Search results for "Plasma protein binding"

showing 10 items of 178 documents

Human Siglec-10 can bind to vascular adhesion protein-1 and serves as its substrate

2009

AbstractLeukocytes migrate from the blood into areas of inflammation by interacting with various adhesion molecules on endothelial cells. Vascular adhesion protein-1 (VAP-1) is a glycoprotein expressed on inflamed endothelium where it plays a dual role: it is both an enzyme that oxidizes primary amines and an adhesin that is involved in leukocyte trafficking to sites of inflammation. Although VAP-1 was identified more than 15 years ago, the counterreceptor(s) for VAP-1 on leukocytes has remained unknown. Here we have identified Siglec-10 as a leukocyte ligand for VAP-1 using phage display screenings. The binding between Siglec-10 and VAP-1 was verified by different adhesion assays, and this…

ImmunologyReceptors Cell SurfaceInflammationCHO CellsPlasma protein bindingBiologyLigandsBiochemistryMice03 medical and health sciencesCricetulus0302 clinical medicinePeptide LibraryVascular BiologyCricetinaeLectinsLeukocyte TraffickingCell AdhesionmedicineAnimalsHumansEndotheliumLymphocytesProtein Structure QuaternaryCell adhesion030304 developmental biologyMice Knockout0303 health sciencesCell adhesion moleculeSoluble cell adhesion moleculesSIGLECCell BiologyHematologyAdhesionrespiratory systembacterial infections and mycosesRecombinant Proteinsrespiratory tract diseasesChemotaxis LeukocyteBiochemistry030220 oncology & carcinogenesisAmine Oxidase (Copper-Containing)medicine.symptomCell Adhesion MoleculesProtein BindingBlood
researchProduct

Design and synthesis of 1-aryl-5-anilinoindazoles as c-Jun N-terminal kinase inhibitors.

2012

Starting from pyrazole HTS hit (1), a series of 1-aryl-1H-indazoles have been synthesized as JNK3 inhibitors with moderate selectivity against JNK1. SAR studies led to the synthesis of 5r as double digital nanomolar JNK3 inhibitor with good in vivo exposure.

IndazolesStereochemistryClinical BiochemistryPharmaceutical SciencePlasma protein bindingPyrazoleBiochemistrychemistry.chemical_compoundStructure-Activity RelationshipIn vivoMitogen-Activated Protein Kinase 10Drug DiscoveryStructure–activity relationshipAnimalsMitogen-Activated Protein Kinase 8Molecular BiologyProtein Kinase InhibitorsAniline CompoundsChemistryKinaseArylOrganic Chemistryc-junJNK Mitogen-Activated Protein KinasesBrainCombinatorial chemistryRatsDrug DesignMolecular MedicineSelectivityHalf-LifeProtein BindingBioorganicmedicinal chemistry letters
researchProduct

Binding analyses of Cry1Ab and Cry1Ac with membrane vesicles from Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis.

2004

The binding properties of Bacillus thuringiensis toxins to brush border membrane vesicles of Dipel-resistant and -susceptible Ostrinia nubilalis larvae were compared using ligand-toxin immunoblot analysis, surface plasmon resonance (SPR), and radiolabeled toxin binding assays. In ligand-toxin immunoblot analysis, the number of Cry1Ab or Cry1Ac toxin binding proteins and the relative toxin binding intensity were similar in vesicles from resistant and susceptible larvae. Surface plasmon resonance with immobilized activated Cry1Ab toxin indicated that there were no significant differences in binding with fluid-phase vesicles from resistant and susceptible larvae. Homologous competition assays …

InsectaTime FactorsBrush borderBacterial ToxinsImmunoblottingBiophysicsBacillus thuringiensisReceptors Cell SurfacePlasma protein bindingBiologyMothsmedicine.disease_causeLigandsBiochemistryBinding CompetitiveCell membraneHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsBinding sitePest Control BiologicalMolecular BiologyBinding SitesBacillus thuringiensis ToxinsDose-Response Relationship DrugMicrovilliToxinVesiclefungiCell Membranefood and beveragesCell BiologySurface Plasmon Resonancebiology.organism_classificationMolecular biologyEndotoxinsKineticsmedicine.anatomical_structureCry1AcBiochemistryInsect ProteinsProtein BindingBiochemical and biophysical research communications
researchProduct

MMGBSA As a Tool To Understand the Binding Affinities of Filamin–Peptide Interactions

