Search results for "Structural Biology."

showing 10 items of 822 documents

Tissue inhibitor of metalloproteinases-2 (TIMP-2) in rat liver cells is increased by lipopolysaccharide and prostaglandin E2

1995

AbstractTo explore the functional role of TIMP-2 in liver, we determined TIMP-2 mRNA levels in primary rat hepatocytes and in total rat liver. Rat hepatocytes constitutively express TIMP-2 mRNA at a low level. Incubation with dexamethasone, prostaglandin E2 and a combination of inflammatory cytokines leads to an up-regulation of TIMP-2 mRNA. In rats in vivo we found a dramatic increase of TIMP-2 expression after intraperitoneal injection of lipopolysaccharide. Compared to our previous findings on TIMP-1 we conclude that TIMP-2 mRNA expression is regulated in a distinct and partially opposite manner. Over-production of TIMP-2 could inhibit the activity of metalloproteinases and thus lead to …

Lipopolysaccharidesmedicine.medical_specialtyLipopolysaccharidemedicine.medical_treatmentInflammatory mediatorIntraperitoneal injectionBiophysicsTissue inhibitor of metalloproteinaseMatrix metalloproteinaseBiochemistryDexamethasoneDinoprostoneCell LineProinflammatory cytokineMicechemistry.chemical_compoundStructural BiologyFibrosisIn vivoInternal medicineGeneticsmedicineAnimalsHumansRNA MessengerProstaglandin E2Molecular BiologyCells CulturedTissue Inhibitor of Metalloproteinase-2ChemistryMetalloendopeptidasesProteinsExtracellular matrixCell BiologyTissue inhibitor of metalloproteinasemedicine.diseaseFibrosisRatsEndocrinologyGene Expression RegulationLiverProtein BiosynthesisCytokinesRat hepatocytemedicine.drug
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Transmission electron microscopical studies on some haemolymph proteins from the marine polychaete Nereis virens.

2001

Abstract The hexagonal bilayer haemoglobin molecule from Nereis virens has been investigated in a comparative study using several different negative stain electron microscopical specimen preparations (i.e. by conventional adsorption to continuous carbon support films, by the negative staining-carbon film technique and by negative staining across the holes of holey carbon support films with air-drying and rapid freezing/cryo-negative staining). The benefits and limitations of these different approaches are indicated, with the overall conclusion that negative staining with ammonium molybdate across holes creates the best possibilities for molecular imaging, and also has the potential for the …

LipoproteinsGeneral Physics and AstronomyNegative Staininglaw.inventionchemistry.chemical_compoundHemoglobinsStructural BiologylawHemolymphHemolymphAnimalsGeneral Materials ScienceAmmonium molybdatebiologyBilayerPolychaetaCell BiologyTrehaloseNegative stainStainingFerritinMicroscopy ElectronchemistryBiochemistryFerritinsbiology.proteinElectron microscopeMicron (Oxford, England : 1993)
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Electric field-induced fusion of large liposomes from natural and polymerizable lipids

1982

LiposomeFusionStructural BiologyChemistryElectric fieldGeneticsBiophysicsBiophysicsCell BiologyMolecular BiologyBiochemistryFEBS Letters
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Preparation of large unilamellar vesicles

1982

Single (unilamellar) and oligolamellar lipid bilayer vesicles of large diameter have great potential in membrane research. In particular, large unilamellar bilayer vesicles (diam. >50 m) would permit the insertion of microelectrodes for the measurement of the electrical properties of lipid bilayer membranes of different compositions. Furthermore, vesicles large enough to be observed by light microscopy could be fused with cells with the aid of the electric field method [l-4]. Since vesicles (liposomes) can be loaded with macromolecules, this might be an elegant means of transferring proteins or plasmids into cells. Large vesicles with different lipid compositions and only one unit membrane …

