Search results for "Protein-protein interactions"

showing 10 items of 12 documents

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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Targeting SARS-CoV-2 RBD Interface: a Supervised Computational Data-Driven Approach to Identify Potential Modulators

2020

Coronavirus disease 2019 (COVID-19) has spread out as a pandemic threat affecting over 2 million people. The infectious process initiates via binding of SARS-CoV-2 Spike (S) glycoprotein to host angiotensin-converting enzyme 2 (ACE2). The interaction is mediated by the receptor-binding domain (RBD) of S glycoprotein, promoting host receptor recognition and binding to ACE2 peptidase domain (PD), thus representing a promising target for therapeutic intervention. Herein, we present a computational study aimed at identifying small molecules potentially able to target RBD. Although targeting PPI remains a challenge in drug discovery, our investigation highlights that interaction between SARS-CoV…

Protein domainPneumonia ViralDruggabilityDrug Evaluation Preclinicalprotein-protein interactionsComputational biologyBiologyMolecular Dynamics SimulationPeptidyl-Dipeptidase AMolecular dynamics01 natural sciencesBiochemistryMolecular Docking SimulationAntiviral Agentsdockingmolecular dynamicProtein–protein interactionSmall Molecule LibrariesBetacoronavirusProtein DomainsDrug DiscoveryHumansGeneral Pharmacology Toxicology and PharmaceuticsPandemicsPharmacologyFull Paperpharmacophore010405 organic chemistryDrug discoverySARS-CoV-2Organic ChemistryCOVID-19Small molecule0104 chemical sciencesProtein-Protein InteractionMolecular Docking Simulation010404 medicinal & biomolecular chemistryDocking (molecular)Spike Glycoprotein CoronavirusdockingMolecular MedicineAngiotensin-Converting Enzyme 2PharmacophoreCoronavirus InfectionsProtein Binding
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MIPPIE: the mouse integrated protein–protein interaction reference

2020

Abstract Cells operate and react to environmental signals thanks to a complex network of protein–protein interactions (PPIs), the malfunction of which can severely disrupt cellular homeostasis. As a result, mapping and analyzing protein networks are key to advancing our understanding of biological processes and diseases. An invaluable part of these endeavors has been the house mouse (Mus musculus), the mammalian model organism par excellence, which has provided insights into human biology and disorders. The importance of investigating PPI networks in the context of mouse prompted us to develop the Mouse Integrated Protein–Protein Interaction rEference (MIPPIE). MIPPIE inherits a robust infr…

Computer scienceved/biology.organism_classification_rank.speciesprotein-protein interactionsCellular homeostasisContext (language use)Computational biologycomputer.software_genreGeneral Biochemistry Genetics and Molecular BiologyProtein–protein interaction03 medical and health sciencesMice0302 clinical medicineProtein Interaction MappingMus musculusAnimalsProtein Interaction MapsModel organismDatabases Proteinmousedatabase030304 developmental biology0303 health sciencesved/biologyComputational BiologyComplex networkprotein interaction networkOriginal ArticleWeb serviceUser interfaceGeneral Agricultural and Biological SciencesProtein networkcomputer030217 neurology & neurosurgerySoftwareInformation SystemsDatabase: The Journal of Biological Databases and Curation
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Synthesis and biological evaluation of some new 2-phenylpropiolamidobenzamides as potential antagonists of the HDM2-p53 protein-protein interactions

2009

antitumoral activity anticancer protein-protein interactions 2-phenylpropiolamidobenzamides synthesis
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A Protein-Interaction Array Inside a Living Cell

2013

Cell phenotype is determined by protein network states that are maintained by the dynamics of multiple protein interactions.1 Fluorescence microscopy approaches that measure protein interactions in individual cells, such as by Forster resonant energy transfer (FRET), are limited by the spectral separation of fluorophores and thus are most suitable to analyze a single protein interaction in a given cell. However, analysis of correlations between multiple protein interactions is required to uncover the interdependence of protein reactions in dynamic signal networks. Available protein-array technologies enable the parallel analysis of interacting proteins from cell extracts, however, they can …

ImmunoprecipitationRecombinant Fusion Proteinsprotein-protein interactionsImmobilized Nucleic AcidsProtein Array AnalysisreceptorsDNA Single-StrandedCatalysisProtein–protein interactionReceptors G-Protein-CoupledBimolecular fluorescence complementationProtein Array AnalysisChlorocebus aethiopsFluorescence microscopeFluorescence Resonance Energy TransferAnimalsProtein Interaction MapsProtein kinase Amultiplexed assayChemistryProteinsProtein-protein interactions Dip Pen Nanolithography Protein KinaseDNA directed immobilizationGeneral MedicineGeneral ChemistryCommunicationssurface-immobilizationKineticsLuminescent ProteinsFörster resonance energy transferBiochemistryMicroscopy FluorescenceCOS CellsBiophysicsSignal transductionAntibodies Immobilizedsignal transduction
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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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Algorithms for Graph and Network Analysis: Graph Alignment

