Search results for "apparatus"

showing 10 items of 192 documents

Missense mutations of dual oxidase 2 (DUOX2) implicated in congenital hypothyroidism have impaired trafficking in cells reconstituted with DUOX2 matu…

2007

Abstract Dual oxidase 2 (DUOX2), a reduced NAD phosphate:O2 oxidoreductase flavoprotein, is a component of the thyrocyte H2O2 generator required for hormone synthesis at the apical plasma membrane. We recently identified a specific DUOX2 maturation factor (DUOXA2) that is necessary and sufficient for expression of functional DUOX2 in mammalian cell lines. We have now used a DUOXA2 reconstituted system to provide the first characterization of natural DUOX2 missense variants (Q36H, R376W, D506N) at the molecular level, analyzing their impact on H2O2 generation, trafficking, stability, folding, and DUOXA2 interaction. The Q36H and R376W mutations completely prevent routing of DUOX2 to the cell…

Protein FoldingMutantMutation MissenseBiologyEndoplasmic ReticulumCell membranesymbols.namesakeEndocrinologyMutant proteinPolysaccharidesCalnexinmedicineCongenital HypothyroidismAnimalsHumansMolecular BiologyCells CulturedFlavoproteinsOxidative foldingEndoplasmic reticulumCell MembraneMembrane ProteinsNADPH OxidasesDual oxidase 2General MedicineHydrogen PeroxideGolgi apparatusDual OxidasesRatsProtein Transportmedicine.anatomical_structureMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseBiochemistrysymbolsOxidation-ReductionMolecular endocrinology (Baltimore, Md.)
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Dithiothreitol Treatment of Madin-Darby Canine Kidney Cells Reversibly Blocks Export from the Endoplasmic Reticulum but Does Not Affect Vectorial Tar…

1995

Addition of dithiothreitol (DTT) to the culture medium of Madin-Darby canine kidney (MDCK) cells blocks transport of newly synthesized gp80 (clusterin, apolipoprotein J), a soluble marker protein for apical exocytosis in this epithelial cell line. In cells treated with DTT during pulse labeling, gp80 is retained in the endoplasmic reticulum. After removal of the reducing agent, gp80 is posttranslationally oxidized and secreted at the apical surface of MDCK cell monolayers. This demonstrates that when folded and oxidized posttranslationally, gp80 can acquire a conformation that exhibits sorting signals for vectorial targeting. In the continuous presence of DTT, the transepithelial electrical…

Protein FoldingProtein ConformationBiologyEndoplasmic ReticulumKidneySulfur RadioisotopesBiochemistryEpitheliumExocytosisDithiothreitolCell LineMembrane Potentialssymbols.namesakechemistry.chemical_compoundDogsMethioninemedicineAnimalsCysteineSalivary Proteins and PeptidesMolecular BiologySecretory pathwayGlycoproteinsTight junctionEndoplasmic reticulumCell MembraneCell BiologyGolgi apparatusEpitheliumCell biologyDithiothreitolClusterinmedicine.anatomical_structureSecretory proteinchemistrysymbolsOxidation-ReductionProtein Processing Post-TranslationalMolecular ChaperonesJournal of Biological Chemistry
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Phylogenetic profiling and cellular analyses of ARL16 reveal roles in traffic of IFT140 and INPP5E

2021

ABSTRACTThe ARF family of regulatory GTPases is ancient, with 16 members predicted to have been present in the last eukaryotic common ancestor. Our phylogenetic profiling of paralogs in diverse species identified four family members whose presence correlates with that of a cilium/flagellum: ARL3, ARL6, ARL13, and ARL16. No prior evidence links ARL16 to cilia or other cell functions, despite its presence throughout eukaryotes. Deletion of ARL16 in MEFs results in decreased ciliogenesis yet increased ciliary length. We also found Arl16 KO in MEFs to alter ciliary protein content, including loss of ARL13B, ARL3, INPP5E, and the IFT-A core component IFT140. Instead, both INPP5E and IFT140 accum…

Protein contentsymbols.namesakeCiliumCiliogenesisINPP5EsymbolsPhylogenetic profilingGTPaseGolgi apparatusBiologyFlagellumCell biology
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Identification of Trans-Golgi Network Proteins in Arabidopsis thaliana Root Tissue

2014

Knowledge of protein subcellular localization assists in the elucidation of protein function and understanding of different biological mechanisms that occur at discrete subcellular niches. Organelle-centric proteomics enables localization of thousands of proteins simultaneously. Although such techniques have successfully allowed organelle protein catalogues to be achieved, they rely on the purification or significant enrichment of the organelle of interest, which is not achievable for many organelles. Incomplete separation of organelles leads to false discoveries, with erroneous assignments. Proteomics methods that measure the distribution patterns of specific organelle markers along densit…

ProteomicsArabidopsis thalianaArabidopsisorganelle proteomicsProteomicsPlant RootsBiochemistryArticlesymbols.namesakeArtificial IntelligenceTandem Mass SpectrometryArabidopsisOrganelleArabidopsis thalianaChromatography Reverse-PhaseimmunoisolationbiologyArabidopsis Proteinstrans-Golgi networkGeneral ChemistryGolgi apparatusbiology.organism_classificationSubcellular localizationLOPITCell biologyIsobaric labelingphenoDiscomachine learningsymbolsIdentification (biology)Journal of Proteome Research
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Beyond The Ignorant Schoolmaster : On Education, Marxism, and Psychoanalysis

