Search results for "membrana"

showing 10 items of 91 documents

Stitching proteins into membranes, not sew simple

2014

Abstract Most integral membrane proteins located within the endomembrane system of eukaryotic cells are first assembled co-translationally into the endoplasmic reticulum (ER) before being sorted and trafficked to other organelles. The assembly of membrane proteins is mediated by the ER translocon, which allows passage of lumenal domains through and lateral integration of transmembrane (TM) domains into the ER membrane. It may be convenient to imagine multi-TM domain containing membrane proteins being assembled by inserting their first TM domain in the correct orientation, with subsequent TM domains inserting with alternating orientations. However a simple threading model of assembly, with s…

BioquímicaChemistryEndoplasmic reticulumClinical BiochemistryProteïnes de membranaMembrane ProteinsNanotechnologyIntracellular MembranesEndoplasmic ReticulumTransloconBiochemistryTransmembrane proteinProtein Structure TertiaryProtein TransportMembraneMembrane proteinBiophysicsAnimalsHumansEndomembrane systemThreading (protein sequence)Molecular BiologyIntegral membrane proteinBiological Chemistry
researchProduct

Insertion and Topology of a Plant Viral Movement Protein in the Endoplasmic Reticulum Membrane

2002

Virus-encoded movement proteins (MPs) mediate cell-to-cell spread of viral RNA through plant membranous intercellular connections, the plasmodesmata. The molecular pathway by which MPs interact with viral genomes and target plasmodesmata channels is largely unknown. The 9-kDa MP from carnation mottle carmovirus (CarMV) contains two potential transmembrane domains. To explore the possibility that this protein is in fact an intrinsic membrane protein, we have investigated its insertion into the endoplasmic reticulum membrane. By using in vitro translation in the presence of dog pancreas microsomes, we demonstrate that CarMV p9 inserts into the endoplasmic reticulum without the aid of any addi…

BioquímicaGlycosylationMolecular Sequence DataPlasmodesmaBiologyEndoplasmic ReticulumTopologyBiochemistryProtein Structure SecondaryViral ProteinsAmino Acid SequenceMolecular BiologyEndoplasmic reticulumCarmovirusProteïnes de membranaMembrane ProteinsSTIM1Translation (biology)Cell Biologybiology.organism_classificationVirusCell biologyPlant Viral Movement ProteinsTobacco Mosaic VirusTransmembrane domainCytoplasmMembrane topologyCarmovirusJournal of Biological Chemistry
researchProduct

Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C):Structure and surface activity

2006

  Udgivelsesdato: 2006-Apr Surfactant protein C (SP-C) is an essential component for the surface tension-lowering activity of the pulmonary surfactant system. It contains a valine-rich alpha helix that spans the lipid bilayer, and is one of the most hydrophobic proteins known so far. SP-C is also an essential component of various surfactant preparations of animal origin currently used to treat neonatal respiratory distress syndrome (NRDS) in preterm infants. The limited supply of this material and the risk of transmission of infectious agents and immunological reactions have prompted the development of synthetic SP-C-derived peptides or recombinant humanized SP-C for inclusion in new prepar…

BioquímicaRecombinant membrain proteinSurface PropertiesSize-exclusion chromatographyMolecular Sequence DataPhospholipidBiophysicsBiologyBiochemistrylaw.inventionchemistry.chemical_compoundAffinity chromatographyPulmonary surfactantMembranes (Biologia)lawAnimalsHumansPulmonary surfactant-associated protein CAmino Acid SequenceLipid bilayerConserved SequencePhospholipidsMammalsDrug CarriersChromatographySequence Homology Amino AcidSP-CProteïnes de membranaSurfactant protein CPulmonary surfactantCell BiologyPulmonary Surfactant-Associated Protein CRecombinant ProteinsKineticschemistryBiochemistryRecombinant DNALipid-protein interactionPeptidesSequence Alignment
researchProduct

The role of hydrophobic matching on transmembrane helix packing in cells

2017

Folding and packing of membrane proteins are highly influenced by the lipidic component of the membrane. Here, we explore how the hydrophobic mismatch (the difference between the hydrophobic span of a transmembrane protein region and the hydrophobic thickness of the lipid membrane around the protein) influences transmembrane helix packing in a cellular environment. Using a ToxRED assay in Escherichia coli and a Bimolecular Fluorescent Complementation approach in human-derived cells complemented by atomistic molecular dynamics simulations we analyzed the dimerization of Glycophorin A derived transmembrane segments. We concluded that, biological membranes can accommodate transmembrane homo-di…

Cancer ResearchPhysiologyCèl·luleslcsh:Medicine010402 general chemistry114 Physical sciences01 natural sciencesBiochemistry Genetics and Molecular Biology (miscellaneous)03 medical and health sciencesHydrophobic mismatchhydrophobic matchhelix packingLipid bilayerlcsh:QH301-705.5030304 developmental biology0303 health sciencesChemistrylcsh:RGlycophorin AProteïnes de membranaGlycophorin ABiological membranetransmembrane domain dimerizationmembrane protein foldingTransmembrane protein0104 chemical sciencesFolding (chemistry)Transmembrane domainMembranelcsh:Biology (General)Membrane proteinBiophysicsMolecular MedicinemismatchResearch ArticleCell Stress
researchProduct

