Search results for " tyrosine"

showing 10 items of 256 documents

Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia

2019

Mitral valve diseases affect approximately 3% of the population and are the most common reasons for valvular surgery because no drug-based treatments exist. Inheritable genetic mutations have now been established as the cause of mitral valve insufficiency, and four different missense mutations in the filamin A gene (FLNA) have been found in patients suffering from non-syndromic mitral valve dysplasia (MVD). The FLNA protein is expressed, in particular, in endocardial endothelia during fetal valve morphogenesis and is key in cardiac development. The FLNA-MVD causing mutations are clustered in the N-terminal region of FLNA. How the mutations in FLNA modify its structure and function, have mos…

Protein FoldingdysplasiatFilamins[SDV]Life Sciences [q-bio]PopulationProtein Tyrosine Phosphatase Non-Receptor Type 12BiophysicsMutation Missensesynnynnäiset sydänviatProtein tyrosine phosphataseBiologyMolecular Dynamics Simulationmedicine.disease_causeFilamin03 medical and health sciences0302 clinical medicinemitral valve dysplasiaMitral valvemedicineFLNAMissense mutationHumanseducationGene030304 developmental biologyGenetics0303 health sciencesMutationeducation.field_of_studyBinding SitesMitral Valve Prolapsecritical structural defectshiippaläppäfilamiinitArticles3. Good healthmedicine.anatomical_structurecardiovascular systemfilamin A mutationsgeneettiset tekijätmutaatiot030217 neurology & neurosurgeryProtein Binding
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Different protein turnover of interleukin-6-type cytokine signalling components.

1999

Interleukin (IL)-6 and IL-6-type cytokines signal through the gp130/Jak/STAT signal transduction pathway. The key components involved are the signal transducing receptor subunit gp130, the Janus kinases Jak1, Jak2 and Tyk2, STAT1 and STAT3 of the family of signal transducers and activators of transcription, the protein tyrosine phosphatase SHP2 and the suppressors of cytokine signalling SOCS1, SOCS2 and SOCS3. Whereas considerable information has been accumulated concerning the time-course of activation for the individual signalling molecules, data on the availability of the proteins involved in IL-6-type cytokine signal transduction are scarce. Nevertheless, availability of these molecules…

Protein Tyrosine Phosphatase Non-Receptor Type 11Protein tyrosine phosphataseBiologyBiochemistrySuppressor of cytokine signallingAntigens CDCytokine Receptor gp130Membrane GlycoproteinsSuppressor of cytokine signaling 1Interleukin-6Protein Tyrosine Phosphatase Non-Receptor Type 6Intracellular Signaling Peptides and ProteinsJAK-STAT signaling pathwaySignal transducing adaptor proteinSTAT2 Transcription FactorProtein-Tyrosine KinasesGlycoprotein 130Recombinant ProteinsCell biologyDNA-Binding ProteinsSTAT1 Transcription FactorBiochemistryTrans-ActivatorsCytokinesSignal transductionProtein Tyrosine PhosphatasesJanus kinaseHalf-LifeSignal TransductionEuropean journal of biochemistry
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In Situ Detection of Phosphorylated Platelet-derived Growth Factor Receptor β Using a Generalized Proximity Ligation Method

2007

Improved methods are needed for in situ characterization of post-translational modifications in cell lines and tissues. For example, it is desirable to monitor the phosphorylation status of individual receptor tyrosine kinases in samples from human tumors treated with inhibitors to evaluate therapeutic responses. Unfortunately the leading methods for observing the dynamics of tissue post-translational modifications in situ, immunohistochemistry and immunofluorescence, exhibit limited sensitivity and selectivity. Proximity ligation assay is a novel method that offers improved selectivity through the requirement of dual recognition and increased sensitivity by including DNA amplification as a…

