Search results for "Complex protein"

showing 10 items of 57 documents

Enniatin B induces expression changes in the electron transport chain pathway related genes in lymphoblastic T-cell line

2018

Abstract Enniatin B is a ionophoric and lipophilic mycotoxin which reaches the bloodstream and has the ability to penetrate into cellular membranes. The purpose of this study was to reveal changes in the gene expression profile caused by enniatin B in human Jurkat lymphoblastic T-cells after 24 h of exposure at 1.5, 3 and 5 μM by next generation sequencing. It was found that up to 27% of human genome expression levels were significantly altered (5750 genes for both down-regulation and up-regulation). In the three enniatin B concentrations studied 245 differentially expressed genes were found to be overlapped, 83 were down and 162 up-regulated. ConsensusPathDB analysis of over-representation…

0301 basic medicineCellular respirationT-LymphocytesDown-RegulationMitochondrionToxicologyJurkat cellsTranscriptomeJurkat Cells03 medical and health sciences0404 agricultural biotechnologyDepsipeptidesGene expressionHumansGeneChemistryRespiratory chain complexNucleoside monophosphate metabolic process04 agricultural and veterinary sciencesGeneral MedicinePrecursor Cell Lymphoblastic Leukemia-Lymphoma040401 food scienceUp-RegulationCell biologyGene Expression Regulation Neoplastic030104 developmental biologyElectron Transport Chain Complex ProteinsTranscriptomeFood ScienceFood and Chemical Toxicology
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The purine analogues abacavir and didanosine increase acetaminophen-induced hepatotoxicity by enhancing mitochondrial dysfunction

2016

Background NRTIs are essential components of HIV therapy with well-documented, long-term mitochondrial toxicity in hepatic cells, but whose acute effects on mitochondria are unclear. As acetaminophen-induced hepatotoxicity also involves mitochondrial interference, we hypothesized that it would be exacerbated in the context of ART. Methods We evaluated the acute effects of clinically relevant concentrations of the most widely used NRTIs, alone or combined with acetaminophen, on mitochondrial function and cellular viability. Results The purine analogues abacavir and didanosine produced an immediate and concentration-dependent inhibition of oxygen consumption and complex I and III activity. Th…

0301 basic medicineMicrobiology (medical)Mitochondrial DiseasesstavudineAnti-HIV Agentsantiretroviral therapyPurine analogueContext (language use)Mitochondria LiverMitochondrionPharmacologymedicine.disease_causeacute liver-failureCell Line03 medical and health sciencesOxygen ConsumptionmedicineHumansPharmacology (medical)Reverse-transcriptase inhibitorsAcetaminophenPharmacologychemistry.chemical_classificationmechanismsReactive oxygen speciesbusiness.industryassociationtoxicityAnalgesics Non-Narcoticmedicine.diseaseGlutathioneReactive Nitrogen SpeciesDideoxynucleosideshep3b cellsAcetaminophenMitochondrial toxicityDidanosine030104 developmental biologyInfectious DiseaseschemistryElectron Transport Chain Complex ProteinsToxicityhypersensitivityChemical and Drug Induced Liver Injurybusinesshepatic cellsOxidative stressmedicine.drug
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Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRET

2018

Abstract Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex. They are highly dynamic under physiological conditions and studying their interaction with nuclear transport receptors (NTRs) is key to understanding the molecular mechanism of nucleocytoplasmic transport. Distinct conformational features of FG-Nups interacting with diverse NTRs can be detected by multiparameter single-molecule fluorescence energy transfer (smFRET), which is a powerful technique for studying the dynamics and interactions of biomolecules in solution. Here we provide a detailed protocol utilizing smFRET to reveal dif…

0301 basic medicineModels MolecularGlycosylationProtein ConformationPhenylalanineGlycineIntrinsically disordered proteinsArticle03 medical and health scienceschemistry.chemical_compoundFluorescence Resonance Energy TransferAnimalsHumansNuclear porechemistry.chemical_classificationBiomoleculeSingle-molecule FRETEquipment DesignIntrinsically Disordered ProteinsNuclear Pore Complex Proteins030104 developmental biologychemistryNucleocytoplasmic TransportBiophysicsNucleoporinNuclear transportProtein BindingIntrinsically Disordered Proteins
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Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors

2018

Summary Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex (NPC). Previous studies showed that nuclear transport receptors (NTRs) were found to interact with FG-Nups by forming an “archetypal-fuzzy” complex through the rapid formation and breakage of interactions with many individual FG motifs. Here, we use single-molecule studies combined with atomistic simulations to show that, in sharp contrast, FG-Nup214 undergoes a coupled reconfiguration-binding mechanism when interacting with the export receptor CRM1. Association and dissociation rate constants are more than an order of magnitude lowe…