2013

Filamins (FLN) are large dimeric proteins that cross-link actin and work as important scaffolds in human cells. FLNs consist of an N-terminal actin-binding domain followed by 24 immunoglobulin-like domains (FLN1-24). FLN domains are divided into four subgroups based on their amino acid sequences. One of these subgroups, including domains 4, 9, 12, 17, 19, 21, and 23, shares a similar ligand-binding site between the β strands C and D. Several proteins, such as integrins β2 and β7, glycoprotein Ibα (GPIbα), and migfilin, have been shown to bind to this site. Here, we computationally estimated the binding free energies of filamin A (FLNa) subunits with bound peptides using the molecular mechan…

Integrin beta ChainsFilaminsGeneral Chemical EngineeringIntegrinPeptidePlasma protein bindingMolecular Dynamics SimulationLibrary and Information SciencesBiologyLigandsFilaminta3111Protein Structure SecondaryProtein structureProtein Interaction MappingHumansFLNAProtein Interaction Domains and MotifsBinding siteta116chemistry.chemical_classificationBinding Sitesta1182General ChemistryComputer Science ApplicationsAmino acidCytoskeletal ProteinsCrystallographyPlatelet Glycoprotein GPIb-IX ComplexchemistryCD18 AntigensBiophysicsbiology.proteinThermodynamicsPeptidesCell Adhesion MoleculesAlgorithmsProtein BindingJournal of Chemical Information and Modeling
researchProduct

Pro-prion Binds Filamin A, Facilitating Its Interaction with Integrin β1, and Contributes to Melanomagenesis

2010

Filamin A (FLNA) is an integrator of cell mechanics and signaling. The spreading and migration observed in FLNA sufficient A7 melanoma cells but not in the parental FLNA deficient M2 cells have been attributed to FLNA. In A7 and M2 cells, the normal prion (PrP) exists as pro-PrP, retaining its glycosylphosphatidyl-inositol (GPI) anchor peptide signal sequence (GPI-PSS). The GPI-PSS of PrP has a FLNA binding motif and binds FLNA. Reducing PrP expression in A7 cells alters the spatial distribution of FLNA and organization of actin and diminishes cell spreading and migration. Integrin β1 also binds FLNA. In A7 cells, FLNA, PrP, and integrin β1 exist as two independent, yet functionally linked,…

Integrin beta ChainsGlycosylphosphatidylinositolsPrionsFilaminsanimal diseasesAmino Acid MotifsIntegrinPlasma protein bindingBiologyFilaminBiochemistryCell membraneContractile ProteinsCell MovementCell Line TumormedicineHumansFLNACytoskeletonMelanomaMolecular BiologyActinMicrofilament ProteinsCell Biologynervous system diseasesCell biologyGene Expression Regulation Neoplasticmedicine.anatomical_structurebiology.proteinCancer researchSignal transductionProtein BindingJournal of Biological Chemistry
researchProduct

The collagen receptor subfamily of the integrins

2003

The four collagen receptor integrins, alpha1beta1, alpha2beta1, alpha10beta1 and alpha11beta1, form a structurally and functionally distinct subgroup when compared to other members of the integrin family. In this review, we discuss the structures of these receptors and their differences in collagen binding and signalling function.

IntegrinsReceptors CollagenSubfamilybiologyChemistryIntegrinCell BiologyPlasma protein bindingLigandsBiochemistryProtein Structure TertiaryCollagen receptorCell biologyIntegrin alpha Mbiology.proteinAnimalsHumansSignal transductionReceptorFunction (biology)Protein BindingSignal TransductionThe International Journal of Biochemistry & Cell Biology
researchProduct

Thermal aggregation of bovine serum albumin at different pH: comparison with human serum albumin.

2007

We report here a study on thermal aggregation of BSA at two different pH values selected to be close to the isoelectric point (pI) of this protein. Our aim is to better understand the several steps and mechanisms accompanying the aggregation process. For this purpose we have performed kinetics of integrated intensity emission of intrinsic and extrinsic dyes, tryptophans and ANS respectively, kinetics of Rayleigh scattering and of turbidity. The results confirm the important role played by conformational changes in the tertiary structure, especially in the exposure of internal hydrophobic regions that promote intermolecular interactions. We also confirm that the absence of electrostatic repu…

KineticsBiophysicsSerum albuminPlasma protein bindingProtein structuremedicineAnimalsHumansScattering RadiationIsoelectric PointBovine serum albuminSerum AlbuminbiologyChemistryCircular DichroismTryptophanSerum Albumin BovineGeneral MedicineHuman serum albuminProtein tertiary structureProtein Structure TertiaryIsoelectric pointBiochemistrybiology.proteinBiophysicsCattlemedicine.drugProtein Binding
researchProduct

