Search results for "Binding protein"

showing 10 items of 1292 documents

Functional characterization of the enhancer blocking element of the sea urchin early histone gene cluster reveals insulator properties and three esse…

2000

Insulator elements can be functionally identified by their ability to shield promoters from regulators in a position-dependent manner or their ability to protect adjacent transgenes from position effects. We have previously reported the identification of a 265 bp sns DNA fragment at the 3' end of the sea urchin H2A early histone gene that blocked expression of a reporter gene in transgenic embryos when placed between the enhancer and the promoter. Here we show that sns interferes with enhancer-promoter interaction in a directional manner. When sns is placed between the H2A modulator and the inducible tet operator, the modulator is barred from interaction with the basal promoter. However, th…

animal structuresenhancer blockingMolecular Sequence DataDNA FootprintingSettore BIO/11 - Biologia MolecolareBiologyRegulatory Sequences Nucleic AcidinsulatorBinding CompetitiveHistonesStructural BiologyTranscription (biology)Gene clustermicroinjectionAnimalsDeoxyribonuclease IH2A enhancerGene SilencingTransgenesEnhancerDownstream EnhancerPromoter Regions GeneticMolecular BiologyTranscription factorRepetitive Sequences Nucleic AcidSequence DeletionReporter geneBase SequenceActivator (genetics)PromoterDNAhistone genesMolecular biologyCell biologyDNA-Binding ProteinsEnhancer Elements GeneticMultigene FamilySea UrchinsProtein Binding
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Lipocalins in Arthropod Chemical Communication.

2021

Abstract Lipocalins represent one of the most successful superfamilies of proteins. Most of them are extracellular carriers for hydrophobic ligands across aqueous media, but other functions have been reported. They are present in most living organisms including bacteria. In animals they have been identified in mammals, molluscs, and arthropods; sequences have also been reported for plants. A subgroup of lipocalins, referred to as odorant-binding proteins (OBPs), mediate chemical communication in mammals by ferrying specific pheromones to the vomeronasal organ. So far, these proteins have not been reported as carriers of semiochemicals in other living organisms; instead chemical communicatio…

arthropods; chemical communication; insects; lipocalins; odorant-binding proteins; phylogenesisArthropod AntennaeAcademicSubjects/SCI01140Vomeronasal organProtein familyGenome Insectodorant-binding proteinsphylogenesisLipocalinBiologyarthropodsPheromones03 medical and health sciences0302 clinical medicineGene duplicationGeneticsAnimalsinsectsGeneEcology Evolution Behavior and Systematics030304 developmental biology0303 health sciencesintegumentary systemAcademicSubjects/SCI01130chemical communicationbiology.organism_classificationLipocalinsAnimal CommunicationEvolutionary biologyPhylogenesisSex pheromoneArthropod030217 neurology & neurosurgeryResearch ArticleGenome biology and evolution
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Focus on the Small GTPase Rab1: A Key Player in the Pathogenesis of Parkinson’s Disease

2021

Parkinson’s disease (PD) is the second most frequent neurodegenerative disease. It is characterized by the loss of dopaminergic neurons in the substantia nigra and the formation of large aggregates in the survival neurons called Lewy bodies, which mainly contain α-synuclein (α-syn). The cause of cell death is not known but could be due to mitochondrial dysfunction, protein homeostasis failure, and alterations in the secretory/endolysosomal/autophagic pathways. Survival nigral neurons overexpress the small GTPase Rab1. This protein is considered a housekeeping Rab that is necessary to support the secretory pathway, the maintenance of the Golgi complex structure, and the regulation of macroau…

autophagyParkinson's diseaseQH301-705.5Substantia nigraReviewBiologyCatalysisInorganic Chemistryα-synucleinmedicineAnimalsHumansSmall GTPaseBiology (General)Physical and Theoretical ChemistryQD1-999Molecular BiologySpectroscopySecretory pathwayRab1GTPasesOrganic ChemistryNeurodegenerationDopaminergicRAB1Parkinson DiseaseLRRK2General Medicinemedicine.diseaseLRRK2Computer Science Applicationssecretory pathwayrab1 GTP-Binding ProteinsChemistrynervous systemParkinson’s diseaseNeuroscienceGolgi fragmentationInternational Journal of Molecular Sciences
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Nuclear calcium signaling: An emerging topic in plants