0301 basic medicineModels MolecularGlycosylationglycosylationProtein ConformationPhenylalanineGlycineSequence (biology)Intrinsically disordered proteinsnuclear transport receptorssingle-molecule FRETGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicineEscherichia coliFluorescence Resonance Energy TransferHumansNuclear poreReceptorlcsh:QH301-705.5Single-molecule FRETmolecular dynamics simulationsbinding mechanismintrinsically disordered proteinFG-Nup3. Good healthNuclear Pore Complex Proteins030104 developmental biologychemistrylcsh:Biology (General)BiophysicsNuclear PoreNucleoporinNuclear transport030217 neurology & neurosurgeryProtein BindingCell Reports
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Ultrafast structural changes within a photosynthetic reaction centre

2021

Nature <London> / Physical science 589, 310 - 314 (2021). doi:10.1038/s41586-020-3000-7

0301 basic medicinePhotosynthetic reaction centreChlorophyllModels MolecularklorofylliCytoplasmUbiquinonePhotosynthetic Reaction Center Complex ProteinsElectrons02 engineering and technologyPhotochemistrymedicine.disease_cause530yhteyttäminenbakteeritElectron Transport03 medical and health sciencesElectron transfermedicineMoleculeddc:530BacteriochlorophyllsbioenergetiikkaComputingMilieux_MISCELLANEOUSHyphomicrobiaceaeMultidisciplinaryBinding SitesCrystallography[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryBlastochloris viridisLaserskalvot (biologia)PheophytinsBiological membraneVitamin K 2021001 nanoscience & nanotechnologyAcceptor030104 developmental biologyPicosecondFemtosecondsense organsProtons0210 nano-technologyOxidation-Reductionröntgenkristallografia
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The N-terminal domain of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for its acclimative proteolysis.

2000

AbstractVariations in the amount of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for regulation of the uptake of light into photosystem II. An endogenous proteolytic system was found to be involved in the degradation of LHCII in response to elevated light intensities and the proteolysis was shown to be under tight regulation [Yang, D.-H. et al. (1998) Plant Physiol. 118, 827–834]. In this study, the substrate specificity and recognition site towards the protease were examined using reconstituted wild-type and mutant recombinant LHCII. The results show that the LHCII apoprotein and the monomeric form of the holoprotein are targeted for proteolysis while t…

Acclimative proteaseChlorophyll aN-terminal domainPhotosystem IImedicine.medical_treatmentProteolysisMutantMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsBiophysicsLight-Harvesting Protein ComplexesRecognition siteEndogenyLight-harvesting complex IIBiochemistrylaw.inventionchemistry.chemical_compoundStructural BiologylawSpinacia oleraceaGeneticsmedicineAmino Acid SequenceMolecular BiologyProteasemedicine.diagnostic_testSequence Homology Amino AcidChemistryBinding proteinHydrolysisPhotosystem II Protein ComplexCell BiologyBiochemistryRecombinant light-harvesting complex IIProteolysisRecombinant DNAFEBS letters
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Analysis of translocations that involve theNUP98 gene in patients with 11p15 chromosomal rearrangements

2004

The NUP98 gene has been reported to be fused with at least 15 partner genes in leukemias with 11p15 translocations. We report the results of screening of cases with cytogenetically documented rearrangements of 11p15 and the subsequent identification of involvement of NUP98 and its partner genes. We identified 49 samples from 46 hematology patients with 11p15 (including a few with 11p14) abnormalities, and using fluorescence in situ hybridization (FISH), we found that NUP98 was disrupted in 7 cases. With the use of gene-specific FISH probes, in 6 cases, we identified the partner genes, which were PRRX1 (PMX1; in 2 cases), HOXD13, RAP1GDS1, HOXC13, and TOP1. In the 3 cases for which RNA was a…

AdultMaleCancer Researchmedicine.medical_specialtyAdolescentMolecular Sequence DataChromosomal translocationBiologyTranslocation GeneticComplementary DNAInternal medicineGeneticsmedicineGuanine Nucleotide Exchange FactorsHumansGenetic Predisposition to DiseaseGeneIn Situ Hybridization FluorescenceHomeodomain ProteinsGeneticsNUP98 GeneLeukemiaHematologyBase Sequencemedicine.diagnostic_testChromosomes Human Pair 11BreakpointInfantMolecular biologyNuclear Pore Complex ProteinsDNA Topoisomerases Type IHOXD13Child PreschoolTranscription FactorsFluorescence in situ hybridizationGenes, Chromosomes and Cancer
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Respiratory chain polymorphisms and obesity in the Spanish population, a cross-sectional study

