Search results for "chaperon"

showing 10 items of 358 documents

Sec61alpha and TRAM are Sequentially Adjacent to a Nascent Viral Membrane Protein during its ER Integration

2007

Co-translational integration of a nascent viral membrane protein into the endoplasmic reticulum membrane takes place via the translocon. We have been studying the early stages of the integration of a double-spanning plant viral movement protein to gain insights into how viral membrane proteins are transferred from the hydrophilic interior of the translocon into the hydrophobic environment of the bilayer, where the transmembrane (TM) segments of the viral proteins can diffuse freely. Photocrosslinking experiments reveal that this integration involves the sequential passage of the TM segments past Sec61alpha and translocating chain-associating membrane protein (TRAM). Each TM segment is first…

Virus IntegrationBiologyEndoplasmic ReticulumModels BiologicalViral Matrix ProteinsDogsMembranes (Biologia)Structural BiologyAnimalsRNA MessengerMolecular BiologyVirus IntegrationMembrane GlycoproteinsViral matrix proteinEndoplasmic reticulumProteïnes de membranaMembrane ProteinsViral membraneTransloconTransmembrane proteinCell biologyPlant Viral Movement ProteinsCross-Linking ReagentsMembrane proteinBiochemistrySEC Translocation ChannelsSEC Translocation ChannelsMolecular Chaperones
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Hsp60 in embryonic and adult submandibular salivary gland: quantitative distribution patterns in normal tissue and comparison with benign and maligna…

2019

Introduction: Heat Shock Protein 60 (Hsp60) is a member of the chaperoning system that assists protein folding inside mitochondria and plays other roles beyond these organelles. It is implicated in the carcinogenic processes in various types of cancer. In human salivary glands, Hsp60 has not yet been measured or mapped in detail and its role in gland development and functioning is virtually unknown. Consequently, its potential as biomarker for gland diseases, including malignancies cannot be assessed. The S-100 protein, a known marker for schwannomas, has been found also in myoepithelial-cell carcinomas of the salivary glands. Here, we present our initial findings on the anatomic-histologic…

Warthin’s tumor (WT)Keywords: Submandibular salivary gland (SMG)Pleomorphic Adenoma (PA)salivary glandHeat shock protein (Hsp)molecular chaperoneHsp60Adenoid Cystic Adenoma (ACC)embryo vs. adult patternS-100 protein (S-100).
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Early stages of beta2-microglobulin aggregation and the inhibiting action of alphaB-crystallin

2008

The interest of nucleation of protein crystals and aggregates (including oligomerization) spans from basic physics theory all the way to biophysics, nanophysics, clinical sciences, biotechnologies, food technologies and polymer-solvent interactions. Understanding nucleation within a theoretical framework capable of providing quantitative predictions and control of nucleation rates, or even the very occurrence of crystallization, is a long-sought goal of remarkable relevance to each of the above fields. A large amount of work has been aimed at such goal, but success has been so far rather limited. Work at our laboratory has more recently highlighted a direct link between nucleation rates and…

Work (thermodynamics)Time Factorssolvent-induced forceLightchaperonamyloid formationBiochemistrylight scatteringchemistry.chemical_compoundDynamic light scatteringStructural BiologyHumansScattering RadiationAlphab crystallinProtein Structure QuaternaryMolecular BiologyselfassemblyBeta-2 microglobulinpre-fibrillar aggregatesEnergy landscapealpha-Crystallin B ChainSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Crystallographyfree energy landscapeMonomerchemistryBiophysicsbeta 2-MicroglobulinSoftwareProtein Binding
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Organization into higher-ordered ring structures counteracts membrane binding of IM30, a protein associated with inner membranes in chloroplasts and …

2017

ABSTRACT PspA, IM30 (Vipp1) and LiaH, which all belong to the PspA/IM30 protein family, form high molecular weight oligomeric structures. For all proteins membrane binding and protection of the membrane structure and integrity has been shown or postulated. Here we discuss the possible membrane chaperoning activity of PspA, IM30 and LiaH and propose that larger oligomeric structures bind to stressed membrane regions, followed by oligomer disassembly and membrane stabilization by protein monomers or smaller/different oligomeric scaffolds.

