Search results for "DOMAIN"

showing 10 items of 2485 documents

Identity Formation in Adulthood: A Longitudinal Study from Age 27 to 50.

2016

Longitudinal patterns of identity formation were analyzed in a representative cohort group of Finnish men and women born in 1959 across ages 27, 36, 42, and 50. The data were drawn from the Jyväskylä Longitudinal Study of Personality. Identity status (diffused, moratorium, foreclosed, achieved) from all four ages was available for 172 participants (54% females). Marcia’s Identity Status Interview used in this research included five domains: religious beliefs, political identity, occupational career, intimate relationships, and lifestyle. The findings indicated great variability in identity status across domains at each age level, and the identity trajectories fluctuated from age 27 to 50. T…

Longitudinal studySociology and Political Sciencemedia_common.quotation_subjectsalience050109 social psychologyidentity developmentReligious identityArticleDevelopmental psychology5. Gender equalityidentity domainsfollow-upPersonality0501 psychology and cognitive sciences10. No inequalityta515media_commonAdult developmentcongruence05 social sciencesOriginal ArticlesMiddle ageCongruenceIdentity developmentoverall identityidentity statusCohortmiddle-agePsychology (miscellaneous)PsychologyIdentity formation050104 developmental & child psychologyIdentity (Mahwah, N.J.)
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Expression inactivation of SMARCA4 by microRNAs in lung tumors

2014

SMARCA4 is the catalytic subunit of the SWI/SNF chromatin-remodeling complex, which alters the interactions between DNA and histones and modifies the availability of the DNA for transcription. The latest deep sequencing of tumor genomes has reinforced the important and ubiquitous tumor suppressor role of the SWI/SNF complex in cancer. However, although SWI/SNF complex plays a key role in gene expression, the regulation of this complex itself is poorly understood. Significantly, an understanding of the regulation of SMARCA4 expression has gained in importance due to recent proposals incorporating it in therapeutic strategies that use synthetic lethal interactions between SMARCA4-MAX and SMAR…

Lung NeoplasmsDeep sequencingHistonesTranscription (biology)Catalytic DomainCell Line TumorGene expressionmicroRNAGeneticsHumansCloning MolecularMolecular BiologyTranscription factorGenetics (clinical)Cell ProliferationCell NucleusRegulation of gene expressionGeneticsbiologyDNA HelicasesHigh-Throughput Nucleotide SequencingNuclear ProteinsReproducibility of ResultsArticlesGeneral MedicineChromatin Assembly and DisassemblyPrognosisUp-RegulationCell biologyGene Expression Regulation NeoplasticMicroRNAsHistonebiology.proteinSMARCA4HeLa CellsTranscription FactorsHuman Molecular Genetics
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Targeted Repolarization of Tumor‐Associated Macrophages via Imidazoquinoline‐Linked Nanobodies

2021

Abstract Tumor‐associated macrophages (TAMs) promote the immune suppressive microenvironment inside tumors and are, therefore, considered as a promising target for the next generation of cancer immunotherapies. To repolarize their phenotype into a tumoricidal state, the Toll‐like receptor 7/8 agonist imidazoquinoline IMDQ is site‐specifically and quantitatively coupled to single chain antibody fragments, so‐called nanobodies, targeting the macrophage mannose receptor (MMR) on TAMs. Intravenous injection of these conjugates result in a tumor‐ and cell‐specific delivery of IMDQ into MMRhigh TAMs, causing a significant decline in tumor growth. This is accompanied by a repolarization of TAMs to…

Lung NeoplasmsGeneral Chemical Engineeringmedicine.medical_treatmentGeneral Physics and AstronomyMedicine (miscellaneous)TLR 7/8 agonist02 engineering and technology01 natural scienceschemistry.chemical_compoundCancer immunotherapyTumor-Associated MacrophagesTumor MicroenvironmentMacrophageM2 macrophagesGeneral Materials ScienceReceptorResearch ArticlesMice KnockoutMembrane GlycoproteinsChemistrytumor associated macrophagesQGeneral EngineeringImidazoles021001 nanoscience & nanotechnologynanobodiesmedicine.anatomical_structureDrug deliveryQuinolines0210 nano-technologyMannose ReceptorResearch ArticleT cellScience010402 general chemistryBiochemistry Genetics and Molecular Biology (miscellaneous)Immune systemmedicineAnimalsrepolarizationcancer immunotherapyCancerSingle-Domain Antibodiesmedicine.disease0104 chemical sciencesImidazoquinolineMice Inbred C57BLDisease Models AnimalToll-Like Receptor 6Toll-Like Receptor 7drug deliveryCancer research
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Histocompatibility reaction in tissue and cells of the marine sponge Suberites domuncula in vitro and in vivo: central role of the allograft inflamma…

