Search results for " Small"

showing 10 items of 806 documents

Combined inhibition of Bcl-2 and NFκB synergistically induces cell death in cutaneous T-cell lymphoma.

2019

Abstract Therapeutic options for cutaneous T-cell lymphoma (CTCL) are limited and curative treatment regimens are not available. Thus, new targeted and well-tolerated therapeutic approaches are urgently needed. In this respect, we have recently shown that dimethyl fumerate (DMF) inhibits NF-κB acting as a survival factor in CTCL. Similarly, inhibition of the antiapoptotic protein B-cell lymphoma 2 (Bcl-2) has been shown to induce cell death in CTCL especially when combined with histone deacetylase inhibitors. Therefore, we hypothesized that inhibition of Bcl-2 should potentiate NF-κB inhibition in a novel combination treatment of CTCL. We show that, in vitro, the Bcl-2 inhibitors ABT-199 an…

Programmed cell deathT cellImmunologyAntineoplastic AgentsApoptosisBiochemistryMicehemic and lymphatic diseasesCell Line TumormedicineAnimalsHumansRNA Small InterferingCell ProliferationNeoplasm StagingCell DeathDose-Response Relationship Drugbusiness.industryCutaneous T-cell lymphomaNF-kappa BDrug SynergismCell BiologyHematologymedicine.diseaseXenograft Model Antitumor AssaysLymphomaLymphoma T-Cell CutaneousHistone Deacetylase InhibitorsDisease Models Animalmedicine.anatomical_structureProto-Oncogene Proteins c-bcl-2ApoptosisCell cultureCancer researchRNA InterferenceHistone deacetylaseSignal transductionbusinessProtein BindingBlood
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The Cleavage Product of Amyloid-β Protein Precursor sAβPPα Modulates BAG3-Dependent Aggresome Formation and Enhances Cellular Proteasomal Activity

2015

Alzheimer's disease (AD) is the major age-associated form of dementia characterized by gradual cognitive decline. Aberrant cleavage of the amyloid-β protein precursor (AβPP) is thought to play an important role in the pathology of this disease. Two principal AβPP processing pathways exist: amyloidogenic cleavage of AβPP resulting in production of the soluble N-terminal fragment sAβPPβ, amyloid-β (Aβ), which accumulates in AD brain, and the AβPP intracellular domain (AICD) sAβPPα, p3 and AICD are generated in the non-amyloidogenic pathway. Prevalence of amyloidogenic versus non-amyloidogenic processing leads to depletion of sAβPPα and an increase in Aβ. Although sAβPPα is a well-accepted neu…

Proteasome Endopeptidase ComplexTime FactorsCell SurvivalLeupeptinsGreen Fluorescent ProteinsCysteine Proteinase InhibitorsProtein degradationProtein aggregationBiologyTransfectionBAG3Rats Sprague-DawleyAmyloid beta-Protein PrecursorAnimalsHumansRNA MessengerRNA Small InterferingProtein precursorCells CulturedAdaptor Proteins Signal TransducingNeuronsAmyloid beta-PeptidesDose-Response Relationship DrugGeneral NeuroscienceHEK 293 cellsBrainGeneral MedicineFibroblastsEmbryo MammalianRatsCell biologyPsychiatry and Mental healthClinical PsychologyHEK293 CellsProteostasisAggresomeGene Expression RegulationBiochemistryProteasomeProteolysisAmyloid Precursor Protein SecretasesGeriatrics and GerontologyApoptosis Regulatory ProteinsJournal of Alzheimer's Disease
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Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers.

