Search results for "plasma protein"

showing 10 items of 193 documents

Thin-layer affinity chromatography in analysis of protein-ligand affinity.

1996

Protein DenaturationHot TemperatureThin layerIon chromatographyBiophysicsPlasma protein bindingLigandsBiochemistryChromatography AffinityAffinity chromatographyHumansMolecular BiologyFluorescent DyesChromatographybiologyChemistryProteinsCell BiologyAvidinFibronectinsFibronectinsbiology.proteinChromatography Thin LayerAzo CompoundsProtein ligandAvidinProtein BindingAnalytical biochemistry
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Heparan sulfate proteoglycans interact exclusively with conformationally intact HPV L1 assemblies: basis for a virus-like particle ELISA.

2004

In this article, we demonstrate that interaction of human papillomavirus-like particles (HPV-VLPs) with the putative glucosaminoglycan binding receptor is strictly dependent on conformational integrity. Such conformations are present on VLPs and capsomeres but not on monomers of the major capsid protein, L1, confirming reports that capsomeres can induce virus-neutralizing antibodies. Furthermore, we show the suitability of this specific interaction for development of VLP-based enzyme-linked immunosorbent assays (ELISAs), using heparin for indirect coupling of VLPs to microtiter plates, which may add an intrinsic quality control. This avoids presentation of linear, often highly cross-reactiv…

Protein DenaturationProtein ConformationvirusesEnzyme-Linked Immunosorbent AssayPlasma protein bindingCross ReactionsAntibodies ViralEpitopeEpitopesProtein structureVirus-like particleNeutralization TestsVirologyCentrifugation Density GradientHumansPapillomaviridaeGlycosaminoglycansbiologyHeparinCapsomerevirus diseasesOncogene Proteins ViralVirologyInfectious DiseasesProteoglycanCapsidbiology.proteinReceptors VirusCapsid ProteinsHeparan Sulfate ProteoglycansConformational epitopeProtein BindingJournal of medical virology
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Heavy Metals and Human Health: Possible Exposure Pathways and the Competition for Protein Binding Sites

2021

Heavy metals enter the human body through the gastrointestinal tract, skin, or via inhalation. Toxic metals have proven to be a major threat to human health, mostly because of their ability to cause membrane and DNA damage, and to perturb protein function and enzyme activity. These metals disturb native proteins’ functions by binding to free thiols or other functional groups, catalyzing the oxidation of amino acid side chains, perturbing protein folding, and/or displacing essential metal ions in enzymes. The review shows the physiological and biochemical effects of selected toxic metals interactions with proteins and enzymes. As environmental contamination by heavy metals is one of the most…

Protein FoldingDNA damagePharmaceutical ScienceOrganic chemistryPlasma protein bindingReviewCosmeticsAnalytical ChemistryBioremediationQD241-441bioremediationDetoxificationMetals HeavyDrug DiscoveryHumansPhysical and Theoretical Chemistryheavy metalschemistry.chemical_classificationBinding SitesbiologyChemistryEnvironmental ExposureinteractionsEnzyme assayproteinsAmino acidEnzymesEnzymeBiodegradation EnvironmentalBiochemistryChemistry (miscellaneous)Foodexposurebiology.proteinMolecular MedicineProtein foldingEnvironmental PollutantsDNA DamageProtein BindingMolecules
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RNA-binding ability of PIPP in requires the entire protein

2003

Post-transcriptional fate of eukaryotic mRNAs depends on association with different classes of RNA-binding proteins (RBPs). Among these proteins, the cold-shock domain (CSD)-containing proteins, also called Y-box proteins, play a key role in controlling the recruitment of mRNA to the translational machinery, in response to environmental cues, both in development and in differentiated cells. We recently cloned a rat cDNA encoding a new CSD-protein that we called PIPPin. This protein also contains two putative double-stranded RNA-binding motifs (PIP(1) and PIP(2)) flanking the central CSD, and is able to bind mRNAs encoding H1 degrees and H3.3 histone variants. In order to clarify the role of…

Protein FoldingNerve Tissue ProteinsSequence alignmentRNA-binding proteinPlasma protein bindingArticleRNA-binding proteinscold-shock domainPIPPinhistone variantsHistonesSettore BIO/10 - BiochimicaComplementary DNAHistone H2AAnimalsRNA MessengerGeneticsMessenger RNAbiologyRNA-Binding ProteinsRNACell BiologyRecombinant ProteinsProtein Structure TertiaryRatsCell biologyHistoneGene Expression Regulationbiology.proteinMolecular MedicineSequence AlignmentProtein BindingJournal of Cellular and Molecular Medicine
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The membrane proximal cytokine receptor domain of the human interleukin-6 receptor is sufficient for ligand binding but not for gp130 association.

