Search results for "plasma protein"

showing 10 items of 193 documents

Conformational dynamism for DNA interaction in the Salmonella RcsB response regulator

2017

17 páginas, 7 figuras, 1 tabla

0301 basic medicineModels MolecularSalmonella typhimuriumProtein Data Bank (RCSB PDB)Plasma protein bindingBiologyCrystallography X-RayDNA-binding protein03 medical and health sciencesBacterial ProteinsProtein DomainsStructural BiologyGeneticsAmino Acid SequencePhosphorylationTranscription factorSequence Homology Amino AcidEffectorPromoterDNACell biologyResponse regulator030104 developmental biologyRegulonBiochemistryNucleic Acid ConformationProtein BindingNucleic Acids Research
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The dimer-monomer equilibrium of SARS-CoV-2 main protease is affected by small molecule inhibitors

2021

AbstractThe maturation of coronavirus SARS-CoV-2, which is the etiological agent at the origin of the COVID-19 pandemic, requires a main protease Mpro to cleave the virus-encoded polyproteins. Despite a wealth of experimental information already available, there is wide disagreement about the Mpro monomer-dimer equilibrium dissociation constant. Since the functional unit of Mpro is a homodimer, the detailed knowledge of the thermodynamics of this equilibrium is a key piece of information for possible therapeutic intervention, with small molecules interfering with dimerization being potential broad-spectrum antiviral drug leads. In the present study, we exploit Small Angle X-ray Scattering (…

0301 basic medicineMolecular biologyProtein ConformationSciencemedicine.medical_treatmentDimerBiophysicsPlasma protein binding010402 general chemistryAntiviral Agents01 natural sciencesArticleDissociation (chemistry)03 medical and health scienceschemistry.chemical_compoundProtein structureX-Ray DiffractionDrug DiscoverymedicineHumansProtease InhibitorsCoronavirus 3C ProteasesVirtual screeningMultidisciplinaryProteaseSARS-CoV-2ChemistryQSARS-CoV-2 main protease Mpro enzymatic activity inhibition Small Angle X-ray Scattering small inhibitors virtual screeningRCOVID-19Computational BiologySmall moleculeComputational biology and bioinformatics0104 chemical sciencesMolecular Docking SimulationDissociation constant030104 developmental biologyBiophysicsMedicineThermodynamicsDimerizationProtein Binding
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Antibody-mediated blockade of JMJD6 interaction with collagen I exerts antifibrotic and antimetastatic activities

2017

JMJD6 is known to localize in the nucleus, exerting histone arginine demethylase and lysyl hydroxylase activities. A novel localization of JMJD6 in the extracellular matrix, resulting from its secretion as a soluble protein, was unveiled by a new anti-JMJD6 mAb called P4E11, which was developed to identify new targets in the stroma. Recombinant JMJD6 binds with collagen type I (Coll-I), and distinct JMJD6 peptides interfere with collagen fibrillogenesis, collagen-fibronectin interaction, and adhesion of human tumor cells to the collagen substrate. P4E11 and collagen binding to JMJD6 are mutually exclusive because the amino acid sequences of JMJD6 necessary for the interaction with Coll-I ar…

0301 basic medicineMonoclonal antibodyXenograft Model Antitumor AssayArginineLysyl hydroxylaseEnzyme-Linked Immunosorbent AssayReceptors Cell SurfacePlasma protein bindingBiochemistryCollagen Type IExtracellular matrix03 medical and health sciencesMiceFibrosisPeptide LibraryCell Line TumormedicineGeneticsAnimalsHumansOsteonectinCell NucleuMolecular BiologyCell NucleusMice KnockoutMice Inbred BALB CbiologyChemistryJmjC familyAnimalAntibodies MonoclonalFibrillogenesisExtracellular matrixmedicine.diseaseXenograft Model Antitumor AssaysImmunohistochemistryCell biologyIn vivo treatment030104 developmental biologybiology.proteinOsteonectinSignal transductionExtracellular matrix; In vivo treatment; JmjC family; Monoclonal antibody; Peptide library; Animals; Antibodies Monoclonal; Cell Line Tumor; Cell Nucleus; Collagen Type I; Enzyme-Linked Immunosorbent Assay; Extracellular Matrix; Humans; Immunohistochemistry; Mice; Mice Inbred BALB C; Mice Knockout; Osteonectin; Peptide Library; Protein Binding; Receptors Cell Surface; Signal Transduction; Xenograft Model Antitumor Assays; Biotechnology; Biochemistry; Molecular Biology; GeneticsHumanProtein BindingSignal TransductionBiotechnology
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2016

