Search results for "PROTEIN-PROTEIN INTERACTION"

showing 10 items of 30 documents

Identifying Early Warning Signals for the Sudden Transition from Mild to Severe Tobacco Etch Disease by Dynamical Network Biomarkers

2019

This article belongs to the Special Issue The Complexity of the Potyviral Interaction Network.

0106 biological sciences0301 basic medicineComplex systemsSystems biologyPotyvirusDiseaseBiologytobacco etch virusSeverity of Illness Index01 natural sciencesArticlePlant VirusesTranscriptomeViral Proteins03 medical and health sciencesPlant-virus interactionpotyvirusGene Expression Regulation PlantVirologyProtein Interaction MappingTobaccoGene Regulatory NetworksProtein Interaction Mapscomplex systemsGenePlant DiseasesGeneticsTransition (genetics)Tobacco etch virusGene Expression Profilingsystems biologyDNBBiotic stressresponse to infectionbiology.organism_classificationplant-virus interactionTobacco etch virusphase transitionsprotein-protein interaction networks030104 developmental biologyInfectious DiseasesPhase transitionsHost-Pathogen InteractionsMutationBiomarker (medicine)BiomarkersSignal Transduction010606 plant biology & botanyViruses
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Gaining Insight into Exclusive and Common Transcriptomic Features Linked with Biotic Stress Responses in Malus

2017

Identifying key information in transcriptomic data is very important, especially when the “omic” study deals with plant responses to stresses in field conditions where a high number of variables and disturbing factors may affect the analysis. In this meta-analysis we collected 12 transcriptomic works in Malus in order to identify which key genes, proteins, gene categories are involved in general plant pathological conditions and those features linked with exclusive biotic stress responses. Those genes that are only related with molecular responses to pathogen attacks and those linked with other plant physiological processes were identified. A pipeline composed by pathway and gene set enrich…

0106 biological sciences0301 basic medicineMalusPlant ScienceComputational biologylcsh:Plant cultureErwinia01 natural sciencesTranscriptometranscriptomics03 medical and health sciencesSettore AGR/07 - Genetica AgrariaHeat shock proteinBotanylcsh:SB1-1110GeneTranscription factorOriginal Researchbiologybiotic stresses; Malus; meta-analysis; protein-protein interaction network; transcriptomicsfood and beveragesBiotic stressbiotic stressesbiology.organism_classificationmeta-analysisCrosstalk (biology)030104 developmental biologyMalusbiotic stresses Malus meta-analysis protein-protein interaction network transcriptomicsprotein-protein interaction network010606 plant biology & botanyFrontiers in Plant Science
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The roles of whole-genome and small-scale duplications in the functional specialization of Saccharomyces cerevisiae genes

2013

Researchers have long been enthralled with the idea that gene duplication can generate novel functions, crediting this process with great evolutionary importance. Empirical data shows that whole-genome duplications (WGDs) are more likely to be retained than small-scale duplications (SSDs), though their relative contribution to the functional fate of duplicates remains unexplored. Using the map of genetic interactions and the re-sequencing of 27 Saccharomyces cerevisiae genomes evolving for 2,200 generations we show that SSD-duplicates lead to neo-functionalization while WGD-duplicates partition ancestral functions. This conclusion is supported by: (a) SSD-duplicates establish more genetic i…

0106 biological sciencesCancer ResearchGenome evolutionlcsh:QH426-470ArabidopsisSaccharomyces cerevisiaeBiology01 natural sciencesGenomeDivergenceEvolution Molecular03 medical and health sciencesMolecular evolutionPhylogeneticsGene DuplicationGene duplicationGeneticsMads-Box genesBiologyMolecular BiologyGenePhylogenyGenetics (clinical)Ecology Evolution Behavior and Systematics030304 developmental biologySmall-scale duplicationsGeneticsEvolutionary BiologyEvolutionary Theory0303 health sciencesAdaptive conflictHuman evolutionary geneticsNull mutationsSaccharomyces cerevisiae genomeProtein-Protein interactionslcsh:GeneticsEvolutionary biologyDiversificationEpistasisMolecular evolutionWhole-genome duplicationsGenome FungalYeast genomeInteractions revealResearch Article010606 plant biology & botany
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The cytoprotective protein MANF promotes neuronal survival independently from its role as a GRP78 cofactor