Mapping of the Discontinuous H-kininogen Binding Site of Plasma Prekallikrein

1999

Plasma prekallikrein, a zymogen of the contact phase system, circulates in plasma as heterodimeric complex with H-kininogen. The binding is mediated by the prekallikrein heavy chain consisting of four apple domains, A1 to A4, to which H-kininogen binds with high specificity and affinity (K(D) = 1.2 x 10(-8) M). Previous work had demonstrated that a discontinuous kininogen-binding site is formed by a proximal part located in A1, a distal part exposed by A4, and other yet unidentified portion(s) of the kallikrein heavy chain. To detect relevant binding segment(s) we recombinantly expressed single apple domains and found a rank order of binding affinity for kininogen of A2 > A4 approximately A…

Kininogen bindingKininogenChemistryHigh-molecular-weight kininogenPrekallikreinCell BiologyKallikreinPlasma protein bindingBiochemistryBiochemistryZymogenBinding siteMolecular Biologycirculatory and respiratory physiologyJournal of Biological Chemistry
researchProduct

Thermodynamics of the Interaction between the Spike Protein of Severe Acute Respiratory Syndrome Coronavirus-2 and the Receptor of Human Angiotensin-…

2020

Since the end of 2019, the coronavirus SARS-CoV-2 has caused more than 1000000 deaths all over the world and still lacks a medical treatment despite the attention of the whole scientific community. Human angiotensin-converting enzyme 2 (ACE2) was recently recognized as the transmembrane protein that serves as the point of entry of SARS-CoV-2 into cells, thus constituting the first biomolecular event leading to COVID-19 disease. Here, by means of a state-of-the-art computational approach, we propose a rational evaluation of the molecular mechanisms behind the formation of the protein complex. Moreover, the free energy of binding between ACE2 and the active receptor binding domain of the SARS…

LetterPneumonia ViralProtein domainThermodynamicsPlasma protein bindingMolecular Dynamics SimulationPeptidyl-Dipeptidase ALigandsmedicine.disease_causeProtein-Protein Binding01 natural sciencesDockingBetacoronavirus03 medical and health sciencesProtein Domains0103 physical sciencesmedicineHumansGeneral Materials SciencePhysical and Theoretical ChemistryBinding siteReceptorPandemics030304 developmental biologyCoronaviruschemistry.chemical_classification0303 health sciencesBinding Sites010304 chemical physicsSARS-CoV-2Spike ProteinCOVID-19PlicamycinTransmembrane proteinEnzymechemistrySettore CHIM/03 - Chimica Generale E InorganicaMolecular Dynamics SimulationsSpike Glycoprotein CoronavirusAngiotensin-converting enzyme 2DiosminThermodynamicsAngiotensin-Converting Enzyme 2Coronavirus InfectionsProtein Binding
researchProduct

Is the Rigidity of SARS-CoV-2 Spike Receptor-Binding Motif the Hallmark for Its Enhanced Infectivity? Insights from All-Atom Simulations

2020

The severe acute respiratory syndrome coronavirus (SARS-CoV-2) pandemic is setting the global health crisis of our time, causing a devastating societal and economic burden. An idiosyncratic trait of coronaviruses is the presence of spike glycoproteins on the viral envelope, which mediate the virus binding to specific host receptor, enabling its entry into the human cells. In spite of the high sequence identity of SARS-CoV-2 with its closely related SARS-CoV emerged in 2002, the atomic-level determinants underlining the molecular recognition of SARS-CoV-2 to the angiotensin-converting enzyme 2 (ACE2) receptor and, thus, the rapid virus spread into human body, remain unresolved. Here, multi-m…

LettervirusesAmino Acid MotifsPneumonia ViralVirus Attachment02 engineering and technologyPlasma protein bindingBiologyPeptidyl-Dipeptidase AMolecular Dynamics SimulationVirus03 medical and health sciencesBetacoronavirusViral ProteinsProtein structureViral envelopeGlobal healthHumansGeneral Materials SciencePhysical and Theoretical ChemistryReceptorProtein Structure QuaternaryPandemics030304 developmental biologyGlycoproteinschemistry.chemical_classificationGeneticsInfectivity0303 health sciencesSARS-CoV-2virus diseasesCOVID-19Hydrogen Bonding021001 nanoscience & nanotechnologySARS VirusProtein Structure TertiarySevere acute respiratory syndrome-related coronaviruschemistrySettore CHIM/03 - Chimica Generale E InorganicaQuantum TheoryAngiotensin-Converting Enzyme 20210 nano-technologyGlycoproteinCoronavirus InfectionsProtein Binding
researchProduct