Search results for "protein–protein interactions"

showing 3 items of 3 documents

Concepts to Reveal Parvovirus–Nucleus Interactions

2021

Parvoviruses are small single-stranded (ss) DNA viruses, which replicate in the nucleoplasm and affect both the structure and function of the nucleus. The nuclear stage of the parvovirus life cycle starts at the nuclear entry of incoming capsids and culminates in the successful passage of progeny capsids out of the nucleus. In this review, we will present past, current, and future microscopy and biochemical techniques and demonstrate their potential in revealing the dynamics and molecular interactions in the intranuclear processes of parvovirus infection. In particular, a number of advanced techniques will be presented for the detection of infection-induced changes, such as DNA modification…

Cell Nucleusanalysis of virus–chromatin interactionsHost Microbial InteractionsviruksetparvovirusesvirusesnucleusReviewmikroskopiaanalysis of protein–protein interactionsVirus ReplicationinfektiotMicrobiologyimaging of viral interactions and dynamicsQR1-502Parvoviridae InfectionsParvovirusMicekuvantaminentumaAnimalsHumansCapsid ProteinsproteiinitparvoviruksetViruses
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Mechanism‐Dependent Modulation of Ultrafast Interfacial Water Dynamics in Intrinsically Disordered Protein Complexes

2018

Abstract The recognition of intrinsically disordered proteins (IDPs) is highly dependent on dynamics owing to the lack of structure. Here we studied the interplay between dynamics and molecular recognition in IDPs with a combination of time‐resolving tools on timescales ranging from femtoseconds to nanoseconds. We interrogated conformational dynamics and surface water dynamics and its attenuation upon partner binding using two IDPs, IBB and Nup153FG, both of central relevance to the nucleocytoplasmic transport machinery. These proteins bind the same nuclear transport receptor (Importinβ) with drastically different binding mechanisms, coupled folding–binding and fuzzy complex formation, resp…

Protein ConformationSolvation Dynamicsprotein–protein interactions010402 general chemistryIntrinsically disordered proteins01 natural sciencestime-resolved spectroscopyCatalysisProtein–protein interactionMolecular recognitionnucleocytoplasmic transport010405 organic chemistryMechanism (biology)ChemistryCommunicationWaterGeneral Chemistrybeta KaryopherinsCommunications0104 chemical sciencesIntrinsically Disordered ProteinsNucleocytoplasmic TransportModulationChemical physicsThermodynamicsTime-resolved spectroscopyNuclear transportAngewandte Chemie International Edition
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Correcting for the study bias associated with protein-protein interaction measurements reveals differences between protein degree distributions from …

2015

Protein–protein interaction (PPI) networks are associated with multiple types of biases partly rooted in technical limitations of the experimental techniques. Another source of bias are the different frequencies with which proteins have been studied for interaction partners. It is generally believed that proteins with a large number of interaction partners tend to be essential, evolutionarily conserved, and involved in disease. It has been repeatedly reported that proteins driving tumor formation have a higher number of PPI partners. However, it has been noticed before that the degree distribution of PPI networks is biased toward disease proteins, which tend to have been studied more often …

cancer genesstudy biasGeneticsprotein–protein interactionsdegree distributionnetwork analysisOriginal ResearchFrontiers in genetics
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