2001

Sponges (Porifera) are the phylogenetically oldest still extant metazoan phylum. Recently elements of their immune system have been cloned and analyzed, primarily from the demosponges Suberites domuncula and Geodia cydonium. By differential display, two genes were identified in S. domuncula, whose translation products are involved in graft rejection/fusion: the allograft inflammatory factor (AIF-1) and the Tcf-like transcription factor (TCF). Since the AIF-1 and TCF genes are upregulated in vivo after tissue transplantation, especially in allografts, we investigated whether this reaction can be monitored in vitro. Therefore, the autogeneic and the allogeneic mixed sponge cell reaction (MSCR…

Lymphoid Enhancer-Binding Factor 1ImmunologyMolecular Sequence DataTacrolimusdemosponges; Suberites domuncula; Geodia cydonium; AIF-1(allograft inflamatory factor 1); TCFMicrobiologyImmune systemGeneticsAnimalsAmino Acid SequenceCloning MoleculareducationTranscription factorPhylogenyeducation.field_of_studyDifferential displaybiologyCalcium-Binding Proteinsbiology.organism_classificationIn vitroRecombinant ProteinsCell biologyHistocompatibilityPoriferaSuberites domunculaDNA-Binding ProteinsSpongeGene Expression RegulationHMG-Box DomainsHistocompatibilityAllograft inflammatory factor 1Transcription Factors
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A chimera carrying the functional domain of the orphan protein SLC7A14 in the backbone of SLC7A2 mediates trans-stimulated arginine transport.

2012

In human skin fibroblasts, a lysosomal transport system specific for cationic amino acids has been described and named system c. We asked if SLC7A14 (solute carrier family 7 member A14), an orphan protein assigned to the SLC7 subfamily of cationic amino acid transporters (CATs) due to sequence homology, may represent system c. Fusion proteins between SLC7A14 and enhanced GFP localized to intracellular vesicles, co-staining with the lysosomal marker LysoTracker(®). To perform transport studies, we first tried to redirect SLC7A14 to the plasma membrane (by mutating putative lysosomal targeting motifs) but without success. We then created a chimera carrying the backbone of human (h) CAT-2 and …

Lysosomal transportArginineRecombinant Fusion ProteinsProtein domainBiological Transport ActiveBiologyArginineBiochemistryCell LineXenopus laevisMembrane BiologyAnimalsHumansMolecular BiologySkinchemistry.chemical_classificationArginine transportCell BiologyMembrane transportFibroblastsHydrogen-Ion ConcentrationFusion proteinSolute carrier familyAmino acidProtein Structure TertiaryBiochemistrychemistryAmino Acid Transport Systems BasicLysosomesThe Journal of biological chemistry
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Divide and rule: The role of ubiquitination in inactivation of the ERK5-MAPK cascade

2014

Recently, we revealed that ubiquitination of MEKK2 and MEKK3 by inhibitor of apoptosis proteins (IAPs) directly disrupts MEK5/ERK5 interaction and subsequently attenuates ERK5 activation. In addition, loss of XIAP promotes human myogenic differentiation in an ERK5-dependent manner. These results reveal another layer of MAPK regulation and a novel role for XIAP in controlling myogenic differentiation.