2011

International audience; The calcium ion is probably one of the most studied second messenger both in plant and animal fields. A large number of reviews have browsed the diversity of cytosolic calcium signatures and evaluated their pleiotropic roles in plant and animal cells. In the recent years, an increasing number of reviews has focused on nuclear calcium, especially on the possible roles of nuclear calcium concentration variations on nuclear activities. Experiments initially performed on animal cells gave conflicting results that brought about a controversy about the ability of the nucleus to generate its own calcium signals and to regulate its calcium level. But in plant cells, several …

biochemistry and molecular biology0106 biological sciences[SDV]Life Sciences [q-bio]aequorinchemistry.chemical_elementBiologyCalciumcalcium signaling01 natural sciencesBiochemistry03 medical and health sciencesCalcium-binding proteinTobaccomedicineHomeostasisPlant Proteins030304 developmental biologyCalcium signalingCell NucleusCalcium metabolism0303 health sciencescalcium homeostasisCalcium-Binding Proteinsnuclear calciumGeneral MedicineCell nucleusmedicine.anatomical_structureBiochemistrychemistry[SDE]Environmental SciencesSecond messenger systemNuclear calciumCalciumNucleusNeuroscience010606 plant biology & botanyBiochimie
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Pneumococcal HxxHxH triad – Copper(II) interactions – How important is the ‘x’?

2019

Abstract PhtA, a Streptococcus pneumoniae polyhistidine triad protein, which contributes to virulence by interacting with components of the immune system, by being involved in adherence of bacteria and in Zn(II) uptake, contains five copies of the HxxHxH sequence. Since this motif is also present in numerous Cu(II) binding proteins, we decided to focus on the bioinorganic chemistry of copper(II) with three of such PhtA repeats, in order to understand which of the PhtA triads binds Cu(II) with the highest affinity and explain if Cu(II) would be able to outcompete Zn(II) from its native binding site under physiological metal concentrations.

biology010405 organic chemistryChemistryStereochemistryVirulencechemistry.chemical_elementBioinorganic chemistry010402 general chemistrymedicine.disease_causebiology.organism_classification01 natural sciencesDNA-binding proteinCopper0104 chemical sciencesInorganic ChemistryMetalvisual_artStreptococcus pneumoniaeMaterials Chemistrymedicinevisual_art.visual_art_mediumPhysical and Theoretical ChemistryBinding siteBacteriaInorganica Chimica Acta
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The Complement System: Activation and Control

1985

One of the hallmarks of immunology has been analysis and characterization of the C system in biological fluids. It is composed of 11 proteins of the “classical” pathway:1 C1q, C1r, C1s, C4, C2, C3, C5, C6, C7, C8, and C9. There are three proteins of the “alternative” pathway (IUIS-WHO Nomenclature Committee 1981) B, D, and P. Finally, there are four control proteins: C1 inhibitor (Cl¯ INH) and C4b binding protein (C4b-bp) for the classical pathway, I (C3b inactivator or C3b INA) and H (β1 or C3b INA accelerator) for the alternative pathway, and anaphylatoxin inactivator. Due to the dramatic advances in protein chemistry, these 19 distinct serum proteins have been highly purified and charact…

biologyC4b-binding proteinChemistrychemical and pharmacologic phenomenaBlood proteinsComplement systemC1-inhibitorClassical complement pathwayBiochemistryImmunologybiology.proteinAlternative complement pathwayLysine carboxypeptidaseComplement membrane attack complex
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Purification by affinity chromatography of H1 RNA-Binding Proteins from rat brain

