglobulin-like domains (FLN1-24). FLN domains are divided into four subgroups based on their amino acid sequences. One of these subgroups, including domains 4, 9, 12, 17, 19, 21, and 23, shares a similar ligand-binding site between the β strands C and D. Several proteins, such as integrins β2 and β7, glycoprotein Ibα (GPIbα), and migfilin, have been shown to bind to this site. Here, we computationally estimated the binding free energies of filamin A (FLNa) subunits with bound peptides using the molecular mechan…

Integrin beta ChainsFilaminsGeneral Chemical EngineeringIntegrinPeptidePlasma protein bindingMolecular Dynamics SimulationLibrary and Information SciencesBiologyLigandsFilaminta3111Protein Structure SecondaryProtein structureProtein Interaction MappingHumansFLNAProtein Interaction Domains and MotifsBinding siteta116chemistry.chemical_classificationBinding Sitesta1182General ChemistryComputer Science ApplicationsAmino acidCytoskeletal ProteinsCrystallographyPlatelet Glycoprotein GPIb-IX ComplexchemistryCD18 AntigensBiophysicsbiology.proteinThermodynamicsPeptidesCell Adhesion MoleculesAlgorithmsProtein BindingJournal of Chemical Information and Modeling
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Interactions of the hormones leptin, ghrelin, adiponectin, resistin, and PYY3-36 with the reproductive system.

2006

Objective To summarize the effects of novel hormones (leptin, ghrelin, adiponectin, resistin, and PYY3-36) secreted from adipose tissue and the gastrointestinal tract that have been discovered to exert different effects on several reproductive functions, such as the hypothalamic–pituitary–gonadal axis, embryo development, implantation physiology, and clinically relevant conditions. Design A MEDLINE computer search was performed to identify relevant articles. Result(s) Leptin and ghrelin exert important roles on body weight regulation, eating behavior, and reproduction, acting on the central nervous system and target reproductive organs. As a marker of adequate nutritional stores, these horm…

LeptinMalemedicine.medical_specialtyMEDLINEPeptide HormonesAdipose tissueHypothalamic–pituitary–gonadal axisBiologyGenitalia MaleInternal medicineProtein Interaction MappingmedicineAnimalsHumansPeptide YYResistinReproductive systemGonadal Steroid HormonesReproductive functionEvidence-Based MedicineAdiponectinLeptinReproductiondigestive oral and skin physiologyObstetrics and GynecologyGenitalia FemaleGhrelinPeptide FragmentsGastrointestinal TractEndocrinologyReproductive MedicineAdipose TissueGhrelinFemaleAdiponectinhormones hormone substitutes and hormone antagonistsHormoneSignal TransductionFertility and sterility
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Effects of different kinds of essentiality on sequence evolution of human testis proteins

2016

We asked if essentiality for either fertility or viability differentially affects sequence evolution of human testis proteins. Based on murine knockout data, we classified a set of 965 proteins expressed in human seminiferous tubules into three categories: proteins essential for prepubertal survival (“lethality proteins”), associated with male sub- or infertility (“male sub-/infertility proteins”), and nonessential proteins. In our testis protein dataset, lethality genes evolved significantly slower than nonessential and male sub-/infertility genes, which is in line with other authors’ findings. Using tissue specificity, connectivity in the protein-protein interaction (PPI) network, and mul…

MaleGene Expression ProfilingComputational BiologyProteinsMolecular Sequence AnnotationSeminiferous TubulesArticle570 Life sciencesEvolution MolecularMiceOrgan SpecificityProtein Interaction MappingTestisAnimalsHumansGene Regulatory NetworksProtein Interaction MapsSpermatogenesisTranscriptomeInfertility Male570 BiowissenschaftenScientific Reports
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A novel bio-orthogonal cross-linker for improved protein/protein interaction analysis

2015

International audience; The variety of protein cross-linkers developed in recent years illustrates the current requirement for efficient reagents optimized for mass spectrometry (MS) analysis. To date, the most widely used strategy relies on commercial cross-linkers that bear an isotopically labeled tag and N-hydroxysuccinimid-ester (NHS-ester) moieties. Moreover, an enrichment step using liquid chromatography is usually performed after enzymatic digestion of the cross-linked proteins. Unfortunately, this approach suffers from several limitations. First, it requires large amounts of proteins. Second, NHS-ester cross-linkers are poorly efficient because of their fast hydrolysis in water. Fin…

Models MolecularAzidesMolecular Sequence DataPeptide[CHIM.THER]Chemical Sciences/Medicinal ChemistryMass spectrometry01 natural sciencesMass SpectrometryAnalytical ChemistryProtein–protein interaction03 medical and health sciencesHydrolysis[CHIM.ANAL]Chemical Sciences/Analytical chemistryProtein Interaction MappingHumansOrganic chemistryAmino Acid SequenceProtein Interaction MapsCross linker030304 developmental biologychemistry.chemical_classification0303 health sciencesRigid coreEnzymatic digestionChemistry[CHIM.ORGA]Chemical Sciences/Organic chemistry010401 analytical chemistryHSC70 Heat-Shock ProteinsParkinson Disease[CHIM.CATA]Chemical Sciences/CatalysisCombinatorial chemistry0104 chemical sciences[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryCross-Linking ReagentsReagentalpha-SynucleinCarbamates[CHIM.CHEM]Chemical Sciences/CheminformaticsChromatography Liquid
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Plasmonic Nanosensors for Simultaneous Quantification of Multiple Protein–Protein Binding Affinities

2014

Most of current techniques used for the quantification of protein-protein interactions require the analysis of one pair of binding partners at a time. Herein we present a label-free, simple, fast, and cost-effective route to characterize binding affinities between multiple macromolecular partners simultaneously, using optical dark-field spectroscopy and individual protein-functionalized gold nanorods as sensing elements. Our NanoSPR method could easily become a simple and standard tool in biological, biochemical, and medical laboratories.

