Search results for "Interaction domains"

showing 10 items of 46 documents

Interaction between Longitudinal Shear and Transverse Bending in Prestressed Concrete Box Girders

2017

In box girder bridges, the quantity and distribution of reinforcement to be put in concrete elements of sections can be evaluated only by considering the deformation of the cross section in addition to the longitudinal analysis of the static scheme, establishing the entire state of stress of box sections. This leads to a need to evaluate the interaction between internal forces obtained by the global analysis and the ones obtained by the local analysis of the cross sections. The frame effect implies the elastic deformation of slabs and webs, whereas eccentrically applied loads lead to cross-section distortion with the loss of the box shape. Hence, the reinforcement is strongly influenced by …

EngineeringTransverse bendingBox girders bridges0211 other engineering and technologies020101 civil engineering02 engineering and technologyPlasticity0201 civil engineeringlaw.inventionPrestressed concreteInteraction domainslawGirder021105 building & constructionReinforcementCivil and Structural Engineeringbusiness.industryBox girders bridges; Interaction domains; Prestressed concrete; Shear; Thin-walled section; Transverse bending; Web; Civil and Structural Engineering; Building and ConstructionShearBox girderBuilding and ConstructionStructural engineeringWebSettore ICAR/09 - Tecnica Delle CostruzioniThin-walled sectionStress resultantsBending momentPrestressed concreteDeformation (engineering)businessJournal of Bridge Engineering
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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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A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model

2014

Chaperonins mediate protein folding in a cavity formed by multisubunit rings. The human CCT has eight non-identical subunits and the His147Arg mutation in one subunit, CCT5, causes neuropathy. Knowledge is scarce on the impact of this and other mutations upon the chaperone's structure and functions. To make progress, experimental models must be developed. We used an archaeal mutant homolog and demonstrated that the His147Arg mutant has impaired oligomeric assembly, ATPase activity, and defective protein homeostasis functions. These results establish for the first time that a human chaperonin gene defect can be reproduced and studied at the molecular level with an archaeal homolog. The major…

Models MolecularProtein FoldingProtein ConformationProtein subunitMutantMolecular Sequence Datahuman CCT5 gene mutation molecular dynamics neuropathy archaeal modelSequence alignmentGene mutationBiologyArticleChaperonin03 medical and health sciences0302 clinical medicineProtein structureHumansProtein Interaction Domains and MotifsAmino Acid Sequence030304 developmental biologyGenetics0303 health sciencesMultidisciplinarySettore BIO/16 - Anatomia UmanaArchaeaSettore CHIM/08 - Chimica FarmaceuticaChaperone (protein)Mutationbiology.proteinThermodynamicsProtein foldingProtein MultimerizationSequence Alignment030217 neurology & neurosurgeryChaperonin Containing TCP-1
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The Protein Structure Context of PolyQ Regions.

2016

Proteins containing glutamine repeats (polyQ) are known to be structurally unstable. Abnormal expansion of polyQ in some proteins exceeding a certain threshold leads to neurodegenerative disease, a symptom of which are protein aggregates. This has led to extensive research of the structure of polyQ stretches. However, the accumulation of contradictory results suggests that protein context might be of importance. Here we aimed to evaluate the structural context of polyQ regions in proteins by analysing the secondary structure of polyQ proteins and their homologs. The results revealed that the secondary structure in polyQ vicinity is predominantly random coil or helix. Importantly, the region…

Models MolecularProtein Conformation alpha-HelicalProtein Structure ComparisonProtein StructureSaccharomyces cerevisiae ProteinsGlutaminelcsh:MedicineNerve Tissue ProteinsSaccharomyces cerevisiaePlant ScienceResearch and Analysis MethodsBiochemistryPlant Roots570 Life sciencesDatabase and Informatics MethodsProtein Structure DatabasesMacromolecular Structure AnalysisHumansProtein Interaction Domains and MotifsAmino AcidsDatabases ProteinProtein Interactionslcsh:ScienceMolecular BiologyMediator ComplexOrganic CompoundsPlant AnatomyAcidic Amino AcidsOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesProteinsRoot StructureChemistryBiological DatabasesProtein-Protein InteractionsPhysical Scienceslcsh:QStructural ProteinsProtein Structure DeterminationPeptidesResearch Article570 BiowissenschaftenPLoS ONE
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Bending-Shear interaction domains for externally prestressed concrete girders

