Search results for " glycoprotein"

showing 10 items of 430 documents

The inorganic polymer, polyphosphate, blocks binding of SARS-CoV-2 spike protein to ACE2 receptor at physiological concentrations

2020

Graphical abstract The inorganic physiological polymer, polyphosphate, blocks binding of SARS-CoV-2 spike protein to ACE2 receptor at physiological concentrations. This discovery proposes polyphosphate as a new member of the host's antiviral innate immune defense.

Models Molecular0301 basic medicineAntiviral AgentsBiochemistryArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePolyphosphatesPolyphosphateHuman Umbilical Vein Endothelial Cellsotorhinolaryngologic diseasesHumansPlateletReceptorneoplasmsPharmacologychemistry.chemical_classificationBinding assayInnate immune systemSARS-CoV-2 spike S-proteinLigand binding assayPolyphosphateCOVID-19pathological conditions signs and symptomsdigestive system diseasesCOVID-19 Drug TreatmentAmino acidsurgical procedures operative030104 developmental biologyEnzymechemistryBiochemistry030220 oncology & carcinogenesisSpike Glycoprotein CoronavirusNanoparticlesAlkaline phosphataseAngiotensin-Converting Enzyme 2Protein BindingReceptors CoronavirusBiochemical Pharmacology
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Role of RNA Guanine Quadruplexes in Favoring the Dimerization of SARS Unique Domain in Coronaviruses

2020

ABSTRACTCoronaviruses may produce severe acute respiratory syndrome (SARS). As a matter of fact, a new SARS-type virus, SARS-CoV-2, is responsible of a global pandemic in 2020 with unprecedented sanitary and economic consequences for most countries. In the present contribution we study, by all-atom equilibrium and enhanced sampling molecular dynamics simulations, the interaction between the SARS Unique Domain and RNA guanine quadruplexes, a process involved in eluding the defensive response of the host thus favoring viral infection of human cells. Our results evidence two stable binding modes involving an interaction site spanning either the protein dimer interface or only one monomer. The …

Models Molecular0301 basic medicineLetterSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)DimerPneumonia ViralCoronaviruProtein dimerMolecular Dynamics SimulationViral infection01 natural sciencesVirusBetacoronavirus03 medical and health scienceschemistry.chemical_compound0302 clinical medicine0103 physical sciencesG-QuadruplexeHumans[CHIM]Chemical SciencesGeneral Materials Science030212 general & internal medicinePhysical and Theoretical ChemistryPandemicsEconomic consequences030304 developmental biology0303 health sciences010304 chemical physicsBetacoronaviruSARS-CoV-2ChemistryCoronavirus InfectionRational designCOVID-19RNASpike Glycoprotein3. Good healthG-Quadruplexes030104 developmental biologySettore CHIM/03 - Chimica Generale E InorganicaSpike Glycoprotein CoronavirusBiophysicsRNA ViralCoronavirus InfectionsGuanine-QuadruplexesDimerizationProtein Binding
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Identification of residues in the putative 5th helical region of human interleukin-6, important for activation of the IL-6 signal transducer, gp130

1996

AbstractWe have previously shown that L58 in the putative 5th helical region of human interleukin-6 (IL-6) is important for activation of the IL-6 signal transducer gp130 [de Hon et al. (1995) FEBS Lett. 369, 187–191]. To further explore the importance of individual residues in this region for gp130 activation we have now combined Ala substitutions of residues E52, S53, S54, K55, E56, L58 and E60 with other substitutions in IL-6, known to affect gp130 activation (Q160E and T163P). The combination mutant protein with L58A completely lost the capacity to induce the proliferation of XG-1 myeloma cells, and could effectively antagonize wild type IL-6 activity on these cells. Moreover, the data …

Models MolecularBiophysicsHuman Interleukin-6BiochemistryProtein Structure SecondaryStructure-function analysisgp130Signal Transducer gp130Antigens CDStructural BiologyMutant proteinCytokine Receptor gp130Escherichia coliTumor Cells CulturedGeneticsHumansPoint MutationCloning MolecularInterleukin 6Molecular BiologyAlanineMembrane GlycoproteinsbiologyInterleukin-6Wild typeCell BiologyGlycoprotein 130Recombinant ProteinsProtein Structure TertiaryCell biologyKineticsBiochemistryMutagenesis Site-Directedbiology.proteinLeukemia Erythroblastic AcuteMultiple MyelomaCell DivisionSignal TransductionFEBS Letters
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Signaling pathways of the TREM-1- and TLR4-mediated neutrophil oxidative burst.