2009

Ligand-mediated dimerization has emerged as a universal mechanism of growth factor receptor activation. Recent structural studies have shown that neurotrophins interact with dimers of the p75 neurotrophin receptor (p75NTR), but the actual mechanism of receptor activation has remained elusive. Here we show that p75NTR forms disulphide-linked dimers independently of neurotrophin binding through the highly conserved Cys257 in its transmembrane domain. Mutation of Cys257 abolished neurotrophin-dependent receptor activity but did not affect downstream signaling by the p75NTR/NgR/Lingo-1 complex in response to MAG, indicating the existence of distinct, ligand-specific activation mechanisms for p7…

Protein ConformationMutantNeuronesReceptor Nerve Growth FactorMiceProtein structureChlorocebus aethiopsNerve Growth FactorLow-affinity nerve growth factor receptorRNA Small InterferingReceptorskin and connective tissue diseasesReceptors neuralsCells CulturedNeuronsCell DeathGeneral NeuroscienceNF-kappa BCell biologyTransmembrane domainSIGNALINGOligopeptidesNeurotrophinProtein BindingSignal Transductionmusculoskeletal diseasesPROTEINSNeuroscience(all)Green Fluorescent ProteinsNerve Tissue ProteinsReceptors Nerve Growth FactorSuperior Cervical GanglionBiologyTransfectionMOLNEUROArticleGrowth factor receptorAnimalsHumansProtein Interaction Domains and MotifsReceptors Growth FactorCysteineBinding SitesMembrane Proteinsbiological factorsRatsnervous systemAnimals NewbornNeurotrophin bindingMutationbiology.proteinsense organsProtein MultimerizationrhoA GTP-Binding ProteinProteïnesNeuron
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Biotechnical applications of small heat shock proteins from bacteria.

2012

The stress responses of most bacteria are thought to involve the upregulation of small heat shock proteins. We describe here some of the most pertinent aspects of small heat shock proteins, to highlight their potential for use in various applications. Bacterial species have between one and 13 genes encoding small heat shock proteins, the precise number depending on the species considered. Major efforts have recently been made to characterize the protein protection and membrane stabilization mechanisms involving small heat shock proteins in bacteria. These proteins seem to be involved in the acquisition of cellular heat tolerance. They could therefore potentially be used to maintain cell via…

Protein FoldingHeterologousmedicine.disease_causeBiochemistryMicrobiologyDownregulation and upregulationBacterial ProteinsStress PhysiologicalHeat shock proteinmedicineHumansViability assayEscherichia coliInclusion BodiesbiologyProtein StabilityProbioticsCell Biologybiology.organism_classificationRecombinant ProteinsCell biologyHeat-Shock Proteins SmallSolubilityShock (circulatory)Food TechnologyProtein foldingmedicine.symptomBacteriaBiotechnologyThe international journal of biochemistrycell biology
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Nucleation and Growth of CaCO3 Mediated by the Egg-White Protein Ovalbumin: A Time-Resolved in situ Study Using Small-Angle Neutron Scattering

2008

Mineralization of calcium carbonate in aqueous solutions starting from its initiation was studied by time-resolved small-angle neutron scattering (SANS). SANS revealed that homogeneous crystallization of CaCO 3 involves an initial formation of thin plate-shaped nuclei which subsequently reassemble to 3-dimensional particles, first of fractal and finally of compact structure. The presence of the egg-white protein ovalbumin leads to a different progression of mineralization through several stages; the first step represents amorphous CaCO 3, whereas the other phases are crystalline. The formation and dissolution of the amorphous phase is accompanied by Ca (2+)-mediated unfolding and cross-link…

Protein FoldingOvalbuminProtein ConformationChemistryNeutron diffractionNucleationWaterGeneral ChemistryNeutron scatteringBiochemistrySmall-angle neutron scatteringCatalysisCalcium Carbonatelaw.inventionAmorphous solidCalcium ChlorideNeutron DiffractionCrystallographyColloid and Surface ChemistrylawVateriteScattering Small AngleCrystallizationCrystallizationDissolutionJournal of the American Chemical Society
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Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity

2009

Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsib…

Protein sumoylationTranscriptional ActivationCancer Researchendocrine systemanimal structuresSUMO proteinHSP27 Heat-Shock ProteinsBiologyurologic and male genital diseasesenvironment and public healthSubstrate Specificity03 medical and health sciencesTransactivation0302 clinical medicineHeat Shock Transcription FactorsHeat shock proteinGeneticsAnimalsHumansAnimals Cell Nucleus/metabolism DNA-Binding Proteins/*metabolism HSP27 Heat-Shock Proteins/chemistry/*metabolism Hela Cells Humans Protein Multimerization Protein Structure[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyHSF1Protein Structure QuaternaryMolecular BiologyTranscription factorUbiquitinsHeat-Shock Proteins030304 developmental biologyCell Nucleus0303 health sciencesMolecular biologyHsp70Cell biologyHeat shock factorDNA-Binding ProteinsProtein TransportQuaternary Protein Transport Small Ubiquitin-Related Modifier Proteins/*metabolism Substrate Specificity Transcription Factors/*metabolism Transcriptional Activation Ubiquitins/*metabolism030220 oncology & carcinogenesisembryonic structuresSmall Ubiquitin-Related Modifier ProteinsProtein MultimerizationHeLa CellsMolecular ChaperonesTranscription Factors
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Identification of proteins cleaved downstream of caspase activation in monocytes undergoing macrophage differentiation.

2006

We have shown previously that caspases were specifically involved in the differentiation of peripheral blood monocytes into macrophages while not required for monocyte differentiation into dendritic cells. To identify caspase targets in monocytes undergoing macrophagic differentiation, we used the human monocytic leukemic cell line U937, whose macrophagic differentiation induced by exposure to 12-O-tetradecanoylphorbol 13-acetate (TPA) can be prevented by expression of the baculovirus caspase-inhibitory protein p35. A comparative two-dimensional gel proteomic analysis of empty vector- and p35-transfected cells after 12 h of exposure to 20 nm TPA, followed by mass spectrometry analysis, iden…

ProteomeCleavage (embryo)Caspase 8TransfectionBiochemistryMonocytesViral ProteinsHumansElectrophoresis Gel Two-DimensionalRNA Small InterferingMolecular BiologyCaspaseCaspase 8biologyU937 cellMacrophagesRNACell DifferentiationCell BiologyTransfectionU937 CellsMolecular biologyCaspase InhibitorsPeptide FragmentsCell biologyEnzyme ActivationCell cultureMonocyte differentiationCaspasesbiology.proteinCarcinogensTetradecanoylphorbol AcetateThe Journal of biological chemistry
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TrpM, a Small Protein Modulating Tryptophan Biosynthesis and Morpho-Physiological Differentiation in Streptomyces coelicolor A3(2).

2016

In the model actinomycete Streptomyces coelicolor A3(2), small open reading frames encoding proteins with unknown functions were identified in several amino acid biosynthetic gene operons, such as SCO2038 (trpX) in the tryptophan trpCXBA locus. In this study, the role of the corresponding protein in tryptophan biosynthesis was investigated by combining phenotypic and molecular analyses. The 2038KO mutant strain was characterized by delayed growth, smaller aerial hyphae and reduced production of spores and actinorhodin antibiotic, with respect to the WT strain. The capability of this mutant to grow on minimal medium was rescued by tryptophan and tryptophan precursor (serine and/or indole) su…

Proteomics0301 basic medicineProtein ExtractionMutantlcsh:MedicineStreptomyces coelicolor A3(2)Settore BIO/19 - Microbiologia GeneraleBiochemistrySerinechemistry.chemical_compoundAromatic Amino AcidsSmall ProteinAntibioticsTRPMMicrobial PhysiologyMedicine and Health SciencesBacterial PhysiologyAmino Acidslcsh:ScienceProtein MetabolismExtraction TechniquesMultidisciplinarybiologyOrganic CompoundsAntimicrobialsStreptomyces coelicolorTryptophanDrugsChemistryBiochemistryPhysical SciencesPhysiological DifferentiationResearch ArticleTryptophan BiosynthesiSmall Protein; Biosynthesis; Morpho-Physiological Differentiation: Streptomyces coelicolorBiosynthesisResearch and Analysis MethodsMicrobiologyStreptomycesActinorhodin03 medical and health sciencesBiosynthesisMicrobial ControlBacterial SporesPharmacology030102 biochemistry & molecular biologyOrganic Chemistrylcsh:RChemical CompoundsTryptophanTrpM; Small Protein; Tryptophan Biosynthesis; Morphological Differentiation; Physiological Differentiation; Streptomyces coelicolor A3(2); ProteomicsBiology and Life SciencesProteinsBacteriologybiology.organism_classificationAmino Acid MetabolismMetabolism030104 developmental biologychemistrylcsh:QMorphological DifferentiationTrpM
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SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear transfer of tri-snRNP complexes

