Search results for "Membrane Protein"

showing 10 items of 956 documents

Membrane Insertion and Biogenesis of the Turnip Crinkle Virus p9 Movement Protein

2010

ABSTRACT Plant viral infection and spread depends on the successful introduction of a virus into a cell of a compatible host, followed by replication and cell-to-cell transport. The movement proteins (MPs) p8 and p9 of Turnip crinkle virus are required for cell-to-cell movement of the virus. We have examined the membrane association of p9 and found that it is an integral membrane protein with a defined topology in the endoplasmic reticulum (ER) membrane. Furthermore, we have used a site-specific photo-cross-linking strategy to study the membrane integration of the protein at the initial stages of its biosynthetic process. This process is cotranslational and proceeds through the signal recog…

VirologiavirusesImmunologyEndoplasmic ReticulumMicrobiologyVirusMembranes (Biologia)VirologyMovement proteinIntegral membrane proteinSignal recognition particlebiologyTurnip crinkle virusEndoplasmic reticulumProteïnes de membranaMembrane Proteinsbiology.organism_classificationVirus-Cell InteractionsVirusCell biologyPlant Viral Movement ProteinsMembrane proteinBiochemistryInsect ScienceBiosynthetic processCarmovirusSignal Recognition ParticleJournal of Virology
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Sec61alpha and TRAM are Sequentially Adjacent to a Nascent Viral Membrane Protein during its ER Integration

2007

Co-translational integration of a nascent viral membrane protein into the endoplasmic reticulum membrane takes place via the translocon. We have been studying the early stages of the integration of a double-spanning plant viral movement protein to gain insights into how viral membrane proteins are transferred from the hydrophilic interior of the translocon into the hydrophobic environment of the bilayer, where the transmembrane (TM) segments of the viral proteins can diffuse freely. Photocrosslinking experiments reveal that this integration involves the sequential passage of the TM segments past Sec61alpha and translocating chain-associating membrane protein (TRAM). Each TM segment is first…

Virus IntegrationBiologyEndoplasmic ReticulumModels BiologicalViral Matrix ProteinsDogsMembranes (Biologia)Structural BiologyAnimalsRNA MessengerMolecular BiologyVirus IntegrationMembrane GlycoproteinsViral matrix proteinEndoplasmic reticulumProteïnes de membranaMembrane ProteinsViral membraneTransloconTransmembrane proteinCell biologyPlant Viral Movement ProteinsCross-Linking ReagentsMembrane proteinBiochemistrySEC Translocation ChannelsSEC Translocation ChannelsMolecular Chaperones
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Depletion ofL-arginine induces autophagy as a cytoprotective response to endoplasmic reticulum stress in human T lymphocytes

2012

PMCID: PMC3494587

X-Box Binding Protein 1Proteasome Endopeptidase ComplexProgrammed cell deathXBP1CD3 ComplexMAP Kinase Signaling SystemRNA SplicingT-LymphocytesT cellDown-RegulationApoptosisRegulatory Factor X Transcription FactorsUbiquitin-Activating EnzymesProtein Serine-Threonine KinasesBiologyArginineLymphocyte ActivationAutophagy-Related Protein 7Jurkat cellsJurkat CellsEndoribonucleasesAutophagymedicineHumansMolecular BiologyCell ProliferationTOR Serine-Threonine KinasesAutophagyMembrane ProteinsCell BiologyBECN1Endoplasmic Reticulum StressG1 Phase Cell Cycle CheckpointsBasic Research Paper3. Good healthCell biologyDNA-Binding Proteinsmedicine.anatomical_structureCytoprotectionApoptosisUnfolded protein responseBeclin-1MitogensApoptosis Regulatory ProteinsLysosomesProto-Oncogene Proteins c-aktTranscription FactorsAutophagy
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Efficient, non-toxic anion transport by synthetic carriers in cells and epithelia.

2016

Transmembrane anion transporters (anionophores) have potential for new modes of biological activity, including therapeutic applications. In particular they might replace the activity of defective anion channels in conditions such as cystic fibrosis. However, data on the biological effects of anionophores are scarce, and it remains uncertain whether such molecules are fundamentally toxic. Here, we report a biological study of an extensive series of powerful anion carriers. Fifteen anionophores were assayed in single cells by monitoring anion transport in real time through fluorescence emission from halide-sensitive yellow fluorescent protein. A bis-(p-nitrophenyl)ureidodecalin shows especial…

