Search results for "PROTEIN INTERACTION"

showing 10 items of 228 documents

Oxidation Enhances Human Serum Albumin Thermal Stability and Changes the Routes of Amyloid Fibril Formation

2014

Oxidative damages are linked to several aging-related diseases and are among the chemical pathways determining protein degradation. Specifically, interplay of oxidative stress and protein aggregation is recognized to have a link to the loss of cellular function in pathologies like Alzheimer's and Parkinson's diseases. Interaction between protein and reactive oxygen species may indeed induce small changes in protein structure and lead to the inhibition/modification of protein aggregation process, potentially determining the formation of species with different inherent toxicity. Understanding the temperate relationship between these events can be of utmost importance in unraveling the molecul…

Macromolecular AssembliesProtein Foldinglcsh:MedicineProtein aggregationBiochemistryPhysical Chemistry01 natural sciencesProtein Structure SecondaryProtein structurePathologylcsh:Sciencechemistry.chemical_classification0303 health sciencesMultidisciplinarybiologyProtein StabilityChemistryPhysicsNeurodegenerationTemperatureNeurodegenerative DiseasesHuman serum albuminChemistryNeurologyBiochemistryMedicineOxidation-ReductionMolecular PathologyResearch Articlemedicine.drugAmyloidBiophysicsSerum albuminProtein degradation010402 general chemistry03 medical and health sciencesDiagnostic MedicinemedicineHumansProtein InteractionsBiologySerum Albumin030304 developmental biologyAmyloid Fluorescence Oxidation Protein aggregation Spectoscopy Light Scattering Serum AlbuminReactive oxygen specieslcsh:RProteinsHydrogen Peroxidemedicine.diseaseProtein tertiary structure0104 chemical sciencesKineticsbiology.proteinlcsh:QProtein MultimerizationGeneral Pathology
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Decoding the Folding of Burkholderia glumae Lipase: Folding Intermediates En Route to Kinetic Stability

2012

The lipase produced by Burkholderia glumae folds spontaneously into an inactive near-native state and requires a periplasmic chaperone to reach its final active and secretion-competent fold. The B. glumae lipase-specific foldase (Lif) is classified as a member of the steric-chaperone family of which the propeptides of alpha-lytic protease and subtilisin are the best known representatives. Steric chaperones play a key role in conferring kinetic stability to proteins. However, until present there was no solid experimental evidence that Lif-dependent lipases are kinetically trapped enzymes. By combining thermal denaturation studies with proteolytic resistance experiments and the description of…

Macromolecular AssembliesProtein StructureProtein FoldingBurkholderiaProtein ConformationStereochemistryBiophysicslcsh:MedicineBiochemistryProtein Chemistrybacterial lipasemolten globuleBacterial ProteinsNative stateBurkholderia glumaeLipaseProtein Interactionslcsh:ScienceBiologyMultidisciplinarybiologylipase-specific foldasePhysicslcsh:RSubtilisinProteinsLipasebiology.organism_classificationMolten globuleEnzymesChaperone ProteinsKineticsBiochemistryChaperone (protein)Enzyme StructureProteolysisFoldasebiology.proteinlcsh:Qsteric chaperoneProtein foldingnear-native folding intermediateResearch ArticleMolecular Chaperones
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Unlocked Concanavalin A Forms Amyloid-like Fibrils from Coagulation of Long-lived "Crinkled'' Intermediates

2013

Understanding the early events during amyloid aggregation processes is crucial to single out the involved molecular mechanisms and for designing ad hoc strategies to prevent and reverse amyloidogenic disorders. Here, we show that, in conditions in which the protein is positively charged and its conformational flexibility is enhanced, Concanavalin A leads to fibril formation via a non-conventional aggregation pathway. Using a combination of light scattering, circular dichroism, small angle X-ray scattering, intrinsic (Tryptophan) and extrinsic (ANS) fluorescence and confocal and 2-photon fluorescence microscopy we characterize the aggregation process as a function of the temperature. We high…