2013

In prestressed concrete structures, the evaluation of the safety level is generally carried out by separating the bending moment strength and the shear force capacity. Actually interaction between bending moment (M) and shear force (V) can have significant consequences on evaluations in service life, especially when the ultimate limit state (ULS) is considered. In this paper, the M-V interaction is addressed for prestressed concrete girders, in the cases of both bonded and unbonded prestressing tendons. It can be demonstrated, by drawing the interaction domains (M-V), that a significant reduction of the safety level has to be considered when shear force is evaluated together with bending mo…

EngineeringArticle SubjectShear forcebending moment-shear interaction; limit state; strength domain; external prestressing; box girderexternal prestressingshearlimit statelaw.inventionPrestressed concretelawGirderInteraction domains; bending; shear; prestressingLimit state designGeotechnical engineeringShear and moment diagramCivil and Structural Engineeringstrength domainbusiness.industrybox girderStructural engineeringbendingStress fieldSettore ICAR/09 - Tecnica Delle CostruzioniShear (geology)lcsh:TA1-2040Bending momentprestressingInteraction domainlcsh:Engineering (General). Civil engineering (General)businessbending moment-shear interaction
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Evolutionary conserved role of eukaryotic translation factor eIF5A in the regulation of actin-nucleating formins

2017

AbstractElongation factor eIF5A is required for the translation of consecutive prolines, and was shown in yeast to translate polyproline-containing Bni1, an actin-nucleating formin required for polarized growth during mating. Here we show that Drosophila eIF5A can functionally replace yeast eIF5A and is required for actin-rich cable assembly during embryonic dorsal closure (DC). Furthermore, Diaphanous, the formin involved in actin dynamics during DC, is regulated by and mediates eIF5A effects. Finally, eIF5A controls cell migration and regulates Diaphanous levels also in mammalian cells. Our results uncover an evolutionary conserved role of eIF5A regulating cytoskeleton-dependent processes…

0301 basic medicineFluorescent Antibody Techniquelcsh:Medicinemacromolecular substancesBiologyArticleMiceEukaryotic cells03 medical and health sciencesEukaryotic translationCell MovementPeptide Initiation FactorsCitosqueletProtein biosynthesisAnimalsProtein Interaction Domains and Motifslcsh:ScienceCytoskeletonActinMultidisciplinaryCèl·lules eucariotesMicrofilament Proteinsfungilcsh:RGene Expression Regulation DevelopmentalRNA-Binding ProteinsTranslation (biology)Biological EvolutionActinsDorsal closureCell biologyElongation factor030104 developmental biologyProtein BiosynthesisForminsMutationbiology.proteinDrosophilalcsh:QEIF5AScientific Reports
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The cytoplasmic PASC domain of the sensor kinase DcuS of Escherichia coli : role in signal transduction, dimer formation, and DctA interaction

2013

The cytoplasmic PAS(C) domain of the fumarate responsive sensor kinase DcuS of Escherichia coli links the transmembrane to the kinase domain. PAS(C) is also required for interaction with the transporter DctA serving as a cosensor of DcuS. Earlier studies suggested that PAS(C) functions as a hinge and transmits the signal to the kinase. Reorganizing the PAS(C) dimer interaction and, independently, removal of DctA, converts DcuS to the constitutive ON state (active without fumarate stimulation). ON mutants were categorized with respect to these two biophysical interactions and the functional state of DcuS: type I-ON mutations grossly reorganize the homodimer, and decrease interaction with Dct…

PAS domainDicarboxylic Acid TransportersModels MolecularfumarateProtein ConformationEscherichia coli ProteinsDNA Mutational AnalysisDctAModels Biological570 Life sciencessignal transduction.Escherichia coliProtein Interaction Domains and MotifsProtein MultimerizationDcuS sensor kinaseProtein KinasesOriginal ResearchSignal Transduction570 Biowissenschaften
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Evaluation of web reinforcements in prestressed concrete box girders through shear-transverse bending domains