2021

Mesencephalic astrocyte-derived neurotrophic factor (MANF) is an endoplasmic reticulum (ER)-stress-regulated protein exhibiting cytoprotective properties through a poorly understood mechanism in various in vitro and in vivo models of neuronal and non-neuronal damage. Although initially characterized as a secreted neurotrophic factor for midbrain dopamine neurons, MANF has recently gained more interest for its intracellular role in regulating the ER homeostasis, including serving as a cofactor of the chaperone glucose-regulated protein 78 (GRP78). We aimed for a better understanding of the neuroprotective mechanisms of MANF. Here we show for the first time that MANF promotes the survival of …

0301 basic medicineBiFC bimolecular fluorescence complementationMST microscale thermophoresisPDIA1 protein disulfide isomerase family A member 1ApoptosisNEUROTROPHIC FACTOR MANFEndoplasmic ReticulumBiochemistryprotein-protein interactionMiceBimolecular fluorescence complementationUPR unfolded protein responseENDOPLASMIC-RETICULUM STRESSMesencephalonNeurotrophic factorsInsulin-Secreting CellsProtein Interaction MappingBINDINGCOMPREHENSIVE RESOURCEATF6unfolded protein response (UPR)PDIA6 protein disulfide isomerase family A member 6PPIs protein-protein interactionsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsNPTN neuroplastinbiologyChemistryapoptosisunfolded protein responsedopamine neurons3. Good healthCell biologyGDNF glial cell line–derived neurotrophic factorIRE1-ALPHASBD substrate-binding domainendoplasmic reticulum stressMANF mesencephalic astrocyte-derived neurotrophic factorTm tunicamycinneuroprotectionResearch ArticleProtein BindingSignal TransductionGRP78Protein Disulfide-Isomerase FamilyCell SurvivalTH tyrosine hydroxylasePrimary Cell CultureSCG superior cervical ganglionProtein Disulfide-IsomerasesIRE1 inositol-requiring enzyme 1ER-STRESSER endoplasmic reticulum03 medical and health sciencesohjelmoitunut solukuolemaC-MANF C-terminal domain of MANFCSPs chemical shift perturbationsAnimalsHumansHSP70 Heat-Shock ProteinsNerve Growth FactorsNBD nucleotide-binding domainNMR nuclear magnetic resonanceMolecular Biology030102 biochemistry & molecular biologyBIPATF6Dopaminergic NeuronsGene Expression ProfilingBinding proteinneuronal cell deathDISSOCIATIONCell BiologyNEI nucleotide exchange inhibitorEmbryo MammalianadenosiinitrifosfaattiATPhermosolutmesencephalic astrocyte-derived neurotrophic factorprotein–protein interactionPERK protein kinase RNA-like ER kinaseHEK293 Cells030104 developmental biologyGene Expression RegulationChaperone (protein)Tg thapsigarginbiology.proteinUnfolded protein responseAP-MS affinity purification mass spectrometry1182 Biochemistry cell and molecular biologyGFP-SH SH-tagged GFPendoplasmic reticulum stress (ER stress)DA dopaminemesencephalic astrocyte-derived neurotrophic factor (MANF)proteiinitNeuroplastin
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CellMap visualizes protein-protein interactions and subcellular localization

2018

Many tools visualize protein-protein interaction (PPI) networks. The tool introduced here, CellMap, adds one crucial novelty by visualizing PPI networks in the context of subcellular localization, i.e. the location in the cell or cellular component in which a PPI happens. Users can upload images of cells and define areas of interest against which PPIs for selected proteins are displayed (by default on a cartoon of a cell). Annotations of localization are provided by the user or through our in-house database. The visualizer and server are written in JavaScript, making CellMap easy to customize and to extend by researchers and developers.

