Search results for "Enos"

showing 10 items of 1576 documents

Aislamiento y caracterización de ABG1, un gen esencial del hongo patógeno oportunista Candida Albicans.

2005

Mediante el inmunorrastreo de una genoteca de expresión de Candida albicans con un anticuerpo policlonal específico de la forma micelial de dicho hongo (PAb anti-gt), se ha aislado un nuevo gen de este microorganismo. La represión del gen aislado ocasionó un severo defecto en la morfogénesis de C. albicans, caracterizado por la formación de cadenas de levaduras, de tamaño decreciente en dirección al extremo apical de la cadena, por lo que el gen fue denominado ABG1 (del inglés, "altered budding growth"), en base al fenotipo de crecimiento por gemación alterado observado en las cepas mutantes para dicho gen. La secuencia de aminoácidos de Abg1p, el producto del gen ABG1, presentó los porcent…

Microbiología.noneHongos patógenos.579F. FarmaciaEcología microbiana.Candida albicans.
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Electrical Pumping of Potassium Ions Against an External Concentration Gradient in a Biological Ion Channel

2013

We show experimentally and theoretically that significant currents can be obtained with a biological ion channel, the OmpF porin of Escherichia coli, using zero-average potentials as driving forces. The channel rectifying properties can be used to pump potassium ions against an external concentration gradient under asymmetric pH conditions. The results are discussed in terms of the ionic selectivity and rectification ratio of the channel. The physical concepts involved may be applied to separation processes with synthetic nanopores and to bioelectrical phenomena. (C) 2013 AIP Publishing LLC.

MicroorganismosPhysics and Astronomy (miscellaneous)PotassiumSeparaciónRatchetAnalytical chemistryBiophysicschemistry.chemical_elementRATCHETPotassium ionsFenómenos bioeléctricosIonSeparationBioelelectric phenomenaRectificationPORINVOLTAGEPotasiomicroorganismsIon channelChemistrypHNANOFLUIDIC DIODEBiomembrane transportIones positivosRECTIFICATIONOMPFTransporte de biomembranasCanales iónicosNanoporeSELECTIVITYPositive ionsFISICA APLICADAIon channelsPotassiumSelectivityConcentration gradientCommunication channelNANOPORES
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Mutations in KATNB1 Cause Complex Cerebral Malformations by Disrupting Asymmetrically Dividing Neural Progenitors

2014

SummaryExome sequencing analysis of over 2,000 children with complex malformations of cortical development identified five independent (four homozygous and one compound heterozygous) deleterious mutations in KATNB1, encoding the regulatory subunit of the microtubule-severing enzyme Katanin. Mitotic spindle formation is defective in patient-derived fibroblasts, a consequence of disrupted interactions of mutant KATNB1 with KATNA1, the catalytic subunit of Katanin, and other microtubule-associated proteins. Loss of KATNB1 orthologs in zebrafish (katnb1) and flies (kat80) results in microcephaly, recapitulating the human phenotype. In the developing Drosophila optic lobe, kat80 loss specificall…

Microtubule-associated proteinNeurogenesisNeuroscience(all)Cell CountKataninSpindle ApparatusBiologymedicine.disease_causeArticleMice03 medical and health sciences0302 clinical medicineNeural Stem CellsNeuroblastmedicineAnimalsDrosophila ProteinsHumansProgenitor cellZebrafishMitosisZebrafishAdenosine TriphosphatasesMutationGeneral NeuroscienceOptic Lobe NonmammalianBrainDendritesbiology.organism_classificationSpindle apparatusmedicine.anatomical_structureCentrosome030220 oncology & carcinogenesisCerebral malformationsMutationMicrocephalybiology.proteinDrosophilaNeuronKataninMicrotubule-Associated ProteinsNeuroscienceCell Division030217 neurology & neurosurgery
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Mitochondrial involvement in non-alcoholic steatohepatitis

2007

Non-alcoholic steatohepatitis (NASH) is an increasing recognized condition that may progress to end-stage liver disease. There are consistent evidences that mitochondrial dysfunction plays a central role in NASH whatever its origin. Mitochondria are the key controller of fatty acids removal and this is part of an intensive gene program that modifies hepatocytes to counteract the excessive fat storage. Mitochondrial dysfunction participates at different levels in NASH pathogenesis since it impairs fatty liver homeostasis and induces overproduction of ROS that in turn trigger lipid peroxidation, cytokines release and cell death. In this review we briefly recall the role of mitochondria in fat…

