Search results for " CHAPERONES."

showing 10 items of 71 documents

A genetic approach reveals different modes of action of prefoldins

2021

17 p.-7 fig.

Regular IssueAcademicSubjects/SCI01280PhysiologyProtein subunitMutantArabidopsisPlant ScienceChaperonin03 medical and health sciences0302 clinical medicineArabidopsisGeneticsBIOQUIMICA Y BIOLOGIA MOLECULARArabidopsis thalianaTranscription factorActinResearch Articles030304 developmental biology0303 health sciencesAcademicSubjects/SCI01270biologyErrataArabidopsis ProteinsAcademicSubjects/SCI02288AcademicSubjects/SCI02287AcademicSubjects/SCI02286Genes Development and EvolutionPrefoldin complexbiology.organism_classificationCell biologyGENETICA030217 neurology & neurosurgeryMolecular ChaperonesTranscription Factors
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DICER and ZRF1 contribute to chromatin decondensation during nucleotide excision repair

2016

Abstract Repair of damaged DNA relies on the recruitment of DNA repair factors in a well orchestrated manner. As a prerequisite, the chromatin needs to be decondensed by chromatin remodelers to allow for binding of repair factors and for DNA repair to occur. Recent studies have implicated members of the SWI/SNF and INO80 families as well as PARP1 in nucleotide excision repair (NER). In this study, we report that the endonuclease DICER is implicated in chromatin decondensation during NER. In response to UV irradiation, DICER is recruited to chromatin in a ZRF1-mediated manner. The H2A–ubiquitin binding protein ZRF1 and DICER together impact on the chromatin conformation via PARP1. Moreover, …

Ribonuclease III0301 basic medicineDNA RepairUltraviolet RaysDNA damageDNA repairgenetic processesPoly (ADP-Ribose) Polymerase-1Genome Integrity Repair and ReplicationBiologyChromatin remodelingCell LineDEAD-box RNA HelicasesHistones03 medical and health scienceschemistry.chemical_compoundUbiquitinCell Line TumorGeneticsAnimalsHumansCaenorhabditis elegansOncogene ProteinsOsteoblastsUbiquitinfungiRNA-Binding ProteinsFibroblastsChromatin Assembly and DisassemblyMolecular biologyChromatinChromatinDNA-Binding Proteinsenzymes and coenzymes (carbohydrates)HEK293 Cells030104 developmental biologychemistrybiology.proteinDNADNA DamageMolecular ChaperonesNucleotide excision repairDicerNucleic Acids Research
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Unveiling novel interactions of histone chaperone Asf1 linked to TREX-2 factors Sus1 and Thp1

2014

13 páginas, 7 figuras, 2 yablas

Saccharomyces cerevisiae ProteinsTranscription Genetic(5-10) yAsf1Histone H2B ubiquitinationCell Cycle ProteinsSAGASaccharomyces cerevisiaeBiologyyeastMethylationTREX-2RNA TransportHistonesSus1Histone H3Histone H1Gene Expression Regulation FungalhistonesHistone H2ANucleosomeHistone codeTAP-MS strategyHistone ChaperonesRNA MessengerHistone octamerGeneticsNuclear ProteinsRNA-Binding ProteinsAcetylationCell BiologyYeastCell biologyRibonucleoproteinsHistone methyltransferaseProtein Processing Post-TranslationalMolecular ChaperonesResearch Paper
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Hsp60 and human aging: Les liaisons dangereuses 

2013

Stressors can cause abnormal intracellular accumulation of Hsp60 and its localization in extramitochondrial sites, secretion, and circulation, with immune system activation. Dysfunction of chaperones associated with their quantitative and qualitative decline with aging (chaperonopathies of aging) characterizes senescence and is a potential causal factor in the physiological deterioration that occurs with it. The role of Hsp60 in aging is not easy to elucidate, because aging is accompanied by pathologies (e.g., cardiovascular and neurodegenerative disorders, osteoporosis, diabetes, cancer, etc.) in which Hsp60 has been implicated but, although those disorders are more frequent in the elderly…

SenescenceAginganimal structuresOsteoporosischemical and pharmacologic phenomenaInflammationDiseaseBiologycomplex mixturesMitochondrial ProteinsPathogenesisImmune systemDiabetes mellitusmedicineHumansCellular SenescenceAutoantibodiesHeart FailurefungiHSP 60 AGING CHAPERONES.Neurodegenerative DiseasesChaperonin 60Atherosclerosismedicine.diseaseMitochondriaImmune SystemImmunologyHSP60Arthropathy Neurogenicmedicine.symptomFrontiers in Bioscience
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Overexpression of apolipoprotein J in human fibroblasts protects against cytotoxicity and premature senescence induced by ethanol and tert-butylhydro…

2008

Human diploid fibroblasts (HDFs) exposed to subcytotoxic stresses under H2O2, tert-butylhydroperoxide (t-BHP), and ethanol (EtOH) undergo stress-induced premature senescence (SIPS) characterized by many biomarkers of HDFs replicative senescence. Among these biomarkers are a growth arrest, an increase in the senescence-associated β-galactosidase activity, a senescent morphology, an overexpression of p21waf-1 and the subsequent inability to phosphorylate pRb, the presence of the common 4977-bp mitochondrial deletion, and an increase in the steady-state level of several senescence-associated genes such as apolipoprotein J (apo J). Apo J has been described as a survival gene against cytotoxic s…