0301 basic medicineBioinformaticssubcellular locationContext (language use)BiologyJavaScriptGeneral Biochemistry Genetics and Molecular BiologyChemical Biology of the CellProtein–protein interactionprotein-protein interaction03 medical and health sciencesUploadHuman–computer interactionGeneral Pharmacology Toxicology and Pharmaceuticscomputer.programming_languagebiological visualization030102 biochemistry & molecular biologyGeneral Immunology and MicrobiologySoftware Tool ArticleNoveltyArticlesGeneral MedicineSubcellular localizationddc:ComputingMethodologies_PATTERNRECOGNITION030104 developmental biologyNeurosciencecomputerF1000Research
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Repurposing of Drugs Targeting YAP-TEAD Functions

2018

Drug repurposing is a fast and consolidated approach for the research of new active compounds bypassing the long streamline of the drug discovery process. Several drugs in clinical practice have been reported for modulating the major Hippo pathway’s terminal effectors, namely YAP (Yes1-associated protein), TAZ (transcriptional co-activator with PDZ-binding motif) and TEAD (transcriptional enhanced associate domains), which are directly involved in the regulation of cell growth and tissue homeostasis. Since this pathway is known to have many cross-talking phenomena with cell signaling pathways, many efforts have been made to understand its importance in oncology. Moreover, this could be rele…

0301 basic medicineCell signalingCell signalingCancer ResearchProtein-protein interactionsHippo pathwayDrug repurposingprotein-protein interactionsComputational biologyReviewBiologylcsh:RC254-28203 medical and health sciencesYAP-TEAD disruptioncell signalingRepurposingTissue homeostasisHippo signaling pathwaydrug repurposingEffectorCell growthDrug discoveryYap-tead disruptionlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensDrug repositioning030104 developmental biologyOncologyCell signaling; Drug repurposing; Hippo pathway; Protein-protein interactions; Yap-tead disruption; Oncology; Cancer ResearchCancers
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Identifying Host Molecular Features Strongly Linked With Responses to Huanglongbing Disease in Citrus Leaves

2018

© 2018 Balan, Ibáñez, Dandekar, Caruso and Martinelli. A bioinformatic analysis of previously published RNA-Seq studies on Huanglongbing (HLB) response and tolerance in leaf tissues was performed. The aim was to identify genes commonly modulated between studies and genes, pathways and gene set categories strongly associated with this devastating Citrus disease. Bioinformatic analysis of expression data of four datasets present in NCBI provided 46–68 million reads with an alignment percentage of 72.95–86.76%. Only 16 HLB-regulated genes were commonly identified between the three leaf datasets. Among them were key genes encoding proteins involved in cell wall modification such as CESA8, pecti…

0301 basic medicineHuanglongbing HLB citrus protein–protein interaction network transcriptomics RNA-SeqPlant BiologyHuanglongbingRNA-SeqPlant Sciencelcsh:Plant cultureBiologycitrusTranscriptometranscriptomics03 medical and health sciencesExpansinSettore AGR/07 - Genetica AgrariaHeat shock proteinGenetics2.1 Biological and endogenous factorslcsh:SB1-1110RNA-SeqAetiologyGeneTranscription factorOriginal Research2. Zero hungerGeneticsHuanglongbing; HLB; citrus; protein–protein interaction network; transcriptomics; RNA-SeqPectinesteraseSettore AGR/03 - Arboricoltura Generale E Coltivazioni ArboreeHLB030104 developmental biologyPectate lyaseprotein–protein interaction networkprotein-protein interaction networkBiotechnologyFrontiers in Plant Science
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Transcription factor NRF2 as a therapeutic target for chronic diseases: a systems medicine approach

2018

Systems medicine has a mechanism-based rather than a symptom- or organ-based approach to disease and identifies therapeutic targets in a nonhypothesis-driven manner. In this work, we apply this to transcription factor nuclear factor (erythroid-derived 2)-like 2 (NRF2) by cross-validating its position in a protein-protein interaction network (the NRF2 interactome) functionally linked to cytoprotection in low-grade stress, chronic inflammation, metabolic alterations, and reactive oxygen species formation. Multiscale network analysis of these molecular profiles suggests alterations of NRF2 expression and activity as a common mechanism in a subnetwork of diseases (the NRF2 diseasome). This netw…

