Search results for " Tertiary"

showing 10 items of 349 documents

Identification of Cysteine Residues in Human Cationic Amino Acid Transporter hCAT-2A That Are Targets for Inhibition by N-Ethylmaleimide

2013

In most cells, cationic amino acids such as l-arginine, l-lysine, and l-ornithine are transported by cationic (CAT) and y(+)L (y(+)LAT) amino acid transporters. In human erythrocytes, the cysteine-modifying agent N-ethylmaleimide (NEM) has been shown to inhibit system y(+) (most likely CAT-1), but not system y(+)L (Devés, R., Angelo, S., and Chávez, P. (1993) J. Physiol. 468, 753-766). We thus wondered if sensitivity to NEM distinguishes generally all CAT and y(+)LAT isoforms. Transport assays in Xenopus laevis oocytes established that indeed all human CATs (including the low affinity hCAT-2A), but neither y(+)LAT isoform, are inhibited by NEM. hCAT-2A inhibition was not due to reduced tran…

Gene isoformMutantMutation MissenseXenopusBiologyBiochemistryXenopus laevischemistry.chemical_compoundMembrane BiologyAnimalsHumansheterocyclic compoundsCysteineAmino acid transporterEnzyme InhibitorsMolecular Biologychemistry.chemical_classificationN-EthylmaleimideTransporterCell Biologybiology.organism_classificationMolecular biologyProtein Structure TertiaryAmino acidAmino Acid SubstitutionchemistryBiochemistryEthylmaleimideOocytesAmino Acid Transport Systems BasicCysteineJournal of Biological Chemistry
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Mediterranean diet adherence and synergy with acute myocardial infarction and its determinants: A multicenter case-control study in Italy

2018

Background Cardiovascular diseases are the leading causes of mortality and morbidity in Western countries. The possible synergistic effect of poor adherence to a Mediterranean diet (MD) and other risk factors for acute myocardial infarction (AMI) such as hypertension, cholesterol, ever smoker, BMI> 25, diabetes, has not been deeply studied. Design Case-control study. Methods Patients with first AMI and controls from four tertiary referral Italian centers were screened for enrolment. Dietary information was collected through a questionnaire and a MD adherence score was calculated. Physical activity and smoking habits were also registered. The Synergy Index was calculated according to Rothman…

Genetics and Molecular Biology (all)MaleMultivariate analysisMediterranean dietTertiary Care CenterMyocardial Infarctionlcsh:MedicineBlood PressureMediterranean030204 cardiovascular system & hematologyPathology and Laboratory MedicineDiet MediterraneanVascular MedicineBiochemistryGeographical locationsTertiary Care CentersHabitschemistry.chemical_compoundEndocrinology0302 clinical medicineRisk FactorsSurveys and QuestionnairesMedicine and Health SciencesSmoking HabitsSurveys and Questionnaire030212 general & internal medicineMyocardial infarctionlcsh:ScienceMultidisciplinarySmokingMiddle AgedEuropeHyperlipidemiaItalyResearch DesignSettore MED/42HypertensionFemaleCase-Control StudieHumanResearch Articlemedicine.medical_specialtyAged; Case-Control Studies; Feeding Behavior; Female; Humans; Hypertension; Italy; Male; Middle Aged; Myocardial Infarction; Risk Factors; Smoking; Surveys and Questionnaires; Tertiary Care Centers; Diet Mediterranean; Patient ComplianceReferralEndocrine DisordersSmoking habitHypercholesterolemiaCardiologyResearch and Analysis Methods03 medical and health sciencesSigns and SymptomsDiagnostic MedicineDiabetes mellitusInternal medicineDiabetes MellitusAged; Case-Control Studies; Feeding Behavior; Female; Humans; Hypertension; Italy; Male; Middle Aged; Myocardial Infarction; Risk Factors; Smoking; Surveys and Questionnaires; Tertiary Care Centers; Diet Mediterranean; Patient Compliance; Biochemistry Genetics and Molecular Biology (all); Agricultural and Biological Sciences (all)medicineHumansEuropean UnionNutritionAgedBehaviorCholesterolbusiness.industryRisk Factorlcsh:RCase-control studyBiology and Life SciencesFeeding Behaviormedicine.diseaseDietAgricultural and Biological Sciences (all)chemistryMetabolic DisordersCase-Control StudiesPatient Compliancelcsh:QPeople and placesbusinessPLOS ONE
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Accelerated Evolution of Fetuin-A (FETUA, also AHSG) is Driven by Positive Darwinian Selection, not GC-Biased Gene Conversion

2009

article i nfo Human Fetuin-A (FETUA, also termed AHSG) is a serum protein composed of two cystatin-like domains D1 and D2 of together 235 amino acids (aa) and an unrelated domain D3 of 114 aa. Though the protein plays a role in diverse physiological and pathological processes, comparably little is known about sequence evolution of FETUA. We therefore analyzed its molecular evolution on the basis of coding sequences of 16 primate species. Ratios of non-synonymous to synonymous substitution rates (dn/ds= ω) suggest that a previously reported acceleration of sequence evolution of exon 7, which encodes domain D3, is driven by positive selection instead of neutral evolution. Irrespective of the …

