Search results for "PEPTIDE"

showing 10 items of 4589 documents

Hydrophobic mismatch of mobile transmembrane helices: Merging theory and experiments

2012

Abstract Hydrophobic mismatch still represents a puzzle for transmembrane peptides, despite the apparent simplicity of this concept and its demonstrated validity in natural membranes. Using a wealth of available experimental 2 H NMR data, we provide here a comprehensive explanation of the orientation and dynamics of model peptides in lipid bilayers, which shows how they can adapt to membranes of different thickness. The orientational adjustment of transmembrane α-helices can be understood as the result of a competition between the thermodynamically unfavorable lipid repacking associated with peptide tilting and the optimization of peptide/membrane hydrophobic coupling. In the positive misma…

BiophysicsAnchoringPeptideBiochemistryProtein Structure SecondaryHydrophobic mismatchXWALP peptide familyDynamics of transmembrane peptidesOrientation of transmembrane peptidesWALP peptide familyLipid bilayerPeptide sequencechemistry.chemical_classificationCell MembraneMembrane ProteinsCell BiologyTransmembrane proteinCrystallographyTransmembrane domainMembranechemistryModels ChemicalBiophysicsHydrophobic and Hydrophilic InteractionsPeptide tilt angleSolid-state 2H NMRBiochimica et Biophysica Acta (BBA) - Biomembranes
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Implication of three isoforms of PLA2in human T-cell proliferation

2002

We observed that human (Jurkat) T-cells constitutively expressed the mRNA, encoding for the four isoforms of phospholipase A(2) (PLA(2)), i.e. two secretory (type IB and type V), and two cytosolic (type IV, Ca(2+)-dependent and type VI, Ca(2+)-independent). In order to assess whether these PLA(2) isoforms are active, we labeled Jurkat T-cells with [(3)H]arachidonic acid ([(3)H]AA) and determined its release into the extracellular medium in the presence of phorbol 12-myristate 13-acetate (PMA) and ionomycin. The three PLA(2) isoforms seem functional as aristolochic acid and bromoenol lactone (BEL), the respective inhibitors of type IB/type V and type VI PLA(2)s, significantly inhibited the r…

BiophysicsAristolochic acidArachidonic AcidsPhospholipaseTritiumBiochemistryJurkat cellsGene Expression Regulation EnzymologicPhospholipases AJurkat Cellschemistry.chemical_compoundPhospholipase A2Structural BiologyGeneticsHumansPhospholipaseRNA MessengerEnzyme InhibitorsMolecular BiologyArachidonyl trifluoromethyl ketoneArachidonic AcidbiologyIonomycinCell BiologyJurkat T-cellIsoenzymesGene Expression RegulationchemistryBiochemistryIonomycinPhorbolbiology.proteinInterleukin-2Tetradecanoylphorbol AcetateCalciumlipids (amino acids peptides and proteins)Arachidonic acidCell DivisionFEBS Letters
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Small unilamellar liposomes from mixed natural and polymeric phospholipids: stability and susceptibility to phospholipase A2.

1991

The concept of the uncorkable liposome composed of phase-separated mixtures of a polymerized phospholipid and an enzymically digestible phospholipid has been investigated, using small unilamellar vesicles composed of mixtures of (polymerized) dienoylphosphatidylcholine (DENPC) and dimyristoylphosphatidylcholine (DMPC). Mixed liposomes, even those containing only 10% DENPC, were much more stable than DMPC liposomes, as indicated by the release of entrapped [3H]inulin or [14C]glucose. DMPC liposomes released entrapped solute on exposure to phospholipase A2, whereas mixed vesicles were resistant. The results are compared with those of an earlier study on monolayers of similar compositions. It …

