Search results for "Phosphor"

showing 10 items of 1952 documents

Cytochrome-P450 phosphorylation as a functional switch

2002

Xenobiotic metabolizing cytochromes P450 (CYP) were shown to be phosphorylated in vitro (using purified protein kinases together with purified CYPs), in intact cells (in V79 cells after transfection of cDNAs coding for individual CYPs, in diagnostic mutants, in hepatocytes), and in whole organisms (rats). CYP phosphorylation is highly isoenzyme selective in that only some CYPs are phosphorylated. Protein kinase A (PKA) was identified as a major catalyst for the phosphorylation of CYPs. The PKA recognition motif Arg-Arg-X-Ser is present in several members of the CYP2 family, but is used by only some of them, most notably by CYP2B1/2B2 and CYP2E1. For CYP2B1 it was shown that a substantial po…

inorganic chemicalsAmino Acid MotifsMutantBiophysicsBiologyTransfectionBiochemistryCatalysisCytochrome P-450 Enzyme SystemCyclic AMPAnimalsheterocyclic compoundsProtein phosphorylationPhosphorylationEnzyme inducerProtein kinase AMolecular BiologyCells CulturedKinaseorganic chemicalsCytochrome P450Transfectionrespiratory systemMolecular biologyRatsKineticsenzymes and coenzymes (carbohydrates)LiverBiochemistryMutagenesis Site-Directedbiology.proteinPhosphorylationRabbitsArchives of Biochemistry and Biophysics
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Redox modulation of Rubisco conformation and activity through its cysteine residues

2008

Treatment of purified Rubisco with agents that specifically oxidize cysteine-thiol groups causes catalytic inactivation and increased proteolytic sensitivity of the enzyme. It has been suggested that these redox properties may sustain a mechanism of regulating Rubisco activity and turnover during senescence or stress. Current research efforts are addressing the structural basis of the redox modulation of Rubisco and the identification of critical cysteines. Redox shifts result in Rubisco conformational changes as revealed by the alteration of its proteolytic fragmentation pattern upon oxidation. In particular, the augmented susceptibility of Rubisco to proteases is due to increased exposure…

inorganic chemicalsChloroplastsbiologyPhysiologyCatabolismCysteamineRibulose-Bisphosphate CarboxylasefungiRuBisCOMutagenesisfood and beveragesChlamydomonas reinhardtiiPlant ScienceOxidative phosphorylationPlantsbiology.organism_classificationRedoxChloroplastBiochemistryPlant Cellsbiology.proteinAmino Acid SequenceOxidation-ReductionCysteineJournal of Experimental Botany
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Phosphorylation of the Goodpasture antigen by type A protein kinases.

1995

Collagen IV is the major component of basement membranes. The human alpha 3 chain of collagen IV contains an antigenic domain called the Goodpasture antigen that is the target for the circulating immunopathogenic antibodies present in patients with Goodpasture syndrome. Characteristically, the gene region encoding the Goodpasture antigen generates multiple alternative products that retain the antigen amino-terminal region with a five-residue motif (KRGDS). The serine therein appears to be the major in vitro cAMP-dependent protein kinase phosphorylation site in the isolated antigen and can be phosphorylated in vitro by two protein kinases of approximately 50 and 41 kDa associated with human …

inorganic chemicalsCollagen Type IVAnti-Glomerular Basement Membrane DiseaseMolecular Sequence DataBiochemistryAutoantigensSerineAntigenmedicineSerineGoodpasture syndromeHumansAmino Acid SequencePhosphorylationProtein kinase AMolecular BiologyBasement membranebiologyBase SequenceKinaseCell Biologymedicine.diseaseMolecular biologyCyclic AMP-Dependent Protein Kinasesenzymes and coenzymes (carbohydrates)medicine.anatomical_structureOligodeoxyribonucleotidesbiology.proteinPhosphorylationCollagenAntibodyThe Journal of biological chemistry
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Complexation of Uranium by Cells and S-Layer Sheets of Bacillus sphaericus JG-A12

