Search results for "Protein Structure"

showing 10 items of 757 documents

Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protei…

2008

Recent studies provide evidence that wild-type Cu/Zn-superoxide dismutase (SOD1(hWT)) might be an important factor in mutant SOD1-mediated amyotrophic lateral sclerosis (ALS). In order to investigate its functional role in the pathogenesis of ALS, we designed fusion proteins of two SOD1 monomers linked by a polypeptide. We demonstrated that wild-type-like mutants, but not SOD1(G85R) homodimers, as well as mutant heterodimers including SOD1(G85R)-SOD1(hWT) display dismutase activity. Mutant homodimers showed an increased aggregation compared with the corresponding heterodimers in cell cultures and transgenic Caenorhabditis elegans, although SOD1(G85R) heterodimers are more toxic in functiona…

Cell SurvivalRecombinant Fusion Proteinsanimal diseasesSOD1MutantProtein aggregationAnimals Genetically ModifiedProtein CarbonylationSuperoxide dismutaseMicechemistry.chemical_compoundSuperoxide Dismutase-1Cell Line TumorGeneticsAnimalsHumansAmino Acid SequenceCaenorhabditis elegansMolecular BiologyGenetics (clinical)Motor NeuronsbiologySuperoxide DismutaseSuperoxideAmyotrophic Lateral SclerosisWild typenutritional and metabolic diseasesHydrogen PeroxideGeneral MedicineFusion proteinProtein Structure Tertiarynervous system diseasesCell biologyAmino Acid Substitutionnervous systemchemistryBiochemistrybiology.proteinDismutaseDimerizationHuman Molecular Genetics
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Synthesis and biological evaluation of a D-ring-contracted analogue of lamellarin D

2017

A D-ring contracted analogue of the strongly cytotoxic marine pyrrole alkaloid lamellarin D was synthesized and investigated for its antiproliferative action towards a wild type and a multidrug resistant (MDR) cancer cell line. The compound was found to inhibit tumor cell growth at submicromolar concentrations and showed a lower relative resistance in the MDR cell line than the antitumor drug camptothecin to which lamellarin D shows cross resistance and with which lamellarin D shares the same binding site.

Cell SurvivalStereochemistryClinical BiochemistryPharmaceutical ScienceAntineoplastic Agents010402 general chemistryHeterocyclic Compounds 4 or More Rings01 natural sciencesBiochemistrychemistry.chemical_compoundCoumarinsCell Line TumorDrug DiscoverymedicineHumansCytotoxic T cellheterocyclic compoundsBinding siteMolecular BiologyBinding Sites010405 organic chemistryChemistryAlkaloidOrganic ChemistryWild typeIsoquinolinesProtein Structure Tertiary0104 chemical sciencesG2 Phase Cell Cycle CheckpointsMolecular Docking SimulationMultiple drug resistanceDNA Topoisomerases Type IDrug Resistance NeoplasmMutagenesisCell cultureLamellarin DM Phase Cell Cycle CheckpointsMolecular MedicineTopoisomerase I InhibitorsCamptothecinmedicine.drugBioorganic & Medicinal Chemistry
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The Functional Role of the Second NPXY Motif of the LRP1 β-Chain in Tissue-type Plasminogen Activator-mediated Activation of N-Methyl-D-aspartate Rec…

2008

The low density lipoprotein receptor-related protein 1 (LRP1) emerges to play fundamental roles in cellular signaling pathways in the brain. One of its prominent ligands is the serine proteinase tissue-type plasminogen activator (tPA), which has been shown to act as a key activator of neuronal mitogen-activated protein kinase pathways via the N-methyl-D-aspartate (NMDA) receptor. However, here we set out to examine whether LRP1 and the NMDA receptor might eventually act in a combined fashion to mediate tPA downstream signaling. By blocking tPA from binding to LRP1 using the receptor-associated protein, we were able to completely inhibit NMDA receptor activation. Additionally, inhibition of …

Cell signalingAmino Acid MotifsPDZ domainIntracellular SpaceBiologyReceptors N-Methyl-D-AspartateBiochemistryProtein Structure SecondaryCell LineRats Sprague-DawleyMiceStructure-Activity RelationshipAnimalsHumansAmino Acid SequencePhosphorylationRNA Small InterferingReceptorProtein kinase AMolecular BiologyMitogen-Activated Protein Kinase 1NeuronsMitogen-Activated Protein Kinase 3Activator (genetics)Intracellular Signaling Peptides and ProteinsMembrane ProteinsReceptor Cross-TalkCell BiologyLRP1RatsCell biologyEnzyme ActivationBiochemistryTissue Plasminogen ActivatorDisks Large Homolog 4 ProteinCalciumDisks Large Homolog 4 ProteinGuanylate KinasesPlasminogen activatorLow Density Lipoprotein Receptor-Related Protein-1PlasmidsSignal TransductionJournal of Biological Chemistry
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PTHrP [67-86] regulates the expression of stress proteins in breast cancer cells inducing modifications in urokinase-plasminogen activator and MMP-1 …