0301 basic medicineRMSystems AnalysisNF-E2-Related Factor 2MedicinaNF-KAPPA-BAnti-Inflammatory AgentsTYPE-2 DIABETES-MELLITUSGENE PROMOTER POLYMORPHISMDiseaseComputational biologyInteractomeenvironment and public healthGLYCOGEN-SYNTHASE KINASETUMOR-SUPPRESSOR PTENNRF203 medical and health sciencesDrug DiscoveryAnimalsHumansTherapeutic targetsMedicineMolecular Targeted TherapyBardoxolone methylPLACEBO-CONTROLLED PHASE-3PharmacologyMechanism (biology)Drug discoverybusiness.industryDrug RepositioningRChronic inflammationrespiratory systemHEME OXYGENASE 1PROTEIN-PROTEIN INTERACTION3. Good healthSystems medicineDrug repositioning030104 developmental biologyDrug developmentEXPERIMENTAL AUTOIMMUNE ENCEPHALOMYELITISChronic DiseaseSystems medicineMolecular MedicineFUMARIC-ACID ESTERSbusiness
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Nuclear inclusions of pathogenic ataxin-1 induce oxidative stress and perturb the protein synthesis machinery

2020

Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. These expansions are responsible for protein misfolding and self-assembly into intranuclear inclusion bodies (IIBs) that are somehow linked to neuronal death. However, owing to lack of a suitable cellular model, the downstream consequences of IIB formation are yet to be resolved. Here, we describe a nuclear protein aggregation model of pathogenic human ataxin-1 and characterize IIB effects. Using an inducible Sleeping Beauty transposon system, we overexpressed the ATXN1(Q82) gene in human mesenchymal stem cells that are resistant to the early cytotoxic effects caused by the expr…

0301 basic medicineSCA1 Spinocerebellar ataxia type-1Intranuclear Inclusion BodiesClinical BiochemistryMSC mesenchymal stem cellProtein aggregationBiochemistry0302 clinical medicineMutant proteinProtein biosynthesisDE differentially expressed genesNuclear proteinlcsh:QH301-705.5FTIR Fourier-transform infrared spectroscopyAtaxin-1lcsh:R5-920biologyChemistryNuclear ProteinspolyQ polyglutamineRibosomeCell biologySB Sleeping BeautyRibosome ; Polyglutamine ; Ataxin-1 ; Oxidative stress ; Transposon ; Sleeping beauty transposon ; Protein networkSpinocerebellar ataxiaProtein foldingCellular modelFunction and Dysfunction of the Nervous Systemlcsh:Medicine (General)Research PaperiPSC induced pluripotent stem cellAtaxin 1Nerve Tissue ProteinsPPI protein-protein interaction03 medical and health sciencesROS reactive oxygen speciesProtein networkSleeping beauty transposonGSEA Gene Set Enrichment AnalysismedicineHumansNPC neural progenitor cellOrganic Chemistrymedicine.diseaseAFM atomic force microscopyOxidative Stress030104 developmental biologylcsh:Biology (General)IIBs intranuclear inclusion bodiesMS mass spectrometryCardiovascular and Metabolic Diseasesbiology.proteinPolyglutamine030217 neurology & neurosurgery
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Protein-protein interactions can be predicted using coiled coil co-evolution patterns

2016

AbstractProtein-protein interactions are sometimes mediated by coiled coil structures. The evolutionary conservation of interacting orthologs in different species, along with the presence or absence of coiled coils in them, may help in the prediction of interacting pairs. Here, we illustrate how the presence of coiled coils in a protein can be exploited as a potential indicator for its interaction with another protein with coiled coils. The prediction capability of our strategy improves when restricting our dataset to highly reliable, known protein-protein interactions. Our study of the co-evolution of coiled coils demonstrates that pairs of interacting proteins can be distinguished from no…

0301 basic medicineStatistics and ProbabilityComputational biologyCorrelated evolutionGeneral Biochemistry Genetics and Molecular BiologyProtein Structure SecondaryProtein–protein interactionConserved sequenceEvolution Molecular03 medical and health sciencesProtein-protein interactionModelling and SimulationImmunology and Microbiology(all)Coiled coilGeneticsCoiled coilPhysicsMedicine(all)030102 biochemistry & molecular biologyGeneral Immunology and MicrobiologyAgricultural and Biological Sciences(all)Models GeneticBiochemistry Genetics and Molecular Biology(all)Applied MathematicsA proteinProteinsGeneral Medicine030104 developmental biologyModeling and SimulationGeneral Agricultural and Biological SciencesJournal of Theoretical Biology
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