Search results for "binding"

showing 10 items of 3896 documents

The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress response element (STR…

1996

The MSN2 and MSN4 genes encode homologous and functionally redundant Cys2His2 zinc finger proteins. A disruption of both MSN2 and MSN4 genes results in a higher sensitivity to different stresses, including carbon source starvation, heat shock and severe osmotic and oxidative stresses. We show that MSN2 and MSN4 are required for activation of several yeast genes such as CTT1, DDR2 and HSP12, whose induction is mediated through stress-response elements (STREs). Msn2p and Msn4p are important factors for the stress-induced activation of STRE dependent promoters and bind specifically to STRE-containing oligonucleotides. Our results suggest that MSN2 and MSN4 encode a DNA-binding component of the…

Hot TemperatureSaccharomyces cerevisiae ProteinsTranscription GeneticSaccharomyces cerevisiaeMolecular Sequence DataPlasma protein bindingSaccharomyces cerevisiaeGeneral Biochemistry Genetics and Molecular BiologyTranscription (biology)Osmotic PressureMolecular BiologyGeneTranscription factorZinc fingerGeneticsGeneral Immunology and MicrobiologybiologyBase SequenceGeneral NeurosciencePromoterZinc Fingersbiology.organism_classificationYeastCell biologyDNA-Binding ProteinsOxidative StressOligodeoxyribonucleotidesResearch ArticleProtein BindingTranscription Factors
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Characterization of Acylating and Deacylating Activities of an Extracellular Phospholipase A2 in a Water-Restricted Environment

1994

The behavior of porcine pancreatic phospholipase A2 (ppPLA2) in monophasic low-water media has been explored, for the first time, in a systematic manner. It has been investigated how a number of variables can modulate both acylating and deacylating activities of the enzyme, and several interesting, unexpected results are presented. Among the most relevant, when placing ppPLA2 in the water-restricted environment, are the following: (i) it displays a remarkable alteration of its specificity toward the substrate polar head relative to all-water medium; (ii) it is quite severely inhibited by lysophosphatidylcholine (LPC), which has important implications, particularly concerning its acylation a…

Hot TemperatureSwineStereochemistryAcylationOleic AcidsBinding CompetitiveBiochemistryPhospholipases ASubstrate SpecificityAcylationchemistry.chemical_compoundPhospholipase A2Enzyme StabilityExtracellularAnimalsPancreasEdetic Acidchemistry.chemical_classificationEsterificationbiologyChemistryHydrolysisLysophosphatidylcholinesWaterSubstrate (chemistry)In vitroKineticsPhospholipases A2LysophosphatidylcholineEnzymeBiochemistryYield (chemistry)Phosphatidylcholinesbiology.proteinCalciumExtracellular SpaceOleic AcidBiochemistry
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Modification of the major tegument protein pp65 of human cytomegalovirus inhibits virus growth and leads to the enhancement of a protein complex with…

2010

The tegument protein pp65 of human cytomegalovirus (HCMV) is abundant in lytically infected human foreskin fibroblasts (HFF), as well as in virions and subviral dense bodies (DB). Despite this, we showed previously that pp65 is dispensable for growth in HFF. In the process of refining a DB-based vaccine candidate, different HCMV mutants were generated, expressing a dominant HLA-A2-presented peptide of the IE1 protein fused to pp65. One of the mutant viruses (RV-VM1) surprisingly showed marked impairment in virus release from HFF. We hypothesized that analysis of the phenotypic alterations of RV-VM1 would provide insight into the functions of pp65, poorly defined thus far. RV-VM1 infection r…

Human cytomegalovirusImmunoprecipitationvirusesMutantCytomegalovirusBiologyVirus ReplicationVirusInclusion bodiesViral Matrix ProteinsViral ProteinsVirologymedicineHumansImmunoprecipitationCells Culturedvirus diseasesRNAViral tegumentFibroblastsPhosphoproteinsmedicine.diseaseVirologyFusion proteinTrans-ActivatorsProtein MultimerizationProtein BindingJournal of General Virology
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Suppression of CD8+ T cell recognition in the immediate-early phase of human cytomegalovirus infection.