2005

ABSTRACT Bacillus sphaericus JG-A12 is a natural isolate recovered from a uranium mining waste pile near the town of Johanngeorgenstadt in Saxony, Germany. The cells of this strain are enveloped by a highly ordered crystalline proteinaceous surface layer (S-layer) possessing an ability to bind uranium and other heavy metals. Purified and recrystallized S-layer proteins were shown to be phosphorylated by phosphoprotein-specific staining, inductive coupled plasma mass spectrometry analysis, and a colorimetric method. We used extended X-ray absorption fine-structure (EXAFS) spectroscopy to determine the structural parameters of the uranium complexes formed by purified and recrystallized S-laye…

inorganic chemicalsDenticityAnalytical chemistrychemistry.chemical_elementBacillusMass spectrometryApplied Microbiology and BiotechnologyBacillus sphaericusMiningchemistry.chemical_compoundBacterial ProteinsMicroscopy Electron TransmissionMembrane GlycoproteinsEcologybiologyExtended X-ray absorption fine structureSpectrum AnalysisX-RaysPhosphorusUraniumPhosphoproteinsbiology.organism_classificationPhosphateGeomicrobiologychemistryTransmission electron microscopyUraniumAbsorption (chemistry)Food ScienceBiotechnologyNuclear chemistryApplied and Environmental Microbiology
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Phosphororganische Verbindungen, 68. Darstellung und Eigenschaften von Tetrakis(diphenylphosphin)‐nickel(0)

1971

Die Titelsubstanz 1 wurde durch Einwirkung von Diphenylphosphin auf Bis-π-allyl-nickel, Tetrakis(triphenylphosphin)-nickel(0) (2), Nickelpulver oder Nickel(II)-bromid dargestellt. Ihre Struktur wurde durch Zerewitinoff-Bestimmung, IR- und NMR-Spektren abgesichert. Eine Alkylierung von metalliertem 1 gelang nicht. Organic Phosphorus Compounds, 68. Preparation and Properties of Tetrakis(diphenylphosphine)nickel(0) The title compound, 1, was prepared by reacting of diphenylphosphine with bis(π-allyl)nickel, tetrakis(triphenylphosphine)nickel(0) (2), nickel-powder, or nickel(II) bromide. The structure of 1 was elucidated by Zerewitinoff method, i. r. and n. m. r. spectra. The alkylation of meta…

inorganic chemicalsInorganic Chemistrychemistry.chemical_compoundNickelDiphenylphosphinechemistryBromidePolymer chemistryotorhinolaryngologic diseasesOrganic phosphoruschemistry.chemical_elementAlkylationTriphenylphosphineChemische Berichte
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The Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) is Sequentially Phosphorylated by Conventional, Novel and Atypical Isotypes of Protein Kin…

1995

The myristoylated alanine-rich C-kinase substrate (MARCKS) is the major protein kinase C (PKC) substrate in many cell types including fibroblasts and brain cells. Here we describe the phosphorylation of MARCKS and the site specificity for different PKC isotypes. Conventional (c)PKC beta 1, novel (n)PKC delta and nPKC epsilon efficiently phosphorylated the MARCKS protein in vitro. The Km values were extremely low, reflecting a high affinity between kinases and substrate. The apparent affinity of nPKC delta (Km = 0.06 microM) was higher than that of nPKC epsilon and cPKC beta 1 (Km = 0.32 microM). The rate of substrate phosphorylation was inversely correlated with affinity and decreased in th…

inorganic chemicalsKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsContext (language use)macromolecular substancesenvironment and public healthBiochemistryMolecular biologyCell biologyIsoenzymesSerineKineticsenzymes and coenzymes (carbohydrates)Substrate-level phosphorylationbacteriaPhosphorylationPhosphorylationMARCKSMyristoylated Alanine-Rich C Kinase SubstrateProtein Kinase CProtein kinase CMyristoylationEuropean Journal of Biochemistry
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Production of Phosphorescent Coatings on 6082 Aluminum Using Sr0.95Eu0.02Dy0.03Al2O4-δ Powder and Plasma Electrolytic Oxidation

