Search results for "Phosphorylation"

showing 10 items of 975 documents

Structure-Activity Relationships and X-ray Structures Describing the Selectivity of Aminopyrazole Inhibitors for c-Jun N-terminal Kinase 3 (JNK3) ove…

2009

c-Jun N-terminal kinase 3alpha1 (JNK3alpha1) is a mitogen-activated protein kinase family member expressed primarily in the brain that phosphorylates protein transcription factors, including c-Jun and activating transcription factor-2 (ATF-2) upon activation by a variety of stress-based stimuli. In this study, we set out to design JNK3-selective inhibitors that had >1000-fold selectivity over p38, another closely related mitogen-activated protein kinase family member. To do this we employed traditional medicinal chemistry principles coupled with structure-based drug design. Inhibitors from the aminopyrazole class, such as SR-3576, were found to be very potent JNK3 inhibitors (IC(50) = 7 nm)…

Models MolecularStereochemistryProtein ConformationPyrazoleCrystallography X-RayBiochemistryp38 Mitogen-Activated Protein Kinaseschemistry.chemical_compoundStructure-Activity RelationshipProtein structureMitogen-Activated Protein Kinase 10Insulin-Secreting CellsStructure–activity relationshipAnimalsHumansEnzyme InhibitorsPhosphorylationProtein kinase AMolecular BiologyCells CulturedIndazolebiologyActivating Transcription Factor 2Active siteCell BiologyActivating transcription factor 2RatschemistryProtein Structure and Foldingbiology.proteinPyrazolesSelectivityJournal of Biological Chemistry
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β2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding

2008

AbstractLeukocyte integrins of the β2 family are essential for immune cell-cell adhesion. In activated cells, β2 integrins are phosphorylated on the cytoplasmic Thr758, leading to 14-3-3 protein recruitment to the β2 integrin. The mutation of this phosphorylation site impairs cell adhesion, actin reorganization, and cell spreading. Thr758 is contained in a Thr triplet of β2 that also mediates binding to filamin. Here, we investigated the binding of filamin, talin, and 14-3-3 proteins to phosphorylated and unphosphorylated β2 integrins by biochemical methods and x-ray crystallography. 14-3-3 proteins bound only to the phosphorylated integrin cytoplasmic peptide, with a high affinity (Kd, 261…

Models MolecularTalinThreonineanimal structuresFilaminsT-LymphocytesStatic ElectricityImmunologyIntegrinCD18macromolecular substancesPlasma protein bindingIn Vitro TechniquesFilaminBiochemistryJurkat Cells03 medical and health sciencesFilamin bindingContractile Proteins0302 clinical medicineCell AdhesionHumansProtein Interaction Domains and MotifsPhosphorylationCell adhesion030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryMicrofilament ProteinsCell BiologyHematologyIntercellular Adhesion Molecule-1Talin bindingRecombinant ProteinsCell biology14-3-3 ProteinsAmino Acid SubstitutionCD18 AntigensMultiprotein Complexes030220 oncology & carcinogenesisbiology.proteinPhosphorylationProtein BindingBlood
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Receptor protein-tyrosine phosphatases: origin of domains (catalytic domain, Ig-related domain, fibronectin type III module) based on the sequence of…

2001

Abstract Reversible tyrosine phosphorylation of proteins is one of the major regulatory physiological events in response to cell-cell- and cell-matrix contact in Metazoa. Previously it was documented that the tyrosine phosphorylating enzymes, the tyrosine kinases (TKs), are autapomorphic characters of Metazoa, including sponges. In this paper the tyrosine dephosphorylating enzymes, the protein-tyrosine phosphatases (PTPs), are studied which can be grouped into two subfamilies, the soluble PTPs and the receptor PTPs (RPTPs). PTPs are characterized by one PTPase domain which interestingly comprises sequence similarity to yeast PTPs. In contrast to the PTPs, the RPTPs – which have been found o…

Molecular Sequence DataImmunoglobulinsBiologyPolymerase Chain ReactionEvolution Molecularchemistry.chemical_compoundCatalytic DomainGene duplicationGeneticsAnimalsAmino Acid SequenceTyrosineCloning MolecularPhylogenychemistry.chemical_classificationPhylogenetic treeSequence Homology Amino AcidTyrosine phosphorylationGeneral MedicineProtein-Tyrosine KinasesAmino acidFibronectinsPoriferaProtein Structure TertiaryOpen reading framechemistryBiochemistryPhosphorylationProtein Tyrosine PhosphatasesTyrosine kinaseSequence AnalysisGene
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Impact of carbon ion irradiation on epidermal growth factor receptor signaling and glioma cell migration in comparison to conventional photon irradia…