LiposomeMaterials scienceBilayerVesicleBiophysicsCell BiologyBiochemistryMicroelectrodeMembraneStructural BiologyMicroscopyGeneticsBiophysicslipids (amino acids peptides and proteins)Lipid bilayerMolecular BiologyMacromoleculeFEBS Letters
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Centrifugation does not alter spatial distribution of `BEP4' mRNA in paracentrotus lividus EGG

1997

AbstractParacentrotus lividus unfertilized eggs were centrifuged in a sucrose gradient, so to split each into two parts: a nucleated light fragment and an anucleated heavy fragment. Northern blot analyses utilizing a bep4 probe as animal marker and H2A histone gene and 12S-mit RNA as controls indicate that the eggs are elongated along the animal-vegetal axis during centrifugation and thereafter split into an animal and a vegetal half. Treatment of the eggs with colchicine before centrifugation abolishes the animal localization of bep4 mRNA.

Localized mRNABiophysicsCentrifugationCell FractionationBiochemistryMicrotubulesParacentrotus lividuschemistry.chemical_compoundStructural BiologyBotanyA/V axisGeneticsCentrifugation Density GradientColchicineAnimalsCentrifugationNorthern blotRNA MessengerMolecular BiologyGeneIn Situ HybridizationOvumMessenger RNAbiologyUnfertilized EggsRNACell PolarityMembrane ProteinsCell Biologybiology.organism_classificationBlotting NorthernMolecular biologychemistrySea Urchinsembryonic structuresCortexColchicineFEBS Letters
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Structural characterization of the α-hemolysin monomer fromStaphylococcus aureus

2008

α-Hemolysin from Staphylococcus aureus is secreted as a water-soluble monomer and assembles on membranes to oligomerize into a homo-heptameric, water-filled pore. These pores lead to lysis and cell death. Although the structure of the heptameric pore is solved by means of X-ray crystallography, structures of intermediate states—from the soluble monomer to all potential “pre-pore” structures—are yet unknown. Here, we propose a model of the monomeric α-hemolysin in solution based on molecular modeling, verified by small angle X-ray scattering data. This structure reveals details of the monomeric conformation of the α-hemolysin, for example inherent flexibility, along with definite differences…

LysisMolecular modelLeukocidinHemolysinBiochemistrychemistry.chemical_compoundCrystallographyMolecular dynamicsMonomerProtein structureMembranechemistryStructural BiologyMolecular BiologyProteins: Structure, Function, and Bioinformatics
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p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113.

1996

Abstract It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the M yristoylated A lanine- R ich C - K inase S ubstrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299–18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.

MAPK/ERK pathwayMARCKSmedicine.medical_treatmentMitogen-activated protein kinase kinaseBiochemistryenvironment and public healthSubstrate SpecificityMiceStructural BiologySerinep42MAPKinasePhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateCells CulturedProtein Kinase CMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorbiologyChemistryIntracellular Signaling Peptides and Proteins3T3 CellsProtein-Tyrosine KinasesCell biologyBiochemistryMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatebiological phenomena cell phenomena and immunityPlatelet-derived growth factor receptorhormones hormone substitutes and hormone antagonistsendocrine systemRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsGeneticsmedicineAnimalsAmino Acid SequenceMARCKSMolecular BiologyProtein kinase CGrowth factorMembrane ProteinsProteinsCell BiologyPeptide FragmentsEnzyme ActivationMolecular Weightenzymes and coenzymes (carbohydrates)Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedMitogensFEBS letters
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Thapsigargin-stimulated MAP kinase phosphorylation via CRAC channels and PLD activation: inhibitory action of docosahexaenoic acid.