1998

Interleukin-6 (IL-6) belongs to the family of the "four-helix bundle" cytokines. The extracellular parts of their receptors consist of several Ig- and fibronectin type III-like domains. Characteristic of these receptors is a cytokine-binding module consisting of two such fibronectin domains defined by a set of four conserved cysteines and a tryptophan-serine-X-tryptophan-serine (WSXWS) sequence motif. On target cells, IL-6 binds to a specific IL-6 receptor (IL-6R), and the complex of IL-6.IL-6R associates with the signal transducing protein gp130. The IL-6R consists of three extracellular domains. The NH2-terminal Ig-like domain is not needed for ligand binding and signal initiation. Here w…

Protein FoldingProtein ConformationEnzyme-Linked Immunosorbent AssayPlasma protein bindingImmunoglobulin domainBiologyLigandsBiochemistryHAMP domainAntigens CDCytokine Receptor gp130HumansMolecular BiologyDNA PrimersMembrane GlycoproteinsBase SequenceInterleukin-6Cell BiologyHydrogen-Ion ConcentrationGlycoprotein 130Precipitin TestsReceptors Interleukin-6Recombinant ProteinsCell biologyKineticsBiochemistryMATH domainSignal transductionCytokine receptorBinding domainProtein BindingSignal TransductionThe Journal of biological chemistry
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Potential of human serum albumin as chiral selector of basic drugs in affinity electrokinetic chromatography-partial filling technique

2006

The enantiomeric resolution of compounds using HSA by means of affinity EKC (AEKC)-partial filling technique is the result of a delicate balance between different experimental variables such as protein concentration, running pH (background electrophoretic buffer (BGE), protein, and compound solutions), and plug length. In this paper, the possibility of using HSA as chiral selector for enantioseparation of 28 basic drugs using this methodology is studied. The effect of the physicochemical parameters, the structural properties of compounds, and compound-HSA protein binding percentages over their chiral resolution with HSA is outlined. Based on the results obtained, a decision tree is proposed…

Resolution (mass spectrometry)Clinical BiochemistryPlasma protein bindingBuffersBiochemistryChromatography AffinityAnalytical ChemistryElectrokinetic phenomenaMolar volumemedicineHumansSerum AlbuminChromatography Micellar Electrokinetic CapillaryChromatographyMolecular StructureChemistryStereoisomerismHydrogen-Ion ConcentrationHuman serum albuminChiral resolutionbody regionsElectrophoresisPharmaceutical Preparationsembryonic structuresEnantiomerHydrophobic and Hydrophilic Interactionsmedicine.drugELECTROPHORESIS
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Direct interaction of the Usher syndrome 1G protein SANS and myomegalin in the retina

2011

Contains fulltext : 96822.pdf (Publisher’s version ) (Closed access) The human Usher syndrome (USH) is the most frequent cause of combined hereditary deaf-blindness. USH is genetically heterogeneous with at least 11 chromosomal loci assigned to 3 clinical types, USH1-3. We have previously demonstrated that all USH1 and 2 proteins in the eye and the inner ear are organized into protein networks by scaffold proteins. This has contributed essentially to our current understanding of the function of USH proteins and explains why defects in proteins of different families cause very similar phenotypes. We have previously shown that the USH1G protein SANS (scaffold protein containing ankyrin repeat…

Scaffold proteinUsher syndromePhosphodiesterase 4D interacting protein (PDE4DIP)Muscle ProteinsPlasma protein bindingMice0302 clinical medicineYeastsChlorocebus aethiopsNuclear proteinCells CulturedGenetics0303 health scienceseducation.field_of_studyNuclear ProteinsCell biologyCOS CellssymbolsPhotoreceptor Cells VertebrateProtein BindingMicrotubule based transportNerve Tissue ProteinsBiologyModels BiologicalRetina03 medical and health sciencessymbols.namesakemedicineAnimalsHumanseducationMolecular BiologyAdaptor Proteins Signal Transducing030304 developmental biologyCell BiologyGlycostation disorders [IGMD 4]Golgi apparatusmedicine.diseaseMacaca mulattaMice Inbred C57BLCytoskeletal ProteinsPhotoreceptor cell functionMyomegalinGenetics and epigenetic pathways of disease Functional Neurogenomics [NCMLS 6]CattleAnkyrin repeatCiliary baseIntracellular transport030217 neurology & neurosurgerySensorineuronal degeneration
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Proprotein convertase 5/6 is critical for embryo implantation in women: regulating receptivity by cleaving ebp50, modulating ezrin binding, and membr…