2013

PURPOSE: Radiotherapy of malignant gliomas may be limited by an interference of radiation with the migratory potential of tumor cells. Therefore, the influence of conventional photon and modern carbon ion ((12)C) irradiation on glioblastoma cell migration and on epidermal growth factor receptor-related (EGFR) signaling was investigated in vitro. MATERIALS AND METHods: EGFR overexpressing glioblastoma cell lines U87 EGFR++ and LN229 EGFR++ were irradiated with 0, 2 or 6 Gy photons or (12)C heavy ions. Migration was analyzed 24 h after treatment in a standardized Boyden Chamber assay. At different time points EGFR, protein kinase B (PKB/AKT) and extracellular signal-related kinases (ERK1/2) w…

MotilityRadiation DosageCell MovementEpidermal growth factorCell Line TumorGliomamedicineHumansHeavy IonsRadiology Nuclear Medicine and imagingEpidermal growth factor receptorProtein kinase BPhotonsRadiological and Ultrasound TechnologybiologyChemistryKinaseDose-Response Relationship Radiationmedicine.diseaseCarbonErbB ReceptorsCell cultureImmunologyCancer researchbiology.proteinPhosphorylationGlioblastomaSignal TransductionInternational Journal of Radiation Biology
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The phosphorylated pathway of serine biosynthesis is essential both for male gametophyte and embryo development and for root growth in Arabidopsis.

2013

This study characterizes the phosphorylated pathway of Ser biosynthesis (PPSB) in Arabidopsis thaliana by targeting phosphoserine phosphatase (PSP1), the last enzyme of the pathway. Lack of PSP1 activity delayed embryo development, leading to aborted embryos that could be classified as early curled cotyledons. The embryo-lethal phenotype of psp1 mutants could be complemented with PSP1 cDNA under the control of Pro35S (Pro35S:PSP1). However, this construct, which was poorly expressed in the anther tapetum, did not complement mutant fertility. Microspore development in psp1.1/psp1.1 Pro35S:PSP1 arrested at the polarized stage. The tapetum from these lines displayed delayed and irregular devel…

MutantCitric Acid CycleGreen Fluorescent ProteinsImmunoblottingArabidopsisPlant ScienceBiologyPlant RootsSerineMicrosporeMicroscopy Electron TransmissionGene Expression Regulation PlantArabidopsisSerineArabidopsis thalianaAmino AcidsPhosphorylationResearch ArticlesTapetumArabidopsis ProteinsReverse Transcriptase Polymerase Chain ReactionGene Expression Regulation DevelopmentalEmbryoPhosphoserine phosphataseCell Biologybiology.organism_classificationPlants Genetically ModifiedPhosphoric Monoester HydrolasesBiosynthetic PathwaysBiochemistryMicroscopy FluorescenceMutationSeedsPollenGlycolysisThe Plant cell
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Identification of a novel type of ITD mutations located in nonjuxtamembrane domains of the FLT3 tyrosine kinase receptor

2009

Abstract In acute myeloid leukemia (AML), internal tandem duplications (ITDs) of the juxtamembrane (JM) of FLT3 have been shown to play a crucial role in driving proliferation and survival of the leukemic clone. Here, we report the identification of FLT3_ITD mutations located in non-JM domains of the FLT3-receptor. This novel type of FLT3_ITD mutation was found in 216 of 753 (28.7%) of unselected FLT3_ITD-positive AML cases. An FLT3 receptor harbouring a prototypic non-JM ITD (FLT3_ITD627E) mediated constitutive phosphorylation of FLT3 and of STAT5, suggesting that non-JM ITDs confer constitutive activation of the receptor. FLT3_ITD627E induced transformation of hematopoietic 32D cells and …

MutationImmunologyClone (cell biology)MedizinMyeloid leukemiaCell BiologyHematologyBiologymedicine.disease_causeBiochemistryMolecular biologyReceptor tyrosine kinasehemic and lymphatic diseasesTrk receptormedicinebiology.proteinPhosphorylationReceptorSTAT5
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αB-crystallin activation in cardiac muscle by acute exercise mirrors the sHSP kinetic in oxidative skeletal muscle fibers: animal and cellular study

2017

Alpha-B-Crystallin (CRYAB), a Small Heat Shock Protein sensitive to oxidative stress, is implicated in various biological processes in many tissues. In cardiac muscle, CRYAB exerts a cardio protective role in ischemia-induced damage preventing apoptosis and necrosis. We aimed to study αB-crystallin’ response in mouse cardiac tissue (H), at different time of recovery from an acute aerobic exercise (1 hour), correlating its modulation with oxidative stress level. We found that a single bout exercise lead to a specific short-term increase of phospho-αB-crystallin level (pCRYAB), without changes of its total expression. Further, the level of 4-hydroxynonenal, a marker of lipidic peroxidation, h…