ProteomicsImmunoglobulinsProximity ligation assayKidneyBiochemistryReceptor tyrosine kinaseCell LineAnalytical ChemistryReceptor Platelet-Derived Growth Factor betaGrowth factor receptorPlatelet-Derived Growth Factor Receptor BetaHumansPhosphorylationMolecular BiologyWound HealingbiologyEndothelial CellsTransfectionFibroblastsImmunohistochemistryPrimary and secondary antibodiesMolecular biologyActinsCell culturebiology.proteinTyrosinePhosphorylationProtein Processing Post-TranslationalSignal TransductionMolecular & Cellular Proteomics
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Entrectinib: a potent new TRK, ROS1, and ALK inhibitor

2015

Abstract: Introduction: Receptor tyrosine kinases (RTKs) and their signaling pathways, control normal cellular processes; however, their deregulation play important roles in malignant transformation. In advanced non-small cell lung cancer (NSCLC), the recognition of oncogenic activation of specific RTKs, has led to the development of molecularly targeted agents that only benefit roughly 20% of patients. Entrectinib is a pan-TRK, ROS1 and ALK inhibitor that has shown potent anti-neoplastic activity and tolerability in various neoplastic conditions, particularly NSCLC. Areas covered: This review outlines the pharmacokinetics, pharmacodynamics, mechanism of action, safety, tolerability, pre-cl…

Receptor Protein-Tyrosine KinasesEntrectinibNTRK1NTRK2NTRK3Receptor tyrosine kinaseEntrectinibMalignant transformationAntineoplastic AgentNeoplasmsProtein-Tyrosine KinaseALK; colorectal cancer; Entrectinib; non-small cell lung cancer; NTRK1; NTRK2; NTRK3; precision medicine; ROS1; salivary gland cancer; TrkA; TrkB; TrkC; Animals; Antineoplastic Agents; Benzamides; Humans; Indazoles; Neoplasms; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Receptor Protein-Tyrosine Kinases; Receptor; trkA; Receptor; trkB; Receptor; trkC; Pharmacology; Pharmacology (medical)Anaplastic Lymphoma KinasePharmacology (medical)salivary gland cancerProto-Oncogene ProteinbiologyTrkAPharmacology. TherapyTrkCTrkBGeneral MedicineProtein-Tyrosine KinasesReceptor Protein-Tyrosine KinaseBenzamidesmedicine.symptomROS1ReceptorHumanIndazolesmedicine.drug_classprecision medicineAntineoplastic Agentscolorectal cancerBenzamideProto-Oncogene ProteinsmedicineROS1AnimalsHumansReceptor trkBReceptor trkCReceptor trkAnon-small cell lung cancerPharmacologyAnimalReceptor Protein-Tyrosine KinasesALK inhibitorIndazoleMechanism of actionALKTrk receptorbiology.proteinCancer researchNeoplasmALK; colorectal cancer; Entrectinib; non-small cell lung cancer; NTRK1; NTRK2; NTRK3; precision medicine; ROS1; salivary gland cancer; TrkA; TrkB; TrkC; Animals; Antineoplastic Agents; Benzamides; Humans; Indazoles; Neoplasms; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Receptor Protein-Tyrosine Kinases; Receptor trkA; Receptor trkB; Receptor trkC; Pharmacology; Pharmacology (medical)Expert Opinion on Investigational Drugs
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Antagonistic feedback loops involving Rau and Sprouty in the Drosophila eye control neuronal and glial differentiation.

2013

During development, differentiation is often initiated by the activation of different receptor tyrosine kinases (RTKs), which results in the tightly regulated activation of cytoplasmic signaling cascades. In the differentiation of neurons and glia in the developing Drosophila eye, we found that the proper intensity of RTK signaling downstream of fibroblast growth factor receptor (FGFR) or epidermal growth factor receptor required two mutually antagonistic feedback loops. We identified a positive feedback loop mediated by the Ras association (RA) domain-containing protein Rau that sustained Ras activity and counteracted the negative feedback loop mediated by Sprouty. Rau has two RA domains t…

