Search results for "Phosphopeptides"

showing 8 items of 8 documents

X!TandemPipeline: a tool to manage sequence redundancy for protein inference and phosphosite identification

2017

X!TandemPipeline is a software designed to perform protein inference and to manage redundancy in the results of phosphosite identification by database search. It provides the minimal list of proteins or phosphosites that are present in a set of samples using grouping algorithms based on the principle of parsimony. Regarding proteins, a two-level classification is performed, where groups gather proteins sharing at least one peptide and subgroups gather proteins that are not distinguishable according to the identified peptides. Regarding phosphosites, an innovative approach based on the concept of phosphoisland is used to gather overlapping phosphopeptides. The graphical interface of X!Tandem…

0106 biological sciences0301 basic medicinePhosphopeptidesProteomicsphosphopeptideComputer sciencecomputer.internet_protocolcomputer.software_genre01 natural sciencesBiochemistrydatabase search03 medical and health sciencesSearch engineUser-Computer InterfaceRedundancy (information theory)SoftwareTandem Mass Spectrometry[ INFO.INFO-BI ] Computer Science [cs]/Bioinformatics [q-bio.QM]HumansDatabase search engineAmino Acid SequenceDatabases ProteinGraphical user interfacemass spectrometrybusiness.industrysoftwareprotein inferenceProteinsGeneral ChemistrybioinformaticsSearch EngineBenchmarking030104 developmental biologyComputingMethodologies_PATTERNRECOGNITIONProtein inferenceData mining[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]businesscomputerXMLAlgorithms010606 plant biology & botany
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Metabolic Evaluation of 94 Patients 5 to 16 Years After Ileocecal Pouch (Mainz Pouch 1) Continent Urinary Diversion

2003

PURPOSE In continent urinary diversion metabolic disturbances may be encountered in long-term followup. We evaluated metabolic consequences in patients with a minimum followup of 5 years after Mainz pouch 1 urinary diversion.At our institution continent urinary diversion using the ileocecal segment was performed between 1983 and 1995 in 458 patients. A total of 94 patients with an ileocecal pouch for a minimum of 5 years were reevaluated for metabolic changes. Median followup was 9.0 years. Routine laboratory parameters, blood gas analysis, vitamin B12, vitamin D25, cross-laps, bone specific alkaline phosphatase, osteocalcin and propeptide of type I collagen were obtained. Bone density was …

AdultMalePhosphopeptidesmedicine.medical_specialtyBone diseaseBone densityUrologymedicine.medical_treatmentUrinary systemOsteocalcinOsteoporosisSodium CitratePostoperative ComplicationsCalcitriolBone DensityReference ValuesPotassium CitrateHumansMedicineCitratesMegaloblastic anemiaAgedbusiness.industryUrinary Reservoirs ContinentUrinary diversionMiddle AgedAlkaline Phosphatasemedicine.diseaseSurgeryVitamin B 12FemaleCollagenBlood Gas AnalysisPouchAcidosisEnergy MetabolismbusinessContinent Urinary DiversionProcollagenFollow-Up StudiesJournal of Urology
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Association between biomarkers of inflammation and left ventricular hypertrophy in moderate chronic kidney disease.

2007

Aims: Left ventricular hyper- trophy (LVH) is a predictor for cardiovascu- lar mortality, and it is considered to be a surro- gate marker of preclinical cardiovascular dis- ease. This study aimed at evaluating whether fetuin-A plasma levels are decreased in pa- tients with moderate chronic kidney disease (CKD) and their linkage to plasma concentra- tions of hs-C-reactive protein (CRP), cardio- trophyn-1 (CT-1), tumor necrosis factor- (TNF-), propeptide of collagen Type I (PIP) and to LVH. Material and methods: We enrolled 64 moderate CKD and 55 essential hypertensives (EH) with normal renal func- tion as controls. All the patients underwent an echocardiographic examination; plasma sam- ples…

NephrologyAdultMalePhosphopeptidesmedicine.medical_specialtyInflammationEnzyme-Linked Immunosorbent AssayLeft ventricular hypertrophyMuscle hypertrophyinflammation left ventricular hypertrophy chronic kidney diseaseStatistical significanceInternal medicineMedicineHumansMass indexcardiovascular diseasesInflammationAnalysis of Variancebusiness.industryTumor Necrosis Factor-alphaCase-control studyGeneral MedicineMiddle Agedmedicine.diseaseEndocrinologyC-Reactive ProteinNephrologyEchocardiographyCase-Control StudiesCardiologyCytokinesKidney Failure ChronicRegression AnalysisFemaleHypertrophy Left Ventricularalpha-Fetoproteinsmedicine.symptombusinessBiomarkersProcollagenKidney diseaseClinical nephrology
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Phosphorylation of GAP-43 (growth-associated protein of 43 kDa) by conventional, novel and atypical isotypes of the protein kinase C gene family: dif…

1996

GAP-43 (growth-associated protein of 43 kDa; also known as neuromodulin, P-57, B-50 and F-1) is a neuronal calmodulin binding protein and a major protein kinase C (PKC) substrate in mammalian brain. Here we describe the phosphorylation by and the site specificity of different PKC isotypes. The conventional PKC beta 1 and the novel PKCs delta and epsilon effectively phosphorylated recombinant GAP-43 in vitro; atypical PKC zeta did not. The K(m) values (between 0.6 and 2.3 microM) were very low, demonstrating a high-affinity interaction between kinase and substrate. All PKC isotypes were shown to phosphorylate serine-41 in GAP-43. When using a 19-amino-acid oligopeptide based on the GAP-43 ph…