Yellow fluorescent proteinpotencyGeneral Chemical Engineeringsynthetic anion carriersCystic Fibrosis Transmembrane Conductance Regulator01 natural sciencesMadin Darby Canine Kidney CellsCell membranedeliverabilityta116Drug CarriersbiologyMolecular StructureChemistryBiological activitypersistenceCystic fibrosis transmembrane conductance regulatorTransmembrane proteinanionophoresmedicine.anatomical_structureBiochemistryPhosphatidylcholinesSteroidsChlorineAnionsCell SurvivalNaphthalenesta3111010402 general chemistryDogsBacterial ProteinsCyclohexanesmedicineAnimalsHumansIon transporterCell ProliferationIon Transport010405 organic chemistryCell MembranetoxicityTransporterEpithelial CellsHydrogen BondingGeneral ChemistryRats Inbred F3440104 chemical sciencesElectrophysiological PhenomenaLuminescent ProteinsMicroscopy FluorescenceCell cultureDrug Designbiology.proteinHeLa CellsNature chemistry
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The membrane proteome of Medicago truncatula roots displays qualitative and quantitative changes in response to arbuscular mycorrhizal symbiosis

2014

International audience; Arbuscular mycorrhizal (AM) symbiosis that associates roots of most land plants with soil-borne fungi (Glomeromycota), is characterized by reciprocal nutritional benefits. Fungal colonization of plant roots induces massive changes in cortical cells where the fungus differentiates an arbuscule, which drives proliferation of the plasma membrane. Despite the recognized importance of membrane proteins in sustaining AM symbiosis, the root microsomal proteome elicited upon mycorrhiza still remains to be explored. In this study, we first examined the qualitative composition of the root membrane proteome of Medicago truncatula after microsome enrichment and subsequent in dep…

[SDV.SA]Life Sciences [q-bio]/Agricultural sciencesGeLC-MS/MS[SDV.BIO]Life Sciences [q-bio]/BiotechnologyProteomeBiophysicsBiological Transport ActiveRoot membrane proteomeBiochemistrySpectral countingFungal ProteinsGlomeromycotaSymbiosisPeriarbuscular membraneMycorrhizaeMedicago truncatulaBotanyEndomembrane systemMycorrhizaArbuscular mycorrhizaRhizophagus irregularisSymbiosisPlant Proteins2. Zero hungerbiologyfungiMembrane Proteins15. Life on landbiology.organism_classificationMedicago truncatulaCell biologyMembrane proteinProteomeSignal Transduction
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Rbt1 Protein Domains Analysis in Candida albicans Brings Insights into Hyphal Surface Modifications and Rbt1 Potential Role during Adhesion and Biofi…

2013

Cell wall proteins are central to the virulence of Candida albicans. Hwp1, Hwp2 and Rbt1 form a family of hypha-associated cell surface proteins. Hwp1 and Hwp2 have been involved in adhesion and other virulence traits but Rbt1 is still poorly characterized. To assess the role of Rbt1 in the interaction of C. albicans with biotic and abiotic surfaces independently of its morphological state, heterologous expression and promoter swap strategies were applied. The N-terminal domain with features typical of the Flo11 superfamily was found to be essential for adhesiveness to polystyrene through an increase in cell surface hydrophobicity. A 42 amino acid-long domain localized in the central part o…

[SDV]Life Sciences [q-bio]lcsh:MedicinebiofilmCell membraneadhésionCandida albicanslcsh:ScienceCandida albicansRecombination Genetic0303 health sciencesFungal proteinMultidisciplinaryCandida albicans;cell wall;protein;Rbt1;adhesion;biofilmbiologyFlow Cytometry3. Good healthCell biologyTransport proteinProtein Transportadhesionmedicine.anatomical_structureprotéineparoi cellulaireHydrophobic and Hydrophilic InteractionsResearch ArticleProtein domainSaccharomyces cerevisiaeHyphaeSaccharomyces cerevisiaeFungal ProteinsStructure-Activity Relationship03 medical and health sciencesCell AdhesionmedicineHumansAmino Acid SequenceCell adhesion030304 developmental biologySequence Homology Amino Acid030306 microbiologyCell Membranelcsh:Rfungibiology.organism_classificationRbt1Protein Structure TertiaryMembrane proteinBiofilmsPolystyrenescell walllcsh:Qprotein
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Thermodynamics and kinetics of ion permeation in wild-type and mutated open active conformation of the human α7 nicotinic receptor

