Search results for "Cell Membrane"

showing 5 items of 635 documents

Amphoteric, prevailingly cationic L-arginine polymers of poly(amidoamino acid) structure: Synthesis, acid/base properties and preliminary cytocompati…

2013

A linear amphoteric poly(amidoamino acid), L-ARGO7, is prepared by Michael-type polyaddition of L-arginine with N,N′-methylenebisacrylamide. Chain-extension of acrylamide end-capped L-ARGO7 oligomers with piperazine leads to high-molecular-weight copolymers in which L-arginine maintains its absolute configuration. Acid/base properties of L-ARGO7 polymers show isolectric points of ≈10 and positive net average charges per repeating unit at pH = 7.4 from 0.25 to 0.40. These arginine-rich synthetic polymers possibly share some of the unique biological properties of polyarginine cell-permeating peptides. In vitro tests with mouse embryo fibroblasts balb/3T3 clone A31 show that L-ARGO7 polymers a…

poly(amidoamine)Materials Chemistry2506 Metals and AlloyAcrylamidesCell Membrane PermeabilityPolymers and PlasticCell SurvivalL -arginine polymerMedicine (all)Static ElectricityBioengineeringHydrogen-Ion ConcentrationArgininebiological application of polymerBiomaterialPiperazinesMicebiocompatibilityNIH 3T3 CellsPolyaminesAnimalsIsoelectric Pointpoly(amidoamino acid)PeptidesHydrophobic and Hydrophilic InteractionsBiotechnology
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Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O

2001

The pore-forming toxin streptolysin O (SLO) can be used to reversibly permeabilize adherent and nonadherent cells, allowing delivery of molecules with up to 100 kDa mass to the cytosol. Using FITC-labeled albumin, 10 5 –10 6 molecules were estimated to be entrapped per cell. Repair of toxin lesions depended on Ca 2+ -calmodulin and on intact microtubules, but was not sensitive to actin disruption or to inhibition of protein synthesis. Resealed cells were viable for days and retained the capacity to endocytose and to proliferate. The active domains of large clostridial toxins were introduced into three different cell lines. The domains were derived from Clostridium difficile B-toxin and Clo…

rho GTP-Binding ProteinsCell Membrane PermeabilityGlycosylationCell SurvivalBacterial ToxinsClostridium difficile toxin AClostridium difficile toxin BBiologymedicine.disease_causeCell LineBacterial ProteinsAlbuminsChlorocebus aethiopsTumor Cells CulturedmedicineAnimalsHumansSecretionParticle SizeActinMultidisciplinaryDose-Response Relationship DrugSecretory VesiclesProteinsBiological TransportDextransBiological SciencesActin cytoskeletonMolecular biologyRatsCell biologyCytosolImmunoglobulin GCOS CellsStreptolysinsras ProteinsClostridium botulinumStreptolysinProceedings of the National Academy of Sciences
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Functional adaptation of sarcolemma to physical stress

2010

sopeutuminenconduction velocityelectromyographyexercise induced damageeccentric exerciselihaksetmuscle fibressolukalvotfyysinen kuormittavuuscell membranes
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SARS-CoV-2 envelope protein topology in eukaryotic membranes

2020

Coronavirus E protein is a small membrane protein found in the virus envelope. Different coronavirus E proteins share striking biochemical and functional similarities, but sequence conservation is limited. In this report, we studied the E protein topology from the new SARS-CoV-2 virus both in microsomal membranes and in mammalian cells. Experimental data reveal that E protein is a single-spanning membrane protein with the N-terminus being translocated across the membrane, while the C-terminus is exposed to the cytoplasmic side (Nt lum /Ct cyt ). The defined membrane protein topology of SARS-CoV-2 E protein may provide a useful framework to understand its interaction with other viral and ho…

virusescoronavirusmedicine.disease_causeViral Envelope Proteinsmembrane insertionPeptide sequencelcsh:QH301-705.5Topology (chemistry)PhylogenyCoronavirusMutationChemistryGeneral NeuroscienceProteïnes de membranaEukaryotavirus diseases129Recombinant ProteinsCell biologysars-cov-2MembraneProtein topologyCoronavirus InfectionsResearch Article1001topologyPneumonia ViralImmunologySequence alignmentBiologyTopologiaVirusGeneral Biochemistry Genetics and Molecular BiologyBetacoronavirusCoronavirus Envelope ProteinsViral envelopeMicrosomesmedicineHumansAmino Acid SequencePandemicsResearchCell MembraneCOVID-1915envelope proteinMembrane proteinlcsh:Biology (General)CytoplasmMutationSequence AlignmentOpen Biology
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An experimental model for mimicking biological systems: the Belousov-Zhabotinsky reaction in Lipid membranes

2006

{LIPID} {BILAYERS}Belousov-Zhabotinsky reaction; Biomimetic systems; Cell membranes; Lipid bilayers; Morphogenesis; Self-organizing systemsEcologyLipid bilayersChemistryExperimental modelBelousov-Zhabotinsky reaction{BELOUSOV-ZHABOTINSKY} {REACTION}; Biomimetic systems; Cell membranes; {LIPID} {BILAYERS}; morphogenesis; Self-organizing systemsSelf-organizing systemsBiomimetic systemsCell membranesMembraneBelousov–Zhabotinsky reactionBiophysicsMorphogenesis{BELOUSOV-ZHABOTINSKY} {REACTION}Lipid bilayerEcology Evolution Behavior and Systematics
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