Macromolecular AssembliesProteomicsCircular dichroismProtein StructureAmyloidProtein FoldingScienceMedical BiotechnologyBiophysics02 engineering and technologyFibrilBiochemistryProtein Chemistry03 medical and health sciencesProtein structureMedicinsk bioteknologiFluorescence microscopeNative stateConcanavalin ACoagulation (water treatment)Protein InteractionsBiology030304 developmental biology0303 health sciencesprotein aggregation amyloid concanavalin A intermediates spectroscopy advanced fluorescence microscopyMultidisciplinaryChemical PhysicsChemistryPhysicsCircular DichroismQRProteins021001 nanoscience & nanotechnologyProtein Structure TertiaryLuminescent ProteinsBiochemistryBiophysicsMedicineProtein folding0210 nano-technologyHydrophobic and Hydrophilic InteractionsFunction (biology)Research Article
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Aminopropyltransferases involved in polyamine biosynthesis localize preferentially in the nucleus of plant cells

2012

Plant aminopropyltransferases consist of a group of enzymes that transfer aminopropyl groups derived from decarboxylated S-adenosyl-methionine (dcAdoMet or dcSAM) to propylamine acceptors to produce polyamines, ubiquitous metabolites with positive charge at physiological pH. Spermidine synthase (SPDS) uses putrescine as amino acceptor to form spermidine, whereas spermine synthase (SPMS) and thermospermine synthase (TSPMS) use spermidine as acceptor to synthesize the isomers spermine and thermospermine respectively. In previous work it was shown that both SPDS1 and SPDS2 can physically interact with SPMS although no data concerning the subcellular localization was reported. Here we study the…

Macromolecular AssembliesProteomicsS-AdenosylmethioninePlant anatomyImmunohistoquímicaArabidopsislcsh:MedicineSecondary MetabolismSpermineExpressionPlant ScienceSpermidine synthaseBiochemistrychemistry.chemical_compoundBimolecular fluorescence complementationCytosolMolecular Cell BiologyPolyaminesPlant Genomicslcsh:SciencePlant Growth and DevelopmentMultidisciplinarybiologyPlant BiochemistryArabidopsis-ThalianaGenomicsImmunohistochemistryMetabolismeFunctional GenomicsBiochemistrySpermine synthasePlant proteinPlant PhysiologyMechanismResearch ArticleHistologyAcyltransferasePlant Cell BiologyActive Transport Cell NucleusSpermidine SynthaseBimolecular fluorescence complementationProtein InteractionsBiologyCell NucleusCrystal-Structurelcsh:RHistologiaBotanyProtein interactionsSubcellular localizationAnatomia vegetalExpressió gènicaMolecular WeightSpermidineMetabolismchemistryDecarboxylasebiology.proteinPutrescineBotànicalcsh:QGene expressionSpermidine synthase
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Construction of Chimeric Dual-Chain Avidin by Tandem Fusion of the Related Avidins

2011

BackgroundAvidin is a chicken egg-white protein with high affinity to vitamin H, also known as D-biotin. Many applications in life science research are based on this strong interaction. Avidin is a homotetrameric protein, which promotes its modification to symmetrical entities. Dual-chain avidin, a genetically engineered avidin form, has two circularly permuted chicken avidin monomers that are tandem-fused into one polypeptide chain. This form of avidin enables independent modification of the two domains, including the two biotin-binding pockets; however, decreased yields in protein production, compared to wt avidin, and complicated genetic manipulation of two highly similar DNA sequences i…