BiophysicsPhospholipidSynthetic membraneTritiumBiochemistryPhospholipases Achemistry.chemical_compoundEndocrinologyPhospholipase A2MonolayerCarbon RadioisotopesPhospholipidsPhospholipase ALiposomeChromatographybiologyVesicleBilayertechnology industry and agricultureInulinTemperatureHydrogen-Ion ConcentrationPhospholipases A2GlucosechemistryLiposomesbiology.proteinlipids (amino acids peptides and proteins)DimyristoylphosphatidylcholineBiochimica et biophysica acta
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Recessive mutations in EPG5 cause Vici syndrome, a multisystem disorder with defective autophagy

2013

Vici syndrome is a recessively inherited multisystem disorder characterized by callosal agenesis, cataracts, cardiomyopathy, combined immunodeficiency and hypopigmentation. To investigate the molecular basis of Vici syndrome, we carried out exome and Sanger sequence analysis in a cohort of 18 affected individuals. We identified recessive mutations in EPG5 (previously KIAA1632), indicating a causative role in Vici syndrome. EPG5 is the human homolog of the metazoan-specific autophagy gene epg-5, encoding a key autophagy regulator (ectopic P-granules autophagy protein 5) implicated in the formation of autolysosomes. Further studies showed a severe block in autophagosomal clearance in muscle a…

BiopsyVesicular Transport ProteinsAutophagy-Related ProteinsGenes RecessiveConsanguinityBiologymedicine.disease_causeArticleCataract03 medical and health sciencesConsanguinity0302 clinical medicineCataractsAntigens NeoplasmGeneticsmedicineAutophagyHumansVici syndromeExomeFamilyMuscle SkeletalExomeImmunodeficiency030304 developmental biologyGenetics0303 health sciencesMutationAutophagyIntracellular Signaling Peptides and ProteinsLysosome-Associated Membrane GlycoproteinsProteinsmedicine.diseaseMutationAutophagy Protein 5Agenesis of Corpus CallosumLysosomes030217 neurology & neurosurgeryNature genetics
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αv-Class integrin binding to fibronectin is solely mediated by RGD and unaffected by an RGE mutation.

2020

Fibronectin (FN) is an essential glycoprotein of the extracellular matrix; binds integrins, syndecans, collagens, and growth factors; and is assembled by cells into complex fibrillar networks. The RGD motif in FN facilitates cell binding and fibrillogenesis through binding to α5β1 and αv-class integrins. However, whether RGD is the sole binding site for αv-class integrins is unclear. Most notably, substituting aspartate with glutamate (RGE) was shown to eliminate integrin binding in vitro, while mouse genetics revealed that FNRGE preserves αv-class integrin binding and fibrillogenesis. To address this conflict, we employed single-cell force spectroscopy, engineered cells, and RGD motif–defi…

BioquímicaBiologiaIntegrin02 engineering and technologyBiologyBiochemistryArticleFocal adhesion03 medical and health sciencesMiceAnimalsReceptors VitronectinBinding siteCell adhesion030304 developmental biologyIntegrin bindingRGD motif0303 health sciencesCorrectionFibrillogenesisCell Biology021001 nanoscience & nanotechnologyMice Mutant StrainsCell biologyFibronectinMutationAdhesionbiology.protein0210 nano-technologyOligopeptidesThe Journal of cell biology
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TORC1 controls G1–S cell cycle transition in yeast via Mpk1 and the greatwall kinase pathway

2015

The target of rapamycin complex 1 (TORC1) pathway couples nutrient, energy and hormonal signals with eukaryotic cell growth and division. In yeast, TORC1 coordinates growth with G1–S cell cycle progression, also coined as START, by favouring the expression of G1 cyclins that activate cyclin-dependent protein kinases (CDKs) and by destabilizing the CDK inhibitor Sic1. Following TORC1 downregulation by rapamycin treatment or nutrient limitation, clearance of G1 cyclins and C-terminal phosphorylation of Sic1 by unknown protein kinases are both required for Sic1 to escape ubiquitin-dependent proteolysis prompted by its flagging via the SCFCdc4 (Skp1/Cul1/F-box protein) ubiquitin ligase complex.…