Receptors SteroidGTP'Blotting WesternIn situ hybridizationEyeBiochemistryReceptor tyrosine kinaseMicroscopy Electron TransmissionAnimalsDrosophila ProteinsEpidermal growth factor receptorReceptorMolecular BiologyTranscription factorIn Situ HybridizationFeedback PhysiologicalbiologyIntracellular Signaling Peptides and ProteinsMembrane ProteinsReceptor Protein-Tyrosine KinasesCell DifferentiationCell BiologyAnatomyPhenotypeImmunohistochemistryCell biologyProtein Structure TertiaryDNA-Binding ProteinsEnzyme ActivationCOUP Transcription FactorsGene Expression RegulationFibroblast growth factor receptorbiology.proteinDrosophilaNeurogliaProtein BindingSignal TransductionScience signaling
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Role of PTPRJ genotype in papillary thyroid carcinoma risk

2010

The strong genetic predisposition to papillary thyroid carcinoma (PTC) might be due to a combination of low-penetrance susceptibility variants. Thus, the research into gene variants involved in the increase of susceptibility to PTC is a relevant field of investigation. The gene coding for the receptor-type tyrosine phosphatase PTPRJ has been proposed as a cancer susceptibility gene, and its role as a tumor suppressor gene is well established in thyroid carcinogenesis. In this study, we want to ascertain the role of PTPRJ genotype in the risk for PTC. We performed a case–control study in which we determined the PTPRJ genotype for the non-synonymous Gln276Pro and Asp872Glu polymorphisms by PC…

RiskOncologyCancer Researchmedicine.medical_specialtyGenotypeendocrine system diseasesEndocrinology Diabetes and MetabolismBiologyPolymerase Chain ReactionArticleSettore MED/13 - EndocrinologiaThyroid carcinomaEndocrinologyGene FrequencyInternal medicineGenotypeOdds RatiomedicineGenetic predispositionHumansGenetic Predisposition to DiseaseThyroid NeoplasmsAlleleAllele frequencyAllelesGenetic Association StudiesPapillay thyroid carcinomaGeneticsChi-Square DistributionPolymorphism GeneticReceptor-Like Protein Tyrosine Phosphatases Class 3ThyroidCase-control studyCarcinoma PapillaryGenotype frequencymedicine.anatomical_structureOncologyCase-Control Studies
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The nucleotide and partial amino acid sequences of rat fetuin. Identity with the natural tyrosine kinase inhibitor of the rat insulin receptor.

1992

Fetuins are among the major plasma proteins, yet their biological role has remained elusive. Here we report the molecular cloning of rat fetuin and the sequence analysis of a full-length clone, RF619 of 1456 bp with an open reading frame of 1056 bp encoding 352 amino acid residues. The coding part of RF619 was identical with the cDNA sequence of the natural inhibitor of the insulin receptor tyrosine kinase from rat (pp63) except for four substitutions and a single base insertion causing divergence of the predicted protein sequences. Partial amino acid sequences of rat plasma fetuin were in agreement with the predictions based on the RF619 cDNA. Purified rat fetuin inhibited the insulin rece…

Sequence analysisMolecular Sequence DataBiochemistryTropomyosin receptor kinase CReceptor tyrosine kinaseSubstrate SpecificityComplementary DNASequence Homology Nucleic AcidAnimalsAmino Acid SequencePhosphorylationchemistry.chemical_classificationbiologyBase SequenceDNAProtein-Tyrosine KinasesFetuinMolecular biologyReceptor InsulinAmino acidRatsInsulin receptorBiochemistrychemistryROR1biology.proteinalpha-FetoproteinsEuropean journal of biochemistry
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Molecular mechanism of T-cell protein tyrosine phosphatase (TCPTP) activation by mitoxantrone.

2013

T-cell protein tyrosine phosphatase (TCPTP) is a ubiquitously expressed non-receptor protein tyrosine phosphatase. It is involved in the negative regulation of many cellular signaling pathways. Thus, activation of TCPTP could have important therapeutic applications in diseases such as cancer and inflammation. We have previously shown that the α-cytoplasmic tail of integrin α1β1 directly binds and activates TCPTP. In addition, we have identified in a large-scale high-throughput screen six small molecules that activate TCPTP. These small molecule activators include mitoxantrone and spermidine. In this study, we have investigated the molecular mechanism behind agonist-induced TCPTP activation.…

