Search results for "PROTEIN INTERACTION"

showing 10 items of 228 documents

Editorial: The Role of Protein Post-Translational Modifications in Protein-RNA Interactions and RNP Assemblies

2022

RNP granulesEditorialQH301-705.5Molecular BiosciencesRNA-protein interactionsPTMs (post-translational modifications)phase separationBiology (General)Biochemistry Genetics and Molecular Biology (miscellaneous)Molecular BiologyBiochemistryintrinsically disordered region (IDR)Frontiers in Molecular Biosciences
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Repeatability in protein sequences

2019

Low complexity regions (LCRs) in protein sequences have special properties that are very different from those of globular proteins. The rules that define secondary structure elements do not apply when the distribution of amino acids becomes biased. While there is a tendency towards structural disorder in LCRs, various examples, and particularly homorepeats of single amino acids, suggest that very short repeats could adopt structures very difficult to predict. These structures are possibly variable and dependant on the context of intra- or inter-molecular interactions. In general, short repeats in LCRs can induce structure. This could explain the observation that very short (non-perfect) rep…

Repetitive Sequences Amino AcidGlobular proteinSaccharomyces cerevisiaeContext (language use)Computational biologyProtein–protein interactionEvolution Molecular03 medical and health sciencesSequence Analysis ProteinStructural BiologyHumansArabidopsis thalianaAmino Acid SequenceDatabases ProteinProtein secondary structure030304 developmental biologychemistry.chemical_classification0303 health sciencesbiology030302 biochemistry & molecular biologyProteinsbiology.organism_classificationAmino acidchemistrySequence AlignmentAlgorithmsFunction (biology)Journal of Structural Biology
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Rtp1p Is a Karyopherin-Like Protein Required for RNA Polymerase II Biogenesis

2013

The assembly and nuclear transport of RNA polymerase II (RNA pol II) are processes that require the participation of many auxiliary factors. In a yeast genetic screen, we identified a previously uncharacterized gene, YMR185w (renamed RTP1), which encodes a protein required for the nuclear import of RNA pol II. Using protein affinity purification coupled to mass spectrometry, we identified interactions between Rtp1p and members of the R2TP complex. Rtp1p also interacts, to a different extent, with several RNA pol II subunits. The pattern of interactions is compatible with a role for Rtp1p as an assembly factor that participates in the formation of the Rpb2/Rpb3 subassembly complex and its bi…

Saccharomyces cerevisiae ProteinsActive Transport Cell NucleusRNA polymerase IISaccharomyces cerevisiaeKaryopherinsBiologyGene Expression Regulation FungalTranscriptional regulationRNA polymerase IProtein Interaction MapsMolecular BiologyRNA polymerase II holoenzymeR2TP complexGeneticsNuclear cap-binding protein complexArticlesCell BiologyPhosphoproteinsUp-RegulationCell biologyNuclear Pore Complex Proteinsbiology.proteinRNA Polymerase IITranscription factor II DCarrier ProteinsGene DeletionSmall nuclear RNATranscription Factors
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A general strategy to determine the congruence between a hierarchical and a non-hierarchical classification

2007

This article is available from: http://www.biomedcentral.com/1471-2105/8/442

Saccharomyces cerevisiae ProteinsComputer scienceDecision treecomputer.software_genrelcsh:Computer applications to medicine. Medical informaticsInteractomeBiochemistryPattern Recognition AutomatedMitochondrial ProteinsUser-Computer InterfaceSimilarity (network science)Structural BiologyArtificial IntelligenceSequence Analysis ProteinProtein Interaction MappingCluster AnalysisDatabases Proteinlcsh:QH301-705.5Molecular BiologyOligonucleotide Array Sequence AnalysisApplied MathematicsMethodology ArticleDendrogramDecision TreesReproducibility of ResultsClassificationPartition (database)Computer Science ApplicationsTree (data structure)Rankinglcsh:Biology (General)Pattern recognition (psychology)lcsh:R858-859.7Data miningcomputerBiological networkBMC Bioinformatics
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Protein Interactions within the Set1 Complex and Their Roles in the Regulation of Histone 3 Lysine 4 Methylation

2006

Set1 is the catalytic subunit and the central component of the evolutionarily conserved Set1 complex (Set1C) that methylates histone 3 lysine 4 (H3K4). Here we have determined protein/protein interactions within the complex and related the substructure to function. The loss of individual Set1C subunits differentially affects Set1 stability, complex integrity, global H3K4 methylation, and distribution of H3K4 methylation along active genes. The complex requires Set1, Swd1, and Swd3 for integrity, and Set1 amount is greatly reduced in the absence of the Swd1-Swd3 heterodimer. Bre2 and Sdc1 also form a heteromeric subunit, which requires the SET domain for interaction with the complex, and Sdc…

Saccharomyces cerevisiae ProteinsProtein subunitLysineRNA polymerase IISaccharomyces cerevisiaeMethylationenvironment and public healthBiochemistryProtein–protein interactionHistonesSerineGene Expression Regulation FungalCoding regionMolecular BiologybiologyLysineHistone-Lysine N-MethyltransferaseCell BiologyMethylationDNA-Binding ProteinsProtein SubunitsHistoneBiochemistrybiology.proteinProtein BindingTranscription FactorsJournal of Biological Chemistry
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A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells.

