Search results for "Centrosome"

showing 6 items of 36 documents

TOPORS, implicated in retinal degeneration, is a cilia-centrosomal protein.

2011

et al.

Retinal degenerationUbiquitin-Protein LigasesBiologymedicine.disease_causeRetinaCell Line03 medical and health scienceschemistry.chemical_compoundMiceNuclear proteins0302 clinical medicineIntraflagellar transportGeneticsmedicineBasal bodyAnimalsHumansPhotoreceptor CellsCiliaMolecular BiologyZebrafishGenetics (clinical)Cells CulturedZebrafish030304 developmental biologyCentrosome0303 health sciencesRetinaMutationUbiquitinCiliumRetinal DegenerationNuclear ProteinsRetinalTOPORS proteinGeneral MedicineArticlesmedicine.diseasebiology.organism_classification3. Good healthCell biologyNeoplasm ProteinsProtein Transportmedicine.anatomical_structurechemistryNeoplasm proteinssense organs030217 neurology & neurosurgeryHuman molecular genetics
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Differential expression and interaction with the visual G-protein transducin of centrin isoforms in mammalian photoreceptor cells.

2004

Photoisomerization of rhodopsin activates a heterotrimeric G-protein cascade leading to closure of cGMP-gated channels and hyperpolarization of photoreceptor cells. Massive translocation of the visual G-protein transducin, Gt, between subcellular compartments contributes to long term adaptation of photoreceptor cells. Ca(2+)-triggered assembly of a centrin-transducin complex in the connecting cilium of photoreceptor cells may regulate these transducin translocations. Here we demonstrate expression of all four known, closely related centrin isoforms in the mammalian retina. Interaction assays revealed binding potential of the four centrin isoforms to Gtbetagamma heterodimers. High affinity b…

Rhodopsingenetic structuresLightBlotting WesternBiologyBiochemistryRetinaRats Sprague-DawleyMiceCalcium-binding proteinHeterotrimeric G proteinmedicineAnimalsProtein IsoformsScattering RadiationCiliaTransducinMicroscopy ImmunoelectronMolecular BiologyCyclic GMPGlutathione TransferaseCentrosomeRetinaChromatographyDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionCiliumCalcium-Binding ProteinsCell BiologySequence Analysis DNARod Cell Outer SegmentRecombinant ProteinsCell biologyRatsMice Inbred C57BLKineticsProtein Transportmedicine.anatomical_structureMicroscopy FluorescenceRhodopsinCentrosomeCentrinbiology.proteinCalciumCattleElectrophoresis Polyacrylamide Gelsense organsTransducinProtein BindingThe Journal of biological chemistry
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RNAi mediated acute depletion of Retinoblastoma protein (pRb) promotes aneuploidy in human primary cells via micronuclei formation

2009

BACKGROUND: Changes in chromosome number or structure as well as supernumerary centrosomes and multipolar mitoses are commonly observed in human tumors. Thus, centrosome amplification and mitotic checkpoint dysfunctions are believed possible causes of chromosomal instability. The Retinoblastoma tumor suppressor (RB) participates in the regulation of synchrony between DNA synthesis and centrosome duplication and it is involved in transcription regulation of some mitotic genes. Primary human fibroblasts were transfected transiently with short interfering RNA (siRNA) specific for human pRb to investigate the effects of pRb acute loss on chromosomal stability. RESULTS: Acutely pRb-depleted fibr…

Small interfering RNAMitosisCell Cycle ProteinsProtein Serine-Threonine KinasesRetinoblastoma ProteinAurora KinasesRNA interferenceChromosomal InstabilityProto-Oncogene ProteinsChromosome instabilitymedicineHumansCentrosome duplicationRNA Small Interferinglcsh:QH573-671MitosisCells CulturedCell NucleusCentrosomebiologylcsh:CytologyRetinoblastomaRetinoblastoma proteinCell BiologyFibroblastsAneuploidymedicine.diseaseCell biologyCentrosomeRNAi Aneuploidy pRBRb anauploidybiology.proteinRNA Interferencebiological phenomena cell phenomena and immunityResearch ArticleBMC Cell Biology
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Crystallization and preliminary X-ray studies of mouse centrin1.