Models MolecularNanotubesBacteriaChemistryMechanical EngineeringProtein proteinBioengineeringNanotechnologyGeneral ChemistrySurface Plasmon ResonanceCondensed Matter PhysicsCytoskeletal ProteinsBacterial ProteinsNanosensorProtein Interaction MappingGeneral Materials ScienceNanorodGoldPlasmonProtein BindingBinding affinitiesMacromoleculeNano Letters
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Brownian dynamics simulations with hard-body interactions: Spherical particles

2012

A novel approach to account for hard-body interactions in (overdamped) Brownian dynamics simulations is proposed for systems with non-vanishing force fields. The scheme exploits the analytically known transition probability for a Brownian particle on a one-dimensional half-line. The motion of a Brownian particle is decomposed into a component that is affected by hard-body interactions and into components that are unaffected. The hard-body interactions are incorporated by replacing the affected component of motion by the evolution on a half-line. It is discussed under which circumstances this approach is justified. In particular, the algorithm is developed and formulated for systems with spa…

PhysicsNumerical analysisFOS: Physical sciencesGeneral Physics and AstronomyProteinsComputational Physics (physics.comp-ph)Condensed Matter - Soft Condensed MatterModels BiologicalDiffusionMotionProbability theoryModels ChemicalProtein Interaction MappingBrownian dynamicsSoft Condensed Matter (cond-mat.soft)Computer SimulationStatistical physicsColloidsPhysical and Theoretical ChemistryPhysics - Computational PhysicsBrownian motionAlgorithms
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Functional characterization of two melanocortin (MC) receptors in lamprey showing orthology to the MC1 and MC4 receptor subtypes

2007

Abstract Background The melanocortin (MC) receptors have a key role in regulating body weight and pigmentation. They belong to the rhodopsin family of G protein-coupled receptors (GPCRs). The purpose of this study was to identify ancestral MC receptors in agnathan, river lamprey. Results We report cloning of two MC receptors from river lamprey. The lamprey receptors, designated MCa and MCb, showed orthology to the MC1 and MC4 receptor subtypes, respectively. The molecular clock analysis suggested that lamprey MC receptor genes were not duplicated recently and diverged from each other more than 400 MYR ago. Expression and pharmacological characterization showed that the lamprey MCa receptor …

Pro-OpiomelanocortinSecond Messenger SystemsGene DuplicationProtein Interaction MappingCyclic AMPPetromyzonReceptorPhylogenyCell Line TransformedSkinGeneticsbiologyReceptors MelanocortinMelanocortin 3 receptorCell biologyOrgan SpecificityRhodopsinReceptor Melanocortin Type 4HagfishesMelanocortinReceptor Melanocortin Type 1Protein BindingResearch ArticleEvolutionRecombinant Fusion ProteinsMolecular Sequence DataBinding CompetitivePeptides CyclicEvolution Moleculargamma-MSHAdrenocorticotropic HormoneSpecies SpecificityMelanocortin receptorbeta-MSHQH359-425AnimalsHumansAmino Acid SequenceEcology Evolution Behavior and SystematicsGene LibraryG protein-coupled receptorBinding SitesSequence Homology Amino AcidFuguLampreybiology.organism_classificationPeptide FragmentsVisceraalpha-MSHbiology.proteinCosyntropinSequence Alignmenthuman activitiesBMC Evolutionary Biology
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Proteome-Wide Characterization of the RNA-Binding Protein RALY-Interactome Using the in Vivo-Biotinylation-Pulldown-Quant (iBioPQ) Approach

2013

RALY is a member of the heterogeneous nuclear ribonucleoproteins, a family of RNA-binding proteins generally involved in many processes of mRNA metabolism. No quantitative proteomic analysis of RALY-containing ribonucleoparticles (RNPs) has been performed so far, and the biological role of RALY remains elusive. Here, we present a workflow for the characterization of RALY's interaction partners, termed iBioPQ, that involves in vivo biotinylation of biotin acceptor peptide (BAP)-fused protein in the presence of the prokaryotic biotin holoenzyme synthetase of BirA so that it can be purified using streptavidin-coated magnetic beads, circumventing the need for specific antibodies and providing e…

ProteomeRecombinant Fusion ProteinsMolecular Sequence DataBiotinRNA-binding proteinBiologyHeterogeneous ribonucleoprotein particleProteomicsPoly(A)-Binding Protein IBiochemistryInteractomeELAV-Like Protein 103 medical and health scienceschemistry.chemical_compound0302 clinical medicineNuclear Matrix-Associated ProteinsBiotinProtein Interaction MappingHumansCarbon-Nitrogen LigasesAmino Acid SequenceProtein Interaction MapsPeptide sequence030304 developmental biology0303 health sciencesEscherichia coli ProteinsHeterogeneous-Nuclear Ribonucleoprotein Group CRNA-Binding ProteinsGeneral ChemistryRepressor ProteinsHEK293 CellsELAV ProteinsGene Expression RegulationBiochemistrychemistryProtein Biosynthesis030220 oncology & carcinogenesisBiotinylationProteomeBiological AssayStreptavidinHeLa CellsProtein BindingJournal of Proteome Research
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