AbstractHuman papillomaviruses enter host cells via a clathrin-independent endocytic pathway involving tetraspanin proteins. However, post-endocytic trafficking required for virus capsid disassembly remains unclear. Here we demonstrate that the early trafficking pathway of internalised HPV particles involves tetraspanin CD63, syntenin-1 and ESCRT-associated adaptor protein ALIX. Following internalisation, viral particles are found in CD63-positive endosomes recruiting syntenin-1, a CD63-interacting adaptor protein. Electron microscopy and immunofluorescence experiments indicate that the CD63-syntenin-1 complex controls delivery of internalised viral particles to multivesicular endosomes. Ac…

0301 basic medicineMultidisciplinaryCD63ChemistryEndosomeEndocytic cycleSignal transducing adaptor proteinPlasma protein bindingCell biology03 medical and health sciences030104 developmental biologyCapsidTetraspaninSyntenin-1Scientific Reports
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Interaction of G protein coupled receptors and cholesterol

2016

G protein coupled receptors (GPCRs) form the largest receptor superfamily in eukaryotic cells. Owing to their seven transmembrane helices, large parts of these proteins are embedded in the cholesterol-rich plasma membrane bilayer. Thus, GPCRs are always in proximity to cholesterol. Some of them are functionally dependent on the specific presence of cholesterol. Over the last years, enormous progress on receptor structures has been achieved. While lipophilic ligands other than cholesterol have been shown to bind either inside the helix bundle or at the receptor-lipid interface, the binding site of cholesterol was either a single transmembrane helix or a groove between two or more transmembra…

0301 basic medicinePlasma protein bindingLigandsBiochemistryReceptors G-Protein-Coupled03 medical and health sciences0302 clinical medicineHumansBinding siteReceptorMolecular BiologyG protein-coupled receptorHelix bundleChemistryOrganic ChemistryCholesterol bindingCell BiologyTransmembrane domainCholesterol030104 developmental biologyBiochemistrylipids (amino acids peptides and proteins)LeucineHydrophobic and Hydrophilic Interactions030217 neurology & neurosurgeryProtein BindingChemistry and Physics of Lipids
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Limited antibody specificity compromises epitranscriptomic analyses

2019

International audience; A controversial discussion on the occurrence of the RNA modification m1A in mRNA takes a new turn, as an antibody with a central role in modification mapping was shown to also bind mRNA cap structures.

0301 basic medicineScienceGeneral Physics and Astronomy02 engineering and technologyPlasma protein bindingAntibodiesGeneral Biochemistry Genetics and Molecular BiologyEpigenesis GeneticTranscriptome03 medical and health sciencesAntibody Specificity[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]AnimalsHumansRNA Messengerlcsh:ScienceEpigenesisRegulation of gene expressionMessenger RNAMultidisciplinarybiologyCommentQRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyGeneral ChemistryDNA MethylationRNA modification021001 nanoscience & nanotechnologyCell biology030104 developmental biologyGene Expression RegulationDNA methylationbiology.proteinRNAlcsh:QAntibodyTranscriptome0210 nano-technologyProtein Binding
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Interactions of human P-glycoprotein transport substrates and inhibitors at the drug binding domain: Functional and molecular docking analyses

2015

Rhodamine 123 (R123) transport substrate sensitizes P-glycoprotein (P-gp) to inhibition by compound 2c (cis-cis) N,N-bis(cyclohexanolamine)aryl ester isomer in a concentration-dependent manner in human MDR1-gene transfected mouse T-lymphoma L5178 cells as shown previously. By contrast, epirubicin (EPI) concentration changes left unaltered 2c IC50 values of EPI efflux. To clarify this discrepancy, defined molecular docking (DMD) analyses of 12 N,N-bis(cyclohexanolamine)aryl esters, the highly flexible aryl ester analog 4, and several P-gp substrate/non-substrate inhibitors were performed on human P-gp drug- or nucleotide-binding domains (DBD or NBD). DMD measurements yielded lowest binding e…