2005

The expression, purification, crystallization and preliminary X-ray diffraction studies of mouse centrin1 are reported. Centrins belong to a family of Ca{sup 2+}-binding EF-hand proteins that play a fundamental role in centrosome duplication and the function of cilia. To shed light on the structure–function relationship of these proteins, mouse centrin1 has been crystallized. The mouse centrin1 has been expressed in Escherichia coli as a GST-centrin fusion protein containing a thrombin protease cleavage site between the fusion partners. Two constructs with different linking-sequence lengths were expressed and purified. Thrombin cleavage yielded functional centrin1 and N-terminally extended …

StereochemistryChromosomal Proteins Non-HistoneMolecular Sequence DataBiophysicsmacromolecular substancesCleavage (embryo)Crystallography X-RayBiochemistrylaw.inventionchemistry.chemical_compoundMiceStructure-Activity RelationshipThrombinStructural BiologylawGeneticsmedicineEscherichia coliAnimalsCentrosome duplicationAmino Acid SequenceCrystallizationDose-Response Relationship DrugCalcium-Binding ProteinsSpace groupCondensed Matter PhysicsFusion proteinRecombinant ProteinsCrystallographyenzymes and coenzymes (carbohydrates)KineticschemistryCrystallization CommunicationsX-ray crystallographybiological scienceshealth occupationsbacteriaCrystallizationEthylene glycolmedicine.drugActa crystallographica. Section F, Structural biology and crystallization communications
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Constitutive hsp70 is essential to mitosis during early cleavage of Paracentrotus lividus embryos: The blockage of constitutive hsp70 impairs mitosis

1999

Localization of constitutive hsp70 in eggs and early embryos of sea urchin Paracentrotus lividus is shown by means of in situ immunostaining. An accumulation of this protein is shown in the mitotic structures (asters, spindles and centrosomes). Microinjection of anti-hsp70 antibodies into eggs causes impairment of formation of mitotic structures and of cell division. This impairment goes from a complete mitotic block, to irregular mitotic apparatus formation with irregular cleavage, depending upon the antibody concentration. The localization of hsp70 after antibody microinjection is also described. Blockage of mitotic apparatus formation by nocodazole also blocks the concentration of hsp70 …

Time FactorsGrowth InhibitorMicroinjectionsCell divisionTime FactorSea UrchinCleavage Stage OvumBiophysicsMitosisCleavage (embryo)BiochemistryParacentrotus lividuschemistry.chemical_compoundbiology.animalAnimalsHSP70 Heat-Shock ProteinsSea urchin embryoMitosisMicroinjectionSea urchinMolecular BiologyConstitutive hsp70HSP70 Heat-Shock ProteinbiologyDose-Response Relationship DrugAnimalNocodazoleCell Biologybiology.organism_classificationMitosiGrowth InhibitorsMicroinjectionCell biologyNocodazolechemistryBiophysicCentrosomeSea UrchinsFertilizationembryonic structures
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Analysis of the Cellular Roles of MOCS3 Identifies a MOCS3-Independent Localization of NFS1 at the Tips of the Centrosome

2019

The deficiency of the molybdenum cofactor (Moco) is an autosomal recessive disease, which leads to the loss of activity of all molybdoenzymes in humans with sulfite oxidase being the essential protein. Moco deficiency generally results in death in early childhood. Moco is a sulfur-containing cofactor synthesized in the cytosol with the sulfur being provided by a sulfur relay system composed of the L-cysteine desulfurase NFS1, MOCS3, and MOCS2A. Human MOCS3 is a dual-function protein that was shown to play an important role in Moco biosynthesis and in the mcm(5)s(2) U thio modifications of nucleosides in cytosolic tRNAs for Lys, Gln, and Glu. In this study, we constructed a homozygous MOCS3 …

inorganic chemicalsCoenzymesBiochemistry03 medical and health scienceschemistry.chemical_compoundRNA Transferddc:570Sulfite oxidaseMetalloproteinsHumansnatural sciencesInstitut für Biochemie und BiologieAconitate HydrataseCentrosome0303 health sciencesPteridinesSulfite Oxidase030302 biochemistry & molecular biologyNucleotidyltransferasesIsocitrate DehydrogenaseCell biologyCarbon-Sulfur LyasesHEK293 CellschemistryCentrosomeSulfurtransferasesbacteriaCRISPR-Cas SystemsMolybdenum cofactorMolybdenum CofactorsHeLa CellsBiochemistry
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