2019

In this study, a new approach for producing phosphorescent aluminum coatings was studied. Using the plasma electrolytic oxidation (PEO) process, a porous oxide coating was produced on the Al6082 aluminum alloy substrate. Afterwards, activated strontium aluminate (SrAl2O4: Eu2+, Dy3+) powder was filled into the cavities and pores of the PEO coating, which resulted in a surface that exhibits long-lasting luminescence. The structural and optical properties were studied using XRD, SEM, and photoluminescence measurements. It was found that the treatment time affects the morphology of the coating, which influences the amount of strontium aluminate powder that can be incorporated into the coating …

inorganic chemicalsMaterials scienceMorphology (linguistics)Photoluminescencechemistry.chemical_element02 engineering and technologyengineering.material01 natural scienceschemistry.chemical_compoundCoatingPlasma electrolytic oxidation (PEO)Aluminium0103 physical sciencesLuminescent coatings:NATURAL SCIENCES:Physics [Research Subject Categories]Materials Chemistry010302 applied physicsAluminum 6082aluminum 6082Phosphorescencetechnology industry and agricultureStrontium aluminateSurfaces and InterfacesPlasma electrolytic oxidationplasma electrolytic oxidation (PEO)021001 nanoscience & nanotechnologySurfaces Coatings and Filmsphosphorescenceluminescent coatingschemistryChemical engineeringengineering0210 nano-technologyLuminescencePhosphorescenceCoatings
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Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes

1998

AbstractPrevious studies directed towards understanding phosphorylation of the chlorophyll a/b binding proteins comprising light harvesting complex II (LHC II) have concentrated on a single phosphorylation site located close to the N-terminus of the mature proteins. Here we show that a series of recombinant pea Lhcb1 proteins, each missing an N-terminal segment including this site, are nevertheless phosphorylated by a protein kinase associated with a photosystem II core complex preparation. An Lhcb1 protein missing the first 58 amino acid residues is not, however, phosphorylated. The results demonstrate that the LHC II proteins are phosphorylated at one or more sites, the implications of wh…

inorganic chemicalsPhotosystem IIMacromolecular SubstancesMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiophysicsmacromolecular substancesBiologyBiochemistryDNA-binding proteinProtein kinaseThylakoid membraneSubstrate Specificitylaw.inventionStructural BiologylawGeneticsProtein phosphorylationAmino Acid SequencePhosphorylationProtein kinase AMolecular BiologyPlant ProteinsKinasePeasPeaPhotosystem II Protein Complexfood and beveragesCell BiologySpinachPeptide FragmentsRecombinant Proteinsenzymes and coenzymes (carbohydrates)BiochemistryThylakoidRecombinant DNALight harvesting proteinPhosphorylationbacteriaCarrier ProteinsProtein KinasesFEBS Letters
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Stromal Interaction Molecule 1 (STIM1) Is Involved in the Regulation of Mitochondrial Shape and Bioenergetics and Plays a Role in Oxidative Stress

2012

Calcium ions are involved in a plethora of cellular functions including cell death and mitochondrial energy metabolism. Store-operated Ca(2+) entry over the plasma membrane is activated by depletion of intracellular Ca(2+) stores and is mediated by the sensor STIM1 and the channel ORAI1. We compared cell death susceptibility to oxidative stress in STIM1 knock-out and ORAI1 knockdown mouse embryonic fibroblasts and in knock-out cells with reconstituted wild type and dominant active STIM1. We show that STIM1 and ORAI1 deficiency renders cells more susceptible to oxidative stress, which can be rescued by STIM1 and ORAI1 overexpression. STIM1 knock-out mitochondria are tubular, have a higher Ca…

inorganic chemicalsProgrammed cell deathORAI1 ProteinEukaryotic Initiation Factor-2Active Transport Cell NucleusApoptosisMitochondrionBiologymedicine.disease_causeBiochemistryMiceeIF-2 KinasemedicineAnimalsStromal Interaction Molecule 1PhosphorylationMolecular BiologyTranscription factorCells CulturedMice KnockoutEIF-2 kinaseMembrane GlycoproteinsEndoplasmic reticulumMolecular Bases of DiseaseSTIM1Cell BiologyFibroblastsEmbryo MammalianMitochondriaCell biologyOxidative Stressbiology.proteinCalciumCalcium ChannelsEnergy MetabolismIntracellularOxidative stressJournal of Biological Chemistry
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Three proteins regulating integrin function - filamin, 14-3-3 and RIAM

2011

integriinitfosforylaatiointegrinphosphorylationRIAMtalinfilamiinitsäätelyproteiinitcytoplasmic interactionsfilamin A variant-1
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