Search results for "Interactions"

showing 10 items of 1963 documents

Astringency and the interactions between a human salivary proline-rich protein and tannins

2015

International audience

Proline-rich protein[CHIM.ANAL] Chemical Sciences/Analytical chemistrySRMS2Mass spectrometryNoncovalent complexesNoncovalent interactions[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM][SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]synchrotron radiation[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsVUVSAXSSalivary Proline-Rich Proteins[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics[SDV.AEN] Life Sciences [q-bio]/Food and Nutrition[CHIM.ANAL]Chemical Sciences/Analytical chemistry[CHIM] Chemical Sciences[CHIM]Chemical Sciences[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM][SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM][SDV.AEN]Life Sciences [q-bio]/Food and NutritionComputingMilieux_MISCELLANEOUS
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Immune depression induced by acanthocephalan parasites in their intermediate crustacean host: consequences for the risk of super-infection and links …

2009

9 pages; International audience; Parasite survival in hosts mainly depends on the capacity to circumvent the host immune response. Acanthocephalan infections in gammarids are linked with decreased activity of the prophenoloxidase (ProPO) system, suggesting an active immunosuppression process. Nevertheless, experimental evidence for this hypothesis is lacking: whether these parasites affect several immune pathways is unknown and the consequences of such immune change have not been investigated. In particular, the consequences for other pathogens are not known; neither are the links with other parasite-induced manipulations of the host. Firstly, using experimental infections of Pomphorhynchus…

ProphenoloxidaseMaleImmune depression[ SDV.MP.PAR ] Life Sciences [q-bio]/Microbiology and Parasitology/ParasitologyHemocytesCyprinidaeBiology[ SDV.IMM.IA ] Life Sciences [q-bio]/Immunology/Adaptive immunologyAcanthocephalanAcanthocephalaHost-Parasite InteractionsBehavioural manipulationFish DiseasesImmune systemImmunityCrustacea[ SDV.EE.IEO ] Life Sciences [q-bio]/Ecology environment/SymbiosisParasite hostingAnimalsGammaridEnzyme PrecursorsHost (biology)Intermediate hostHaemocytebiology.organism_classificationGammarus pulexInfectious DiseasesImmunologyParasitologyPomphorhynchus laevisFemaleImmunocompetenceImmunocompetenceCatechol OxidaseInternational journal for parasitology
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Calpain 1 and 2 Are Required for RNA Replication of Echovirus 1▿

2007

ABSTRACT Calpains are calcium-dependent cysteine proteases that degrade cytoskeletal and cytoplasmic proteins. We have studied the role of calpains in the life cycle of human echovirus 1 (EV1). The calpain inhibitors, including calpeptin, calpain inhibitor 1, and calpain inhibitor 2 as well as calpain 1 and calpain 2 short interfering RNAs, completely blocked EV1 infection in the host cells. The effect of the inhibitors was not specific for EV1, because they also inhibited infection by other picornaviruses, namely, human parechovirus 1 and coxsackievirus B3. The importance of the calpains in EV1 infection also was supported by the fact that EV1 increased calpain activity 3 h postinfection. …

ProteasesImmunoelectron microscopyImmunologyParechovirusVirus ReplicationMicrobiologyCell LineViral entryVirologyHumansGene SilencingEnzyme InhibitorsMicroscopy ImmunoelectronMicroscopy ConfocalbiologyCalpainCytoplasmic VesiclesRNACalpainMolecular biologyCell biologyVirus-Cell InteractionsEnterovirus B HumanViral replicationCell cultureInsect ScienceCalpain-2biology.proteinRNA Viral
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Microbiological control of soil-borne phytopathogenic fungi with special emphasis on wilt-inducing Fusarium oxysporum

2009

Contents   Summary  529 I. Biological control of plant diseases: state of the art  530 II. Main modes of action of biological control agents  530 III. The protective strains of F. oxysporum: an unexplored model  532 IV. Future directions for the study of the protective capacity of strains of F. oxysporum  539 V. How to make biological control successful in the field?  540   References  541 Summary Plant diseases induced by soil-borne plant pathogens are among the most difficult to control. In the absence of effective chemical control methods, there is renewed interest in biological control based on application of populations of antagonistic micro-organisms. In addition to Pseudomonas spp. a…

Protective capacityPhysiologymedia_common.quotation_subjectBiological pest controlCOMPETITIONPlant ScienceModels BiologicalPlant RootsCompetition (biology)MicrobiologyFusariumSpecies SpecificityECOLOGICAL FITNESSPLANT DEFENSE REACTIONSFusarium oxysporumPest Control BiologicalControl (linguistics)EcosystemSoil MicrobiologyPlant DiseasesPlant Proteinsmedia_commonBIOLOGIE DES POPULATIONSVirulencebiologybusiness.industryINDUCED RESISTANCEPseudomonasfood and beveragesPRIMINGbiology.organism_classificationBiotechnology[SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyBIOCONTROLSoil borneTrichodermaHost-Pathogen InteractionsBIOTROPHYbusinessROOT COLONIZATIONAntimicrobial Cationic Peptides
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Folding and insertion of transmembrane helices at the ER