Macromolecular Assemblieslcsh:MedicineBiosensing TechniquesPolymerase Chain ReactionBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureBiotinMacromolecular Structure AnalysisProtein biosynthesisBiomacromolecule-Ligand InteractionsSurface plasmon resonancelcsh:Science0303 health sciencesMultidisciplinarybiologyrespiratory systemRecombinant ProteinsBiochemistryBiotinylationChromatography GelBiophysic Al SimulationsResearch ArticleProtein StructureStructural similarityRecombinant Fusion Proteins030303 biophysicsBiophysicsBiotinMolecular Dynamics SimulationBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biology03 medical and health sciencesstomatognathic systemDefense ProteinsEscherichia coliAnimalsGene familyProtein InteractionsBiology030304 developmental biologylcsh:RProteinsComputational BiologySurface Plasmon ResonanceAvidinchemistrySmall MoleculesFermentationbiology.proteinlcsh:QChickensAvidinPLoS ONE
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Mating systems and protein–protein interactions determine evolutionary rates of primate sperm proteins

2013

To assess the relative impact of functional constraint and post-mating sexual selection on sequence evolution of reproductive proteins, we examined 169 primate sperm proteins. In order to recognize potential genome-wide trends, we additionally analysed a sample of altogether 318 non-reproductive (brain and postsynaptic) proteins. Based on cDNAs of eight primate species (Anthropoidea), we observed that pre-mating sperm proteins engaged in sperm composition and assembly show significantly lower incidence of site-specific positive selection and overall lower non-synonymous to synonymous substitution rates ( d N / d S ) across sites as compared with post-mating sperm proteins involved in capac…

Male1001DNA ComplementaryAcrosome reactionBiologysperm competitionGeneral Biochemistry Genetics and Molecular BiologyProtein–protein interactionEvolution MolecularSexual Behavior Animalbrain proteinsCapacitationTestisAnimalsmating systemsexual selectionProtein Interaction Domains and MotifsSperm competitionResearch Articlesreproductive and urinary physiologyGeneral Environmental ScienceGeneticsGeneral Immunology and MicrobiologyHyperactivation70HaplorhiniSequence Analysis DNAGeneral MedicineMating Preference Animal129Mating systemSpermatozoaSpermfunctional constraintSexual selectionbehavior and behavior mechanismssperm proteinsGeneral Agricultural and Biological SciencesProceedings of the Royal Society B: Biological Sciences
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De novo loss-of-function KCNMA1 variants are associated with a new multiple malformation syndrome and a broad spectrum of developmental and neurologi…

2019

Abstract KCNMA1 encodes the large-conductance Ca2+- and voltage-activated K+ (BK) potassium channel α-subunit, and pathogenic gain-of-function variants in this gene have been associated with a dominant form of generalized epilepsy and paroxysmal dyskinesia. Here, we genetically and functionally characterize eight novel loss-of-function (LoF) variants of KCNMA1. Genome or exome sequencing and the participation in the international Matchmaker Exchange effort allowed for the identification of novel KCNMA1 variants. Patch clamping was used to assess functionality of mutant BK channels. The KCNMA1 variants p.(Ser351Tyr), p.(Gly356Arg), p.(Gly375Arg), p.(Asn449fs) and p.(Ile663Val) abolished the …

MaleAtaxiaGenotypeDevelopmental DisabilitiesMutation MissenseBiology03 medical and health sciences0302 clinical medicineNeurodevelopmental disorderProtein DomainsLoss of Function MutationGeneticsmedicineHumansMissense mutationAbnormalities MultipleGenetic Predisposition to DiseaseProtein Interaction Domains and MotifsAlleleLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMolecular BiologyAllelesGenetic Association StudiesGenetics (clinical)Loss functionExome sequencing030304 developmental biologyGenetics0303 health sciencesInfant NewbornGeneral MedicineParoxysmal dyskinesiamedicine.diseaseElectrophysiological PhenomenaPedigreePhenotypeAmino Acid SubstitutionSpeech delayFemaleGeneral Articlemedicine.symptom030217 neurology & neurosurgeryHuman Molecular Genetics
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Synaptosomes: new vesicles for neuronal mitochondrial transplantation