YjfJPspAmembrane stressLiaHIM30oligomerVipp1Article Addendummembrane chaperonePspA/IM30 familyCommunicative & Integrative Biology
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Etude dynamique et structurale de biomolécules par microscopie à force atomique HS-AFM : application à une petite protéine de choc thermique sHsp

2012

The atomic force microscopy (AFM) gives access to the topography of organic and inorganic samplesat the atomic scale. The latest innovations offer the possiblity to understand the sample nano-mechanicalproperties (elasticity, adhesion...). Its feature set allows overcoming the demands of nanotechnology,both in the fields of physics, chemistry and biology.However, understanding biological processes require faster acquisitions for the atomic forcemicroscopy, less than a second per frame. As conventional equipment does not offer the possibility toovercome the constraint of time for dynamical studies, a prototype of high-speed atomic forcemicroscope (HS-AFM) was developed in partnership with Pr…

[SDV.SA]Life Sciences [q-bio]/Agricultural sciences[SDV.SA] Life Sciences [q-bio]/Agricultural sciencesSHspActivité chaperonne et lipochaperonneChaperone and lipochaperonne activityFonctionnalisation de surfacesHigh-speed atomic force microscopy (HS-AFM)[ PHYS.COND.CM-GEN ] Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other]Microscopie à force atomique (AFM)Biomimetic surfacesFunctionalization of surfacesMicroscopie à force atomique haute-vitesse (HSAFM)[PHYS.COND.CM-GEN] Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other][CHIM.OTHE] Chemical Sciences/Other[PHYS.COND.CM-GEN]Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other]Atomic force microscopy (AFM)[ CHIM.OTHE ] Chemical Sciences/OtherSurfaces biomimétique[CHIM.OTHE]Chemical Sciences/Other[ SDV.SA ] Life Sciences [q-bio]/Agricultural sciences
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New insights about the role of the chaperon-like protein Cdc48, a target for nitric oxide in plant immunity

2015

[SDV] Life Sciences [q-bio][SDE] Environmental Sciencesnitric oxide[SDV]Life Sciences [q-bio][SDE]Environmental Sciences[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal Biologyplant immunitychaperon-like protein Cdc48
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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

2016

Seuls les 100 premiers auteurs dont les auteurs INRA ont été entrés dans la notice. La liste complète des auteurs et de leurs affiliations est accessible sur la publication.; International audience; In 2008 we published the first set of guidelines for standardizing research in autophagy. Since then, research on this topic has continued to accelerate, and many new scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Accordingly, it is important to update these guidelines for monitoring autophagy in different organisms. Various reviews have described the range of assays that have been used for this purpose. Nevertheless, there continues…

[SDV]Life Sciences [q-bio]autophagosomeReview Articleddc:616.07stressstreLC3MESH: AnimalsSettore MED/49 - Scienze Tecniche Dietetiche ApplicateSettore BIO/06 - Anatomia Comparata E Citologiachaperone-mediated autophagyComputingMilieux_MISCELLANEOUSSettore BIO/11Pharmacology. TherapySettore BIO/13standards [Biological Assay]autolysosomeMESH: Autophagy*/physiologylysosomemethods [Biological Assay]Biological AssaySettore BIO/17 - ISTOLOGIAErratumHumanBiochemistry & Molecular BiologySettore BIO/06physiology [Autophagy]Chaperonemediated autophagy[SDV.BC]Life Sciences [q-bio]/Cellular BiologyNOautophagy guidelines molecular biology ultrastructureautolysosome; autophagosome; chaperone-mediated autophagy; flux; LC3; lysosome; macroautophagy; phagophore; stress; vacuoleMESH: Biological Assay/methodsMESH: Computer Simulationddc:570Autolysosome Autophagosome Chaperonemediated autophagy Flux LC3 Lysosome Macroautophagy Phagophore Stress VacuoleAutophagyAnimalsHumansComputer SimulationSettore BIO/10ddc:612BiologyphagophoreMESH: HumansvacuoleAnimalLC3; autolysosome; autophagosome; chaperone-mediated autophagy; flux; lysosome; macroautophagy; phagophore; stress; vacuole; Animals; Biological Assay; Computer Simulation; Humans; Autophagy0601 Biochemistry And Cell BiologyfluxmacroautophagyMESH: Biological Assay/standards*Human medicineLC3; autolysosome; autophagosome; chaperone-mediated autophagy; flux; lysosome; macroautophagy; phagophore; stress; vacuole
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Hsp60, a Novel Target for Antitumor Therapy: Structure-Function Features and Prospective Drugs Design