GeneticsBase Sequencealpha-2-HS-GlycoproteinNull modelGene ConversionLocus (genetics)Blood ProteinsGeneral MedicineBiologyCleavage (embryo)Protein Structure TertiaryEvolution MolecularExonMolecular evolutionGeneticsAnimalsHumansGene conversionSelection GeneticCodonSynonymous substitutionNeutral theory of molecular evolutionGene
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Parkin and relatives: the RBR family of ubiquitin ligases

2004

Mutations in the parkin gene cause autosomal-recessive juvenile parkinsonism. Parkin encodes a ubiquitinprotein ligase characterized by having the RBR domain, composed of two RING fingers plus an IBR/DRIL domain. The RBR family is defined as the group of genes whose products contain an RBR domain. RBR family members exist in all eukaryotic species for which significant sequence data is available, including animals, plants, fungi, and several protists. The integration of comparative genomics with structural and functional data allows us to conclude that RBR proteins have multiple roles, not only in protein quality control mechanisms, but also as indirect regulators of transcription. A recent…

GeneticsComparative genomicschemistry.chemical_classificationDNA ligasebiologyPhysiologyUbiquitin-Protein LigasesParkinson DiseaseGenomicsParkinProtein Structure TertiaryUbiquitin ligaseProtein structureUbiquitinchemistryGeneticsbiology.proteinTranscriptional regulationAnimalsGenePhylogenyPhysiological Genomics
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Exploration of Evolutionary Relations between Protein Structures

2008

We describe a new method for the exploration of evolutionary relations between protein structures.

GeneticsProtein structureChemistryProtein domainProtein designProtein function predictionProtein engineeringSupersecondary structureComputational biologyProtein structure predictionProtein tertiary structure
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Methyl-CpG-binding proteins

2000

CpG methylation, the most common epigenetic modification of vertebrate genomes, is primarily associated with transcriptional repression. MeCP2, MBD1, MBD2, MBD3 and MBD4 constitute a family of vertebrate proteins that share the methyl-CpG-binding domain (MBD). The MBD, consisting of about 70 residues, possesses a unique alpha/beta-sandwich structure with characteristic loops, and is able to bind single methylated CpG pairs as a monomer. All MBDs except MBD4, an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1, form complexes with histone deacetylase. It has been established that MeCP2, MBD1 and MBD2 are involved in histone deacetylase-dependent repression and it i…

GeneticsTranscription GeneticChromosomal Proteins Non-HistoneMethyl-CpG-Binding Protein 2Molecular Sequence DataDNADNA MethylationBiologyBiochemistryProtein Structure TertiaryMethyl-CpG-binding domainDNA-Binding ProteinsRepressor ProteinsEpigenetics of physical exerciseHistone methyltransferaseDNA methylationHistone methylationHistone H2AAnimalsHumansHistone codeCpG IslandsAmino Acid SequenceGene SilencingCancer epigeneticsEuropean Journal of Biochemistry
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Specific and promiscuous functions of multiple DnaJ proteins in Synechocystis sp. PCC 6803

2011

Cyanobacterial genomes typically encode multiple Hsp70 (DnaK) and Hsp40 (DnaJ) chaperones, and in the genome of the cyanobacteriumSynechocystisPCC 6803, three DnaK proteins are encoded together with seven DnaJ proteins. While only two of the DnaJ proteins can complement the growth defect of anEscherichia coliΔdnaJstrain, only disruption of thednaJgenesll0897resulted in a growth defect at elevated temperatures. Based on the domain structure and the phenotype observed following disruption of the encoding gene, Sll0897 can be classified as a canonical heat-shock protein inSynechocystis. Furthermore, mostdnaJgenes could be deleted individually, whereas disruption of the gene encoding the DnaJ S…

Geneticsendocrine systembiologySynechocystisSynechocystisHSP40 Heat-Shock Proteinsbiology.organism_classificationDNAJ ProteinMicrobiologyGenomePhenotypeProtein Structure TertiaryProtein structureBacterial ProteinsMultigene FamilyDNAJA2DNAJB1GeneMicrobiology
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Thermal aggregation of glycated bovine serum albumin

2010

International audience; Aggregation and glycation processes in proteins have a particular interest in medicine fields and in food technology. Serum albumins are model proteins which are able to self-assembly in aggregates and also sensitive to a non-enzymatic glycation in cases of diabetes. In this work, we firstly reported a study on the glycation and oxidation effects on the structure of bovine serum albumin (BSA). The experimental approach is based on the study of conformational changes of BSA at secondary and tertiary structures by FTIR absorption and fluorescence spectroscopy, respectively. Secondly, we analysed the thermal aggregation process on BSA glycated with different glucose con…