Gènes fongiques liés au calcium impliqués dans la mycorhize à arbuscules

2012

Fluctuations in intracellular (Ca2+) calcium levels generate signaling events and regulate different cellular processes. Whilst the implication of Ca2+ in plant cell responses during arbuscular mycorrhiza (AM) interactions is well documented, nothing is known about the regulation or role of this secondary meesenger in the fungal symbiont. The molecular basis of fungal calcium homeostasis in the AM symbiosis was analyzed by investigating the expression of Ca2+-related fungal genes. In a first study, G. mosseae genes putatively encoding a MAP3k-like protein kinase (Gm2) and a P-type ATPase (Gm152) were investigated. Both Ca2+-related genes were up-regulated by A. sinicum root exudates, sugges…

Cell signalingGlomus mosseaeHoméostase calcique[SDV]Life Sciences [q-bio]Protéines membranaires/nucléairesCa2+ homeostasiscalcium;gene;fungal;arbuscular mycorrhiza[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyChampignons mycorhizogènesGènes liés au Ca2+thesegeneMembrane/nuclear proteinsMycorrhizal fungi[SDV.SA] Life Sciences [q-bio]/Agricultural sciencescalciumarbuscular mycorrhizaCa2+-related genesTempo-spatial expressionInteractions symbiotiquesSignalisation cellulairefungal[SDE]Environmental SciencesGlomus intraradicesSymbiotic interactionsExpression tempo-spatiale
researchProduct

Réponses des cellules de Nicotiana tabacum à des molécules microbiennes : évènements de signalisation précoce, influence de la dynamique membranaire …

2018

In their natural environment plants are in close interaction with beneficial, neutral, or pathogenic microbes, which are highly dependent on carbon resources exuded by plant roots. Sugar transport, which is a key process of plant physiology, is essential to support the fate of plant-microbe interactions. During evolution, plants have acquired the ability to perceive microbial molecules, initiating specific signal transduction cascades and leading to adapted response for microbe lifestyles (avirulent, virulent, or benefic). Plant survival will depend on the nature of the induced mechanisms. My PhD work, carried out on a simplified experimental system, contributes to the understanding of mech…

Chitotetrasacchraides[SDV.SA]Life Sciences [q-bio]/Agricultural sciences[SDV.SA] Life Sciences [q-bio]/Agricultural sciencesInteractions plantes-MicroorganismesCryptogéineChitotétrasacchraidesNicotiana tabacum[SDV.EE.IEO] Life Sciences [q-bio]/Ecology environment/SymbiosisTrafic membranaireTransport de sucresSugar transportPlant-Microbe interactions[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyCryptogeinMembrane dynamics[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/Symbiosis
researchProduct

Roles of a conserved proline in the internal fusion peptide of Ebola glycoprotein

2004

AbstractThe structural determinants underlying the functionality of viral internal fusion peptides (IFPs) are not well understood. We have compared EBOwt (GAAIGLAWIPYFGPAAE), representing the IFP of the Ebola fusion protein GP, and EBOmut (GAAIGLAWIPYFGRAAE) derived from a non-functional mutant with conserved Pro537 substituted by Arg. P537R substitution did not abrogate peptide-membrane association, but interfered with the ability to induce bilayer destabilization. Structural determinations suggest that Pro537 is required to preserve a membrane-perturbing local conformation in apolar environments.

Circular dichroismEbola glycoproteinProtein insertion into membranesProlinePeptide conformationMutantMolecular Sequence DataBiophysicsBiochemistrySendai viruschemistry.chemical_compoundStructural BiologyGeneticsProlineAmino Acid SequenceMolecular BiologyPeptide sequencePOPCchemistry.chemical_classificationChemistryProteïnes de membranaCell BiologyEbolavirusFusion proteinPeptide FragmentsPeptide ConformationViral fusion peptideBiochemistryAvian Sarcoma VirusesLiposomesHIV-1PèptidsGlycoproteinPeptide–lipid interactionViral Fusion ProteinsFEBS Letters
researchProduct

Membrane protein integration into the Endoplasmic Reticulum

2011

Most integral membrane proteins are targeted, inserted and assembled in the endoplasmic reticulum (ER) membrane. The sequential and potentially overlapping events necessary for membrane protein integration take place at sites termed translocons, which comprise a specific set of membrane proteins acting in concert with ribosomes and, probably, molecular chaperones to ensure the success of the whole process. In this minireview, we summarize our current understanding of helical membrane protein integration at the endoplasmic reticulum, and highlight specific characteristics that affect the biogenesis of multispanning membrane proteins.

Cèl·lulesProteïnes de membrana
researchProduct

Leucociti polimorfonucleati e diabete mellito

2011

Fluidità della membrana leucocitaria integrine leucocitarie attivazione leucocitaria
researchProduct

Foto-reattori a membrana per la valorizzazione del CO2

2019

In questo lavoro è stata studiata la foto-riduzione del CO2 sotto irraggiamento con luce UV-Visibile, accoppiando per la prima volta la tecnologia del reattore continuo a membrana con l’utilizzo di catalizzatori a base di C3N4 puro o compositi C3N4-TiO2 dispersi in una matrice polimerica di Nafion.

Fotoreattori a membrana riduzione del CO2 fotocatalisiSettore CHIM/07 - Fondamenti Chimici Delle Tecnologie
researchProduct