Search results for "Structural Biology."

showing 10 items of 822 documents

Structural and mechanistic insights into the interaction of the circadian transcription factor BMAL1 with the KIX domain of the CREB-binding protein

2019

JBC papers in press xx, 16604-16619 (2019). doi:10.1074/jbc.RA119.009845

0301 basic medicineendocrine systemCircadian clockTranscription factor complex610BiochemistryProtein Structure SecondaryProtein–protein interaction03 medical and health sciencesTransactivationMiceProto-Oncogene Proteins c-mybProtein DomainsX-Ray DiffractionCircadian ClocksScattering Small AngleAnimalsddc:610Amino Acid SequenceCREB-binding proteinMolecular BiologyTernary complexTranscription factorBinding Sites030102 biochemistry & molecular biologybiologyChemistryARNTL Transcription FactorsCell BiologyHistone-Lysine N-MethyltransferaseSurface Plasmon ResonanceCREB-Binding ProteinRecombinant ProteinsCell biologyProtein Structure Tertiary030104 developmental biologyStructural biologyProtein Structure and Foldingbiology.proteinMutagenesis Site-DirectedMyeloid-Lymphoid Leukemia ProteinProtein Binding
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Recombinant mussel protein Pvfp-5β: A potential tissue bioadhesive

2019

During their lifecycle, many marine organisms rely on natural adhesives to attach to wet surfaces for movement and self-defence in aqueous tidal environments. Adhesive proteins from mussels are biocompatible and elicit only minimal immune responses in humans. Therefore these proteins have received increased attention for their potential applications in medicine, biomaterials and biotechnology. The Asian green mussel Perna viridis secretes several byssal plaque proteins, molecules that help anchor the mussel to surfaces. Among these proteins, protein-5β (Pvfp-5β) initiates interactions with the substrate, displacing interfacial water molecules before binding to the surface. Here, we establis…

0301 basic medicinemedicine.disease_causeBiochemistryepidermal growth factor (EGF)law.inventionMiceCell Movementlawbiophysicsstructural biologyrecombinantCells CulturedbiologyChemistryMarine proteinsAdhesionRecombinant ProteinsadhesionProtein Structure and FoldingRecombinant DNAadhesion proteinsbiomaterialsPernaCell SurvivalSurface PropertiesBioadhesivemussel03 medical and health sciencesmedicineAnimalsHumansMolecular BiologyEscherichia coliCell ProliferationTissue Engineering030102 biochemistry & molecular biologyProteinsCell BiologyMusselbiology.organism_classificationEGF-like motifs; Marine proteins; adhesion; adhesion proteins; biomaterials; biophysics; epidermal growth factor (EGF); structural biologyEGF-like motifs030104 developmental biologyStructural biologyCell cultureNIH 3T3 CellsBiophysicsTissue AdhesivesHeLa CellsPerna viridisJournal of Biological Chemistry
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Mobility of a Mononucleotide within a Lipid Matrix: A Neutron Scattering Study

2017

International audience; An essential question in studies on the origins of life is how nucleic acids were first synthesized and then incorporated into compartments about 4 billion years ago. A recent discovery is that guided polymerization within organizing matrices could promote a non-enzymatic condensation reaction allowing the formation of RNA-like polymers, followed by encapsulation in lipid membranes. Here, we used neutron scattering and deuterium labelling to investigate 5'-adenosine monophosphate (AMP) molecules captured in a multilamellar phospholipid matrix. The aim of the research was to determine and compare how mononucleotides are captured and differently organized within matric…

0301 basic medicinemultilamellar lipid matrix[PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]neutron scattering; multilamellar lipid matrix; mononucleotide mobility; hydrationPhospholipidNeutron scattering010402 general chemistry01 natural sciencesGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health scienceschemistry.chemical_compoundMoleculelcsh:ScienceLipid bilayerEcology Evolution Behavior and Systematicschemistry.chemical_classification[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]neutron scatteringPaleontologyPolymer0104 chemical sciencesmononucleotide mobility[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]030104 developmental biologyMembranechemistryBiochemistryDeuteriumPolymerizationSpace and Planetary ScienceChemical physicslcsh:Qlipids (amino acids peptides and proteins)hydration
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In-Depth Proteomic Characterization of Classical and Non-Classical Monocyte Subsets