Glycation End Products AdvancedGlycosylationHot TemperatureGlycoxidation02 engineering and technologyProtein aggregationBiochemistryProtein Structure SecondaryAnalytical Chemistrychemistry.chemical_compoundProtein structureGlycationSpectroscopy Fourier Transform InfraredScattering RadiationGlycated Serum AlbuminBovine serum albuminGlycation0303 health sciencesbiologyChemistryTryptophanSerum Albumin Bovine021001 nanoscience & nanotechnology3. Good healthSpectrophotometryProtein aggregation0210 nano-technologyOxidation-ReductionGlycosylationBiophysicsSerum albuminIn Vitro Techniques03 medical and health sciencesAnimalsMolecular BiologySerum Albumin030304 developmental biologyChromatographyAlbuminAlbuminLight scatteringSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein tertiary structureProtein Structure TertiaryKineticsFTIR spectroscopyGlucoseSpectrometry FluorescenceUnfolded Protein Responsebiology.proteinCattleProtein Multimerization[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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The inhibition of glycerol permeation through aquaglyceroporin-3 induced by mercury(II)

2016

Mercurial compounds are known to inhibit water permeation through aquaporins (AQPs). Although in the last years some hypotheses were proposed, the exact mechanism of inhibition is still an open question and even less is known about the inhibition of the glycerol permeation through aquaglyceroporins. Molecular dynamics (MD) simulations of human aquaporin-3 (AQP3) have been performed up to 200 ns in the presence of Hg2+ ions. For the first time, we have observed the unbiased passage of a glycerol molecule from the extracellular to cytosolic side. Moreover, the presence of Hg2+ ions covalently bound to Cys40 leads to a collapse of the aromatic/arginine selectivity filter (ar/R SF), blocking th…

Glycerol0301 basic medicineMolecular dynamicCell Membrane PermeabilityBiochemistryProtein Structure Secondarychemistry.chemical_compoundGLPFCOORDINATIONCRYSTALEscherichia coli ProteinsPermeationBiochemistryCovalent bondSettore CHIM/03 - Chimica Generale E InorganicaPhosphatidylcholinesCOMPLEXESProtein BindingSTRUCTURAL BASISCations DivalentPlasmodium falciparumAquaporinCYSTEINE-189Molecular Dynamics SimulationMolecular dynamicsAquaporinsWATER CHANNELInorganic Chemistry03 medical and health sciencesEscherichia coliGlycerolExtracellularHumansMoleculePERMEABILITYProtein Structure QuaternaryAquaporin 3Binding SitesAQUAPORIN INHIBITIONWaterBiological TransportMembranes ArtificialAquaglyceroporinMercurySIMULATIONSProtein Structure TertiaryCytosolWater permeation030104 developmental biologyAquaglyceroporinschemistryStructural Homology ProteinBiophysicsGlycerol permeationJournal of Inorganic Biochemistry
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Role of the Netrin-like Domain of Procollagen C-Proteinase Enhancer-1 in the Control of Metalloproteinase Activity

2010

The netrin-like (NTR) domain is a feature of several extracellular proteins, most notably the N-terminal domain of tissue inhibitors of metalloproteinases (TIMPs), where it functions as a strong inhibitor of matrix metalloproteinases and some other members of the metzincin superfamily. The presence of a C-terminal NTR domain in procollagen C-proteinase enhancers (PCPEs), proteins that stimulate the activity of astacin-like tolloid proteinases, raises the possibility that this might also have inhibitory activity. Here we show that both long and short forms of the PCPE-1 NTR domain, the latter beginning at the N-terminal cysteine known to be critical for TIMP activity, show no inhibition, at …

Glycobiology and Extracellular MatricesMatrix metalloproteinaseBiochemistryBONE MORPHOGENETIC PROTEIN-1AdamalysinFIBRILLAR PROCOLLAGENSTolloid ProteinaseExtracellular Matrix Proteins0303 health sciencesADAMTSFRIZZLED-RELATED PROTEINS030302 biochemistry & molecular biologyTissue Inhibitor of Metalloproteinases11 Medical And Health SciencesALPHA-CONVERTING-ENZYMEI PROCOLLAGENADAM ProteinsExtracellular MatrixPLASMINOGEN ACTIVATIONBiochemistryCollagen03 Chemical SciencesLife Sciences & BiomedicineProcollagenBiochemistry & Molecular BiologyTERMINAL DOMAINTolloid-Like MetalloproteinasesADAMTSBiologyBone morphogenetic protein 1Cell Line03 medical and health sciencesDisintegrinHumansHUMAN TISSUE INHIBITORMatrix MetalloproteinaseMolecular BiologyGlycoproteins030304 developmental biologyThrombospondinScience & TechnologyHeparinADAMCell Biology06 Biological SciencesMATRIX-METALLOPROTEINASESProtein Structure TertiaryADAM ProteinsProcollagen peptidaseSULFATED GLYCOSAMINOGLYCANSEnzymologybiology.proteinJournal of Biological Chemistry
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