Search results for "adenosine"

showing 10 items of 542 documents

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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Design, Synthesis, and Biological Evaluation of 3,4-Diarylmaleimides as Angiogenesis Inhibitors

2006

The new analogue 2 of combretastatin A-4 was discovered to be an inhibitor of tubulin polymerization with an IC50 of 7.6 microM and reduced angiogenesis in the in vivo chick embryo model. Interestingly, in a series of 2,3-diarylmaleimides closely related to this lead, no other compound was found to be active in the tubulin polymerization assay. However, by screening in the in vivo chick embryo assay 10 was identified as a potent angiogenesis inhibitor indicating an alternative target. Indeed, molecular modeling studies suggest a reasonable binding mode of 10 at the ATP-binding site of the model kinase CDK2. Motivated by these results, analogues of 10 were screened for inhibitory activity in…

Models MolecularIndolesanimal structuresAngiogenesisAngiogenesis InhibitorsChick EmbryoIn Vitro TechniquesMaleimidesStructure-Activity Relationshipchemistry.chemical_compoundAdenosine TriphosphateIn vivoDrug DiscoveryAnimalsStructure–activity relationshipPyrrolesBinding siteCombretastatinBinding SitesbiologyChemistryKinaseCyclin-dependent kinase 2Vascular Endothelial Growth Factor Receptor-2Angiogenesis inhibitorBiochemistryDrug Designbiology.proteinMolecular MedicineJournal of Medicinal Chemistry
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Effect of ATP Binding and Hydrolysis on Dynamics of Canine Parvovirus NS1▿ †

2010

ABSTRACT The replication protein NS1 is essential for genome replication and protein production in parvoviral infection. Many of its functions, including recognition and site-specific nicking of the viral genome, helicase activity, and transactivation of the viral capsid promoter, are dependent on ATP. An ATP-binding pocket resides in the middle of the modular NS1 protein in a superfamily 3 helicase domain. Here we have identified key ATP-binding amino acid residues in canine parvovirus (CPV) NS1 protein and mutated amino acids from the conserved A motif (K406), B motif (E444 and E445), and positively charged region (R508 and R510). All mutations prevented the formation of infectious viruse…

Models MolecularParvovirus CaninevirusesImmunologyMolecular Sequence DataPlasma protein bindingViral Nonstructural ProteinsMicrobiologyCell Linechemistry.chemical_compoundAdenosine TriphosphateDogsVirologyAnimalsAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisDNA replicationHelicaseFluorescence recovery after photobleachingFusion proteinMolecular biologyGenome Replication and Regulation of Viral Gene ExpressionProtein Structure TertiaryViral replicationchemistryBiochemistryAmino Acid SubstitutionInsect Sciencebiology.proteinCatsMutagenesis Site-DirectedSequence AlignmentDNAProtein Binding
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A3 adenosine receptor: Homology modeling and 3D-QSAR studies

2012

Adenosine receptors (AR) belong to the superfamily of G-protein-coupled receptors (GPCRs). They are divided into four subtypes (A1, A2A, A2B, and A3) [1], and can be distinguished on the basis of their distinct molecular structures, distinct tissues distribution, and selectivity for adenosine analogs [2,3]. The hA3R, the most recently identified adenosine receptor, is involved in a variety of intracellular signaling pathways and physiological functions [4]. Expression of A3R was reported to be elevated in cancerous tissues [5], and A3 antagonists have been proposed for therapeutic treatments of cancer. The recent literature availability of crystal structure of hA2A adenosine receptor (PDB c…

Models MolecularQuantitative structure–activity relationshipReceptor Adenosine A2AAdenosine A3 Receptor AntagonistsQuantitative Structure-Activity RelationshipComputational biologyBiologyPharmacologyDrug DiscoveryMolecular dynamics simulationMaterials ChemistrymedicineHumansAmino Acid SequenceHomology modelingPhysical and Theoretical ChemistryReceptorA3 INHIBITORS HOMOLOGY MODELING 3D-QSARSpectroscopyG protein-coupled receptorA3 ReceptorBinding SitesTriazinesReceptor Adenosine A3Intracellular Signaling Peptides and ProteinsTriazolesA3 ADENOSINE RECEPTORComputer Graphics and Computer-Aided DesignAdenosine receptorAdenosineSettore CHIM/08 - Chimica FarmaceuticaPharmacophoresHomology modellingPharmacophoreProtein Bindingmedicine.drug
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Inside the Hsp90 inhibitors binding mode through induced fit docking

2009

Abstract During the last few decades, the development of new anticancer strategies had to face the instability of many tumors, occurring when the genetic plasticity of cells produces new drug-resistant cancers. It has been shown that a chaperone protein, heat shock protein 90 (Hsp90), is one of the fundamental factors involved in the cell response to stresses, and its role in many biochemical pathways has been demonstrated. Thus, the inhibition of Hsp90 represents a new target of antitumor therapy, since it may influence many specific signaling pathways. The natural antibiotic Geldanamycin is the first Hsp90 inhibitor that has been identified. Nevertheless, more potent and water-soluble sma…

Models MolecularStereochemistryLactams MacrocyclicMolecular Sequence DataComputational biologyCrystallography X-RayLigandsHsp90 inhibitorchemistry.chemical_compoundAdenosine TriphosphateHeat shock proteinCatalytic DomainMaterials ChemistryBenzoquinonesAmino Acid SequenceHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistrySpectroscopyInduced fitBinding SitesbiologyMolecular StructureHeat shock proteinDrug discoveryActive siteGeldanamycinRadicicolComputer Graphics and Computer-Aided DesignSmall moleculeHsp90Settore CHIM/08 - Chimica FarmaceuticachemistryDocking (molecular)Molecular dockingbiology.proteinGeldanamicynSequence AlignmentProtein Binding
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