2011

Establishment of endometrial receptivity is vital for successful embryo implantation; its failure causes infertility. Epithelial receptivity acquisition involves dramatic structural changes in the plasma membrane and cytoskeleton. Proprotein convertase 5/6 (PC6), a serine protease of the proprotein convertase (PC) family, is up-regulated in the human endometrium specifically at the time of epithelial receptivity and stromal cell decidualization. PC6 is the only PC member tightly regulated in this manner. The current study addressed the importance and mechanisms of PC6 action in regulating receptivity in women. PC6 was dysregulated in the endometrial epithelium during the window of implantat…

Scaffold proteinmedicine.medical_specialtySodium-Hydrogen ExchangersPlasma protein bindingBiologyEndometriumMiceEndocrinologyEzrinInternal medicinemedicineAnimalsHumansEmbryo ImplantationCytoskeletonCytoskeletonCellular localizationBinding proteinDecidualizationEpithelial CellsPhosphoproteinsProprotein convertaseCytoskeletal ProteinsEndocrinologyProprotein Convertase 5FemaleProtein Binding
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The role of the silicatein-alpha interactor silintaphin-1 in biomimetic biomineralization.

2008

Biosilicification in sponges is initiated by formation of proteinaceous filaments, predominantly consisting of silicateins. Silicateins enzymatically catalyze condensation of silica nanospheres, resulting in symmetric skeletal elements (spicules). In order to create tailored biosilica structures in biomimetic approaches it is mandatory to elucidate proteins that are fundamental for the assembly of filaments. Silintaphin-1 is a core component of modularized filaments and also part of a spicule-enfolding layer. It bears no resemblance to other proteins, except for the presence of an interaction domain that is fundamental for its function as scaffold/template. In the presence of silicatein sil…

ScaffoldMaterials scienceDNA ComplementaryMolecular Sequence DataSilicic AcidBiophysicsNanoparticleBioengineeringNanotechnologyPlasma protein bindingFerric CompoundsAntibodiesBiomaterialsSponge spiculeCalcification PhysiologicBiomimetic MaterialsTwo-Hybrid System TechniquesAnimalsRegenerationInteractorAmino Acid SequencebiologyCore componentProteinsbiology.organism_classificationEnzymes ImmobilizedCathepsinsRecombinant ProteinsProtein TransportMechanics of MaterialsCeramics and CompositesSuberitesSuberitesBiomineralizationProtein BindingBiomaterials
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Albumin-driven disassembly of lipidic nanoparticles: the specific case of the squalene-adenosine nanodrug

2020

International audience; In the field of nanomedicine, nanostructured nanoparticles (NPs) made of self-assembling prodrugs emerged in the recent years with promising properties. In particular, squalene-based drug nanoparticles have already shown their efficiency through in vivo experiments. However, a complete pattern of their stability and interactions in the blood stream is still lacking. In this work we assess the behavior of squalene-adenosine (SQAd) nanoparticles-whose neuroprotective effect has already been demonstrated in murine models-in the presence of fetal bovine serum (FBS) and of bovine serum albumin (BSA), the main protein of blood plasma. Extensive physicochemical characteriza…

SqualeneAdenosinecomplexationserum albuminSerum albumin02 engineering and technologyPlasma protein binding010402 general chemistry01 natural sciencesMiceDrug StabilitymedicineAnimalsHumansGeneral Materials ScienceProdrugsColloidsBovine serum albuminComputingMilieux_MISCELLANEOUSBinding Sitesbiology[CHIM.ORGA]Chemical Sciences/Organic chemistryChemistryAlbuminIsothermal titration calorimetry[CHIM.MATE]Chemical Sciences/Material chemistry021001 nanoscience & nanotechnologyHuman serum albumindisassembly0104 chemical sciencesnanodrugbiology.proteinBiophysicsNanomedicineNanoparticles0210 nano-technologyFetal bovine serummedicine.drugProtein Binding
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