2003

It was previously reported that a midregion domain of parathyroid hormone-related protein (PTHrP), that is, [67-86]-amide, is able to restrain growth and promote matrigel penetration by the 8701-BC cell line, derived from a biopsy fragment of a primary ductal infiltrating carcinoma of the human breast, and that cell invasion in vitro is drastically impaired by inactivation of urokinase-plasminogen activator (uPa). In this study we started a more detailed investigation of the possible effects on gene expression arising from the interaction between PTHrP [67-86]-amide and 8701-BC breast cancer cells by a combination of conventional-, differential display-and semi-quantitative multiplex-polyme…

CellBreast NeoplasmsBiologyHeat Shock Transcription FactorsDownregulation and upregulationCell Line TumorHeat shock proteinmedicineHumansNeoplasm InvasivenessHSP90 Heat-Shock ProteinsEnzyme InhibitorsHSF1Heat-Shock ProteinsMatrigelActivator (genetics)CarcinomaParathyroid Hormone-Related ProteinCell BiologyOligonucleotides AntisenseUrokinase-Type Plasminogen ActivatorMolecular biologyPeptide FragmentsProtein Structure TertiaryUp-RegulationDNA-Binding ProteinsGene Expression Regulation NeoplasticHeat shock factormedicine.anatomical_structureCell cultureCancer researchFemaleQuercetinMatrix Metalloproteinase 1Transcription FactorsJournal of Cell Science
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The Role of the Heme Oxygenase System in the Metabolic Syndrome

2014

Molecular chaperones and the heat shock response play a major role in the maintenance of cellular homeostasis under various pathological conditions. In particular, their role is to regulate protein conformation, protect proteins from misfolding and aggregation, and maintain signalling and organellarnetworks. Among variousheat shock proteins, Hsp32 also known as heme oxygenase-1 (HO-1), has demonstrated an important role in metabolic syndrome. In particular, the HO system seems to play a major role in the complex pathophysiological cascade involved in insulin resistance mechanisms, and adipocyte functions as measured by the release of important adipokynes. The aim of the present review is to…

Cellular homeostasisBiologychemistry.chemical_compoundProtein structureInsulin resistanceDrug DiscoverymedicineHumansMetabolic syndrome heme oxygenase insulin sensitivity adiponectin heat shock proteins.Heat shockHemeHeat-Shock ProteinsMetabolic SyndromePharmacologySettore BIO/16 - Anatomia Umanamedicine.diseaseCell biologyHeme oxygenasechemistryBiochemistryShock (circulatory)Insulin Resistancemedicine.symptomMetabolic syndromeHeme Oxygenase-1Molecular Chaperones
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Comm Sorts Robo to Control Axon Guidance at the Drosophila Midline

2002

AbstractAxon growth across the Drosophila midline requires Comm to downregulate Robo, the receptor for the midline repellent Slit. We show here that comm is required in neurons, not in midline cells as previously thought, and that it is expressed specifically and transiently in commissural neurons. Comm acts as a sorting receptor for Robo, diverting it from the synthetic to the late endocytic pathway. A conserved cytoplasmic LPSY motif is required for endosomal sorting of Comm in vitro and for Comm to downregulate Robo and promote midline crossing in vivo. Axon traffic at the CNS midline is thus controlled by the intracellular trafficking of the Robo guidance receptor, which in turn depends…

Central Nervous SystemEmbryo NonmammalianEndosomeGrowth ConesMolecular Sequence DataEndocytic cycleDown-RegulationNerve Tissue ProteinsReceptors Cell SurfaceCell CommunicationEndosomesBiologyModels BiologicalFunctional LateralityGeneral Biochemistry Genetics and Molecular BiologySequence Homology Nucleic AcidEctodermmedicineAnimalsDrosophila ProteinsReceptors ImmunologicAxonTransport VesiclesReceptorSequence Homology Amino AcidBiochemistry Genetics and Molecular Biology(all)Stem CellsCell MembraneGraft SurvivalGene Expression Regulation DevelopmentalMembrane ProteinsCell DifferentiationAnatomyCommissureSlitProtein Structure TertiaryCell biologyProtein TransportDrosophila melanogastermedicine.anatomical_structureCOS CellsRoundaboutAxon guidanceStem Cell TransplantationCell
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The Process-inducing Activity of Transmembrane Agrin Requires Follistatin-like Domains