2021

In eukaryotic cells, the endoplasmic reticulum (ER) is the entry point for newly synthesized proteins that are subsequently distributed to organelles of the endomembrane system. Some of these proteins are completely translocated into the lumen of the ER while others integrate stretches of amino acids into the greasy 30 Å wide interior of the ER membrane bilayer. It is generally accepted that to exist in this non-aqueous environment the majority of membrane integrated amino acids are primarily non-polar/hydrophobic and adopt an α-helical conformation. These stretches are typically around 20 amino acids long and are known as transmembrane (TM) helices. In this review, we will consider how tra…

Protein Conformation alpha-HelicalfoldingProtein FoldingQH301-705.5ReviewEndoplasmic ReticulumRibosomeCatalysisinsertionInorganic Chemistrytransmembrane segmentAnimalsHumansEndomembrane systemmembrane proteinPhysical and Theoretical ChemistryBiology (General)Molecular BiologyQD1-999Spectroscopytransloconchemistry.chemical_classificationEndoplasmic reticulumOrganic ChemistryProteïnes de membranaMembrane ProteinsGeneral MedicineTransloconTransmembrane proteinComputer Science ApplicationsAmino acidTransmembrane domainChemistrychemistryMembrane proteinribosomeBiophysicsHydrophobic and Hydrophilic InteractionsRibosomes
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Sequence Determines Degree of Knottedness in a Coarse-Grained Protein Model

2015

Knots are abundant in globular homopolymers but rare in globular proteins. To shed new light on this long-standing conundrum, we study the influence of sequence on the formation of knots in proteins under native conditions within the framework of the hydrophobic-polar (HP) lattice protein model. By employing large scale Wang-Landau simulations combined with suitable Monte Carlo trial moves we show that, even though knots are still abundant on average, sequence introduces large variability in the degree of self-entanglements. Moreover, we are able to design sequences which are either almost always or almost never knotted. Our findings serve as proof of concept that the introduction of just o…

Protein ConformationFOS: Physical sciencesGeneral Physics and AstronomyCondensed Matter - Soft Condensed Matterstomatognathic systemComputer SimulationMathematicsSequence (medicine)chemistry.chemical_classificationQuantitative Biology::BiomoleculesDegree (graph theory)Proteinsfood and beveragesBiomolecules (q-bio.BM)Knot theoryAmino acidsurgical procedures operativeModels ChemicalQuantitative Biology - BiomoleculeschemistryFOS: Biological sciencesProtein modelSoft Condensed Matter (cond-mat.soft)Biological systemHydrophobic and Hydrophilic InteractionsMonte Carlo MethodPhysical Review Letters
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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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Hydrophilicity Regulates the Stealth Properties of Polyphosphoester‐Coated Nanocarriers

2018

Increasing the plasma half-life is an important goal in the development of drug carriers, and can be effectively achieved through the attachment of polymers, in particular poly(ethylene glycol) (PEG). While the increased plasma half-life has been suggested to be a result of decreased overall protein adsorption on the hydrophilic surface in combination with the adsorption of specific proteins, the molecular reasons for the success of PEG and other hydrophilic polymers are still widely unknown. We prepared polyphosphoester-coated nanocarriers with defined hydrophilicity to control the stealth properties of the polymer shell. We found that the log P value of the copolymer controls the composit…

Protein Corona02 engineering and technology010402 general chemistry01 natural sciencesCatalysisPolyethylene GlycolsMicechemistry.chemical_compoundDrug Delivery SystemsPEG ratioAnimalsHumanschemistry.chemical_classificationDrug CarriersMolecular StructureChemistryGeneral ChemistryPolymer021001 nanoscience & nanotechnology0104 chemical sciencesRAW 264.7 CellsBiophysicsPEGylationNanoparticlesNanocarriers0210 nano-technologyDrug carrierHydrophobic and Hydrophilic InteractionsEthylene glycolHeLa CellsProtein adsorptionAngewandte Chemie International Edition
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Methodological approaches for the analysis of transmembrane domain interactions: A systematic review

2021

The study of protein-protein interactions (PPI) has proven fundamental for the understanding of the most relevant cell processes. Any protein domain can participate in PPI, including transmembrane (TM) segments that can establish interactions with other TM domains (TMDs). However, the hydrophobic nature of TMDs and the environment they occupy complicates the study of intramembrane PPI, which demands the use of specific approaches and techniques. In this review, we will explore some of the strategies available to study intramembrane PPI in vitro, in vivo, and, in silico, focusing on those techniques that could be carried out in a standard molecular biology laboratory regarding its previous e…

Protein FoldingBacteriaChemistryIn silicoProtein domainBiophysicsMembrane ProteinsCell CommunicationCell BiologyComputational biologyBiochemistryTransmembrane proteinIn vitroProtein–protein interactionTransmembrane domainProtein DomainsMembrane proteinProtein foldingProtein Interaction MapsHydrophobic and Hydrophilic InteractionsBiochimica et Biophysica Acta (BBA) - Biomembranes
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