Search results for " folding"

showing 10 items of 226 documents

Transfer Free Energies of Test Proteins Into Crowded Protein Solutions Have Simple Dependence on Crowder Concentration

2019

The effects of macromolecular crowding on the thermodynamic properties of test proteins are determined by the latter's transfer free energies from a dilute solution to a crowded solution. The transfer free energies in turn are determined by effective protein-crowder interactions. When these interactions are modeled at the all-atom level, the transfer free energies may defy simple predictions. Here we investigated the dependence of the transfer free energy (Δμ) on crowder concentration. We represented both the test protein and the crowder proteins atomistically, and used a general interaction potential consisting of hard-core repulsion, non-polar attraction, and solvent-screened electrostati…

0301 basic medicineWork (thermodynamics)macromolecular crowdingThermodynamicsBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistrytransfer free energy03 medical and health sciences0302 clinical medicinecrowder concentrationMolecular Bioscienceslcsh:QH301-705.5Molecular BiologyOriginal ResearchPhysicsComponent (thermodynamics)Electrostatics030104 developmental biologylcsh:Biology (General)Virial coefficient030220 oncology & carcinogenesisExcluded volumeexcluded-volumeVirial expansionProtein foldingMacromolecular crowdingsoft attractionFrontiers in Molecular Biosciences
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Complex Destabilization in the Mitochondrial Chaperonin Hsp60 Leads to Disease.

2020

Several neurological disorders have been linked to mutations in chaperonin genes and more specifically to the HSPD1 gene. In humans, HSPD1 encodes for the mitochondrial Heat Shock Protein 60 (mtHsp60) chaperonin, which carries out essential protein refolding reactions that help maintain mitochondrial and cellular homeostasis. It functions as a macromolecular complex that provides client proteins an environment that favors proper folding in an ATP dependent manner. It has been established that mtHsp60 plays a crucial role in the proper folding of mitochondrial proteins involved in ATP producing pathways. Recently, various single-point mutations in the mtHsp60 encoding gene have been directly…

0301 basic medicinechaperoninMini ReviewCellular homeostasisBiologyBiochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryGroELChaperonin03 medical and health sciences0302 clinical medicineHeat shock proteinprotein foldingmtHsp60Molecular BiosciencesMolecular Biologylcsh:QH301-705.5Point mutationGroELFKBP5 GeneCell biology030104 developmental biologylcsh:Biology (General)030220 oncology & carcinogenesisHSP60Protein foldingchaperonopathyFrontiers in molecular biosciences
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Structural and mechanistic insights into the interaction of the circadian transcription factor BMAL1 with the KIX domain of the CREB-binding protein

2019

JBC papers in press xx, 16604-16619 (2019). doi:10.1074/jbc.RA119.009845

0301 basic medicineendocrine systemCircadian clockTranscription factor complex610BiochemistryProtein Structure SecondaryProtein–protein interaction03 medical and health sciencesTransactivationMiceProto-Oncogene Proteins c-mybProtein DomainsX-Ray DiffractionCircadian ClocksScattering Small AngleAnimalsddc:610Amino Acid SequenceCREB-binding proteinMolecular BiologyTernary complexTranscription factorBinding Sites030102 biochemistry & molecular biologybiologyChemistryARNTL Transcription FactorsCell BiologyHistone-Lysine N-MethyltransferaseSurface Plasmon ResonanceCREB-Binding ProteinRecombinant ProteinsCell biologyProtein Structure Tertiary030104 developmental biologyStructural biologyProtein Structure and Foldingbiology.proteinMutagenesis Site-DirectedMyeloid-Lymphoid Leukemia ProteinProtein Binding
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Heat Shock Proteins in Alzheimer’s Disease: Role and Targeting

2018

Among diseases whose cure is still far from being discovered, Alzheimer’s disease (AD) has been recognized as a crucial medical and social problem. A major issue in AD research is represented by the complexity of involved biochemical pathways, including the nature of protein misfolding, which results in the production of toxic species. Considering the involvement of (mis)folding processes in AD aetiology, targeting molecular chaperones represents a promising therapeutic perspective. This review analyses the connection between AD and molecular chaperones, with particular attention toward the most important heat shock proteins (HSPs) as representative components of the human chaperome: Hsp60,…

