Search results for " TYR"

showing 10 items of 362 documents

Do too many choices have negative consequences? An empirical review

2013

Various experiments demonstrated that having too much choice has negative consequences on the motivation to choose and on the satisfaction with the chosen option. However, the literature reports conflicting results showing that choosing from large assortments has advantages. This paper reviews the main empirical results in favor and against the negative effect of too much choice and identifies possible directions for further research. Copyright © 2013 by Società editrice il Mulino.

Choice overloadDecision complexityDecision complexity choice overload tyranny of choice too-much-choice effect consumer hyperchoiceConsumer hyperchoiceTyranny of choiceToo-much-choice effect
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Receptor Tyrosine Kinase, an Autapomorphic Character of Metazoa: Identification in Marine Sponges

1999

In the present review we summarize sequence data obtained from cloning of sponge receptor tyrosine kinases [RTK]. The cDNA sequences were mainly obtained from the marine sponge Geodia cydonium. RTKs (i) with immunoglobulin [Ig]-like domains in the extracellular region, (ii) of the type of insulinlike receptors, as well as (iii) RTKs with one extracellular speract domain, have been identified. The analyses revealed that the RTK genes are constructed in blocks [domains], suggesting a blockwise evolution. The phylogenetic relationships of the sequences obtained revealed that all sponge sequences fall into one branch of the evolutionary tree, while related sequences from higher Metazoa, human, …

CloningbiologyPhylogenetic treeEcologyPhylumbiology.organism_classificationGeneral Biochemistry Genetics and Molecular BiologyReceptor tyrosine kinaseSpongeMonophylyNeurologyEvolutionary biologyComplementary DNAbiology.proteinGeneGeneral Environmental ScienceActa Biologica Hungarica
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Genome-Wide Association Study of Diabetic Kidney Disease Highlights Biology Involved in Glomerular Basement Membrane Collagen

2019

BACKGROUND: Although diabetic kidney disease demonstrates both familial clustering and single nucleotide polymorphism heritability, the specific genetic factors influencing risk remain largely unknown.METHODS: To identify genetic variants predisposing to diabetic kidney disease, we performed genome-wide association study (GWAS) analyses. Through collaboration with the Diabetes Nephropathy Collaborative Research Initiative, we assembled a large collection of type 1 diabetes cohorts with harmonized diabetic kidney disease phenotypes. We used a spectrum of ten diabetic kidney disease definitions based on albuminuria and renal function.RESULTS: Our GWAS meta-analysis included association result…

Collagen Type IVMale0301 basic medicineEXPRESSIONNEPHROPATHY030232 urology & nephrologyPROTEINGenome-wide association studyRECEPTOR TYROSINE KINASESBiologySUSCEPTIBILITYBioinformaticsurologic and male genital diseasesAutoantigensNephropathyEnd stage renal diseaseCohort StudiesDiabetic nephropathy03 medical and health sciences0302 clinical medicineSDG 3 - Good Health and Well-beingDiabetes mellitusGlomerular Basement MembranemedicineHumansDiabetic NephropathiesAlport syndromeLetter to the EditorCOMPLICATIONSNITRIC-OXIDEMUTATIONS1184 Genetics developmental biology physiologyGeneral Medicinemedicine.diseaseGENE3. Good healthDiabetes Mellitus Type 1030104 developmental biologyNephrology3121 General medicine internal medicine and other clinical medicineMutationAlbuminuria/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingFemale3111 Biomedicinemedicine.symptomCOLLECTIN 11 CL-11Genome-Wide Association StudyKidney disease
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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity …

1999

ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathione S-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLDeltaKIM mutant was impaired. The in vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2.P…

Cytoplasmanimal structuresProtein Kinase C-alphaRecombinant Fusion ProteinsCèl·lulesNerve Tissue ProteinsProtein tyrosine phosphataseMitogen-activated protein kinase kinaseTransfectionenvironment and public healthBiochemistrySH3 domainReceptor tyrosine kinaseMAP2K7Substrate SpecificitySerineAnimalsc-RafAmino Acid SequenceMolecular BiologyProtein Kinase CSequence DeletionMitogen-Activated Protein Kinase 1Binding SitesMitogen-Activated Protein Kinase 3biologyCyclin-dependent kinase 2Intracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyCyclic AMP-Dependent Protein KinasesIsoenzymesenzymes and coenzymes (carbohydrates)KineticsBiochemistryAmino Acid SubstitutionCOS CellsCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedCyclin-dependent kinase 9CattleMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesProteïnes
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A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase

