Search results for "PRECIPITATION"

showing 10 items of 826 documents

Protein Kinase C μ Is Regulated by the Multifunctional Chaperon Protein p32

2000

We identified the multifunctional chaperon protein p32 as a protein kinase C (PKC)-binding protein interacting with PKCalpha, PKCzeta, PKCdelta, and PKC mu. We have analyzed the interaction of PKC mu with p32 in detail, and we show here in vivo association of PKC mu, as revealed from yeast two-hybrid analysis, precipitation assays using glutathione S-transferase fusion proteins, and reciprocal coimmunoprecipitation. In SKW 6.4 cells, PKC mu is constitutively associated with p32 at mitochondrial membranes, evident from colocalization with cytochrome c. p32 interacts with PKC mu in a compartment-specific manner, as it can be coimmunoprecipitated mainly from the particulate and not from the so…

ImmunoprecipitationRecombinant Fusion ProteinsGolgi ApparatusSaccharomyces cerevisiaeSpodopteraMitogen-activated protein kinase kinaseBiologyTransfectionBiochemistryCell LineMitochondrial ProteinsAnimalsHumansCloning MolecularKinase activityMolecular BiologyProtein Kinase CProtein kinase CGlutathione TransferaseB-LymphocytesBinding SitesMembrane GlycoproteinsKinaseAutophosphorylationJNK Mitogen-Activated Protein KinasesCell BiologyFusion proteinMitochondriaReceptors ComplementCell biologybody regionsHyaluronan ReceptorsProtein kinase domainBiochemistryMitogen-Activated Protein KinasesCarrier ProteinsMolecular ChaperonesProtein BindingJournal of Biological Chemistry
researchProduct

Dissection of human papillomavirus type 33 L2 domains involved in nuclear domains (ND) 10 homing and reorganization

2003

Abstract We have recently shown that the minor capsid protein L2 of human papillomavirus type 33 (HPV33) recruits the transcriptional repressor Daxx into nuclear domains (ND) 10 and causes the loss of the transcriptional activator Sp100 from these subnuclear structures (Florin et al., 2002b) . In order to dissect L2 domains involved in nuclear translocation, ND10 homing, loss of Sp100, and recruitment of Daxx, a detailed deletion mutagenesis of L2 was performed. Using immunofluorescence and green fluorescent protein fusions, we have identified two nuclear localization signals (NLS) in the central and C-terminal part of L2, respectively, homologous to previously identified NLS in HPV6B L2 (S…

ImmunoprecipitationRecombinant Fusion ProteinsGreen Fluorescent ProteinsNuclear Localization SignalsActive Transport Cell NucleusFluorescent Antibody TechniqueBiologyImmunofluorescenceAutoantigensGreen fluorescent proteinDeath-associated protein 6DaxxVirologyTumor Cells CulturedmedicineSp100HumansNLSPapillomaviridaeAdaptor Proteins Signal TransducingCell Nucleusmedicine.diagnostic_testIntracellular Signaling Peptides and ProteinsND10Nuclear ProteinsAntigens NuclearL2Oncogene Proteins ViralPapillomavirusbiochemical phenomena metabolism and nutritionMolecular biologyDeletion MutagenesisLuminescent ProteinsCapsidMutagenesisCapsid ProteinsCarrier ProteinsCo-Repressor ProteinsGene DeletionNuclear localization sequenceMolecular ChaperonesVirology
researchProduct

A Protein-Interaction Array Inside a Living Cell

2013

Cell phenotype is determined by protein network states that are maintained by the dynamics of multiple protein interactions.1 Fluorescence microscopy approaches that measure protein interactions in individual cells, such as by Forster resonant energy transfer (FRET), are limited by the spectral separation of fluorophores and thus are most suitable to analyze a single protein interaction in a given cell. However, analysis of correlations between multiple protein interactions is required to uncover the interdependence of protein reactions in dynamic signal networks. Available protein-array technologies enable the parallel analysis of interacting proteins from cell extracts, however, they can …

ImmunoprecipitationRecombinant Fusion Proteinsprotein-protein interactionsImmobilized Nucleic AcidsProtein Array AnalysisreceptorsDNA Single-StrandedCatalysisProtein–protein interactionReceptors G-Protein-CoupledBimolecular fluorescence complementationProtein Array AnalysisChlorocebus aethiopsFluorescence microscopeFluorescence Resonance Energy TransferAnimalsProtein Interaction MapsProtein kinase Amultiplexed assayChemistryProteinsProtein-protein interactions Dip Pen Nanolithography Protein KinaseDNA directed immobilizationGeneral MedicineGeneral ChemistryCommunicationssurface-immobilizationKineticsLuminescent ProteinsFörster resonance energy transferBiochemistryMicroscopy FluorescenceCOS CellsBiophysicsSignal transductionAntibodies Immobilizedsignal transduction
researchProduct

Interaction of syntenin-1 and the NG2 proteoglycan in migratory oligodendrocyte precursor cells.

