Search results for "interaction [hadron hadron]"

showing 10 items of 212 documents

The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates

2017

16 páginas, 7 figuras, 2 tablas

0301 basic medicineModels MolecularAdenosine Triphosphate / metabolismProtein ConformationScienceMalatesBacterial proteins/chemistry/metabolism/geneticsPlasma protein bindingBiologyModels BiologicalArticleConserved sequence03 medical and health sciencesAdenosine TriphosphateBacterial ProteinsAdenosine Triphosphate / chemistryDicarboxylic AcidsProtein Interaction Domains and MotifsAmino Acid SequenceKinase activityPhosphorylationLactobacilus cassei/classification/physiologyMalates/metabolismPromoter Regions GeneticConserved SequencePhylogenyMultidisciplinaryQAutophosphorylationfungiRTwo-component regulatory systemResponse regulatorLacticaseibacillus casei030104 developmental biologyBiochemistryMedicineModelsbiologica/moleculPhosphorylationCconserved secuenceProtein MultimerizationBinding domainProtein BindingScientific Reports
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Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor

2017

Bacteria use membrane-integral sensor histidine kinases (HK) to perceive stimuli and transduce signals from the environment to the cytosol. Information on how the signal is transmitted across the membrane by HKs is still scarce. Combining both liquid- and solid-state NMR, we demonstrate that structural rearrangements in the extracytoplasmic, citrate-sensing Per-Arnt-Sim (PAS) domain of HK CitA are identical for the isolated domain in solution and in a longer construct containing the membrane-embedded HK and lacking only the kinase core. We show that upon citrate binding, the PAS domain contracts, resulting in a shortening of the C-terminal β-strand. We demonstrate that this contraction of t…

0301 basic medicineModels MolecularHistidine Kinase030106 microbiologyMolecular ConformationCitric Acid03 medical and health sciencesStructure-Activity RelationshipBacterial ProteinsPAS domainProtein Interaction Domains and MotifsAmino Acid SequenceHistidineMultidisciplinaryChemistryKinaseHistidine kinaseGeobacillusMembrane ProteinsBiological SciencesTransmembrane proteinCell biologyCytosolHelixSignal transductionProtein BindingSignal Transduction
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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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Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE

2017

17 p.-8 fig.

0301 basic medicineProtein ConformationDimerlcsh:MedicineMolecular DynamicsCrystallography X-RayPhysical ChemistryBiochemistryDEAD-box RNA HelicasesMolecular dynamicschemistry.chemical_compoundComputational ChemistryNucleophileBiochemical Simulationslcsh:ScienceMultidisciplinaryCrystallographyChemistryOrganic CompoundsPhysicsEscherichia coli ProteinsCondensed Matter Physics3. Good healthPhysical sciencesChemistryCarbon-Sulfur LyasesBiochemistryCrystal StructureResearch ArticleChemical ElementsProtein subunitChemical physicschemistry.chemical_elementOxidative phosphorylationMolecular Dynamics Simulation03 medical and health sciencesThiolsEscherichia coliSolid State PhysicsProtein Interaction Domains and MotifsChemical BondingOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesComputational BiologyDimers (Chemical physics)Hydrogen BondingCell BiologySulfurAcceptorRedox sensitiveOxidative Stress030104 developmental biologyBiophysicslcsh:QProtein MultimerizationSulfur
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The latent geometry of the human protein interaction network

2017

Abstract Motivation A series of recently introduced algorithms and models advocates for the existence of a hyperbolic geometry underlying the network representation of complex systems. Since the human protein interaction network (hPIN) has a complex architecture, we hypothesized that uncovering its latent geometry could ease challenging problems in systems biology, translating them into measuring distances between proteins. Results We embedded the hPIN to hyperbolic space and found that the inferred coordinates of nodes capture biologically relevant features, like protein age, function and cellular localization. This means that the representation of the hPIN in the two-dimensional hyperboli…