2009

Clustering or overexpression of the transmembrane form of the extracellular matrix proteoglycan agrin in neurons results in the formation of numerous highly motile filopodia-like processes extending from axons and dendrites. Here we show that similar processes can be induced by overexpression of transmembrane-agrin in several non-neuronal cell lines. Mapping of the process-inducing activity in neurons and non-neuronal cells demonstrates that the cytoplasmic part of transmembrane agrin is dispensable and that the extracellular region is necessary for process formation. Site-directed mutagenesis reveals an essential role for the loop between beta-sheets 3 and 4 within the Kazal subdomain of t…

Central Nervous SystemFollistatinanimal structuresBiologyCytoplasmic partPC12 CellsBiochemistryProtein Structure SecondaryNeuromuscular junctionCell membraneExtracellular matrixMolecular Basis of Cell and Developmental BiologyProtein structureChlorocebus aethiopsmedicineAnimalsHumansAgrinMolecular BiologyNeuronsAgrinCell MembraneCell BiologyTransmembrane proteinProtein Structure TertiaryRatsCell biologymedicine.anatomical_structurenervous systemProteoglycanBiochemistryCOS CellsMutagenesis Site-Directedbiology.proteinFemaleChickenshormones hormone substitutes and hormone antagonistsJournal of Biological Chemistry
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RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin

2005

The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR(ORF15) (ORF15(C2)) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mas…

CentrioleFluorescent Antibody TechniqueMicechemistry.chemical_compoundChlorocebus aethiopsGuanine Nucleotide Exchange FactorsProtein IsoformsBasal bodyConserved SequenceGenetics (clinical)CentriolesGlutathione Transferaseintegumentary systemNuclear ProteinsExonsGeneral MedicineRetinitis pigmentosa GTPase regulatorImmunohistochemistryNocodazoleCOS CellsNucleophosminCell NucleolusRecombinant Fusion ProteinsMolecular Sequence DataBiologyOpen Reading FramesMicrotubuleTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceEye ProteinsMolecular BiologyNucleophosminSequence Homology Amino AcidProteinsPrecipitin TestsMolecular biologyeye diseasesProtein Structure TertiaryMice Inbred C57BLCytoskeletal ProteinschemistryCentrosomeCytoplasmSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCattleHeLa CellsHuman Molecular Genetics
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Supramolecular assembly using helical peptides

1997

Abstract We investigated supramolecular assemblies of various hydrophobic helical peptides. The assemblies were formed at the air/water interface or in aqueous medium. The hexadecapeptide, Boc-(Ala-Aib)8-OMe (BA16M), was reported to take α-helical structure by X-ray analysis. Several derivatives were prepared, which have the repeating sequence of Ala-Aib, Lys(Z)-Aib or Leu-Aib, or have the terminal chemically modified. CD spectra of the peptides indicated helical conformation in ethanol solution. The surface pressure-area isotherms of the peptide monolayers showed an inflection at the surface area corresponding to the cross section along the helix axis, and the monolayers were collapsed by …

ChemistryAirBiophysicsSupramolecular chemistryWaterInfrared spectroscopySurface pressureBiochemistryProtein Structure SecondarySupramolecular assemblyCrystallographyMicroscopy FluorescenceDynamic light scatteringHelixMonolayerPeptidesDispersion (chemistry)Advances in Biophysics
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Direct Evidence of the Amino Acid Side Chain and Backbone Contributions to Protein Anharmonicity

2010

Elastic incoherent neutron scattering has been used to study the temperature dependence of the mean-square displacements of nonexchangeable hydrogen atoms in powders of a series of homomeric polypeptides (polyglycine, polyalanine, polyphenylalanine and polyisoleucine) in comparison with myoglobin at the same hydration level (h = 0.2). The aim of the work was to measure the dynamic behavior of different amino acid residues separately and assess the contribution of each type of side chain to the anharmonic dynamics of proteins. The results provide direct experimental evidence that the first anharmonic activation, at approximately 150 K, is largely due to methyl group rotations entering the ti…

ChemistryStereochemistryDirect evidenceMyoglobinAnharmonicityProteinsGeneral ChemistryNeutron scatteringNeutron scatteringMolecular Dynamics SimulationRing (chemistry)BiochemistryCatalysisProtein Structure Secondarychemistry.chemical_compoundCrystallographyColloid and Surface ChemistryMyoglobinSide chainProtein dynamicMethyleneAmino AcidsPeptidesMethyl group
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