2020

In concrete box girders, the amount and distribution of reinforcements in the webs have to be estimated considering the local effects due to eccentric external loads and cross-sectional distortion and not only the global effect due to the resultant forces of a longitudinal analysis: shear, torsion and bending. This work presents an analytical model that allows designers to take into account the interaction of all these effects, global and local, for the determination of the reinforcements. The model is based on the theory of stress fields and it has been compared to a 3D finite element analysis, in order to validate the interaction domains. The results show how the proposed analytical mode…

thin-walled section0211 other engineering and technologies020101 civil engineeringbox girders bridges; interaction domains; prestressed concrete; shear; thin-walled section; transverse bending; web reinforcement02 engineering and technologyshear0201 civil engineeringlaw.inventionPrestressed concretelawGirder021105 building & constructionbox girders bridgesReinforcementCivil and Structural Engineeringinteraction domainsbusiness.industryprestressed concreteweb reinforcementtransverse bendingBuilding and ConstructionStructural engineeringSettore ICAR/09 - Tecnica Delle CostruzioniShear (geology)Transverse shear deformationbusinessGeology
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rbFOX1/MBNL1 competition for CCUG RNA repeats binding contributes to myotonic dystrophy type 1/type 2 differences

2018

Myotonic dystrophy type 1 and type 2 (DM1, DM2) are caused by expansions of CTG and CCTG repeats, respectively. RNAs containing expanded CUG or CCUG repeats interfere with the metabolism of other RNAs through titration of the Muscleblind-like (MBNL) RNA binding proteins. DM2 follows a more favorable clinical course than DM1, suggesting that specific modifiers may modulate DM severity. Here, we report that the rbFOX1 RNA binding protein binds to expanded CCUG RNA repeats, but not to expanded CUG RNA repeats. Interestingly, rbFOX1 competes with MBNL1 for binding to CCUG expanded repeats and overexpression of rbFOX1 partly releases MBNL1 from sequestration within CCUG RNA foci in DM2 muscle ce…

0301 basic medicineModels MolecularProtein Conformation alpha-Helical[SDV]Life Sciences [q-bio]General Physics and AstronomyGene ExpressionRNA-binding proteinCrystallography X-Raychemistry.chemical_compoundMOLECULAR-BASISGene expressionMBNL1Myotonic DystrophyComputingMilieux_MISCELLANEOUSMultidisciplinaryCHLORIDE CHANNELQRNA-Binding ProteinsRecombinant Proteins3. Good healthCell biologyCONGENITAL HEART-DISEASEDrosophila melanogasterThermodynamicsSKELETAL-MUSCLERNA Splicing FactorsCUG REPEATSProtein BindingRNA Splicing Factorsmusculoskeletal diseasesSTEADY-STATEcongenital hereditary and neonatal diseases and abnormalitiesScienceRBFOX1BiologyMyotonic dystrophyBinding CompetitiveGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesmedicineEscherichia coliAnimalsHumansProtein Interaction Domains and MotifsBinding siteNucleotide MotifsMuscle SkeletalSPLICING REGULATOR RBFOX2MUSCLEBLIND PROTEINSBinding SitesPRE-MESSENGER-RNARNAGeneral Chemistrymedicine.diseaseDisease Models AnimalKinetics030104 developmental biologychemistryTRIPLET REPEATRNAProtein Conformation beta-Strand3111 Biomedicine
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Identification of the integrin-binding site on coagulation factor VIIa required for proangiogenic PAR2 signaling.

2018

The tissue factor (TF) pathway serves both hemostasis and cell signaling, but how cells control these divergent functions of TF remains incompletely understood. TF is the receptor and scaffold of coagulation proteases cleaving protease-activated receptor 2 (PAR2) that plays pivotal roles in angiogenesis and tumor development. Here we demonstrate that coagulation factor VIIa (FVIIa) elicits TF cytoplasmic domain-dependent proangiogenic cell signaling independent of the alternative PAR2 activator matriptase. We identify a Lys-Gly-Glu (KGE) integrin-binding motif in the FVIIa protease domain that is required for association of the TF-FVIIa complex with the active conformer of integrin β1. A po…

0301 basic medicineCell signalingImmunologyIntegrinNeovascularization PhysiologicFactor VIIa030204 cardiovascular system & hematologyBiochemistryThromboplastinThrombosis and Hemostasis03 medical and health sciencesTissue factorMice0302 clinical medicineAnimalsHumansReceptor PAR-2Protein Interaction Domains and MotifsProtein Interaction MapsProtein kinase ACells CulturedIntegrin bindingBinding SitesbiologyChemistryIntegrin beta1Cell BiologyHematologyCell biologyCrosstalk (biology)030104 developmental biologyADP-Ribosylation Factor 6biology.proteinNIH 3T3 CellsPhosphorylationSignal transductionProtein BindingSignal TransductionBlood
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