2008

Migration of oligodendrocyte precursors along axons is a necessary prerequisite for myelination, but little is known about underlying mechanisms. NG2 is a large membrane proteoglycan implicated in oligodendrocyte migration. Here we show that a PDZ domain protein termed syntenin-1 interacts with NG2 and that syntenin-1 is necessary for normal rates of migration. The association of syntenin-1 with NG2, identified in a yeast two-hybrid screen, was confirmed by colocalization of both proteins within processes of oligodendroglial precursor cells and by coimmunoprecipitation from cell extracts. Syntenin-1 also colocalizes with NG2 in "co-capping" assays, demonstrating a lateral association of bot…

ImmunoprecipitationSynteninsCellPDZ domainAmino Acid MotifsBiologyBiochemistryMiceCell MovementPrecursor cellTwo-Hybrid System TechniquesmedicineAnimalsHumansAntigensRNA Small InterferingMolecular BiologyCells CulturedNG2 proteoglycanColocalizationCell DifferentiationCell BiologyMolecular biologyOligodendrocyteCell biologyOligodendrogliamedicine.anatomical_structurenervous systemProteoglycanbiology.proteinProteoglycansNeurogliaProtein BindingThe Journal of biological chemistry
researchProduct

Cell surface display of rat invariant γ chain: detection by monoclonal antibodies directed against a C-terminal γ chain segment

1992

A series of 14 monoclonal antibodies (mAb) directed against the C-terminal part of the rat invariant gamma chain (amino acid 142-216) was generated using distinct fusion proteins that contain this gamma segment for immunization and hybridoma screening. Additional fusion protein were prepared carrying discrete regions of the gamma chain. Employing these reagents confirmed that the obtained mAb do indeed recognize the C-terminal portion of the invariant chain, as demonstrated by Western blot analysis. All mAb established recognize epitopes present on the native gamma chain, as revealed by immunoprecipitation analysis using nonionic detergent extracts of metabolically labeled Lewis rat splenoc…

Immunoprecipitationmedicine.drug_classRecombinant Fusion ProteinsBlotting WesternGenetic VectorsImmunologyMonoclonal antibodyEpitopeMiceWestern blotEscherichia colimedicineAnimalsImmunology and AllergyElectrophoresis Gel Two-DimensionalCloning MolecularGel electrophoresisMice Inbred BALB CHybridomasbiologymedicine.diagnostic_testHistocompatibility Antigens Class IIAntibodies MonoclonalFlow CytometryFusion proteinPrimary and secondary antibodiesMolecular biologyRatsAntigens Differentiation B-LymphocyteBiochemistryRats Inbred LewAntigens Surfacebiology.proteinAntibodySpleenPlasmidsEuropean Journal of Immunology
researchProduct

An L2 SUMO interacting motif is important for PML localization and infection of human papillomavirus type 16

2014

Summary Human papillomaviruses (HPV) induce warts and cancers on skin and mucosa. The HPV16 capsid is composed of the proteins L1 and L2. After cell entry and virus disassembly, the L2 protein accompanies the viral DNA to promyelocytic leukaemia nuclear bodies (PML-NBs) within the host nuclei enabling viral transcription and replication. Multiple components of PML-NBs are regulated by small ubiquitin-like modifiers (SUMOs) either based on covalent SUMO modification (SUMOylation), or based on non-covalent SUMO interaction via SUMO interacting motifs (SIMs). We show here that the HPV16 L2 comprises at least one SIM, which is crucial for the L2 interaction with SUMO2 in immunoprecipitation and…

ImmunoprecipitationvirusesImmunologyMutantSUMO proteinvirus diseasesColocalizationSUMO2BiologyMicrobiologyMolecular biologyVirusCapsidTranscription (biology)Virologyembryonic structuresCellular Microbiology
researchProduct

Crystalline Non‐Equilibrium Phase of a Cobalt(II) Complex with Tridentate Ligands

2015

In six-coordinate complexes, flexible tridentate ligands enable mer, cis-fac, and trans-fac stereoisomers. With labile metal ions of the first transition metal series, typically only the final thermodynamic product is available because of the rapid isomerization processes. Here we report on the structural characterization of a so far elusive kinetic intermediate of [Co(ddpd)2](BF4)2 (1; ddpd = N,N′-dimethyl-N,N′-dipyridine-2-yl-pyridine-2,6-diamine). Microcrystals of the cis-fac isomer of 1 were obtained by rapid precipitation. The solid-state structure of cis-fac-1 was determined from electron diffraction data.