2004

AbstractThis study was conducted on human Jurkat T-cells to investigate the role of depletion of intracellular Ca2+ stores in the phosphorylation of two mitogen-activated protein kinases (MAPKs), i.e. extracellular signal-regulated kinase (ERK) 1 and ERK2, and their modulation by a polyunsaturated fatty acid, docosahexaenoic acid (DHA). We observed that thapsigargin (TG) stimulated MAPK activation by store-operated calcium (SOC) influx via opening of calcium release-activated calcium (CRAC) channels as tyrphostin-A9, a CRAC channel blocker, and two SOC influx inhibitors, econazole and SKF-96365, diminished the action of the former. TG-stimulated ERK1/ERK2 phosphorylation was also diminished…

MAPK/ERK pathwayThapsigarginDocosahexaenoic AcidsBiophysicschemistry.chemical_elementCalciumBiochemistryDiglycerideschemistry.chemical_compoundJurkat CellsStructural BiologyGeneticsPhospholipase DHumansPhosphorylationMolecular BiologyProtein kinase CProtein Kinase CDiacylglycerol kinaseMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Phospholipase CChemistryKinasePhospholipase DRyanodine Receptor Calcium Release ChannelCell BiologyJurkat T-cellCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)Docosahexaenoic acidFatty Acids UnsaturatedThapsigarginlipids (amino acids peptides and proteins)CalciumMitogen-Activated Protein KinasesFEBS letters
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The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature

2021

A crystal structure of a photolyase at room temperature confirms the structural information obtained from cryogenic crystallography and paves the way for time-resolved studies of the photolyase at an X-ray free-electron laser.

MECHANISMMaterials scienceAbsorption spectroscopyDNA repairfotobiologia02 engineering and technologyCrystal structureREPAIR ACTIVITY03 medical and health sciencesCOLI DNA PHOTOLYASEX-RAY-DIFFRACTIONCryptochromeStructural BiologyAnimalsserial crystallographyCRYSTAL-STRUCTURECRYPTOCHROMEPhotolyaseSERIAL FEMTOSECOND CRYSTALLOGRAPHY030304 developmental biology0303 health sciencesCrystallographyflavoproteinsFADResolution (electron density)TemperaturebanaanikärpänenDNAkidetiede(6-4) photolyase021001 nanoscience & nanotechnologyResearch PapersRADICAL TRANSFER(6–4) photolyaseroom-temperature structureCrystallographyphotolyasesDrosophila melanogasterRECONSTITUTIONX-ray crystallography1182 Biochemistry cell and molecular biologylämpötilaproteiinit0210 nano-technologyDeoxyribodipyrimidine Photo-LyasePHOTOACTIVATIONVisible spectrumActa Crystallographica Section D Structural Biology
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PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins

2020

Abstract The Protein Ensemble Database (PED) (https://proteinensemble.org), which holds structural ensembles of intrinsically disordered proteins (IDPs), has been significantly updated and upgraded since its last release in 2016. The new version, PED 4.0, has been completely redesigned and reimplemented with cutting-edge technology and now holds about six times more data (162 versus 24 entries and 242 versus 60 structural ensembles) and a broader representation of state of the art ensemble generation methods than the previous version. The database has a completely renewed graphical interface with an interactive feature viewer for region-based annotations, and provides a series of descriptor…

MESH: Databases ProteinMESH: Search EngineAcademicSubjects/SCI00010[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM][SDV]Life Sciences [q-bio]media_common.quotation_subjectBiologycomputer.software_genreIntrinsically disordered proteins03 medical and health sciencesDatabases0302 clinical medicineInformation and Computing SciencesGeneticsFeature (machine learning)Database IssueHumansDatabases ProteinRepresentation (mathematics)Function (engineering)MESH: Tumor Suppressor Protein p53ComputingMilieux_MISCELLANEOUS030304 developmental biologymedia_commonGraphical user interfaceStructure (mathematical logic)MESH: Intrinsically Disordered Proteins0303 health sciencesMESH: HumansDatabase[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]business.industryProteinBiological Sciences[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]MetadataSearch EngineIntrinsically Disordered ProteinsState (computer science)Generic health relevanceTumor Suppressor Protein p53businesscomputer030217 neurology & neurosurgeryEnvironmental SciencesDevelopmental Biology
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