Search results for "Folding"

showing 10 items of 330 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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Acetylcholine-binding protein in the hemolymph of the planorbid snail Biomphalaria glabrata is a pentagonal dodecahedron (60 subunits).

2012

Nicotinic acetylcholine receptors (nAChR) play important neurophysiological roles and are of considerable medical relevance. They have been studied extensively, greatly facilitated by the gastropod acetylcholine-binding proteins (AChBP) which represent soluble structural and functional homologues of the ligand-binding domain of nAChR. All these proteins are ring-like pentamers. Here we report that AChBP exists in the hemolymph of the planorbid snail Biomphalaria glabrata (vector of the schistosomiasis parasite) as a regular pentagonal dodecahedron, 22 nm in diameter (12 pentamers, 60 active sites). We sequenced and recombinantly expressed two ∼25 kDa polypeptides (BgAChBP1 and BgAChBP2) wit…

Macromolecular AssembliesProtein StructureProtein FoldingScienceBiophysicsBiochemistryProtein ChemistryHomology (biology)Ion ChannelsProtein Structure Secondarylaw.inventionDodecahedronAcetylcholine bindinglawHemolymphHemolymphMacromolecular Structure AnalysisBiomphalaria glabrataAnimal PhysiologyAnimalsBiomacromolecule-Ligand InteractionsBiologyAcetylcholine receptorMultidisciplinaryHemoproteinsbiologyBiomphalariaQRActive siteProteinsComputational BiologyAnatomybiology.organism_classificationRecombinant ProteinsAcetylcholineProtein Structure TertiaryBiochemistryAcetylcholine Receptorsbiology.proteinRecombinant DNAMedicineCarrier ProteinsZoologyResearch ArticlePLoS ONE
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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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X-linked primary ciliary dyskinesia due to mutations in the cytoplasmic axonemal dynein assembly factor PIH1D3

2017

By moving essential body fluids and molecules, motile cilia and flagella govern respiratory mucociliary clearance, laterality determination and the transport of gametes and cerebrospinal fluid. Primary ciliary dyskinesia (PCD) is an autosomal recessive disorder frequently caused by non-assembly of dynein arm motors into cilia and flagella axonemes. Before their import into cilia and flagella, multi-subunit axonemal dynein arms are thought to be stabilized and pre-assembled in the cytoplasm through a DNAAF2–DNAAF4–HSP90 complex akin to the HSP90 co-chaperone R2TP complex. Here, we demonstrate that large genomic deletions as well as point mutations involving PIH1D3 are responsible for an X-li…

MaleCytoplasmProtein FoldingAxoneme[SDV]Life Sciences [q-bio][SDV.GEN] Life Sciences [q-bio]/Genetics[SDV.MHEP.PSR]Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tractouterGenes X-LinkedChilddefectsPhylogenyZebrafisharmsSequence DeletionvariantsIntracellular Signaling Peptides and ProteinsGenetic Diseases X-LinkedPedigreeMultidisciplinary Sciences[SDV] Life Sciences [q-bio]motilityChild PreschoolMicrotubule ProteinsSperm MotilityScience & Technology - Other TopicsFemaleAdultAdolescentinnerUK10K Rare Groupr2tp complexof-function mutationsArticleMicroscopy Electron TransmissionMD MultidisciplinaryExome SequencingAnimalsHumansPoint MutationCiliaHSP90 Heat-Shock Proteins[SDV.GEN]Life Sciences [q-bio]/GeneticsScience & TechnologyKartagener SyndromeInfant NewbornAxonemal DyneinsDisease Models AnimalHEK293 Cells[SDV.MHEP.PSR] Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tractidentifies mutationsproteinApoptosis Regulatory ProteinsSequence AlignmentMolecular ChaperonesNature Communications
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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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Gastric α-synuclein immunoreactive inclusions in Meissner's and Auerbach's plexuses in cases staged for Parkinson's disease-related brain pathology

2005

The progressive degenerative process associated with sporadic Parkinson's disease (sPD) is characterized by formation of alpha-synuclein-containing inclusion bodies in a few types of projection neurons in both the enteric and central nervous systems (ENS and CNS). In the brain, the process apparently begins in the brainstem (dorsal motor nucleus of the vagal nerve) and advances through susceptible regions of the basal mid-and forebrain until it reaches the cerebral cortex. Anatomically, all of the vulnerable brain regions are closely interconnected. Whether the pathological process begins in the brain or elsewhere in the nervous system, however, is still unknown. We therefore used immunocyt…