2018

Monocytes are bone marrow-derived leukocytes that are part of the innate immune system. Monocytes are divided into three subsets: classical, intermediate and non-classical, which can be differentiated by their expression of some surface antigens, mainly CD14 and CD16. These cells are key players in the inflammation process underlying the mechanism of many diseases. Thus, the molecular characterization of these cells may provide very useful information for understanding their biology in health and disease. We performed a multicentric proteomic study with pure classical and non-classical populations derived from 12 healthy donors. The robust workflow used provided reproducible results among t…

0301 basic medicinequantitative proteomicsInnate immune systemFunctional analysisMechanism (biology)CD14Clinical BiochemistryQuantitative proteomicslcsh:QR1-502monocytes; protein profiling; quantitative proteomicsDiseaseComputational biologyCD16Biologyprotein profilingBiochemistryArticlelcsh:Microbiology03 medical and health sciences030104 developmental biologyAntigenStructural BiologymonocytesMolecular Biology
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NMR Exchange Format: a unified and open standard for representation of NMR restraint data

2015

SCOPUS: le.j

0303 health sciencesElectronic Data ProcessingMagnetic Resonance SpectroscopyComputer sciencebusiness.industryeducationRepresentation (systemics)virus diseasesGénéralitésNuclear magnetic resonance spectroscopy010402 general chemistry01 natural sciencesArticle0104 chemical sciencesComputational science03 medical and health sciencesSoftwareNuclear magnetic resonanceStructural BiologyOpen standard[CHIM.ANAL]Chemical Sciences/Analytical chemistrybusinessMolecular BiologySoftware030304 developmental biologyNature structural & molecular biology
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Selenomethionine labeling of large biological macromolecular complexes: probing the structure of marine bacterial virus PM2.

2008

There is a need for improved tools for labeling protein species within large macromolecular assemblies. Here we describe a method for the efficient selenomethionine labeling of the membrane-containing bacterial virus PM2 for structural studies. By examining potential host cells a strain was found which was auxotrophic for methionine, and by performing a multiparameter search of conditions it was possible to derive a robust protocol which simultaneously minimized the toxic effects of the selenomethionine, so that a reasonable virus yield was maintained, whilst still achieving essentially complete labeling. This has allowed us to fingerprint the protein constituents of the virus in a relative…

0303 health sciencesbiologyStrain (chemistry)030306 microbiologyAuxotrophyCorticoviridaechemistry.chemical_elementCrystallography X-Raybiology.organism_classificationVirusBacteriophage03 medical and health scienceschemistryBiochemistryStructural BiologyYield (chemistry)MethodsBacterial virusSelenomethionineSelenium030304 developmental biologyMacromoleculeJournal of structural biology
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Visualizing Human Protein‐Protein Interactions and Subcellular Localizations on Cell Images Through CellMap

2020

Visualizing protein data remains a challenging and stimulating task. Useful and intuitive visualization tools may help advance biomolecular and medical research; unintuitive tools may bar important breakthroughs. This protocol describes two use cases for the CellMap (http://cellmap.protein.properties) web tool. The tool allows researchers to visualize human protein-protein interaction data constrained by protein subcellular localizations. In the simplest form, proteins are visualized on cell images that also show protein-protein interactions (PPIs) through lines (edges) connecting the proteins across the compartments. At a glance, this simultaneously highlights spatial constraints that prot…

0303 health sciencesgenetic structuresComputer scienceCells030305 genetics & heredityProteinsA proteinComputational biologyBiochemistryWeb toolProtein subcellular localization predictionVisualizationProtein–protein interaction03 medical and health sciencesImaging Three-DimensionalStructural BiologyProtein Interaction MappingHumansProtocol (object-oriented programming)SoftwareSubcellular Fractions030304 developmental biologyCurrent Protocols in Bioinformatics
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1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain

2021

AbstractLEE-encoded effector EspF (EspF) is an effector protein part of enteropathogenic Escherichia coli’s (EPEC’s) arsenal for intestinal infection. This intrinsically disordered protein contains three highly conserved repeats which together compose over half of the protein’s complete amino acid sequence. EPEC uses EspF to hijack host proteins in order to promote infection. In the attack EspF is translocated, together with other effector proteins, to host cell via type III secretion system. Inside host EspF stimulates actin polymerization by interacting with Neural Wiskott-Aldrich syndrome protein (N-WASP), a regulator in actin polymerization machinery. It is presumed that EspF acts by di…