0301 basic medicineStereochemistryCell Culture TechniquesCancer drug resistance; Molecular docking; NN-Bis(cyclohexanolamine)aryl ester; P-glycoproteinPlasma protein bindingP-glycoproteinTransfectionBiochemistryRhodamine 123Substrate Specificity03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineCell Line TumorAnimalsRhodamine 123ATP Binding Cassette Transporter Subfamily B Member 1Binding siteP-glycoproteinEpirubicinPharmacologyBinding SitesbiologyMolecular StructureArylEstersCancer drug resistanceNCyclohexanolsMolecular Docking SimulationProtein Transport030104 developmental biologychemistryDocking (molecular)030220 oncology & carcinogenesisMolecular dockingbiology.proteinN-Bis(cyclohexanolamine)aryl esterEffluxBinding domainProtein Binding
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Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2

2016

We show that a peptide from Chikungunya virus nsP3 protein spanning residues 1728–1744 binds the amphiphysin-2 (BIN1) Src homology-3 (SH3) domain with an unusually high affinity (Kd 24 nM). Our NMR solution complex structure together with isothermal titration calorimetry data on several related viral and cellular peptide ligands reveal that this exceptional affinity originates from interactions between multiple basic residues in the target peptide and the extensive negatively charged binding surface of amphiphysin-2 SH3. Remarkably, these arginines show no fixed conformation in the complex structure, indicating that a transient or fluctuating polyelectrostatic interaction accounts for this …

0301 basic medicinenuclear magnetic resonance (NMR)Amino Acid MotifsStatic ElectricityPeptideTarget peptidePlasma protein bindingViral Nonstructural ProteinsBiologyhost-pathogen interactionBiochemistrySH3 domainsrc Homology Domainsamphiphysin SH3Structure-Activity Relationship03 medical and health sciencesProtein structuredynaminHumansShort linear motifprotein structureNuclear Magnetic Resonance BiomolecularMolecular BiologySrc homology 3 domain (SH3 domain)Adaptor Proteins Signal Transducingchemistry.chemical_classificationTumor Suppressor Proteinsta1182Nuclear ProteinsIsothermal titration calorimetryCell Biologyintrinsically disordered protein030104 developmental biologychemistryBiochemistrynsP3Protein Structure and FoldingAmphiphysinBiophysicsPeptidesChikungunya virusProtein BindingJournal of Biological Chemistry
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Physico-chemical study of the radiopharmaceuticals 99mTc-DMSA, 99mTc-EDTA and 99mTc-DTPA interaction with plasmatic proteins.

1989

This report studies the binding rate of the radiopharmaceuticals 99mTc-DTPA, 99mTc-EDTA and 99mTc-DMSA to plasmatic proteins. The proteins bind to the tested radiopharmaceuticals in the following sequence: 99mTc-DTPA less than 99mTc-DMSA(C1) less than 99mTc-EDTA less than 99mTc-DMSA(C2) where C1 and C2 represent two different Tc-DMSA complexes. The thermodynamic study suggests a quantitative relationship of radiopharmaceutical:protein = 1:1 and an almost nonexistent influence of the temperature, which means that the interacting forces in this process are relatively weak.

99mtc dtpaPentetic acid99mTc-DMSAGeneral Engineeringchemistry.chemical_elementTechnetiumPlasma protein bindingBlood ProteinsOrganotechnetium CompoundsPentetic AcidTechnetiumBlood proteinschemistry.chemical_compoundchemistryBiochemistryTechnetium Tc 99m Dimercaptosuccinic AcidTechnetium Tc 99m PentetateEdetic AcidTechnetium Tc 99m Dimercaptosuccinic AcidSulfhydryl CompoundsSuccimerEdetic AcidProtein BindingInternational journal of radiation applications and instrumentation. Part A, Applied radiation and isotopes
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Measuring single small molecule binding via rupture forces of a split aptamer.

2011

The rupture force of a split (bipartite) aptamer that forms binding pockets for adenosine monophosphate (AMP) was measured by atomic force spectroscopy. Changes in the rupture force were observed in the presence of AMP, while this effect was absent when mutant aptamers or inosine were used. Thus, changes in the rupture force were a direct consequence of specific binding of AMP to the split aptamer. The split aptamer concept allowed the detection of nonlabeled AMP and enabled us to determine the dissociation constant on a single-molecule level.

Adenosine monophosphateChemistryAptamerForce spectroscopyGeneral ChemistryPlasma protein bindingAptamers NucleotideMicroscopy Atomic ForceBiochemistryCatalysisAdenosine MonophosphateDissociation constantCrystallographychemistry.chemical_compoundColloid and Surface ChemistrymedicineDirect consequenceSmall molecule bindingInosinemedicine.drugProtein BindingJournal of the American Chemical Society
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