2008

The triggering receptor expressed on myeloid cells 1 (TREM-1) is involved in the innate inflammatory response to microbial infections. Activation and expression of TREM-1 by polymorphonuclear neutrophils (PMN) occurs in concert with Toll-like receptors (TLR) such as TLR4 for bacterial lipopolysaccharide. However, it is currently unclear how this is mediated on a molecular level. Using pharmacological inhibitors and Western blot analysis we demonstrate that phosphatidyl inositide 3-kinase, phospholipase C and the mitogen-activated kinase p38MAPK are essential for the TREM-1- and TLR4-induced oxidative burst of human PMN. The activation of protein kinase B and extracellular signal-related kin…

Models MolecularLipopolysaccharideNeutrophilsBlotting WesternCell Separationp38 Mitogen-Activated Protein Kinaseschemistry.chemical_compoundPhosphatidylinositol 3-KinasesImmunology and AllergyHumansReceptors ImmunologicReceptorProtein kinase BRespiratory BurstMembrane GlycoproteinsPhospholipase CKinaseFlow CytometryTriggering Receptor Expressed on Myeloid Cells-1Respiratory burstCell biologyEnzyme ActivationToll-Like Receptor 4chemistryTLR4Signal transductionProto-Oncogene Proteins c-aktSignal TransductionJournal of innate immunity
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Mass Spectrometry and Structural Biology Techniques in the Studies on the Coronavirus-Receptor Interaction

2020

Mass spectrometry and some other biophysical methods, have made substantial contributions to the studies on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and human proteins interactions. The most interesting feature of SARS-CoV-2 seems to be the structure of its spike (S) protein and its interaction with the human cell receptor. Mass spectrometry of spike S protein revealed how the glycoforms are distributed across the S protein surface. X-ray crystallography and cryo-electron microscopy made huge impact on the studies on the S protein and ACE2 receptor protein interaction, by elucidating the three-dimensional structures of these proteins and their conformational changes. The…

Models MolecularProtein Conformation alpha-HelicalvirusesGene ExpressionPharmaceutical ScienceReviewPlasma protein bindingSevere Acute Respiratory Syndromemedicine.disease_causeAnalytical Chemistry0302 clinical medicineDrug Discovery030212 general & internal medicineReceptorPeptide sequenceCoronavirus0303 health sciencesChemistrySevere acute respiratory syndrome-related coronavirusBiochemistryChemistry (miscellaneous)Host-Pathogen InteractionsSpike Glycoprotein CoronavirusReceptors VirusMolecular MedicineAngiotensin-Converting Enzyme 2Coronavirus InfectionsProtein BindingglycosylationSARS coronavirusPneumonia Viralstructural techniquesSequence alignmentPeptidyl-Dipeptidase AMass spectrometrylcsh:QD241-441Betacoronavirus03 medical and health scienceslcsh:Organic chemistryspike protein-ACE2 interactionmedicineHumansProtein Interaction Domains and MotifsAmino Acid SequencePhysical and Theoretical ChemistryBinding sitePandemics030304 developmental biologyBinding SitesSARS-CoV-2Organic ChemistryCOVID-19MSStructural biologyProtein Conformation beta-StrandSequence AlignmentMolecules
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Membrane insertion and topology of the TRanslocating chain-Associating Membrane protein (TRAM)

2011

The translocating chain-associating membrane protein (TRAM) is a glycoprotein involved in the translocation of secreted proteins into the endoplasmic reticulum (ER) lumen and in the insertion of integral membrane proteins into the lipid bilayer. As a major step toward elucidating the structure of the functional ER translocation/insertion machinery, we have characterized the membrane integration mechanism and the transmembrane topology of TRAM using two approaches: photocross-linking and truncated C-terminal reporter tag fusions. Our data indicate that TRAM is recognized by the signal recognition particle and translocon components, and suggest a membrane topology with eight transmembrane seg…

Models MolecularProtein ConformationEndoplasmic ReticulumModels BiologicalProtein Structure SecondaryMiceMembranes (Biologia)Structural BiologyAnimalsMolecular BiologyIntegral membrane proteinSignal recognition particleMembrane GlycoproteinsbiologyMembrane transport proteinPeripheral membrane proteinProteïnes de membranaIntracellular MembranesTransloconTransmembrane proteinProtein Structure TertiaryMembrane proteinBiochemistryMembrane topologybiology.proteinBiophysics
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Interleukin-6 and Soluble Interleukin-6 Receptor: Direct Stimulation of gp130 and Hematopoiesis

1998

T HE INTERLEUKIN-6 (IL-6) family of cytokines acts via receptor complexes that contain at least one subunit of the signal transducing protein gp130.[1][1] The family comprises IL-6, IL-11, ciliary neurotrophic factor (CNTF), cardiotrophin-1 (CT-1), leukemia inhibitory factor (LIF), and oncostatin M