Mitochondrial DNAmedicine.medical_specialtyClinical BiochemistryBiologyMitochondrionModels BiologicalBiochemistryEnergy homeostasisAdenosine TriphosphateInternal medicinemedicineAnimalsHumansMolecular BiologyFatty liverGeneral MedicineTFAMLipid Metabolismmedicine.diseaseMitochondriaFatty LiverEndocrinologyMitochondrial respiratory chainMolecular MedicineSteatohepatitisSteatosisReactive Oxygen SpeciesMolecular Aspects of Medicine
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Nitric oxide inhibits the ATPase activity of the chaperone-like AAA+ ATPase CDC48, a target for S-nitrosylation in cryptogein signalling in tobacco c…

2012

NO has important physiological functions in plants, including the adaptative response to pathogen attack. We previously demonstrated that cryptogein, an elicitor of defence reaction produced by the oomycete Phytophthora cryptogea , triggers NO synthesis in tobacco. To decipher the role of NO in tobacco cells elicited by cryptogein, in the present study we performed a proteomic approach in order to identify proteins undergoing S-nitrosylation. We provided evidence that cryptogein induced the S-nitrosylation of several proteins and identified 11 candidates, including CDC48 (cell division cycle 48), a member of the AAA+ ATPase (ATPase associated with various cellular activities) family. In vit…

Models Molecular0106 biological sciencesProtein Conformation[SDV]Life Sciences [q-bio]Nicotiana tabacumATPaseMolecular Sequence DataCell Cycle ProteinsNitric Oxide01 natural sciencesBiochemistrycryptogeinFungal Proteins03 medical and health sciencesValosin Containing ProteinTobaccoAmino Acid Sequencenitric oxide (no)Molecular BiologyPlant Proteins030304 developmental biologyAdenosine Triphosphatases0303 health sciencesbiologyWalker motifsCell BiologyS-Nitrosylationcell division cycle 48 (cdc48)Biotic stressbiology.organism_classificationAAA proteinsProtein Structure TertiaryElicitorBiochemistryChaperone (protein)[SDE]Environmental Sciencesbiology.proteins-nitrosylationplant defence responses010606 plant biology & botanyBiochemical Journal
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Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1

2017

Coactivator associated arginine methyltransferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and methylates a range of proteins in eukaryotic cells. Overexpression of CARM1 is implicated in a number of cancers, and it is therefore seen as a potential therapeutic target. Peptide sequences derived from the well-defined CARM1 substrate poly(A)-binding protein 1 (PABP1) were covalently linked to an adenosine moiety as in the AdoMet cofactor to generate transition state mimics. These constructs were found to be potent CARM1 inhibitors and also formed stable complexes with the enzyme. High-resolution crystal structures of CARM1 in complex with these compounds co…

Models Molecular0301 basic medicineProtein-Arginine N-MethyltransferasesAdenosineMethyltransferaseCARM1ArgininePRMTCrystallography X-RayPoly(A)-Binding Protein ICofactorMice03 medical and health sciences0302 clinical medicineCatalytic DomainCoactivatorAnimalsAmino Acid Sequencetransition state mimicschemistry.chemical_classificationBinding SitesMultidisciplinarybiologycocrystal structuresActive siteProtein arginine N-methyltransferase; PRMT; CARM1; Transition state mimics; Cocrystal structuresMethylationBiological Sciencesprotein arginine N-methyltransferase030104 developmental biologyEnzymeCARM1chemistryBiochemistry030220 oncology & carcinogenesisbiology.proteinPeptidesProtein Binding
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Determination of enrichment factors for modified RNA in MeRIP experiments

2019

In the growing field of RNA modification, precipitation techniques using antibodies play an important role. However, little is known about their specificities and protocols are missing to assess their effectiveness. Here we present a method to assess enrichment factors after MeRIP-type pulldown experiments, here exemplified with a commercial antibody against N6-methyladenosine (m6A). Testing different pulldown and elution conditions, we measure enrichment factors of 4-5 using m6A-containing mRNAs against an unmodified control of identical sequence. Both types of mRNA carry 32P labels at different nucleotides, allowing their relative quantification in a mixture after digestion to nucleotides…

Models MolecularAdenosineAbsolute quantificationMethylationProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular BiologyViral Proteins03 medical and health sciencesAdenosine TriphosphateRNA modificationEscherichia coliHumansImmunoprecipitationProtein Interaction Domains and MotifsNucleotideRNA MessengerMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMessenger RNACell-Free SystemChemistryElution030302 biochemistry & molecular biologyRNADNA-Directed RNA PolymerasesBiochemistryImmunoglobulin GIsotope LabelingChromatography Thin LayerPhosphorus RadioisotopesProtein BindingMethods
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2,8-Diazido-ATP — a short-length bifunctional photoaffinity label for photoaffinity cross-linking of a stable F1 in ATP synthase (from thermophilic b…

1995

Abstract To demonstrate the direct interfacial position of nucleotide binding sites between subunits of proteins we have synthesized the bifunctional photoaffinity label 2,8-diazidoadenosine 5′-triphosphate (2,8-DiN3ATP). UV irradiation of the F1-ATPase (TF1) from the thermophilic bacterium PS3 in the presence of 2,8-DiN3ATP results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of α-β crosslinks. The results confirm an interfacial localization of all the nucleotide binding sites on TF1.