2008

Contains fulltext : 69178.pdf (Publisher’s version ) (Closed access) The human Usher syndrome (USH) is the most frequent cause of combined deaf-blindness. USH is genetically heterogeneous with at least 12 chromosomal loci assigned to three clinical types, USH1-3. Although these USH types exhibit similar phenotypes in human, the corresponding gene products belong to very different protein classes and families. The scaffold protein harmonin (USH1C) was shown to integrate all identified USH1 and USH2 molecules into protein networks. Here, we analyzed a protein network organized in the absence of harmonin by the scaffold proteins SANS (USH1G) and whirlin (USH2D). Immunoelectron microscopic anal…

Scaffold proteinGenetics and epigenetic pathways of disease [NCMLS 6]XenopusCell Cycle ProteinsNerve Tissue ProteinsBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]TransfectionModels BiologicalReceptors G-Protein-CoupledMiceChlorocebus aethiopsProtein Interaction MappingGeneticsPerception and Action [DCN 1]otorhinolaryngologic diseasesAnimalsHumansNeurosensory disorders [UMCN 3.3]Cell Cycle ProteinMicroscopy ImmunoelectronMolecular BiologyIntegral membrane proteinGenetics (clinical)Adaptor Proteins Signal TransducingRenal disorder [IGMD 9]GeneticsMice KnockoutExtracellular Matrix ProteinsCiliumSignal transducing adaptor proteinMembrane ProteinsGeneral MedicineTransmembrane proteinCell biologyMice Inbred C57BLCytoskeletal ProteinsEctodomainGenetic defects of metabolism [UMCN 5.1]COS CellsNIH 3T3 CellsCervical collarUsher SyndromesFunctional Neurogenomics [DCN 2]Photoreceptor Cells VertebrateSubcellular FractionsImmunity infection and tissue repair [NCMLS 1]
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Phosphorylation of the Usher syndrome 1G protein SANS controls Magi2-mediated endocytosis.

2014

Item does not contain fulltext The human Usher syndrome (USH) is a complex ciliopathy with at least 12 chromosomal loci assigned to three clinical subtypes, USH1-3. The heterogeneous USH proteins are organized into protein networks. Here, we identified Magi2 (membrane-associated guanylate kinase inverted-2) as a new component of the USH protein interactome, binding to the multifunctional scaffold protein SANS (USH1G). We showed that the SANS-Magi2 complex assembly is regulated by the phosphorylation of an internal PDZ-binding motif in the sterile alpha motif domain of SANS by the protein kinase CK2. We affirmed Magi2's role in receptor-mediated, clathrin-dependent endocytosis and showed tha…

Scaffold proteinGuanylate kinaseMolecular Sequence DataPrimary Cell CultureNerve Tissue ProteinsBiologyEndocytosisPhotoreceptor cellExocytosisMiceCiliogenesisGeneticsmedicineAnimalsHumansProtein Interaction Domains and MotifsAmino Acid SequencePhosphorylationRNA Small InterferingSensory disorders Radboud Institute for Molecular Life Sciences [Radboudumc 12]Molecular BiologyGenetics (clinical)Adaptor Proteins Signal TransducingBinding SitesGeneral MedicineClathrinEndocytosisCell biologyMice Inbred C57BLRenal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11]medicine.anatomical_structureHEK293 CellsGene Expression RegulationCiliary pocketCarrier ProteinsSterile alpha motifGuanylate KinasesSequence AlignmentUsher SyndromesPhotoreceptor Cells VertebrateProtein BindingSignal TransductionHuman molecular genetics
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Isolation of the silicatein-α interactor silintaphin-2 by a novel solid-phase pull-down assay.

2011

The skeleton of siliceous sponges consists of amorphous biogenous silica (biosilica). Biosilica formation is driven enzymatically by means of silicatein(s). During this unique process of enzymatic polycondensation, skeletal elements (spicules) that enfold a central proteinaceous structure (axial filament), mainly comprising silicatein, are formed. However, only the concerted action of silicatein and other proteins can explain the genetically controlled diversity of spicular morphotypes, from simple rods with pointed ends to intricate structures with up to six rays. With the scaffold protein silintaphin-1, a first silicatein interactor that facilitates the formation of the axial filament and…

Scaffold proteinSpiculeImmunoprecipitationMolecular Sequence DataNanotechnologyBiologyFlagellumBiochemistry03 medical and health sciencesSponge spiculePhase (matter)Two-Hybrid System TechniquesProtein Interaction MappingAnimalsInteractorAmino Acid Sequence030304 developmental biology0303 health sciences030302 biochemistry & molecular biologySilicon DioxideCathepsinsYeastProtein TransportSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationBiophysicsAutoradiographyCalciumSuberitesProtein BindingBiochemistry
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Identification of Key miRNAs in Regulation of PPI Networks

2020

In this paper, we explore the interaction between miRNA and deregulated proteins in some pathologies. Assuming that miRNA can influence mRNA and consequently the proteins regulation, we explore this connection by using an interaction matrix derived from miRNA-target data and PPI network interactions. From this interaction matrix and the set of deregulated proteins, we search for the miRNA subset that influences the deregulated proteins with a minimum impact on the not deregulated ones. This regulation problem can be formulated as a complex optimization problem. In this paper, we have tried to solve it by using the Genetic Algorithm Heuristic. As the main result, we have found a set of miRNA…

Settore ING-INF/05 - Sistemi Di Elaborazione Delle Informazioni0301 basic medicineOptimization problemSettore INF/01 - InformaticaHeuristic (computer science)Computer sciencemiRNA expression profiles Protein-protein interaction networks Genetic algorithmsComputational biologyGenetic algorithmsmiRNA expression profilesProtein-protein interaction networks03 medical and health sciencesIdentification (information)030104 developmental biologyPpi networkGenetic algorithmmicroRNAKey (cryptography)Set (psychology)
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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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