1999

Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal–regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit …

Cytoplasmanimal structuresRecombinant Fusion ProteinsCèl·lulesAmino Acid MotifsNerve Tissue ProteinsProtein tyrosine phosphataseSH2 domainTransfectionenvironment and public healthModels Biologicalp38 Mitogen-Activated Protein KinasesReceptor tyrosine kinaseSH3 domainCell LinePhosphoserinetyrosine phosphatasesAnimalsHumansProtein phosphorylationPKAReceptor-Like Protein Tyrosine Phosphatases Class 7PhosphorylationPTP-SLCell NucleusMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyBrief ReportIntracellular Signaling Peptides and ProteinsBiological TransportCell BiologyProtein Tyrosine Phosphatases Non-ReceptorCyclic AMP-Dependent Protein KinasesEnzyme Activationenzymes and coenzymes (carbohydrates)MAP kinasesBiochemistryMitogen-activated protein kinaseCOS CellsMutationbiology.proteinPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesEnzimssignal transductionProto-oncogene tyrosine-protein kinase Src
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RNA Transfer by Electroporation into Mature Dendritic Cells Leading to Reactivation of Effector-Memory Cytotoxic T Lymphocytes: A Quantitative Analys…

2005

Previous studies have analyzed transfer of RNA-encoded tumor-associated antigens (TAAs) into immature dendritic cells (DCs) because of their exceptional ability to internalize antigens. Concerns have been raised regarding the use of immature DCs in clinical studies because of their capacity to tolerize T cells. Therefore, we focused on optimizing RNA transfer into mature DCs using the method of electroporation and obtained high protein expression in 90% of mature DCs. Particular emphasis was placed on quantifying RNA transfer. Reconstitution of peptide-MHC (pMHC) ligands on RNA-pulsed DCs was measured with the help of effector-memory cytotoxic T lymphocytes (CTLs) specific for the melanoma-…

Cytotoxicity Immunologicchemical and pharmacologic phenomenaBiologyLymphocyte ActivationTransfectionEpitopeAntigenCell Line TumorDrug DiscoveryGeneticsHumansCytotoxic T cellMelanomaMolecular BiologyPharmacologyEffectorElectroporationRNAhemic and immune systemsDendritic CellsTransfectionMolecular biologyElectroporationPhenotypedendritic cells; RNA transfection; electroporation; effector-memory cytotoxic T lymphocytes; peptide-MHC ligands; tumor immunotherapy; melanoma; tyrosinase; CDK4; EGFPRNAMolecular MedicineImmunotherapyRNA transfectionT-Lymphocytes CytotoxicMolecular Therapy
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Increased Expression of Integrin and Receptor Tyrosine Kinase Genes During Autograft Fusion in the SpongeGeodia cydonium

1999

Recently cDNAs coding for cell surface molecules have been isolated from sponges. The molecules for alpha-integrin, galectin, and receptor tyrosine kinase (RTK), obtained from the marine sponge, Geodia cydonium, have been described earlier. In the present study also the cDNA for one putative beta-integrin has been identified from G. cydonium. The deduced aa sequence comprises the characteristic signatures, found in other metazoan beta-integrin molecules; the estimated size is 95,215 Da. To obtain first insights into the molecular events which proceed during autograft fusion, the expressions of these genes were determined on transcriptional and translational level. The cDNAs as well as antib…

DNA ComplementaryMolecular Sequence DataIntegrinGene ExpressionReceptor tyrosine kinaselaw.inventionlawTranscription (biology)Complementary DNAAnimalsHumansAmino Acid SequenceNorthern blotCloning MolecularGenePhylogenyGalectinBase SequenceSequence Homology Amino AcidStaining and LabelingbiologyIntegrin beta1Receptor Protein-Tyrosine KinasesGeneral MedicineMolecular biologyPoriferabiology.proteinRecombinant DNACell Adhesion and Communication
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Experimental indication in favor of the introns-late theory: the receptor tyrosine kinase gene from the sponge Geodia cydonium.