SpermidineProtein tyrosine phosphataseBiochemistryAnalytical Chemistry0302 clinical medicinePhosphorylationDatabases Protein0303 health sciencesProtein Tyrosine Phosphatase Non-Receptor Type 2biologyChemistrySmall molecule3. Good healthCell biologyisothermal titration calorimetryMolecular Docking Simulationmolecular dynamics simulation030220 oncology & carcinogenesis/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingThermodynamicsHydrophobic and Hydrophilic InteractionsProtein BindingSignal TransductionCell signalingintegrinIntegrinPhosphataseStatic ElectricityBiophysicsAntineoplastic AgentsMolecular Dynamics Simulationta3111mitoxantroneIntegrin alpha1beta1Small Molecule Libraries03 medical and health sciencesSDG 3 - Good Health and Well-beingdifferential scanning fluorimetryHumansBinding siteMolecular Biology030304 developmental biologyT-cell protein tyrosine phosphataseta1182ta3122In vitroProtein Structure TertiaryKineticsCytoplasmbiology.proteinMitoxantronePeptidesBiochimica et Biophysica Acta: Proteins and Proteomics
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Antineoplastic Drug-Induced Cardiotoxicity: A Redox Perspective

2018

Antineoplastic drugs can be associated with several side effects, including cardiovascular toxicity (CTX). Biochemical studies have identified multiple mechanisms of CTX. Chemoterapeutic agents can alter redox homeostasis by increasing the production of reactive oxygen species (ROS) and reactive nitrogen species RNS. Cellular sources of ROS/RNS are cardiomyocytes, endothelial cells, stromal and inflammatory cells in the heart. Mitochondria, peroxisomes and other subcellular components are central hubs that control redox homeostasis. Mitochondria are central targets for antineoplastic drug-induced CTX. Understanding the mechanisms of CTX is fundamental for effective cardioprotection, without…

Stromal cellPhysiologymedicine.medical_treatmentTyrosine kinase inhibitorChemotherapy; HER-2 inhibitors; Oxidative/nitrosative stress; Tyrosine kinase inhibitors; Vascular endothelial growth factorReviewOxidative phosphorylation030204 cardiovascular system & hematologyMitochondrionPharmacologyChemotherapy; HER-2 inhibitors; Oxidative/nitrosative stress; Tyrosine kinase inhibitors; Vascular endothelial growth factor; Physiology; Physiology (medical)chemotherapyHER-2 inhibitorlcsh:Physiology03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePhysiology (medical)tyrosine kinase inhibitorsMedicinechemotherapy HER-2 inhibitors oxidative/nitrosative stress vascular endothelial growth factor tyrosine kinase inhibitorsReactive nitrogen specieschemistry.chemical_classificationCardioprotectionReactive oxygen speciesChemotherapyCardiotoxicitylcsh:QP1-981vascular endothelial growth factorbusiness.industryOxidative/nitrosative strechemistry030220 oncology & carcinogenesisbusinessHER-2 inhibitorsoxidative/nitrosative stress
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Interplay of three G‑quadruplex units in the KIT promoter

2019

The proto-oncogene KIT encodes for a tyrosine kinase receptor, which is a clinically validated target for treating gastrointestinal stromal tumors. The KIT promoter contains a G-rich domain within a relatively long sequence potentially able to form three adjacent G-quadruplex (G4) units, namely, K2, SP, and K1. These G4 domains have been studied mainly as single quadruplex units derived from short truncated sequences and are currently considered promising targets for anticancer drugs, alternatively to the encoded protein. Nevertheless, the information reported so far does not contemplate the interplay between those neighboring G4s in the context of the whole promoter, possibly thwarting dru…

Stromal cellbiologyChemistryGeneral ChemistryG-quadruplexBiochemistryMolecular biologyProto-Oncogene MasCatalysisReceptor tyrosine kinaseG‐Quadruplex Multiple G4 cancerG-QuadruplexesProto-Oncogene Proteins c-kitColloid and Surface ChemistrySettore CHIM/03 - Chimica Generale E Inorganicabiology.proteinHumansPromoter Regions GeneticGene
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