2021

Abstract Background Mitochondrial dysfunction is a critical factor in the onset and progression of neurodegenerative diseases. Recently, mitochondrial transplantation has been advised as an innovative and attractive strategy to transfer and replace damaged mitochondria. Here we propose, for the first time, to use rat brain extracted synaptosomes, a subcellular fraction of isolated synaptic terminal that contains mitochondria, as mitochondrial delivery systems. Results Synaptosome preparation was validated by the presence of Synaptophysin and PSD95. Synaptosomes were characterized in terms of dimension, zeta potential, polydispersity index and number of particles/ml. Nile Red or CTX-FITCH la…

MaleFIS1Mitochondrial DNAlcsh:Medical technologylcsh:BiotechnologyBiomedical EngineeringPharmaceutical ScienceMedicine (miscellaneous)BioengineeringMitochondrionDNA MitochondrialApplied Microbiology and BiotechnologyMembrane Potentials03 medical and health sciencesDrug Delivery Systems0302 clinical medicinelcsh:TP248.13-248.65medicineAnimalsHomeostasisProtein Interaction Domains and MotifsNeurodegenerationDelivery system030304 developmental biologyMitochondrial transplantationSynaptosome0303 health sciencesbiologyChemistryResearchCytochrome cNeurodegenerationSynaptosomes Mitochondria Neurodegeneration Delivery system Mitochondrial transplantationCytochromes cmedicine.diseaseRatsCell biologyMitochondriaTransplantationlcsh:R855-855.5Cytoplasmbiology.proteinMolecular Medicine030217 neurology & neurosurgerySubcellular FractionsSynaptosomes
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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 protein quality control pathway regulated by linear ubiquitination.

2019

Neurodegenerative diseases are characterized by the accumulation of misfolded proteins in the brain. Insights into protein quality control mechanisms to prevent neuronal dysfunction and cell death are crucial in developing causal therapies. Here, we report that various disease-associated protein aggregates are modified by the linear ubiquitin chain assembly complex (LUBAC). HOIP, the catalytic component of LUBAC, is recruited to misfolded Huntingtin in a p97/VCP-dependent manner, resulting in the assembly of linear polyubiquitin. As a consequence, the interactive surface of misfolded Huntingtin species is shielded from unwanted interactions, for example with the low complexity sequence doma…

MaleHuntingtinSp1 protein humanProtein aggregationHTT protein humanDeubiquitinating enzymegenetics [Huntington Disease]Micegenetics [Sp1 Transcription Factor]0302 clinical medicineUbiquitinpathology [Brain]Valosin Containing Proteincytology [Fibroblasts]pathology [Neurons]PolyubiquitinCells CulturedMice Knockout0303 health sciencesHuntingtin ProteinGeneral NeuroscienceNF-kappa Bgenetics [Huntingtin Protein]Middle AgedCell biologymetabolism [Polyubiquitin]pathology [Huntington Disease]metabolism [Neurons]metabolism [NF-kappa B]Protein foldingFemalemetabolism [Fibroblasts]Protein BindingSignal TransductionAdultmetabolism [Valosin Containing Protein]Sp1 Transcription Factorcytology [Embryo Mammalian]genetics [Valosin Containing Protein]BiologyGeneral Biochemistry Genetics and Molecular Biologymetabolism [Sp1 Transcription Factor]03 medical and health sciencesddc:570Gene silencingAnimalsHumansmetabolism [Huntington Disease]Protein Interaction Domains and MotifsMolecular Biologymetabolism [Embryo Mammalian]030304 developmental biologyAgedSp1 transcription factorGeneral Immunology and MicrobiologyUbiquitinationProteotoxicitymetabolism [Brain]Case-Control Studiesmetabolism [Huntingtin Protein]biology.proteinProtein Processing Post-Translational030217 neurology & neurosurgerygenetics [NF-kappa B]
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