0301 basic medicineStatistics and ProbabilityGeometric analysisComputer scienceHyperbolic geometrySystems biologyComplex systemContext (language use)GeometryBiochemistryProtein–protein interaction03 medical and health sciencesInteraction networkHumansProtein Interaction MapsRepresentation (mathematics)Cluster analysisMolecular BiologySystems BiologyHyperbolic spaceProteinsFunction (mathematics)Original PapersComputer Science ApplicationsComputational Mathematics030104 developmental biologyComputational Theory and MathematicsEmbeddingSignal transductionAlgorithmsSignal Transduction
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A Systematic Study of Dysregulated MicroRNA in Type 2 Diabetes Mellitus

2017

MicroRNAs (miRNAs) are small noncoding RNAs that modulate the cellular transcriptome at the post-transcriptional level. miRNA plays important roles in different disease manifestation, including type 2 diabetes mellitus (T2DM). Many studies have characterized the changes of miRNAs in T2DM, a complex systematic disease; however, few studies have integrated these findings and explored the functional effects of the dysregulated miRNAs identified. To investigate the involvement of miRNAs in T2DM, we obtained and analyzed all relevant studies published prior to 18 October 2016 from various literature databases. From 59 independent studies that met the inclusion criteria, we identified 158 dysregu…

0301 basic medicineSystematic surveytype 2 diabetes mellitussystematic study030209 endocrinology & metabolismDiseaseBioinformaticsCatalysisArticleInorganic ChemistryTranscriptomelcsh:Chemistry03 medical and health sciences0302 clinical medicineDiabetes mellitusmiRNA-mRNA interaction networkmicroRNAmedicineHumansGene Regulatory NetworksRNA MessengerPhysical and Theoretical Chemistry10. No inequalityMolecular Biologylcsh:QH301-705.5SpectroscopyAdipocytokine Signaling PathwaymicroRNA; type 2 diabetes mellitus; miRNA-mRNA interaction network; systematic studymicroRNAbusiness.industryGene Expression ProfilingOrganic ChemistryType 2 Diabetes MellitusGeneral Medicinemedicine.diseaseComputer Science ApplicationsMicroRNAs030104 developmental biologyDiabetes Mellitus Type 2Gene Expression Regulationlcsh:Biology (General)lcsh:QD1-999Organ SpecificityRNA InterferenceDisease manifestationbusinessTranscriptomeSignal TransductionInternational Journal of Molecular Sciences
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Neuronal Cytoskeleton in Intellectual Disability: From Systems Biology and Modeling to Therapeutic Opportunities

2021

Intellectual disability (ID) is a pathological condition characterized by limited intellectual functioning and adaptive behaviors. It affects 1–3% of the worldwide population, and no pharmacological therapies are currently available. More than 1000 genes have been found mutated in ID patients pointing out that, despite the common phenotype, the genetic bases are highly heterogeneous and apparently unrelated. Bibliomic analysis reveals that ID genes converge onto a few biological modules, including cytoskeleton dynamics, whose regulation depends on Rho GTPases transduction. Genetic variants exert their effects at different levels in a hierarchical arrangement, starting from the molecular lev…

0301 basic medicineactin cytoskeletonReview0302 clinical medicineBorderline intellectual functioningIntellectual disabilityDisabilità Intellettiva GTPasi CitoscheletroBiology (General)CytoskeletonSpectroscopyNeuronseducation.field_of_studysystems biologyCognitionGeneral MedicinePhenotypeComputer Science ApplicationsChemistryPhenotypeintellectual disabilitySignal TransductionBoolean modelingQH301-705.5NeurogenesisIn silicoSystems biologyPopulationBiologyCatalysismicrotubulesInorganic Chemistry03 medical and health sciencesmedicineAnimalsHumansPhysical and Theoretical ChemistryeducationQD1-999Molecular BiologyGTPase signalingsmall Rho GTPasesOrganic Chemistrypharmacological modulationprotein:protein interaction networkActin cytoskeletonmedicine.disease030104 developmental biologySynapsesneuronal networksNeuroscience030217 neurology & neurosurgery
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Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family