2003

Post-transcriptional regulation of mRNA metabolism is involved in processes as different as cell fate specification in development and cell response to a large variety of environmental cues. Regulation of all steps of RNA metabolism depends on RNA-binding proteins (RBPs). By using a T1 RNase protection assay, we previously identified three H1° RNA-binding factors (p40, p70 and p110), highly expressed in the rat brain. Here we report enrichment of these factors from brain extracts, obtained by affinity chromatography of biotinylated H1° RNA-protein complexes on streptavidin-conjugated paramagnetic particles. The purified proteins maintain RNA-binding ability and preference for histone messag…

biologyCellRNA-binding proteinGeneral MedicineCell cycleCell fate determinationMolecular biologymedicine.anatomical_structureHistoneBiochemistryAffinity chromatographyBiotinylationGeneticsmedicinebiology.proteinrat brain developing brain RNA-binding factors histone variants RNA affinity chromatography streptavidin conjugated paramagnetic particlesGene
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The binding of G-protein to rod outer segment phospholipids at the nitrogen–water interface

1989

In the visual process, one photoexcited rhodopsin (R*) catalyzes the activation of hundreds of G-proteins. It remains to be determined whether G-protein and R* find one another by membrane surface diffusion of these components (diffusion model) or by diffusion of G-protein through the aqueous phase (hopping model). A monolayer of each main rod outer segment (ROS) phospholipid interacting with a subphase containing G-protein, has been used to simulate the interaction of G-protein with the cytoplasmic surface of discal membranes. The possible diffusion of G-protein through the aqueous phase was then measured by observing its adsorption–desorption in the monolayer of each main ROS phospholipi…

biologyChemistryAqueous two-phase systemPhospholipidMembrane ProteinsCell BiologySurface pressureBiochemistryCrystallographychemistry.chemical_compoundMembraneGTP-Binding ProteinsCytoplasmRhodopsinMonolayerbiology.proteinAnimalsCattlePhotoreceptor CellsDiffusion (business)Molecular BiologyPhospholipidsBiochemistry and Cell Biology
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Local vs global motions in protein folding

2013

It is of interest to know whether local fluctuations in a polypeptide chain play any role in the mechanism by which the chain folds to the native structure of a protein. This question is addressed by analyzing folding and non-folding trajectories of a protein; as an example, the analysis is applied to the 37-residue triple β-strand WW domain from the Formin binding protein 28 (FBP28) (PDB ID: 1E0L). Molecular dynamics (MD) trajectories were generated with the coarse-grained united-residue force field, and one- and two-dimensional free-energy landscapes (FELs) along the backbone virtual-bond angle θ and backbone virtual-bond-dihedral angle γ of each residue, and principal components, respect…

biologyChemistryBinding proteinProtein Data Bank (RCSB PDB)NanotechnologyForce field (chemistry)ArticleComputer Science ApplicationsWW domainMolecular dynamicsForminsPrincipal component analysisbiology.proteinProtein foldingPhysical and Theoretical ChemistryBiological system
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Novel structural insights into F-actin-binding and novel functions of calponin homology domains.

2008

Tandem calponin homology (CH) domains are well-known actin filaments (F-actin) binding motifs. There has been a continuous debate about the details of CH domain-actin interaction, mainly because atomic level structures of F-actin are not available. A recent electron microscopy study has considerably advanced our structural understanding of CH domain:F-actin complex. On the contrary, it has recently also been shown that CH domains can bind other macromolecular systems: two CH domains from separate polypeptides Ncd80, Nuf2 can form a microtubule-binding site, as well as tandem CH domains in the EB1 dimer, while the single C-terminal CH domain of alpha-parvin has been observed to bind to a alp…

biologyTandemChemistryDimerCalponinCalcium-Binding ProteinsMicrofilament ProteinsF-actin bindingmacromolecular substancesMicrotubulesActinschemistry.chemical_compoundCrystallographyActin CytoskeletonMicroscopy ElectronStructural BiologyStructural Homology Proteinbiology.proteinProtein Interaction Domains and MotifsPaxillinMolecular BiologyActinPaxillinMacromoleculeProtein Binding
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