2021

Abstract Splicing is catalyzed by the spliceosome, a compositionally dynamic complex assembled stepwise on pre-mRNA. We reveal links between splicing machinery components and the intrinsically disordered ciliopathy protein SANS. Pathogenic mutations in SANS/USH1G lead to Usher syndrome—the most common cause of deaf-blindness. Previously, SANS was shown to function only in the cytosol and primary cilia. Here, we have uncovered molecular links between SANS and pre-mRNA splicing catalyzed by the spliceosome in the nucleus. We show that SANS is found in Cajal bodies and nuclear speckles, where it interacts with components of spliceosomal sub-complexes such as SF3B1 and the large splicing cofact…

ProteomicsAcademicSubjects/SCI00010Ribonucleoprotein U4-U6 Small NuclearSF3B1 GeneMass Spectrometry0302 clinical medicineRNA Small NuclearRNA PrecursorsIn Situ Hybridization FluorescenceRibonucleoprotein0303 health sciencesChemistryRibonucleoproteins Small NuclearImmunohistochemistryCell biologyDNA-Binding Proteinsmedicine.anatomical_structureGene Knockdown TechniquesRNA splicingRNA Splicing FactorsUsher SyndromesSpliceosomeCoiled BodiesNerve Tissue ProteinsBiologyMinor Histocompatibility Antigens03 medical and health sciencesMicroscopy Electron TransmissionRNA and RNA-protein complexesGeneticsmedicineHumanssnRNPEye ProteinsGeneCell Proliferation030304 developmental biologyCell NucleusRNAmedicine.diseasePhosphoproteinsCiliopathyAlternative SplicingCell nucleusHEK293 CellsCajal bodyCytoplasmSpliceosomesNucleus030217 neurology & neurosurgeryTranscription FactorsNucleic Acids Research
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The Wnt-specific astacin proteinase HAS-7 restricts head organizer formation in Hydra

2021

Abstract Background The Hydra head organizer acts as a signaling center that initiates and maintains the primary body axis in steady state polyps and during budding or regeneration. Wnt/beta-Catenin signaling functions as a primary cue controlling this process, but how Wnt ligand activity is locally restricted at the protein level is poorly understood. Here we report a proteomic analysis of Hydra head tissue leading to the identification of an astacin family proteinase as a Wnt processing factor. Results Hydra astacin-7 (HAS-7) is expressed from gland cells as an apical-distal gradient in the body column, peaking close beneath the tentacle zone. HAS-7 siRNA knockdown abrogates HyWnt3 proteo…

ProteomicsPhysiologyHydraQH301-705.5XenopusPlant ScienceProteinaseGeneral Biochemistry Genetics and Molecular BiologyStructural BiologyAstacinAxis formationAnimalsRNA Small InterferingBiology (General)Wnt Signaling PathwayEcology Evolution Behavior and SystematicsActinbeta CateninBody PatterningGene knockdownBuddingbiologyRegeneration (biology)Wnt signaling pathwayMetalloendopeptidasesCell Biologybiology.organism_classificationWnt signalingCell biologyWnt ProteinsProteolysisLernaean HydraAstacinGeneral Agricultural and Biological SciencesHeadDevelopmental BiologyBiotechnologyResearch ArticleBMC Biology
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