2020

Molecular studies of human pentameric ligand-gated ion channels (LGICs) expressed in neurons and at neuromuscular junctions are of utmost importance in the development of therapeutic strategies for neurological disorders. We focus here on the nicotinic acetylcholine receptor nAChR-α7, a homopentameric channel widely expressed in the human brain, with a proven role in a wide spectrum of disorders including schizophrenia and Alzheimer's disease. By exploiting an all-atom structural model of the full (transmembrane and extracellular) protein in the open, agonist-bound conformation we recently developed, we evaluate the free energy and the mean first passage time of single-ion permeation using …

alpha7 Nicotinic Acetylcholine ReceptorProtein ConformationGeneral Chemical EngineeringMutantProtonationLibrary and Information SciencesMolecular Dynamics SimulationReceptors Nicotinic01 natural sciencesArticleMolecular dynamics0103 physical sciencesHumansPotential of mean forceIon channel010304 chemical physicsChemistryWild typeGeneral ChemistryTransmembrane protein0104 chemical sciencesComputer Science Applications010404 medicinal & biomolecular chemistryNicotinic acetylcholine receptorKineticsnicotinic receptor ion permeation Milestoning free energyBiophysicsThermodynamics
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Activation of TRK Genes in Ewingʼs Sarcoma Trk A Receptor Expression Linked to Neural Differentiation

1997

Trk receptors have been identified by immunohistochemical methods in primitive neuroectodermal tumor (PNET)/Ewing's sarcoma (ES). However, the presence of different members of the Trk family of receptors in PNET/ES has not been specified. We have examined whether Trk A, B, and C receptors are specifically expressed in ES both with and without features of neural differentiation. Ten ES tumors (five primary tumors of bone and five extraosseous tumors transplanted into nude mice) were investigated for expression of Trk receptors by immunohistochemistry and reverse transcription-polymerase chain reaction. One primary ES and the five grafted ES tumors exhibited signs of neural differentiation; t…

animal structuresReceptor expressionReceptors Nerve Growth FactorSarcoma EwingBiologyPathology and Forensic MedicineMiceProto-Oncogene ProteinsmedicineAnimalsNeuroectodermal Tumors PrimitiveReceptor trkCReceptor trkAReceptorReceptor Ciliary Neurotrophic FactorMolecular BiologyNeuronsMembrane ProteinsReceptor Protein-Tyrosine KinasesEwing's sarcomaCell DifferentiationCell BiologyProtein-Tyrosine Kinasesmedicine.diseaseMolecular biologyGene Expression Regulation Neoplasticenzymes and coenzymes (carbohydrates)nervous systemTrk receptorPrimitive neuroectodermal tumorembryonic structuresImmunohistochemistrySarcomaImmunostainingDiagnostic Molecular Pathology
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The binding of G-protein to rod outer segment phospholipids at the nitrogen–water interface

1989

In the visual process, one photoexcited rhodopsin (R*) catalyzes the activation of hundreds of G-proteins. It remains to be determined whether G-protein and R* find one another by membrane surface diffusion of these components (diffusion model) or by diffusion of G-protein through the aqueous phase (hopping model). A monolayer of each main rod outer segment (ROS) phospholipid interacting with a subphase containing G-protein, has been used to simulate the interaction of G-protein with the cytoplasmic surface of discal membranes. The possible diffusion of G-protein through the aqueous phase was then measured by observing its adsorption–desorption in the monolayer of each main ROS phospholipi…

biologyChemistryAqueous two-phase systemPhospholipidMembrane ProteinsCell BiologySurface pressureBiochemistryCrystallographychemistry.chemical_compoundMembraneGTP-Binding ProteinsCytoplasmRhodopsinMonolayerbiology.proteinAnimalsCattlePhotoreceptor CellsDiffusion (business)Molecular BiologyPhospholipidsBiochemistry and Cell Biology
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**Arabidopsis thaliana** sequence analysis confirms the presence of cyt b-561 in plants: evidence for a novel protein family

2000

Recent advances in the Arabidopsis sequencing project has elucidated the presence of two genes Atb561-A and Atb561-B that show limited homology to the DNA sequence encoding for the mammalian chromaffin granule cytochrome b-561 (cyt b-561). Detailed analysis of the structural features and conserved residues reveals, however, that the structural homology between the presumptive Arabidopsis proteins and the animal proteins is very high. All proteins are hydrophobic and show highly conserved transmembrane helices. The presumably heme-binding histidine residues in the plant and animal sequences as well as the suggested binding site for the electron acceptor, monodehydroascorbate, are strictly co…

biologyPhysiologySequence analysisPlant ScienceChromaffin granule membranebiology.organism_classificationAscorbic acidTransmembrane proteinHomology (biology)Transmembrane domainMembrane proteinBiochemistryArabidopsisGeneticsPlant physiology and biochemistry
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