2012

Human cytomegalovirus (HCMV) interferes with MHC class I-restricted antigen presentation and thereby reduces recognition by CD8+ T-cells. This interference is mediated primarily by endoplasmic reticulum-resident glycoproteins that are encoded in the US2–11 region of the viral genome. Such a suppression of recognition would be of particular importance immediately after infection, because several immunodominant viral antigens are already present in the cell in this phase. However, which of the evasion proteins gpUS2–11 interfere(s) with antigen presentation to CD8+ T-cells at this time of infection is not known. Here we address this question, using recombinant viruses (RV) that express only o…

Human cytomegalovirusVirulence FactorsvirusesAntigen presentationCytomegalovirusCD8-Positive T-LymphocytesCell LineImmune toleranceViral ProteinsViral Envelope ProteinsAntigenVirologyMHC class IImmune TolerancemedicineHumansCytotoxic T cellImmune EvasionbiologyHistocompatibility Antigens Class IRNA-Binding Proteinsvirus diseasesmedicine.diseaseVirologyCell cultureCytomegalovirus InfectionsImmunologybiology.proteinCD8
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Immune evasion proteins gpUS2 and gpUS11 of human cytomegalovirus incompletely protect infected cells from CD8 T cell recognition

2009

AbstractHuman cytomegalovirus (HCMV) encodes four glycoproteins, termed gpUS2, gpUS3, gpUS6 and gpUS11 that interfere with MHC class I biosynthesis and antigen presentation. Despite gpUS2–11 expression, however, HCMV infection is efficiently controlled by cytolytic CD8 T lymphocytes (CTL). To address the role of gpUS2 and gpUS11 in antigen presentation during viral infection, HCMV mutants were generated that expressed either gpUS2 or gpUS11 alone without coexpression of the three other proteins. Fibroblasts infected with these viruses showed reduced HLA-A2 and HLA-B7 surface expression. Surprisingly, however, CTL directed against the tegument protein pp65 and the regulatory IE1 protein stil…

Human cytomegalovirusvirusesAntigen presentationIE1CytomegalovirusCD8-Positive T-LymphocytesVirus ReplicationMajor histocompatibility complexpp65US2Immediate-Early ProteinsViral Matrix ProteinsHLA-B7 AntigenInterferon-gammaViral ProteinsImmune systemViral Envelope ProteinsVirologyHLA-A2 AntigenMHC class ImedicineHumansCytotoxic T cellCells CulturedAntigen PresentationbiologyImmune evasionRNA-Binding Proteinsvirus diseasesbiochemical phenomena metabolism and nutritionPhosphoproteinsmedicine.diseaseVirologyCTL*MutagenesisCTLCytomegalovirus InfectionsMHC class Ibiology.proteinUS11CD8Virology
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Polo-like kinase 1 as a target for human cytomegalovirus pp65 lower matrix protein

1999

ABSTRACT Human cytomegalovirus (HCMV) pp65 protein is the major constituent of viral dense bodies but is dispensable for viral growth in vitro. pp65 copurifies with a S/T kinase activity and has been implicated in phosphorylation of HCMV IE1 immediate-early protein and its escape from major histocompatibility complex 1 presentation. Furthermore, the presence of pp65 correlates with a virion-associated kinase activity. To clarify the role of pp65, yeast two-hybrid system (THS) screening was performed to identify pp65 cellular partners. A total of 18 out of 48 yeast clones harboring cDNAs for putative pp65 binding proteins encoded the Polo-like kinase 1 (Plk1) C-terminal domain. Plk1 behaved …

Human cytomegalovirusvirusesRecombinant Fusion ProteinsImmunologyCytomegalovirusCell Cycle ProteinsPolo-like kinaseBiologyProtein Serine-Threonine KinasesMicrobiologyDNA-binding proteinPLK1Cell LineViral Matrix ProteinsVirologyProto-Oncogene ProteinsmedicineAnimalsHumansKinase activityViral matrix proteinKinasevirus diseasesmedicine.diseasePhosphoproteinsMolecular biologyVirus-Cell Interactionssurgical procedures operativeInsect ScienceCOS CellsPhosphorylationProtein KinasesHeLa Cells
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Ubiquitin-independent function of optineurin in autophagic clearance of protein aggregates.

2013

Summary Aggregation of misfolded proteins and the associated loss of neurons are considered a hallmark of numerous neurodegenerative diseases. Optineurin is present in protein inclusions observed in various neurodegenerative diseases including amyotrophic lateral sclerosis (ALS), Huntington's disease, Alzheimer's disease, Parkinson's disease, Creutzfeld-Jacob disease and Pick's disease. Optineurin deletion mutations have also been described in ALS patients. However, the role of optineurin in mechanisms of protein aggregation remains unclear. In this report, we demonstrate that optineurin recognizes various protein aggregates via its C-terminal coiled-coil domain in a ubiquitin-independent m…

HuntingtinSOD1AggrephagyCell Cycle ProteinsMice TransgenicProtein aggregationBiologyArticle03 medical and health sciencesMice0302 clinical medicineTANK-binding kinase 1UbiquitinTranscription Factor TFIIIAAutophagyAnimalsHumansPhosphorylationZebrafishZebrafish030304 developmental biologyOptineurin0303 health sciencesUbiquitinamyotrophic lateral sclerosis; Huntington disease; Huntingtin; optineurin; phosphorylation; SOD1; TBK1; ubiquitinMembrane Transport ProteinsNeurodegenerative DiseasesCell Biologybiology.organism_classification3. Good healthMice Inbred C57BLDisease Models AnimalCancer researchbiology.protein030217 neurology & neurosurgeryHeLa CellsProtein BindingJournal of cell science
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Expression of genes encoding the calcium signalosome in cellular and transgenic models of Huntington's disease