0301 basic medicineheat shock proteinDiseaseReviewprotein TauHsp70lcsh:ChemistrychaperoneEnzyme Inhibitorslcsh:QH301-705.5SpectroscopybiologyGeneral MedicineHsp60Hsp90Computer Science Applicationsamyloid peptideModels AnimalHSP60Protein foldingAlzheimer’s diseaseheat shock proteins; chaperones; Alzheimer’s disease; amyloid peptide; protein Tau; Hsp60; Hsp70; Hsp90Tau proteintau ProteinsHsp90Computational biologyCatalysisInorganic ChemistryMitochondrial Proteins03 medical and health sciencesAlzheimer DiseaseHeat shock proteinAnimalsHumanschaperonesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistryMolecular BiologyAmyloid beta-PeptidesSettore BIO/16 - Anatomia UmanaOrganic ChemistryChaperonin 60Settore CHIM/06 - Chimica OrganicaHsp70030104 developmental biologylcsh:Biology (General)lcsh:QD1-999heat shock proteinsbiology.protein
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Recombinant mussel protein Pvfp-5β: A potential tissue bioadhesive

2019

During their lifecycle, many marine organisms rely on natural adhesives to attach to wet surfaces for movement and self-defence in aqueous tidal environments. Adhesive proteins from mussels are biocompatible and elicit only minimal immune responses in humans. Therefore these proteins have received increased attention for their potential applications in medicine, biomaterials and biotechnology. The Asian green mussel Perna viridis secretes several byssal plaque proteins, molecules that help anchor the mussel to surfaces. Among these proteins, protein-5β (Pvfp-5β) initiates interactions with the substrate, displacing interfacial water molecules before binding to the surface. Here, we establis…

0301 basic medicinemedicine.disease_causeBiochemistryepidermal growth factor (EGF)law.inventionMiceCell Movementlawbiophysicsstructural biologyrecombinantCells CulturedbiologyChemistryMarine proteinsAdhesionRecombinant ProteinsadhesionProtein Structure and FoldingRecombinant DNAadhesion proteinsbiomaterialsPernaCell SurvivalSurface PropertiesBioadhesivemussel03 medical and health sciencesmedicineAnimalsHumansMolecular BiologyEscherichia coliCell ProliferationTissue Engineering030102 biochemistry & molecular biologyProteinsCell BiologyMusselbiology.organism_classificationEGF-like motifs; Marine proteins; adhesion; adhesion proteins; biomaterials; biophysics; epidermal growth factor (EGF); structural biologyEGF-like motifs030104 developmental biologyStructural biologyCell cultureNIH 3T3 CellsBiophysicsTissue AdhesivesHeLa CellsPerna viridisJournal of Biological Chemistry
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Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2

2016

We show that a peptide from Chikungunya virus nsP3 protein spanning residues 1728–1744 binds the amphiphysin-2 (BIN1) Src homology-3 (SH3) domain with an unusually high affinity (Kd 24 nM). Our NMR solution complex structure together with isothermal titration calorimetry data on several related viral and cellular peptide ligands reveal that this exceptional affinity originates from interactions between multiple basic residues in the target peptide and the extensive negatively charged binding surface of amphiphysin-2 SH3. Remarkably, these arginines show no fixed conformation in the complex structure, indicating that a transient or fluctuating polyelectrostatic interaction accounts for this …

0301 basic medicinenuclear magnetic resonance (NMR)Amino Acid MotifsStatic ElectricityPeptideTarget peptidePlasma protein bindingViral Nonstructural ProteinsBiologyhost-pathogen interactionBiochemistrySH3 domainsrc Homology Domainsamphiphysin SH3Structure-Activity Relationship03 medical and health sciencesProtein structuredynaminHumansShort linear motifprotein structureNuclear Magnetic Resonance BiomolecularMolecular BiologySrc homology 3 domain (SH3 domain)Adaptor Proteins Signal Transducingchemistry.chemical_classificationTumor Suppressor Proteinsta1182Nuclear ProteinsIsothermal titration calorimetryCell Biologyintrinsically disordered protein030104 developmental biologychemistryBiochemistrynsP3Protein Structure and FoldingAmphiphysinBiophysicsPeptidesChikungunya virusProtein BindingJournal of Biological Chemistry
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The Yeast eIF2 Kinase Gcn2 Facilitates H 2 O 2 -Mediated Feedback Inhibition of Both Protein Synthesis and Endoplasmic Reticulum Oxidative Folding du…

2021

Recombinant protein production is a known source of oxidative stress. However, knowledge of which reactive oxygen species are involved or the specific growth phase in which stress occurs remains lacking. Using modern, hypersensitive genetic H2O2-specific probes, microcultivation, and continuous measurements in batch culture, we observed H2O2 accumulation during and following the diauxic shift in engineered Saccharomyces cerevisiae, correlating with peak α-amylase production. In agreement with previous studies supporting a role of the translation initiation factor kinase Gcn2 in the response to H2O2, we find that Gcn2-dependent phosphorylation of eIF2α increases alongside translational atten…