MAPK/ERK pathwayInhibitor of apoptosis domainCancer ResearchAkt/PKB signaling pathwayChemistryMAPK cascadeInhibitor of apoptosisMAP2K7XIAPCell biologyCancer researchMolecular MedicineAuthor's ViewProtein kinase BMolecular & Cellular Oncology
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Influences of TP53 and the anti-aging DDR1 receptor in controlling Raf/MEK/ERK and PI3K/Akt expression and chemotherapeutic drug sensitivity in prost…

2020

Background TP53 plays critical roles in sensitivity to chemotherapy, and aging. Collagen is very important in aging. The molecular structure and biochemical properties of collagen changes during aging. The discoidin domain receptor (DDR1) is regulated in part by collagen. Elucidating the links between TP53 and DDR1 in chemosensitivity and aging could improve therapies against cancer and aging. Results Restoration of WT-TP53 activity resulted in increased sensitivity to chemotherapeutic drugs and elevated expression of key components of the Raf/MEK/ERK, PI3K/Akt and DDR1 pathways. DDR1 could modulate the levels of Raf/MEK/ERK and PI3K/Akt pathways as well as sensitize the cells to chemothera…

MAPK/ERK pathwayMalecollagenAgingRAF/MEK/ERKMAP Kinase Signaling SystemAntineoplastic Agentsdiscoidin domain receptor (DDR1)DDRCollagen receptorPhosphatidylinositol 3-KinasesDiscoidin Domain Receptor 1Cell Line TumorHumansRapamycinTP53ReceptorProtein kinase BPI3K/AKT/mTOR pathwayDDR1ChemistryWild typeProstateProstatic NeoplasmschemoresistanceCell Biologyprostate cancerDrug Resistance NeoplasmMutationCancer researchraf KinasesTumor Suppressor Protein p53Discoidin domainResearch Paper
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The role of death effector domain (DED)-containing proteins in acute oxidative cell injury in hepatocytes

2012

Abstract Apoptosis is a mechanism that regulates hepatic tissue homeostasis and contributes to both acute and chronic injury in liver disease. The apoptotic signaling cascade involves activation of the death-inducing signaling complex (DISC) and subsequent recruitment of proteins containing death effector domains (DED), which regulate downstream effector molecules. Prominent among these are the Fas-associated death domain (FADD) and the cellular caspase 8-like inhibitory protein (cFLIP), and alterations in these proteins can lead to severe disruption of physiological processes, including acute liver failure or hepatocellular carcinoma. Their role in cell signaling events independent of the …

MAPK/ERK pathwayProgrammed cell deathDeath Domain Receptor Signaling Adaptor ProteinsbiologyBlotting WesternBiochemistryArticleCell biologyMiceMicroscopy FluorescencePhysiology (medical)Cell Line TumorDeath-inducing signaling complexModels Animalbiology.proteinHepatocytesAnimalsHumansDeath effector domainFADDSignal transductionCaspaseDeath domainSignal Transduction
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Transmembrane form agrin-induced process formation requires lipid rafts and the activation of Fyn and MAPK.

2009

Overexpression or clustering of the transmembrane form of the extracellular matrix heparan sulfate proteoglycan agrin (TM-agrin) induces the formation of highly dynamic filopodia-like processes on axons and dendrites from central and peripheral nervous system-derived neurons. Here we show that the formation of these processes is paralleled by a partitioning of TM-agrin into lipid rafts, that lipid rafts and transmembrane-agrin colocalize on the processes, that extraction of lipid rafts with methyl-β-cyclodextrin leads to a dose-dependent reduction of process formation, that inhibition of lipid raft synthesis prevents process formation, and that the continuous presence of lipid rafts is requ…

MAPK/ERK pathwayanimal structuresMAP Kinase Signaling SystemChick EmbryoBiologyProto-Oncogene Proteins c-fynBiochemistryExtracellular matrixFYNMembrane MicrodomainsMolecular Basis of Cell and Developmental BiologyAnimalsSrc family kinasePseudopodiaPhosphorylationMolecular BiologyLipid raftCells CulturedMitogen-Activated Protein Kinase KinasesAgrinDose-Response Relationship Drugbeta-CyclodextrinsCell BiologyDendritesTransmembrane proteinAxonsCell biologyEnzyme Activationnervous systemPhosphorylationlipids (amino acids peptides and proteins)ChickensThe Journal of biological chemistry
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Differential inhibition of TRAIL-mediated DR5-DISC formation by decoy receptors 1 and 2.