2013

Huntington's disease (HD) is a hereditary neurodegenerative disease caused by the expansion of a polyglutamine stretch in the huntingtin (HTT) protein and characterized by dysregulated calcium homeostasis. We investigated whether these disturbances are correlated with changes in the mRNA level of the genes that encode proteins involved in calcium homeostasis and signaling (i.e., the calciosome). Using custom-made TaqMan low-density arrays containing probes for 96 genes, we quantified mRNA in the striatum in YAC128 mice, a model of HD, and wildtype mice. HTT mutation caused the increased expression of some components of the calcium signalosome, including calretinin, presenilin 2, and calmyri…

Huntingtinhuntingtincalcium signalosomechemistry.chemical_elementtransgenic miceCalciumlcsh:RC321-571Cellular and Molecular Neurosciencehuntingtin-associated protein 1mental disordersGene expressionOriginal Research Articlelcsh:Neurosciences. Biological psychiatry. NeuropsychiatryMolecular BiologyCalcium metabolismTaqMan low-density arraysbiologyHuntingtin-associated protein 1Calcium channelTaqMan Low Density Arraysstore-operated calcium entrycalcyclin-binding proteinHuntington's diseaseMolecular biologyStore-operated calcium entrynervous systemchemistrybiology.proteinCalretininHuntington’s diseaseNeuroscienceFrontiers in Molecular Neuroscience
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Identification of biological markers of liver X receptor (LXR) activation at the cell surface of human monocytes.

2012

Background Liver X receptor (LXR) α and LXR β (NR1H3 and NR1H2) are oxysterol-activated nuclear receptors involved in the control of major metabolic pathways such as cholesterol homeostasis, lipogenesis, inflammation and innate immunity. Synthetic LXR agonists are currently under development and could find applications in various fields such as cardiovascular diseases, cancer, diabetes and neurodegenerative diseases. The clinical development of LXR agonists requires the identification of biological markers for pharmacodynamic studies. In this context, monocytes represent an attractive target to monitor LXR activation. They are easily accessible cells present in peripheral blood; they expres…

Hydrocarbons FluorinatedCD226Celllcsh:MedicineBiochemistryMonocytesDrug DiscoveryMolecular Cell Biologypolycyclic compoundsSignaling in Cellular Processeslcsh:ScienceLiver X ReceptorsSulfonamidesMultidisciplinarymedicine.diagnostic_testfood and beveragesCell DifferentiationOrphan Nuclear ReceptorsFlow CytometryNuclear SignalingCholesterolmedicine.anatomical_structureGene Knockdown Techniqueslipids (amino acids peptides and proteins)Research ArticleSignal TransductionAgonistmedicine.drug_classImmune CellsImmunologyContext (language use)Biologydigestive systemFlow cytometryAntigens CDDNA-binding proteinsmedicineHumansRNA MessengerLiver X receptorBiologyCluster of differentiationMacrophagesCell Membranelcsh:RProteinsLipid MetabolismMetabolismGene Expression RegulationNuclear receptorImmunologyCancer researchlcsh:QBiomarkersCytometryFoam CellsDevelopmental BiologyPLoS ONE
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Hydrogen Bonding and Anion Binding in Structures of Tris(pyrazolyl)boratenickel(II) and Phosphate Esters

2008

This paper presents the syntheses, crystal structures and spectroscopic properties of a series of nickel(II) complexes containing hydrotris(3,5-dimethylpyrazolyl)borate and phosphate esters: [Tp*Ni(Hpz*)2(L)][(RO)2PO2] [R = Et, Bu; L = H2O (1), (BuO)2P(O)OH (2)] and [Tp*Ni(Hpz*)(H2O)2][(EtO)2PO2] (5) {Tp* = hydrotris(3,5-dimethylpyrazolyl)borate, Hpz* = 3,5-dimethylpyrazole}. The complexes [Ni(Tp*)2] (3) and [(Tp*Ni)2(μ-pz*)(μ-OH)](4) were also prepared and fully characterized. X-ray crystallographic studies of 1 and 2 reveal that the pyrazole moieties are hydrogen bonded to the guest phosphate ester anion. In complex 5, the phosphate anion is hydrogen-bonded by two O–H groups of the water …

Hydrogen bondInorganic chemistrychemistry.chemical_elementCrystal structureNuclear magnetic resonance spectroscopyPyrazoleMedicinal chemistryInorganic ChemistryNickelchemistry.chemical_compoundchemistryProton NMRMoleculeAnion bindingEuropean Journal of Inorganic Chemistry
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