Models MolecularAzidesNucleotide binding siteLightStereochemistryImmunoblottingBiophysicsDirect interfacial localizationShort lengthBiochemistry8-azidoadenosine 5'-triphosphatechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyGeneticsNucleotide binding sitesBifunctionalMolecular BiologyThermophilic bacterium PS3Photoaffinity cross-linkingchemistry.chemical_classificationATP synthasebiologyBacteriaThermophileAffinity LabelsCell BiologyProton-Translocating ATPasesEnzymeCross-Linking ReagentsBiochemistrychemistrybiology.proteinF1-ATPase: Short-length bifunctional photoaffinity labelFEBS Letters
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Functional cysteine-less subunits of the transporter associated with antigen processing (TAP1 and TAP2) by de novo gene assembly

2002

AbstractWithin the adaptive immune system the transporter associated with antigen processing (TAP) plays a pivotal role in loading of peptides onto major histocompatibility (MHC) class I molecules. As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human TAP subunits by de novo gene synthesis, replacing all 19 cysteines in TAP1 and TAP2. After expression in TAP-deficient human fibroblasts, cysteine-less TAP1 and TAP2 are functional with respect to adenosine triphosphate (ATP)-dependent peptide transport and inhibition by ICP47 from herpes simplex virus. Cysteine-less TAP1 and TAP2 restore maturation and intracellular trafficking of MHC c…

Models MolecularBiophysicsBiological Transport ActiveBiologyMajor histocompatibility complexTransfectionBiochemistryCell Linechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyATP Binding Cassette Transporter Subfamily B Member 3Cysteine-scanning mutagenesisMHC class IGeneticsHumansCysteineATP Binding Cassette Transporter Subfamily B Member 2Molecular BiologyAntigen PresentationAntigen processingHistocompatibility Antigens Class ICell BiologyTransporter associated with antigen processingMolecular biologyRecombinant ProteinsCell biologyProtein SubunitschemistryAmino Acid SubstitutionAntigen processingPeptide transportMembrane proteinbiology.proteinAdenosine triphosphate-binding cassette transporterTAP2ATP-Binding Cassette TransportersTAP1Adenosine triphosphateFEBS Letters
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Mechanistic insights into the phosphoryl transfer reaction in cyclin-dependent kinase 2: a QM/MM study

2019

AbstractCyclin-dependent kinase 2 (CDK2) is an important member of the CDK family exerting its most important function in the regulation of the cell cycle. It catalyzes the transfer of the gamma phosphate group from an ATP (adenosine triphosphate) molecule to a Serine/Threonine residue of a peptide substrate. Due to the importance of this enzyme, and protein kinases in general, a detailed understanding of the reaction mechanism is desired. Thus, in this work the phosphoryl transfer reaction catalyzed by CDK2 was revisited and studied by means of hybrid quantum mechanics/molecular mechanics (QM/MM) calculations. Our results show that the base-assisted mechanism is preferred over the substrat…

Models MolecularComposite ParticlesProtein ConformationPhysical ChemistryBiochemistry01 natural sciencesSubstrate Specificitychemistry.chemical_compoundPhosphorylationPost-Translational ModificationFree Energy0303 health sciencesMultidisciplinarybiologyKinasePhysicsQChemical ReactionsRChemistryReaction DynamicsPhysical SciencesThermodynamicsMedicineProtonsResearch ArticleChemical ElementsAtomsStereochemistryScienceMolecular Dynamics Simulation010402 general chemistryMolecular mechanicsReactantsQM/MMStructure-Activity Relationship03 medical and health sciencesCyclin-dependent kinaseParticle PhysicsNuclear PhysicsNucleons030304 developmental biologyChemical BondingCyclin-Dependent Kinase 2Cyclin-dependent kinase 2Biology and Life SciencesProteinsActive siteHydrogen BondingTransition StateBond order0104 chemical sciencesOxygenModels Chemicalchemistrybiology.proteinQuantum TheoryAdenosine triphosphate
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