MaleNervous systemProtein FoldingPathologymedicine.medical_specialtyPrionsModels NeurologicalCentral nervous systemMyenteric PlexusBiologyAxonal TransportCentral nervous system diseaseNeural PathwaysDisease Transmission InfectiousmedicineHumansAgedAged 80 and overInclusion BodiesNeuronsGeneral NeuroscienceBrainParkinson DiseaseVagus NerveSubmucous PlexusMiddle Agedmedicine.diseasemedicine.anatomical_structureDorsal motor nucleusGastric MucosaCerebral cortexForebrainalpha-SynucleinFemaleEnteric nervous systemBrainstemNerve NetNeuroscienceNeuroscience Letters
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A New Prosthetic Implant for Inguinal Hernia Repair: Its Features in a Porcine Experimental Model

2011

Even after more than 100 years of inguinal hernia repair, the rate of complications and recurrence remains unacceptably high. In the last decades, few effective advances in surgical technique and materials have been made. The authors see them as minor adjustments in the shape and materials of the prosthetic implants. Still, the underlying genesis of inguinal hernia remains undefined. Based upon this, it seems the surgical repair of inguinal protrusions cannot be based upon the pathogenesis because the etiology to date has not been addressed. Most hernia repairs are performed with some degree of point fixation (sutures/tacks) to stop the mesh from migrating and creating high recurrence rates…

MaleSettore MED/18 - Chirurgia GeneraleTissue ScaffoldsHernia Inguinal Biocompatible materials Prostheses and implants Incorporation Guided tissue regeneration Tissue scaffoldingGuided Tissue RegenerationSwineAnimalsits features in a porcine experimental model [A new prosthetic implant for inguinal hernia repair]Hernia InguinalProstheses and ImplantsA new prosthetic implant for inguinal hernia repair: its features in a porcine experimental modelPolypropylenes
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Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy.

2008

Hsp60 in eukaryotes is considered typically a mitochondrial chaperone (also called Cpn60) but in the last few years it has become clear that it also occurs in the cytosol, the cell surface, the extracellular space, and in the peripheral blood. Studies with prokaryotic models have shown that Hsp60 plays a role in assisting nascent polypeptides to reach a native conformation, and that it interacts with Hsp10 (which also resides in the mitochondria and is also named Cpn10). In addition to its role in polypeptide folding in association with Hsp10, other functions and interacting molecules have been identified for Hsp60 in the last several years. Some of these newly identified functions are asso…

MalechaperoninCancer ResearchProtein Foldinganimal structuresChaperoninsCell SurvivalCelldifferential diagnosiGene ExpressionAntineoplastic AgentsApoptosisBiologyMitochondrionmedicine.disease_causeBioinformaticsDiagnosis Differentialtumor-cell survivalCell Line TumorNeoplasmstumor diagnosiExtracellularmedicineHumansHsp60 (Cpn60)chaperonotherapyPharmacologyClinical Oncologymonitoring response to treatmentanti-tumor immune responsefungiHsp60 (Cpn60); tumor-cell survival; apoptosis; tumor diagnosis; differential diagnosis; assessing prognosis; monitoring response to treatment; chaperonotherapy; anti-tumor immune response; chaperonin; protein foldingassessing prognosiChaperonin 60PrognosisapoptosiCell biologyCytosolmedicine.anatomical_structureOncologyChaperone (protein)biology.proteinMolecular MedicineHSP60FemaleCarcinogenesisSignal TransductionCancer biologytherapy
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Binge drinking upregulates accumbens mGluR5-Homer2-PI3K signaling: functional implications for alcoholism.

2009

The glutamate receptor-associated protein Homer2 regulates alcohol-induced neuroplasticity within the nucleus accumbens (NAC), but the precise intracellular signaling cascades involved are not known. This study examined the role for NAC metabotropic glutamate receptor (mGluR)-Homer2-phosphatidylinositol 3-kinase (PI3K) signaling in regulating excessive alcohol consumption within the context of the scheduled high alcohol consumption (SHAC) model of binge alcohol drinking. Repeated bouts of binge drinking ( approximately 1.5 g/kg per 30 min) elevated NAC Homer2a/b expression and increased PI3K activity in this region. Virus-mediated knockdown of NAC Homer2b expression attenuated alcohol intak…

Malemedicine.medical_specialtyReceptor Metabotropic Glutamate 5Binge drinkingContext (language use)Mice TransgenicNucleus accumbensReceptors Metabotropic GlutamateNucleus AccumbensArticleWortmanninchemistry.chemical_compoundMicePhosphatidylinositol 3-KinasesHomer Scaffolding ProteinsInternal medicinemental disordersmedicineAnimalsEthanolEthanolMetabotropic glutamate receptor 5business.industryGeneral NeuroscienceAntagonistUp-RegulationMice Inbred C57BLAlcoholismEndocrinologyPhenotypechemistryMetabotropic glutamate receptorbusinessCarrier ProteinsNeuroscienceSignal TransductionThe Journal of neuroscience : the official journal of the Society for Neuroscience
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