2019

ObjectiveTo study the association of genes involved in the mitochondrial respiratory chain (MRC) pathway with body mass index (BMI) and obesity risk.DesignThis work studies three cross-sectional populations from Spain, representing three provinces: HORTEGA (Valladolid, Northwest/Centre), SEGOVIA (Segovia, Northwest/centre) and PIZARRA (Malaga,South).SettingForty-eight single nucleotide polymorphisms (SNPs) from MRC genes were selected and genotyped by SNPlex method. Association studies with BMI and obesity risk were performed for each population. These associations were then verified by analysis of the studied population as a whole (3731 samples).ParticipantsA total of 3731 Caucasian indivi…

AdultMaleobesityGenotypeCross-sectional studyPopulationRespiratory chainmitochondrial respiratory chain030209 endocrinology & metabolismSingle-nucleotide polymorphismPolymorphism Single NucleotideWhite PeopleBody Mass IndexMitochondrial Proteins03 medical and health sciences0302 clinical medicineRisk FactorsMedicineHumans1506educationAlleles030304 developmental biologyGenetic associationAged0303 health scienceseducation.field_of_studybusiness.industryResearch1697Genetics and GenomicssnpGeneral MedicineMiddle Agedmedicine.diseaseObesityMitochondrial respiratory chainCross-Sectional StudiesElectron Transport Chain Complex ProteinsSpainFemalebusinessBody mass indexDemographyBMJ Open
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Mitochondrial transcriptional study of the effect of aflatoxins, enniatins and carotenoids in vitro in a blood brain barrier model

2020

C. maxima (var. Delica), a variety of pumpkin, is well known for its high concentration on carotenoids, possessing dietary benefits and antioxidant properties. Aflatoxins and enniatins are common mycotoxins present in food and feed with an extended toxicity profile in humans and animals. Both types of substances reach a wide range of tissues and organs and have the capability to penetrate the blood brain barrier. Since carotenoids and mycotoxins have been reported to modify diverse mitochondrial processes individually, transcriptional in vitro studies on human epithelial cells ECV 304 were conducted to analyze the relative expression of 13 mitochondria related genes. ECV 304 cells were diff…

AflatoxinMitochondrial DNAAntioxidantmedicine.medical_treatmentAlzheimer Antioxidants Mycotoxicity Neurodegenerative diseases Carotenoids qPCR ECV 304MitochondrionToxicologyBlood–brain barrierAntioxidantsCell LineNOchemistry.chemical_compoundAflatoxinsCucurbitaDepsipeptidesHuman Umbilical Vein Endothelial CellsmedicineHumansECV 304MycotoxinMycotoxicityCarotenoidchemistry.chemical_classificationLS9_6Neurodegenerative diseasesfood and beveragesGeneral MedicineCarotenoidsIn vitroMitochondriaqPCRmedicine.anatomical_structureElectron Transport Chain Complex ProteinschemistryBiochemistryBlood-Brain BarrierAlzheimerFood Science
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Detection of mitochondrial electron chain carrier redox status by transhepatic light intensity during rat liver reperfusion.

2003

The aim of the study was to investigate mitochondrial electron transfer during rat liver reperfusion after cold storage and hypothermic machine perfusion. Livers from male Brown Norway rats were preserved (UW) for 10h either by cold storage (CS) or by hypothermic oxygenated perfusion extracorporal (HOPE). Transhepatic photometric analysis allowed determination of the redox status of mitochondrial cytochromes during preservation, rewarming and reperfusion. Mitochondrial electron chain carriers were inhibited at different sites with rotenone and cyanide in some experiments. reversed transcriptional polymerase chain reaction (RT-PCR) was performed after reperfusion concerning transcription of …

AnionsMaleTime FactorsCytochromeLightCold storageCaspase 3ElectronsDNA FragmentationMitochondrionGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundSuperoxidesAnimalsCaspase-9CryopreservationCyanidesbiologySuperoxideCaspase 3Reverse Transcriptase Polymerase Chain ReactionTumor Necrosis Factor-alphaJNK Mitogen-Activated Protein KinasesTemperatureNADH DehydrogenaseGeneral MedicineRotenoneDNAOrgan PreservationLipid MetabolismCaspase 9MitochondriaRatsCold TemperatureOxygenLight intensitychemistryBiochemistryElectron Transport Chain Complex ProteinsLiverCaspasesReperfusionbiology.proteinCytochromesLipid PeroxidationMitogen-Activated Protein KinasesGeneral Agricultural and Biological SciencesReactive Oxygen SpeciesOxidation-ReductionCryobiology
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