Search results for "Plasma protein binding"

showing 10 items of 178 documents

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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Low density lipoproteins and human serum albumin as the carriers of squalenoylated drugs: insights from molecular simulations

2018

We have studied the interaction of three clinically promising squalenoylated drugs (gemcitabine-squalene, adenine-squalene, and doxorubicin-squalene) with low-density lipoproteins (LDL) by means of atomistic molecular dynamics simulations. It is shown that all studied squalenoylated drugs accumulate inside the LDL particles. This effect is promoted by the squalene moiety, which acts as an anchor and drives the hydrophilic drugs into the hydrophobic core of the LDL lipid droplet. Our data suggest that LDL particles could be a universal carriers of squalenoylated drugs in the bloodstream. Interaction of gemcitabine-squalene with human serum albumin (HSA) was also studied by ensemble of dockin…

Squalene[PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]Drug CompoundingPharmaceutical ScienceSerum Albumin Human02 engineering and technologyPlasma protein bindingMolecular Dynamics Simulation010402 general chemistry01 natural sciencesMolecular Docking SimulationDeoxycytidineSqualenechemistry.chemical_compound[ PHYS.PHYS.PHYS-BIO-PH ] Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]Lipid dropletDrug DiscoverymedicineMoietyHumansComputingMilieux_MISCELLANEOUSDrug CarriersBinding SitesAdenine[SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences021001 nanoscience & nanotechnologyHuman serum albuminGemcitabine3. Good health0104 chemical sciences[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryLipoproteins LDLMolecular Docking Simulation[ SDV.SP ] Life Sciences [q-bio]/Pharmaceutical scienceschemistryDocking (molecular)Doxorubicin[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistryBiophysicsMolecular MedicineNanoparticles0210 nano-technologyDrug carrierHydrophobic and Hydrophilic Interactionsmedicine.drugProtein Binding
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Characterization of the binding of benzodiazepines to human serum albumin

1973

The binding of eleven benzodiazepine derivatives to human serum albumin (HSA) was determined by means of sephadex gel filtration. The albumin binding of the substances was characterized by the percentage of bound drug, the binding constants k +, K 1 and m, the number of binding sites per albumin molecule, and the free binding energy. Under the conditions chosen in these experiments there seems to exist only one binding site of the same type for all investigated benzodiazepines at the HSA molecule. The affinities of the benzodiazepines to this binding site are very different. It is discussed which part of the benzodiazepine molecule represents the main binding group.

StereochemistryBinding energySerum albuminPlasma protein bindingFlurazepammedicineHumansNitrazepamBovine serum albuminBinding siteSerum AlbuminPharmacologyBinding SitesbiologyOxazepamChemistryAlbuminChlordiazepoxideGeneral MedicineBenzazepinesHuman serum albuminSephadexChromatography Gelbiology.proteinProtein Bindingmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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Antibodies directed to drug epitopes to investigate the structure of drug-protein photoadducts. Recognition of a common photobound substructure in ti…

2001

Drug-induced photoallergy is an immune adverse reaction to the combined effect of drugs and light. From the mechanistic point of view, it first involves covalent binding of drug to protein resulting in the formation of a photoantigen. Hence, determination of the structures of drug-protein photoadducts is of great relevance to understand the molecular basis of photoallergy and cross-immunoreactivity among drugs. Looking for new strategies to investigate the covalent photobinding of drugs to proteins, we generated highly specific antibodies to drug chemical substructures. The availability of such antibodies has allowed us to discriminate between the different modes by which tiaprofenic acid (…

StereochemistrySuprofenSuprofenPlasma protein bindingThiophenesToxicologyEpitopeAntibodieschemistry.chemical_compoundEpitopesStructure-Activity RelationshipThiophenemedicineMoietyStructure–activity relationshipAnimalsHumansDermatitis PhotoallergicAnti-Inflammatory Agents Non-SteroidalBenzeneGeneral MedicinechemistryCovalent bondKetoprofenAntibody FormationRabbitsPropionatesTiaprofenic acidmedicine.drugProtein BindingChemical research in toxicology
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