PhosphopeptidesCalmodulinMolecular Sequence DataNerve Tissue ProteinsPeptidePeptide MappingBiochemistrySubstrate SpecificityGAP-43 ProteinAmino Acid SequencePhosphorylationGap-43 proteinMolecular BiologyProtein Kinase CProtein kinase Cchemistry.chemical_classificationOligopeptideMembrane GlycoproteinsbiologyKinaseBinding proteinCell BiologyMolecular biologyRecombinant ProteinsIsoenzymesKineticsBiochemistrychemistryMultigene Familybiology.proteinPhosphorylationPeptidesOligopeptidesResearch ArticleBiochemical Journal
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Effect of Caseinophosphopeptides from αs- and β-Casein on Iron Bioavailability in HuH7 Cells

2015

International audience; Two pools of caseinophosphopeptides (CPPs) obtained from αs- and β-casein fractions (α-CPPs and β-CPPs) were characterized. A total of 16 CPPs were identified in the α-CPPs pool, 9 of them derived from αs1-casein and 7 from αs2-casein. A total of 18 CPPs were identified in the β-CPPs pool. Four of the identified CPPs contained the characteristic phosphoseryl-glutamic acid cluster SpSpSpEE. Calcein assay was used to compare the iron-binding capacity of the α- and β-CPPs pools. At the concentration of 12.5 μM CPPs used in the iron bioavailability assays, β-CPPs pools show greater iron-binding capacity than α-CPPs pools. HuH7 human hepatoma cells show many differentiate…

PhosphopeptidesIronBiological AvailabilitydigestionModels BiologicalMass Spectrometryproduit laitierchemistry.chemical_compoundcaséinophosphopeptideIn vivoCell Line TumorReceptors Transferrinferritine[SDV.IDA]Life Sciences [q-bio]/Food engineeringHumanscellule HuH7Chromatography High Pressure LiquidComputingMilieux_MISCELLANEOUSSoluble transferrin receptorbiologytransferrine solubleCaseinsGeneral ChemistryMolecular biologyBioavailabilityFerritinCalceinnutritionchemistryβ caseinBiochemistryFerritinsbiology.proteinGeneral Agricultural and Biological Sciences[SDV.AEN]Life Sciences [q-bio]/Food and NutritionJournal of Agricultural and Food Chemistry
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PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

1996

AbstractThe 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) in a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified ‘PKC’ sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.

PhosphopeptidesMARCKSPRKRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsKidneyBiochemistryCell-free systemCell LineSerineStructural BiologyProtein kinase CGeneticsAnimalsAmino Acid SequenceBinding siteMARCKSPKCPhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateMolecular BiologyProtein kinase CGlutathione TransferaseBinding SitesCell-Free SystemKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsCell BiologyHaplorhiniPeptide FragmentsBiochemistryPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionSequence AnalysisSignal TransductionFEBS Letters
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Milk versus caseinophosphopeptides added to fruit beverage: Resistance and release from simulated gastrointestinal digestion

2010

The influence of simulated gastrointestinal digestion on caseinophosphopeptides (CPPs) formation in milk-based fruit beverage was evaluated, together with resistance of a pool of CPPs added to fruit beverage. In milk-based fruit beverage, four CPPs were identified that can be justified by their presence in raw milk or due to processing. When it was subjected to simulated gastrointestinal digestion, 10 CPPs were identified, and only 1 presented the cluster (SpSpSpEE) (3 phosphoseryl group followed by 2 glutamic acid residues), which corresponded to αs2-CN(1-19)4P. CPPs added to fruit beverage are resistant to simulated gastrointestinal digestion, and 16 CPPs were identified originating from …

PhosphopeptidesPhysiologyChemistryFruit drinksMolecular Sequence DataCaseinsfood and beveragesRaw milkBiochemistryPeptide FragmentsGastrointestinal digestionBeveragesGastrointestinal TractCellular and Molecular NeuroscienceMilkEndocrinologyMineral bioavailabilityMilk productsFruitAnimalsHumansDigestionAmino Acid SequenceFood scienceDigestion
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Correlations in palmitoylation and multiple phosphorylation of rat bradykinin B2 receptor in Chinese hamster ovary cells.

1999

Rat bradykinin B2 receptor from unstimulated Chinese hamster ovary cells transfected with the corresponding cDNA has been isolated, and subsequent mass spectrometric analysis of multiple phosphorylated species and of the palmitoylation attachment site is described. Bradykinin B2 receptor was isolated on oligo(dT)-cellulose using N-(epsilon-maleimidocaproyloxy)succinimide-Met-Lys-bradykinin coupled to a protected (dA)30-mer. This allowed a one-step isolation of the receptor on an oligo(dT)-cellulose column via variation solely of salt concentration. After enzymatic in-gel digestion, matrix-assisted laser desorption ionization and electrospray ion trap mass spectrometric analysis of the isola…

PhosphopeptidesReceptor Bradykinin B2AcylationMolecular Sequence DataPalmitatesCHO CellsTransfectionBiochemistryMass SpectrometryCell membranePhosphoserinePalmitoylationCricetinaemedicineAnimalsTrypsinAmino Acid SequenceBradykinin receptorPhosphorylationReceptorPhosphotyrosineMolecular BiologyChemistryChinese hamster ovary cellReceptors BradykininCell BiologyTransfectionPeptide FragmentsRatsmedicine.anatomical_structurePhosphothreonineBiochemistryPhosphorylationSignal transductionProtein Processing Post-TranslationalThe Journal of biological chemistry
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