Inorganic ChemistryCrystallographyEquilibrium phaseElectron diffractionTransition metalChemistryPrecipitation (chemistry)Metal ions in aqueous solutionchemistry.chemical_elementKinetic energyCobaltIsomerizationEuropean Journal of Inorganic Chemistry
researchProduct

The Fibril-associated Collagen IX Provides a Novel Mechanism for Cell Adhesion to Cartilaginous Matrix

2004

Collagen IX is the prototype fibril-associated collagen with interruptions in triple helix. In human cartilage it covers collagen fibrils, but its putative cellular receptors have been unknown. The reverse transcription-PCR analysis of human fetal tissues suggested that based on their distribution all four collagen receptor integrins, namely alpha1beta1, alpha2beta1, alpha10beta1, and alpha11beta1, are possible receptors for collagen IX. Furthermore primary chondrocytes and chondrosarcoma cells express the four integrins simultaneously. Chondrosarcoma cells, as well as Chinese hamster ovary cells transfected to express alpha1beta1, alpha2beta1, or alpha10beta1 integrin as their only collage…

Integrin alpha1Integrin alpha2LigandsPolymerase Chain ReactionBiochemistryCollagen receptorMiceCricetinaeReceptorbiologyReverse Transcriptase Polymerase Chain ReactionChemistryChinese hamster ovary cellRecombinant ProteinsCell biologyBiochemistryCollagenIntegrin alpha ChainsProtein BindingMolecular Sequence DataIntegrinChondrosarcomaCHO CellsFibrilCollagen Type IXCell LineChondrocytesMicroscopy Electron TransmissionCell Line TumorCell AdhesionEscherichia coliAnimalsHumansImmunoprecipitationAmino Acid SequenceRNA MessengerBinding siteCell adhesionMolecular BiologyBinding SitesSequence Homology Amino AcidCell BiologyProtein Structure TertiaryRatsMicroscopy ElectronCollagen type I alpha 1CartilageMutationMutagenesis Site-Directedbiology.proteinRNAPeptidesJournal of Biological Chemistry
researchProduct

Intercalation of [M(ox)3]3− (M=Cr, Rh) complexes into NiIIFeIII-LDH

2010

Abstract Layered Double Hydroxides (LDH) containing paramagnetic NiII and FeIII ions in the hydroxide layers and chromium or rhodium oxalate complexes at the interlayer space were prepared by ion exchange from a NiFe-LDH precursor with sebacate anions between the hydroxide layers. The precursor was synthesized by coprecipitation at controlled pH in order to avoid the formation of solid phases different from LDH. Magnetic studies demonstrated that both LDHs, NiFe–Cr(ox)3 and NiFe–Rh(ox)3, exhibited a behaviour similar to the precursor. Nevertheless, the substitution of intercalated sebacate anions with oxalate complexes compresses the LDH basal spacing, increasing the intensity of dipolar in…

Ion exchangeCoprecipitationIntercalation (chemistry)Inorganic chemistryLayered double hydroxidesGeologyengineering.materialOxalatechemistry.chemical_compoundParamagnetismchemistryGeochemistry and PetrologyengineeringHydroxideHybrid materialApplied Clay Science
researchProduct

Response of the oxygen sensor NreB to air in vivo: Fe-S-containing NreB and apo-NreB in aerobically and anaerobically growing Staphylococcus carnosus.

2009

ABSTRACT The sensor kinase NreB from Staphylococcus carnosus contains an O 2 -sensitive [4Fe-4S] 2+ cluster which is converted by O 2 to a [2Fe-2S] 2+ cluster, followed by complete degradation and formation of Fe-S-less apo-NreB. NreB·[2Fe-2S] 2+ and apoNreB are devoid of kinase activity. NreB contains four Cys residues which ligate the Fe-S clusters. The accessibility of the Cys residues to alkylating agents was tested and used to differentiate Fe-S-containing and Fe-S-less NreB. In a two-step labeling procedure, accessible Cys residues in the native protein were first labeled by iodoacetate. In the second step, Cys residues not labeled in the first step were alkylated with the fluorescent…

Iron-Sulfur ProteinsbiologyAerobic bacteriaStaphylococcusGene Expression Regulation BacterialAlkylationbiology.organism_classificationMicrobiologyModels BiologicalAerobiosisOxygenBiochemistryBacterial ProteinsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationNative stateImmunoprecipitationAnaerobic bacteriaAnaerobiosisCysteineKinase activityMolecular BiologyBacteriaCysteineStaphylococcus carnosusSignal TransductionJournal of bacteriology
researchProduct