2019

In this article we discuss the problem of graph alignment, which has been longly referred to for the purpose of analyzing and comparing biological networks. In particular, we describe different facets of graph alignment, according to the number of input networks, the fixed output objective, the possible heterogeneity of input data. Accordingly, we will discuss pairwise and multiple alignment, global and local alignment, etc. Moreover, we provide a comprehensive overview of the algorithms and techniques proposed in the literature to solve each of the specific considered types of graph alignment. In order to make the material presented here complete and useful to guide the reader in the use o…

Smith–Waterman algorithmSoftwareMultiple sequence alignmentAsymmetric alignmentBiological networksCellular interactionsGlobal alignmentGraph alignmentLocal alignmentMolecular componentsMultiple alignmentPairwise alignmentProtein-protein interactionsComputer sciencebusiness.industryGraph alignmentGraph (abstract data type)Pairwise comparisonbusinessAlgorithmBiological networkNetwork analysis
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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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The Amino Acid Transporter JhI-21 Coevolves with Glutamate Receptors, Impacts NMJ Physiology, and Influences Locomotor Activity in Drosophila Larvae

2015

AbstractChanges in synaptic physiology underlie neuronal network plasticity and behavioral phenomena, which are adjusted during development. The Drosophila larval glutamatergic neuromuscular junction (NMJ) represents a powerful synaptic model to investigate factors impacting these processes. Amino acids such as glutamate have been shown to regulate Drosophila NMJ physiology by modulating the clustering of postsynaptic glutamate receptors and thereby regulating the strength of signal transmission from the motor neuron to the muscle cell. To identify amino acid transporters impacting glutmatergic signal transmission, we used Evolutionary Rate Covariation (ERC), a recently developed bioinforma…

0301 basic medicinejuvenile-hormonemelanogasterAmino Acid Transport Systemsextracellular glutamateprotein-protein interactionsPhysiology[ SDV.BA ] Life Sciences [q-bio]/Animal biologySynaptic Transmissionin-vivo0302 clinical medicinePostsynaptic potentialDrosophila Proteinsgenesglial xctMotor NeuronsAnimal biologyMultidisciplinary[SDV.BA]Life Sciences [q-bio]/Animal biologyGlutamate receptorBiological Evolutiondrosophilemedicine.anatomical_structureReceptors GlutamateLarvaExcitatory postsynaptic potentialDrosophila[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Drosophila ProteinSignal Transductionevolutionary rate covariationNeuromuscular JunctionPresynaptic TerminalsNeurotransmissionBiologyMotor ActivityArticlesynaptic vesicle03 medical and health sciencesGlutamatergicneuromuscular-junctionBiologie animalemedicineAnimalsAmino acid transporterevolutionary rate covariation;protein-protein interactions;juvenile-hormone;neuromuscular-junction;synaptic vesicle;in-vivo;extracellular glutamate;glial xct;melanogaster;genesfungiNeurosciencesExcitatory Postsynaptic PotentialsMotor neuron030104 developmental biology[ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Neurons and CognitionMutation030217 neurology & neurosurgeryScientific Reports
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Small molecule inhibitors of Apaf-1-related caspase- 3/-9 activation that control mitochondrial-dependent apoptosis

2006

10 pages, 5 figures.-- PMID: 16341125 [PubMed].-- Available online Dec 9, 2005.

Multiprotein complexCytochromeProtein-protein interactionsApoptosisCaspase 3MitochondrionLigandsCell LineChemical librarychemistry.chemical_compoundPeptide LibraryApoptosomesPeptoidHumansCombinatorial libraries inhibitorApoptosomeProtein PrecursorsMolecular BiologybiologyCaspase 3Intrinsic apoptosisCytochromes cCell BiologyCaspase InhibitorsCaspase 9Recombinant ProteinsMitochondriaCell biologyEnzyme ActivationCaspasa-9Apoptotic Protease-Activating Factor 1chemistryBiochemistryN-substituted GlycinesApoptosisCaspasa-3biology.proteinApoptosomeApaf-1Molecular recognitionSmall moleculeProtein BindingCell Death & Differentiation
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