MyogenesisCardiac muscleOxidative phosphorylationBiologymedicine.disease_causeBiochemistryCell biologymedicine.anatomical_structureBiochemistryPhysiology (medical)Heat shock proteinmedicineAerobic exerciseMyofibrilC2C12Oxidative stressFree Radical Biology and Medicine
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Synergistic targeting of FLT3 mutations in AML via combined menin-MLL and FLT3 inhibition

2020

Abstract The interaction of menin (MEN1) and MLL (MLL1, KMT2A) is a dependency and provides a potential opportunity for treatment of NPM1-mutant (NPM1mut) and MLL-rearranged (MLL-r) leukemias. Concomitant activating driver mutations in the gene encoding the tyrosine kinase FLT3 occur in both leukemias and are particularly common in the NPM1mut subtype. In this study, transcriptional profiling after pharmacological inhibition of the menin-MLL complex revealed specific changes in gene expression, with downregulation of the MEIS1 transcription factor and its transcriptional target gene FLT3 being the most pronounced. Combining menin-MLL inhibition with specific small-molecule kinase inhibitors…

NPM1Transcription GeneticImmunologyApoptosisBiochemistryMiceRandom AllocationMice Inbred NODCell Line TumorProto-Oncogene Proteinshemic and lymphatic diseasesAntineoplastic Combined Chemotherapy ProtocolsGene expressionmedicineAnimalsHumansMEN1PhosphorylationMyeloid Ecotropic Viral Integration Site 1 ProteinProtein Kinase InhibitorsneoplasmsbiologyGene Expression Regulation LeukemicKinaseNuclear ProteinsMyeloid leukemiaDrug SynergismHistone-Lysine N-MethyltransferaseCell BiologyHematologymedicine.diseaseCoculture TechniquesNeoplasm ProteinsLeukemia Myeloid AcuteLeukemiaKMT2Afms-Like Tyrosine Kinase 3biology.proteinCancer researchNucleophosminProtein Processing Post-TranslationalTyrosine kinaseMyeloid-Lymphoid Leukemia ProteinBlood
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The role of oxidative stress in pro-inflammatory activation of human endothelial cells on Ti6Al4V alloy

2013

Inflammation is an important step in the early phase of tissue regeneration around an implanted metallic orthopaedic device. However, prolonged inflammation, which can be induced by metallic corrosion products, can lead to aseptic loosening and implant failure. Cells in peri-implant tissue as well as metal corrosion can induce reactive oxygen species (ROS) formation, thus contributing to an oxidative microenvironment around an implant. Understanding cellular reactions to implant-induced oxidative stress and inflammatory activation is important to help prevent an adverse response to metallic materials. In an earlier study we have shown that endothelial cells grown on Ti6Al4V alloy are subjec…

NecrosisMaterials scienceBiophysicsEnzyme-Linked Immunosorbent AssayBioengineeringInflammationOxidative phosphorylationmedicine.disease_causeAntioxidantsCell LineBiomaterialsTissue cultureAlloysmedicineHumansTitaniumchemistry.chemical_classificationReactive oxygen speciesReverse Transcriptase Polymerase Chain ReactionTumor Necrosis Factor-alphaInterleukin-8Endothelial CellsIntercellular Adhesion Molecule-1Cell biologyEndothelial stem cellOxidative StresschemistryMechanics of MaterialsCell cultureImmunologyCeramics and Compositesmedicine.symptomReactive Oxygen SpeciesOxidative stressBiomaterials
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O-glycosylation of the tail domain of neurofilament protein M in human neurons and in spinal cord tissue of a rat model of amyotrophic lateral sclero…

2005

Mammalian neurofilaments (NFs) are modified by post-translational modifications that are thought to regulate NF assembly and organization. Whereas phosphorylation has been intensely studied, the role of another common modification, the attachment of O-linked N-acetylglucosamine (GlcNAc) to individual serine and threonine residues, is hardly understood. We generated a novel monoclonal antibody that specifically recognizes an O-glycosylated epitope in the tail domain of NF-M and allows determination of the glycosylation state at this residue. The antibody displays strong species preference for human NF-M, shows some reactivity with rat but not with mouse or bovine NF-M. By immunohistochemistr…

NeurofilamentGlycosylationGlycosylationMolecular Sequence DataHyperphosphorylationBiologyMitogen-activated protein kinase kinaseBiochemistryAnimals Genetically Modifiedchemistry.chemical_compoundEpitopesMiceWestern blotNeurofilament ProteinsCell Line TumorAcetylglucosaminidasemedicineAnimalsHumansAmino Acid SequenceProtein kinase AMolecular BiologyMitogen-Activated Protein Kinase KinasesNeuronsmedicine.diagnostic_testKinaseAmyotrophic Lateral SclerosisAntibodies MonoclonalCell BiologyAxonsCell biologyProtein Structure TertiaryRatsDisease Models AnimalchemistryBiochemistrySpinal CordNIH 3T3 CellsPhosphorylationCattleThe Journal of biological chemistry
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