0303 health sciencesEcologyChemistryEndoplasmic reticulumOxidative folding030302 biochemistry & molecular biologyApplied Microbiology and BiotechnologyCell biology03 medical and health sciencesCytosolProtein biosynthesisUnfolded protein responseProtein disulfide-isomeraseProtein kinase ATranslational attenuation030304 developmental biologyFood ScienceBiotechnologyApplied and Environmental Microbiology
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Evidence that autophagy, but not the unfolded protein response, regulates the expression of IL-23 in the gut of patients with ankylosing spondylitis …

2013

OBJECTIVES: Interleukin (IL)-23 has been implicated in the pathogenesis of ankylosing spondylitis (AS). The aim of the study was to clarify the mechanisms underlying the increased IL-23 expression in the gut of AS patients. METHODS: Consecutive gut biopsies from 30 HLA-B27(+) AS patients, 15 Crohn's disease (CD) patients and 10 normal subjects were obtained. Evidence for HLA-B27 misfolding was studied. Unfolded protein response (UPR) and autophagy were assessed by RT-PCR and immunohistochemistry. The contribution of UPR and autophagy in the regulation of IL-23 expression was evaluated in in vitro experiments on isolated lamina propria mononuclear cells (LPMCs). RESULTS: Intracellular coloca…

AdultMaleProtein FoldingBiopsyImmunologyATG5Gene ExpressionInflammationdigestive systemArticleGeneral Biochemistry Genetics and Molecular BiologyATG12Young AdultCrohn DiseaseRheumatologyDownregulation and upregulationSettore BIO/13 - Biologia Applicataankylosing spondylitisAutophagymedicineInterleukin 23HumansImmunology and AllergySpondylitis AnkylosingHLA-B27 AntigenAgedMucous Membranebusiness.industryAutophagyInterleukinIleitisMiddle AgedIntestinesInterleukin 23Settore MED/16 - ReumatologiaImmunologyInterleukin-23 Subunit p19Unfolded Protein ResponseUnfolded protein responseFemalemedicine.symptombusinessAnnals of the Rheumatic Diseases
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De novo mutation in a male patient with Fabry disease: a case report

2014

Abstract Background Fabry disease is an X-linked inherited metabolic condition where the deficit of the α-galactosidase A enzyme, encoded by the GLA gene, leads to glycosphingolipid storage, mainly globotriaosylceramide. To date, more than 600 mutations have been identified in human GLA gene that are responsible for FD, including missense and nonsense mutations, small and large deletions. Such mutations are usually inherited, and cases of de novo onset occur rarely. Case presentation In this article we report an interesting case of a 44-year-old male patient suffering from a severe form of Fabry disease, with negative family history. The patient showed signs such as cornea verticillata, ang…

AdultMaleProtein Foldingα-galactosidase ADe novo mutationNonsense mutationD165H mutationGlobotriaosylceramideMutation MissenseCase ReportBiologymedicine.disease_causeGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundGermline mutationmedicineMissense mutationHumansPoint MutationThrombophiliaEnzyme Replacement TherapyAmino Acid SequenceChildGLA geneConserved SequenceGerm-Line MutationMedicine(all)GeneticsMutationFabry diseaseSequence Homology Amino AcidBiochemistry Genetics and Molecular Biology(all)Point mutationGeneral MedicineEnzyme replacement therapymedicine.diseaseFabry diseasePedigreeStrokechemistryAmino Acid Substitutionalpha-GalactosidaseKidney Failure ChronicFemaleSymptom AssessmentSequence AlignmentBMC Research Notes
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Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems.

2010

Aging entails progressive deterioration of molecules and supramolecular structures, including Hsp chaperones and their complexes, paralleled by functional decline. Recent research has changed our views on Hsp chaperones. They work inside and outside cells in many locations, alone or forming teams, interacting with cells, receptors, and molecules that are not chaperones, in roles that are not typically attributed to chaperones, such as protein folding. Hsp chaperones form a physiological system with a variety of functions and interactions with other systems, for example, the immune system. We propose that chaperone malfunctioning due to structural damage or gene dysregulation during aging ha…

AgingProtein Foldingchaperonopathies by mistakeSettore BIO/16 - Anatomia Umanachaperoning systemImmune Systemchaperoning system interactionchaperonopathieCarrier Proteinschaperonotherapy Hsp60Molecular ChaperonesAnnals of the New York Academy of Sciences
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