2017

AbstractWe introduce LytU, a short member of the lysostaphin family of zinc-dependent pentaglycine endopeptidases. It is a potential antimicrobial agent for S. aureus infections and its gene transcription is highly upregulated upon antibiotic treatments along with other genes involved in cell wall synthesis. We found this enzyme to be responsible for the opening of the cell wall peptidoglycan layer during cell divisions in S. aureus. LytU is anchored in the plasma membrane with the active part residing in the periplasmic space. It has a unique Ile/Lys insertion at position 151 that resides in the catalytic site-neighbouring loop and is vital for the enzymatic activity but not affecting the …

0301 basic medicineentsyymitantimicrobial compoundsPROTEINchemistry.chemical_compoundCatalytic DomainCELL-WALLBINDINGMultidisciplinaryACTIVE-SITEQRESISTANT STAPHYLOCOCCUS-AUREUSRHydrogen-Ion ConcentrationAnti-Bacterial AgentsZincBiochemistryMedicineHISTIDINESProtein BindingStaphylococcus aureusScienceenzymesBiologyCleavage (embryo)metalloproteinasesArticleCofactorBACILLUS-SUBTILISCell wallStructure-Activity Relationship03 medical and health sciencesEndopeptidasesProtein Interaction Domains and MotifsAmino Acid Sequencestaphylococciantimikrobiset yhdisteetBinding SitesLysostaphinCell MembraneActive siteIsothermal titration calorimetryPeriplasmic spaceVANCOMYCINstafylokokitmetalloproteinaasitMODEL030104 developmental biologyRESOLUTIONchemistryMutationProteolysisLysostaphinbiology.protein1182 Biochemistry cell and molecular biologyPeptidoglycanScientific Reports
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Dynamics of a Protein Interaction Network Associated to the Aggregation of polyQ-Expanded Ataxin-1

2020

Background: Several experimental models of polyglutamine (polyQ) diseases have been previously developed that are useful for studying disease progression in the primarily affected central nervous system. However, there is a missing link between cellular and animal models that would indicate the molecular defects occurring in neurons and are responsible for the disease phenotype in vivo. Methods: Here, we used a computational approach to identify dysregulated pathways shared by an in vitro and an in vivo model of ATXN1(Q82) protein aggregation, the mutant protein that causes the neurodegenerative polyQ disease spinocerebellar ataxia type-1 (SCA1). Results: A set of common dysregulated pathwa…

0301 basic medicinelcsh:QH426-470Ataxin 1Mice TransgenicNerve Tissue ProteinsProtein aggregationBlood–brain barrierblood-brain-barrierArticledrugspolyQ03 medical and health sciences0302 clinical medicineataxin-1Interaction networkIn vivoMutant proteinCerebellumGeneticsmedicineAnimalsGene Regulatory NetworksProtein Interaction MapsGenetics (clinical)NeuronsbiologypathwayGene Expression Profilingmedicine.diseaselcsh:Genetics030104 developmental biologymedicine.anatomical_structureGene Expression Regulationnetworkbiology.proteinSpinocerebellar ataxiaPeptidesNeuroscience030217 neurology & neurosurgeryFunction (biology)Genes
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Editorial: Protein Interaction Networks in Health and Disease

2016

The identification and annotation of protein-protein interactions (PPIs) is of great importance in systems biology. Big data produced from experimental or computational approaches allow not only the construction of large protein interaction maps but also expand our knowledge on how proteins build up molecular complexes to perform sophisticated tasks inside a cell. However, if we want to accurately understand the functionality of these complexes, we need to go beyond the simple identification of PPIs. We need to know when and where an interaction happens in the cell and also understand the flow of information through a protein interaction network. Another perspective of the research on PPI n…

0301 basic medicineprotein networkdiseasePhysiologySystems biologyCellular homeostasissystems biologyComputational biologyprotein functionBiologyProteomicscomputer.software_genreprotein interactionsInteractomeProtein–protein interaction03 medical and health sciences030104 developmental biologyHuman interactomeInteraction networkGeneticsMolecular MedicineData miningcomputerGenetics (clinical)Biological networkFrontiers in Genetics
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