030303 biophysicsRegulatormacromolecular substancesBiochemistryArticleType three secretion system03 medical and health sciencesStructural BiologyEnteropathogenic Escherichia coliNMR-spektroskopiaN-WASPPeptide sequenceActin030304 developmental biologysolution NMRSolution NMR0303 health sciencesEffectorChemistryResonance assignmentsresonance assignmentsNuclear magnetic resonance spectroscopyintrinsically disordered protein3. Good healthCell biologytype III secretion systemType III secretion systemIntrinsically disordered proteinEPEC EspFproteiinitGTPase bindingBiomolecular Nmr Assignments
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Association of liver steatosis with lipid oversecretion and hypotriglyceridaemia in C57BL/6j mice fed trans-10, cis-12-linoleic acid

2003

AbstractConjugated linoleic acids (CLA) have recently been recognized to reduce body fat and plasma lipids in some animals. This study demonstrated that the steatosis accompanying the fat loss induced by trans-10,cis-12-C18:2 (CLA2) and not cis-9,trans-11-C18:2 (CLA1) isomer in C57BL/6j mice was not due to an alteration of the liver lipoprotein production that was even increased. The 3-fold decrease in plasma triacylglycerol contents and the induction of mRNA expression of low-density lipoprotein receptors concomitantly observed in CLA2-fed mice suggested an increase in the lipoprotein clearance at the level of the liver itself. CLA1 feeding produced similar but attenuated effects on trigly…

030309 nutrition & dieteticsConjugated linoleic acidLiver steatosisLipoproteins VLDLBiochemistrychemistry.chemical_compoundMiceStructural BiologyLipoproteinReceptorComputingMilieux_MISCELLANEOUSchemistry.chemical_classification0303 health sciencesFatty AcidsLiverlipids (amino acids peptides and proteins)Conjugated linoleic acidmedicine.medical_specialtyLinoleic acidBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyTriacylglycerolLinoleic Acid03 medical and health sciencesInternal medicineGeneticsmedicineAnimalsLow-density lipoprotein receptorRNA MessengerMolecular BiologyTriglycerides030304 developmental biologyDNA PrimersBase SequenceEsterificationMyocardiumBody WeightRNAFatty acidCell BiologyFatty acidmedicine.diseaseFatty LiverMice Inbred C57BLEndocrinologychemistryLDL receptorSteatosisLipoprotein
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9-cis-Retinoic acid enhances fatty acid-induced expression of the liver fatty acid-binding protein gene

1997

The role of retinoic acids (RA) on liver fatty acid- binding protein (L-FABP) expression was investigated in the well differentiated FAO rat hepatoma cell line. 9-cis-Retinoic acid (9-ci's-RA) specifically enhanced L-FABP mRNA levels in a time- and dose-dependent manner. The higher induction was found 6 h after addition of 10 -6 M 9-CK-RA in the medium. RA also enhanced further both L-FABP mRNA levels and cytosolic L-FABP protein content induced by oleic acid. The retinoid X receptor (RXR) and the peroxisome proliferator-activated receptor (PPAR), which are known to be activated, respectively, by 9-c/s-RA and long chain fatty acid (LCFA), co-operated to bind specifically the peroxisome prol…

9-cw-Retinoic acidReceptors Retinoic Acid[SDV]Life Sciences [q-bio]Receptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorMyelin P2 ProteinMicrobodiesBiochemistry0302 clinical medicineStructural BiologyTumor Cells CulturedAlitretinoinchemistry.chemical_classification0303 health sciencesChemistryFatty AcidsDrug SynergismPeroxisomeNeoplasm Proteins9-cis-Retinoic acidLiverBiochemistryFree fatty acid receptorlipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaLong chain fatty acidFatty Acid-Binding Protein 7DimerizationPeroxisome proliferator-activated receptor gammaCarcinoma HepatocellularBiophysicsNerve Tissue ProteinsTretinoinRetinoid X receptorFatty Acid-Binding ProteinsLiver fatty acid-binding protein03 medical and health sciencesGeneticsAnimalsRNA MessengerMolecular Biology030304 developmental biologyFAO hepatoma cellFatty acidCell BiologyFatty acidRatsRetinoid X ReceptorsGene Expression RegulationNuclear receptorGene expressionCarrier Proteins[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition030217 neurology & neurosurgeryTranscription FactorsFEBS Letters
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