Models Molecularendocrine systemmedicine.medical_specialtyRecombinant Fusion ProteinsImmunologyMice TransgenicLeukemia inhibitory factor receptorOncostatin MBiologyCiliary neurotrophic factorBiochemistryDesigner DrugsMiceStructure-Activity RelationshipAntigens CDInternal medicineCytokine Receptor gp130medicineAnimalsHumansInterleukin 6Membrane GlycoproteinsInterleukin-6Oncostatin MOncostatin M receptorCell DifferentiationReceptors InterleukinCell BiologyHematologyHematopoietic Stem CellsGlycoprotein 130Receptors Interleukin-6Molecular biologyHematopoiesisEndocrinologyLiverSolubilitybiology.proteinSignal transductionPeptidesLeukemia inhibitory factorSpleenBlood
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Leucine-58 in the putative 5th helical region of human interleukin (IL)-6 is important for activation of the IL-6 signal transducer, gp130

1995

A model of the tertiary structure of human IL-6, derived from the crystal-structure of granulocyte-colony stimulating factor, reveals a 5th helical region in the loop between the first and second alpha-helix. To investigate the importance of this region for biological activity of IL-6, residues Glu-52, Ser-53, Ser-54, Lys-55, Glu-56, Leu-58, and Glu-60 were individually replaced by alanine. IL-6.Leu-58Ala displayed a 5-fold reduced biological activity on the IL-6 responsive human cell lines XG-1 and A375. This reduction in bioactivity was shown to be due to a decreased capacity of the mutant protein to trigger IL-6 receptor-alpha-chain-dependent binding to the IL-6 signal transducer, gp130.

Models Molecularmedicine.medical_specialtyMolecular Sequence DataBiophysicsBiologyBiochemistryBinding CompetitiveProtein Structure SecondaryMiceStructure-function analysisgp130Structural BiologyMutant proteinAntigens CDLeucineInternal medicineGeneticsmedicineCytokine Receptor gp130Tumor Cells CulturedAnimalsHumansAmino Acid SequenceMolecular BiologyAlanineHybridomasMembrane GlycoproteinsBase SequenceInterleukin-6InterleukinBiological activityCell BiologyReceptors InterleukinGlycoprotein 130Receptors Interleukin-6Protein tertiary structureCell biologyProtein Structure TertiaryEndocrinologyMutationLeucineSignal transductionSequence AlignmentCell DivisionSignal TransductionFEBS Letters
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The family of the IL-6-type cytokines: specificity and promiscuity of the receptor complexes.

1997

The cytokines IL-6, LIF, CNTF, OSM, IL-11, and CT-1 have been grouped into the family of IL-6-type cytokines, since they all require gp130 for signal transduction. Interestingly, gp130 binds directly to OSM, whereas complex formation with the other cytokines depends on additional receptor subunits. Only limited structural information on these cytokines and their receptors is available. X-ray structures have been solved for the cytokines LIF and CNTF, whose up-up-down-down four-helix bundle is common to all of these cytokines, and for the receptors of hGH and prolactin, which contain two domains with a fibronectin III-like fold. Since cocrystallization and x-ray analysis of the up to four di…

Models Molecularmedicine.medical_treatmentMolecular Sequence DataBiologyBiochemistryMiceInterleukin 20Structural BiologyAntigens CDmedicineCytokine Receptor gp130AnimalsHumansAmino Acid SequenceReceptorMolecular BiologyCommon gamma chainMembrane GlycoproteinsSequence Homology Amino AcidInterleukin-6Rational designReceptors InterleukinGlycoprotein 130Receptors Interleukin-6Cell biologyFibronectinCytokineImmunologybiology.proteinCytokinesSignal transductionProteins
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Redistribution of aquaporin-4 in human glioblastoma correlates with loss of agrin immunoreactivity from brain capillary basal laminae

2003

Vasogenic edema is one of the most serious clinical problems in brain tumors and tightly connected to water shifts between the different fluid compartments in the brain. Aquaporin water channels have been recognized to have an important impact on the development of edematous swelling in the brain. Astrocytes, which are believed to induce or at least maintain the blood-brain barrier in the brain capillary endothelial cells, express the aquaporin isoform AQP4. Normally, AQP4 is highly concentrated in the glial membrane where astrocytes contact mesenchymal space, such as perivascular or brain superficial regions. Parenchymal membranes do not show any immunocytochemical AQP4-specific signal. We…

Models NeurologicalSynucleinsAquaporinNerve Tissue ProteinsBiologyAquaporinsBlood–brain barrierBasement MembranePathology and Forensic MedicineCellular and Molecular NeuroscienceGliomaUtrophinmedicineExtracellularAnimalsHumansAgrinDystroglycansAquaporin 4Membrane GlycoproteinsAgrinBrain NeoplasmsEndothelial Cellsmedicine.diseaseImmunohistochemistryRatsCell biologyCytoskeletal Proteinsmedicine.anatomical_structureAquaporin 4Immunologysense organsNeurology (clinical)GlioblastomaAstrocyteActa Neuropathologica
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