1997

Abstract We have analyzed the gene that encodes receptor tyrosine kinase (RTK) from the marine sponge Geodia cydonium, which belongs to the most ancient and simple metazoan groups, the Porifera. RTKs are enzymes found only in metazoa. The sponge gene contains two introns in the extracellular part of the protein. However, the rest of the protein (transmembrane and intracellular part), including the tyrosine kinase (TK)-domain, is encoded by a single exon. In contrast, all TK genes, so far known only from higher animals (vertebrates), contain several introns especially in the TK-domain. The TK-domain of G. cydonium shows similarity with numerous members of receptor as well as nonreceptor TKs.…

DNA ComplementaryMolecular Sequence DataReceptor tyrosine kinaseCatalysisExonSequence Homology Nucleic AcidGeneticsAnimalsHumansReceptor Tyrosine Kinase GeneAmino Acid SequenceCloning MolecularIntrons; Evolution; Tyrosine kinases; SpongesMolecular BiologyIntracellular partGeneEcology Evolution Behavior and SystematicsPhylogenyGeneticsbiologyPhylogenetic treeBase SequenceSequence Homology Amino AcidIntronReceptor Protein-Tyrosine KinasesIntronsPoriferaBiochemistrybiology.proteinTyrosine kinaseJournal of molecular evolution
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Molecular cloning of a tyrosine kinase gene from the marine spongeGeodia cydonium: a new member belonging to the receptor tyrosine kinase class II fa…

1994

We have isolated and characterized a cDNA from the marine sponge Geodia cydonium coding for a new member of the tyrosine protein kinase (TK) family. The cDNA encodes a protein of M(r) = 68,710, termed GCTK, which is homologous to class II receptor tyrosine kinases (RTKs). GCTK contains conserved amino acids (aa) characteristic of all protein kinases, and the sequences DLATRN and PIRWMATE which are highly specific for TKs. Furthermore, the sequence N-L-Y-x(3)-Y-Y-R is highly homologous to the sequence D-[LIV]-Y-x(3)-Y-Y-R found only in class II RTKs. The sponge TK, when compared with mammalian class II RTKs, shows maximum 31% homology in the TK domain indicating that this the oldest member o…

DNA ComplementaryMolecular Sequence DataReceptor tyrosine kinaseSH3 domainCytosolAnimalsGeodiaAmino Acid SequenceRNA MessengerCloning MolecularKinase activityTyrosineProtein kinase AMolecular BiologyBase SequenceSequence Homology Amino AcidbiologyCell MembraneReceptor Protein-Tyrosine KinasesCell BiologyProtein-Tyrosine Kinasesbiology.organism_classificationBiological EvolutionMolecular biologyPoriferaMolecular WeightBiochemistryROR1biology.proteinTyrosine kinaseMolecular Membrane Biology
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Cloning and expression of new receptors belonging to the immunoglobulin superfamily from the marine sponge Geodia cydonium

1999

A cDNA encoding a receptor tyrosine kinase (RTK) was previously cloned and expressed from the marine sponge (Porifera) Geodia cydonium. In addition to the two intracellular regions characteristic for RTKs, two immunoglobulin (Ig)-like domains are found in the extracellular part of the sponge RTK. In the present study it is shown that no further Ig-like domain is present in the upstream region of the cDNA as well as of the gene hitherto known from the sponge RTK. Two different full-length cDNAs have been isolated and characterized in the present study, which possess two Ig-like domains, one transmembrane segment, and only a short intracellular part, without a TK domain. The two deduced polyp…

DNA ComplementaryTranscription GeneticMolecular Sequence DataImmunologyImmunoglobulinsBiologyReceptor tyrosine kinaseComplementary DNAGeneticsAnimalsHumansAmino Acid SequenceNorthern blotReceptors ImmunologicPeptide Chain Initiation TranslationalIntracellular partPolymorphism GeneticBase SequenceReceptor Protein-Tyrosine KinasesBlotting NorthernImmunohistochemistryMolecular biologyPoriferaProtein Structure TertiaryTransplantationOpen reading frameTransmembrane domainbiology.proteinImmunoglobulin superfamilyCell Adhesion MoleculesImmunogenetics
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