SenescenceCell SurvivalGene ExpressionSimian virus 40Biologymedicine.disease_causeTritiumBiochemistrytert-ButylhydroperoxideGene expressionmedicineHumansOsteonectinRNA MessengerCytotoxicityCells CulturedCellular SenescenceCell Line TransformedGlycoproteinsClusterinEthanolCentral Nervous System DepressantsCell BiologyTransfectionOriginal ArticlesFibroblastsbeta-GalactosidaseMolecular biologyRecombinant ProteinsFibronectinsOxidative StressClusterinbiology.proteinPhosphorylationMitogensCell agingOxidative stressMolecular ChaperonesThymidineCell Stress and Chaperones
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The Chaperone System in Breast Cancer: Roles and Therapeutic Prospects of the Molecular Chaperones Hsp27, Hsp60, Hsp70, and Hsp90

2022

Breast cancer (BC) is a major public health problem, with key pieces of information needed for developing preventive and curative measures still missing. For example, the participation of the chaperone system (CS) in carcinogenesis and anti-cancer responses is poorly understood, although it can be predicted to be a crucial factor in these mechanisms. The chief components of the CS are the molecular chaperones, and here we discuss four of them, Hsp27, Hsp60, Hsp70, and Hsp90, focusing on their pro-carcinogenic roles in BC and potential for developing anti-BC therapies. These chaperones can be targets of negative chaperonotherapy, namely the elimination/blocking/inhibition of the chaperone(s)…

Settore BIO/16 - Anatomia UmanaCarcinogenesisOrganic ChemistryHSP27 Heat-Shock ProteinsBreast NeoplasmsChaperonin 60General MedicineCatalysisComputer Science ApplicationsInorganic ChemistryHumansbreast cancer chaperone system Hsp inhibitors Hsp27Hsp60Hsp70Hsp90 molecular chaperones immunotherapy negative chaperonotherapyCarcinogenesisFemaleHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistryMolecular BiologySpectroscopyInternational Journal of Molecular Sciences
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EXPRESSION AND LOCALIZATION OF “CHAPEROKINE” HSP60 IN BRONCHIAL CULTURE MODELS MIMING COPD

Settore BIO/16 - Anatomia UmanaMolecular chaperones inflammatory chronic disease exosomes three-dimensional cultures
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The Chaperone System in Salivary Glands: Hsp90 Prospects for Differential Diagnosis and Treatment of Malignant Tumors

2022

Salivary gland tumors represent a serious medical problem and new tools for differential diagnosis and patient monitoring are needed. Here, we present data and discuss the potential of molecular chaperones as biomarkers and therapeutic targets, focusing on Hsp10 and Hsp90. The salivary glands are key physiological elements but, unfortunately, the information and the means available for the management of their pathologies, including cancer, are scarce. Progress in the study of carcinogenesis has occurred on various fronts lately, one of which has been the identification of the chaperone system (CS) as a physiological system with presence in all cells and tissues (including the salivary gland…

Settore BIO/16 - Anatomia UmanaOrganic ChemistryAntineoplastic AgentsGeneral MedicineSettore MED/08 - Anatomia PatologicaSalivary Gland NeoplasmsSalivary GlandsCatalysisComputer Science ApplicationsDiagnosis DifferentialInorganic ChemistryHumanschaperone system differential diagnosis Ganetespib Hsp90 Hsp90 biomarker Hsp90 pathogenic negative chaperonotherapysalivary gland tumors Diagnosis Differential Humans Molecular Chaperones Salivary Glands Antineoplastic Agents Salivary Gland NeoplasmsHSP90 Heat-Shock ProteinsPhysical and Theoretical Chemistrysalivary gland tumors; chaperone system; Hsp90; Hsp90 pathogenic; negative chaperonotherapy; Ganetespib; Hsp90 biomarker; differential diagnosisMolecular BiologySpectroscopyMolecular Chaperones
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Exosomal HSP60 levels and related miRNAs in brain tumors

In cancer, Extracellular Vesicles (EVs), such as exosomes, contribute to tumor progression by regulating local and systemic parameters [1,2]. Since exosomes are released into body fluids, they may be used in nanomedicine as a valuable source of diagnostic biomarkers [3]. The prognosis of brain tumors is poor even after surgical resection followed by post-operatory chemo- and radio-therapies and it is cogent to find innovative treatments. The discovery that molecular chaperones can be determinant factors in tumorigenesis and the increasing understanding of exosomes, particularly in what refers to their release by tumor cells and contents, including chaperones and miRNA, provide elements to d…

Settore BIO/16 - Anatomia Umanamolecular chaperones HSP60 exosomes brain tumor new therapeutic tools
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HSP-MOLECULAR CHAPERONES IN CANCER BIOGENESIS AND TUMOR THERAPY: AN OVERVIEW

2012

Molecular chaperones, many of which are heat-shock proteins (HSPs), are an important class of molecules with various functions. Pathological conditions in which chaperones become etiological and/or pathogenic factors are called chaperonopathies, and are classified into by defect, by excess, and by "mistake". In the latter case, the chaperone is structurally and functionally normal but paqrtecipates in pathwais that favor diseases, aòlthough in some cases the chaperone may have post-translational modifications that may lead it to change its location and function and, thus, to become pathogenic. For example, HSP-chaperones are involved in acrcinogenesis in various ways, so that some forms of …

Settore MED/18 - Chirurgia GeneraleCell Transformation NeoplasticSettore MED/09 - Medicina InternaSettore BIO/16 - Anatomia UmanaNeoplasmsmolecular chaperones chapoeronig system chaperonology chaperonopathy by mistake cancer HSP60 chaperonin chaperonopathy.AnimalsHumansMolecular Targeted TherapyCancer VaccinesHeat-Shock Proteins
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