BioquímicaBiologiaSaccharomyces cerevisiae ProteinsImmunoblottingGeneral Physics and AstronomyCell Cycle ProteinsSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1ArticleGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineCyclin-dependent kinaseCyclinsImmunoprecipitationProtein Phosphatase 2Cell division control protein 4PhosphorylationProtein kinase ACyclin-Dependent Kinase Inhibitor Proteins030304 developmental biology0303 health sciencesMultidisciplinarybiologyTOR Serine-Threonine KinasesUbiquitin-Protein Ligase ComplexesGeneral ChemistryBlotting NorthernFlow CytometryG1 Phase Cell Cycle CheckpointsSic1Cyclin-Dependent KinasesCell biologyBiochemistryMultiprotein Complexes030220 oncology & carcinogenesisUbiquitin ligase complexbiology.proteinIntercellular Signaling Peptides and ProteinsPhosphorylationTOR Serine-Threonine KinasesMitogen-Activated Protein KinasesPeptidesProtein KinasesCyclin-dependent kinase inhibitor proteinNature Communications
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Valproate and Short-Chain Fatty Acids Activate Transcription of the Human Vitamin D Receptor Gene through a Proximal GC-Rich DNA Region Containing Tw…

2022

The vitamin D receptor (VDR) mediates 1,25-dihydroxyvitamin D3 pleiotropic biological actions through transcription regulation of target genes. The expression levels of this ligand-activated nuclear receptor are regulated by multiple mechanisms both at transcriptional and post-transcriptional levels. Vitamin D3 is the natural VDR activator, but other molecules and signaling pathways have also been reported to regulate VDR expression and activity. In this study, we identify valproic acid (VPA) and natural short-chain fatty acids (SCFAs) as novel transcriptional activators of the human VDR (hVDR) gene. We further report a comprehensive characterization of VPA/SCFA-responsive elements in the 5…

BioquímicaBiologiaVDR induction; human VDR promoter; valproic acid; SCFA; Sp1.Binding SitesNutrition and DieteticsSp1 Transcription FactorValproic AcidDNAHumansReceptors Calcitriollipids (amino acids peptides and proteins)ChildPromoter Regions GeneticFood Science
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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
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Double-spanning Plant Viral Movement Protein Integration into the Endoplasmic Reticulum Membrane Is Signal Recognition Particle-dependent, Translocon…

2005

The current model for cell-to-cell movement of plant viruses holds that transport requires virus-encoded movement proteins that intimately associate with endoplasmic reticulum membranes. We have examined the early stages of the integration into endoplasmic reticulum membranes of a double-spanning viral movement protein using photocross-linking. We have discovered that this process is cotranslational and proceeds in a signal recognition particle-dependent manner. In addition, nascent chain photocross-linking to Sec61alpha and translocating chain-associated membrane protein reveal that viral membrane protein insertion takes place via the translocon, as with most eukaryotic membrane proteins, …

BioquímicaSec61Vesicle-associated membrane protein 8Receptors PeptideLipid BilayersReceptors Cytoplasmic and NuclearBiologyEndoplasmic ReticulumBiochemistryViral ProteinsMembranes (Biologia)Escherichia coliMolecular BiologySignal recognition particle receptorSignal recognition particleMembrane GlycoproteinsEndoplasmic reticulumCalcium-Binding ProteinsMembrane ProteinsSTIM1Cell BiologyTransloconTransmembrane proteinCell biologyPlant Viral Movement ProteinsCross-Linking ReagentsMutagenesisRNA ViralCarmovirusSignal Recognition ParticleSEC Translocation Channels
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Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein

2004

This article is available from: http://www.biomedcentral.com/1472-6807/4/7

BioquímicaSerum Amyloid A Proteinendocrine systemArabidopsis ProteinsProtein ConformationMolecular Sequence DataOsmolar ConcentrationArabidopsisBiological TransportProtein Structure Secondarylcsh:Biology (General)Amino Acid SequencePeptidesProteïneslcsh:QH301-705.5CopperMolecular ChaperonesResearch Article
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