2013

Heat shock protein 60 kDa (Hsp60) is a chaperone classically believed to be involved in assisting the correct folding of other mitochondrial proteins. Hsp60 also plays a role in cytoprotection against cell stressors, displaying for example, antiapoptotic potential. Despite the plethora of studies devoted to the mechanism of Hsp60's function, especially in prokaryotes, fundamental issues still remain unexplored, including the definition of its role in cancer. Key questions still unanswered pertain to the differences in structure-function features that might exist between the well-studied prokaryotic GroEL and the largely unexplored eukaryotic Hsp60 proteins. In this article we discuss these …

animal structuresBinding pocketCellAntineoplastic Agentschemical and pharmacologic phenomenaComputational biologyBiologyBioinformaticsFunctional domaincomplex mixturesChaperoninStructure-Activity RelationshipNeoplasmsHeat shock proteinDrug DiscoverymedicineHumansPharmacologyCompound dockingSettore BIO/16 - Anatomia UmanaCell growthfungiSettore CHIM/06 - Chimica OrganicaChaperonin 60Hsp60Settore CHIM/08 - Chimica FarmaceuticaCytoprotectionGroELmedicine.anatomical_structureSettore CHIM/03 - Chimica Generale E InorganicaCancer treatmentDrug DesignChaperone (protein)biology.proteinHSP60Protein foldingEpolactaeneCurrent Pharmaceutical Design
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Chaperonopathies and chaperonotherapy. Hsp60 as therapeutic target in cancer: potential benefits and risks.

2013

In this minireview we focus on Hsp60 as a target for anticancer therapy. We discuss the new concepts of chaperonopathies and chaperonotherapy and present information on Hsp60 localization in the cell membrane of human tumor cells. We describe novel mechanisms for Hsp60 reaching the extracellular environment that involve membrane-associated stages, as well as data on anti-Hsp60 antibodies found in human sera, both in normal subjects and patients affected by autoimmune diseases. Finally, we discuss possible therapeutic applications of anti-Hsp60 antibodies in cancer treatment, evaluating also side effects on non-tumor cells. In conclusion, the way for investigating Hsp60-targeted anti-tumor t…

animal structuresCellchemical and pharmacologic phenomenaAntineoplastic AgentsBiologycomplex mixturesRisk AssessmentCell membraneDrug Delivery SystemsRisk FactorsNeoplasmsDrug DiscoverymedicineExtracellularAnimalsHumansSecretionPharmacologyMechanism (biology)fungiCancerChaperonin 60medicine.diseasemedicine.anatomical_structureImmunologybiology.proteinCancer researchHsp60 Cpn60 HSPD1 plasma membrane antibodies autoantibodies antitumor immunotherapy anticancer therapy chaperonopathies human sera.HSP60AntibodyCurrent pharmaceutical design
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Sea Urchin Mitochondrial Matrix Contains a 56-kDa Chaperonine-like Protein

1997

Abstract Paracentrotus lividus mitochondrial matrix contains a constitutive hsp of 56-KDa which cross reacts with a serum anti-hsp-60 chaperonine from yeast mitochondria. The localization of hsps preexisting or newly synthesized in different subcellular fractions of gastrula embryos is also analyzed by two-dimensional electrophoresis.

animal structuresChaperoninsBlotting WesternBiophysicsMitochondrionBiochemistryParacentrotus lividusbiology.animalAnimalsElectrophoresis Gel Two-DimensionalImmunoelectrophoresisMolecular BiologySea urchinbiologyEmbryoCell Biologybiology.organism_classificationMolecular biologyYeastMitochondriaGastrulationBiochemistryMitochondrial matrixSea Urchinsbiological sciencesembryonic structuresBiochemical and Biophysical Research Communications
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