2006

International audience; Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) is a member of the TNF family that induces cancer cell death by apoptosis with some selectivity. TRAIL-induced apoptosis is mediated by the transmembrane receptors death receptor 4 (DR4) (also known as TRAIL-R1) and DR5 (TRAIL-R2). TRAIL can also bind decoy receptor 1 (DcR1) (TRAIL-R3) and DcR2 (TRAIL-R4) that fail to induce apoptosis since they lack and have a truncated cytoplasmic death domain, respectively. In addition, DcR1 and DcR2 inhibit DR4- and DR5-mediated, TRAIL-induced apoptosis and we demonstrate here that this occurs through distinct mechanisms. While DcR1 prevents the assembly of the…

MESH : Hela CellsMESH: Membrane GlycoproteinsMESH: Membrane MicrodomainsDecoy Receptor 1ApoptosisMESH : Membrane GlycoproteinsReceptors Tumor Necrosis FactorTNF-Related Apoptosis-Inducing LigandMESH : TNF-Related Apoptosis-Inducing LigandJurkat Cells0302 clinical medicineMESH : Tumor Necrosis Factor Decoy ReceptorsMESH: Jurkat CellsDecoy receptorsReceptorCells CulturedMESH : Jurkat CellsMESH : Tumor Necrosis Factor-alpha0303 health sciencesMembrane GlycoproteinsMESH : Protein BindingArticlesMESH : Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsTumor Necrosis Factor Receptor-Associated Peptides and ProteinsCell biology030220 oncology & carcinogenesisCaspasesDeath-inducing signaling complexApoptosis/drug effects; Apoptosis Regulatory Proteins/antagonists & inhibitors; Apoptosis Regulatory Proteins/pharmacology; Caspases/metabolism; Cells Cultured; Death Domain Receptor Signaling Adaptor Proteins; Enzyme Activation/drug effects; GPI-Linked Proteins; HeLa Cells; Humans; Jurkat Cells; Membrane Glycoproteins/antagonists & inhibitors; Membrane Glycoproteins/pharmacology; Membrane Microdomains/drug effects; Protein Binding/drug effects; Receptors TNF-Related Apoptosis-Inducing Ligand; Receptors Tumor Necrosis Factor/metabolism; TNF-Related Apoptosis-Inducing Ligand; Tumor Necrosis Factor Decoy Receptors; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins/metabolism; Tumor Necrosis Factor-alpha/antagonists & inhibitors; Tumor Necrosis Factor-alpha/pharmacologyMESH : Apoptosis Regulatory ProteinsMESH: TNF-Related Apoptosis-Inducing LigandProtein BindingMESH: Cells CulturedDeath Domain Receptor Signaling Adaptor ProteinsMESH: Enzyme ActivationBiologyMESH: Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsGPI-Linked Proteins03 medical and health sciencesMembrane MicrodomainsCell surface receptorMESH : Cells Cultured[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyReceptors Tumor Necrosis Factor Member 10cHumansMESH: Protein Binding[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Receptors TNF-Related Apoptosis-Inducing LigandMESH : Receptors TNF-Related Apoptosis-Inducing LigandMolecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology030304 developmental biologyDeath domainMESH: CaspasesMESH: HumansTumor Necrosis Factor-alphaMESH: Apoptosis Regulatory ProteinsMESH: ApoptosisMESH : HumansCell BiologyMESH: Receptors Tumor Necrosis FactorMESH: Tumor Necrosis Factor Decoy ReceptorsMESH : Receptors Tumor Necrosis FactorEnzyme ActivationMESH: Hela CellsReceptors TNF-Related Apoptosis-Inducing LigandTumor Necrosis Factor Decoy ReceptorsApoptosisMESH: Tumor Necrosis Factor-alphaMESH : Membrane MicrodomainsMESH : CaspasesApoptosis Regulatory ProteinsMESH : Enzyme ActivationMESH : ApoptosisMESH : Death Domain Receptor Signaling Adaptor ProteinsTumor Necrosis Factor Decoy ReceptorsHeLa CellsMESH: Death Domain Receptor Signaling Adaptor Proteins
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