2016

This first chapter introduces the main concepts of Marxist sociology and Freudian psychoanalysis, two theories that have been intensely devoted to investigating and overcoming the epistemological effects caused by the phenomenal forms which inhered in the mode of production and the psychic apparatus, their respective subject matters. Their two prominent spearheads, Karl Marx and Sigmund Freud, soon understood that their scientific endeavors depended on deciphering the mechanisms which, in each case, generated these distorted reflections. These mechanisms were class division—the complex network that in any given social milieu consolidates around specific relations of production—and the split…

PsychicMarxist sociologyPsychoanalysisUnconscious mindPhilosophyId ego and super-egomedia_common.quotation_subjectSubject (philosophy)IdeologyFreudian slipPsychic apparatusmedia_common
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A novel radiation exposure control apparatus for microwave assisted chemical reactions

2004

AbstractA radiation exposure control apparatus is used for microwave (2.45 GHz) treatment of chemical reactions in controlled and reproducible conditions. A spectrophotometer has been interfaced with the microwave set-up in order to monitor the reaction evolution in situ. Both numerical and experimental dosimetries are carried out in order to evaluate the field distribution within the sample. Finally, particular working conditions are suggested.

Radiation exposureMaterials scienceMechanics of MaterialsMechanical EngineeringAnalytical chemistryDosimetryGeneral Materials ScienceCondensed Matter PhysicsChemical reactionMicrowave assistedMicrowaveMicrowave apparatus Microwaves assisted chemical reaction DosimetrySettore CHIM/02 - Chimica Fisica
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Arabidopsis p24δ5 and p24δ9 facilitate Coat Protein I-dependent transport of the K/HDEL receptor ERD2 from the Golgi to the endoplasmic reticulum.

2014

The p24 proteins belong to a family of type I membrane proteins which cycle between the endoplasmic reticulum (ER) and Golgi via coat protein I (COPI) and COPII vesicles. Current nomenclature classifies them into four subfamilies, although plant p24 proteins belong to either the p24β or the p24δ subfamilies. Here, we show that Arabidopsis p24δ5/δ9 and HDEL ligands shift the steady-state distribution of the K/HDEL receptor ERD2 from the Golgi to the ER. We also show that p24δ5/δ9 interact directly with ERD2. This interaction requires the Golgi dynamics (GOLD) domain in p24δ5 and is much higher at acidic than at neutral pH, consistent with both proteins interacting at the cis-Golgi. In additi…

Receptors PeptideArabidopsisGolgi ApparatusPlant ScienceBiologyEndoplasmic ReticulumCoat Protein Complex Isymbols.namesakeGeneticsAnimalsSecretionCOPIIVesicular-tubular clusterArabidopsis ProteinsEndoplasmic reticulumMembrane ProteinsCell BiologyCOPIGolgi apparatusCell biologyTransport proteinDNA-Binding ProteinsProtein TransportMembrane proteinsymbolsTranscription FactorsThe Plant journal : for cell and molecular biology
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In vivo Trafficking and Localization of p24 Proteins in Plant Cells

2008

p24 proteins constitute a family of putative cargo receptors that traffic in the early secretory pathway. p24 proteins can be divided into four subfamilies (p23, p24, p25 and p26) by sequence homology. In contrast to mammals and yeast, most plant p24 proteins contain in their cytosolic C-terminus both a dilysine motif in the -3, -4 position and a diaromatic motif in the -7, -8 position. We have previously shown that the cytosolic tail of Arabidopsis p24 proteins has the ability to interact with ARF1 and coatomer (through the dilysine motif) and with COPII subunits (through the diaromatic motif). Here, we establish the localization and trafficking properties of an Arabidopsis thaliana p24 pr…

Recombinant Fusion ProteinsMolecular Sequence DataArabidopsisGolgi ApparatusVacuoleProtein Sorting SignalsBiologyEndoplasmic ReticulumBiochemistrysymbols.namesakeStructural BiologyArabidopsisGeneticsAnimalsHumansProtein IsoformsAmino Acid SequenceMolecular BiologyCOPIISecretory pathwayArabidopsis ProteinsLysineEndoplasmic reticulumMembrane ProteinsCell BiologyCOPIGolgi apparatusbiology.organism_classificationActinsCell biologyDNA-Binding ProteinsProtein TransportBiochemistryCoatomerVacuolessymbolsCOP-Coated VesiclesCarrier ProteinsTranscription FactorsTraffic
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Structure and Dynamics of Confined Liquids: Challenges and Perspectives for the X-ray Surface Forces Apparatus

2019

Preprint of the open access article Weiss, H., Cheng, H.-W., Mars, J., Li, H., Merola, C., Renner, F. U., Honkimäki, V., Valtiner, M., & Mezger, M. (2019). Structure and Dynamics of Confined Liquids: Challenges and Perspectives for the X-ray Surface Forces Apparatus. Langmuir, 35(51), 16679–16692. https://doi.org/10.1021/acs.langmuir.9b01215

SFAMaterials sciencesynchrotron radiationDynamics (mechanics)Structure (category theory)NanotechnologySurface forces apparatus02 engineering and technologySurfaces and InterfacesX-SFA010402 general chemistry021001 nanoscience & nanotechnologyCondensed Matter Physics01 natural sciencesInvited Feature Article0104 chemical sciencesPhysics::Fluid DynamicsCondensed Matter::Soft Condensed MatterconfinementElectrochemistryGeneral Materials Science0210 nano-technologySpectroscopy
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Direct interaction of the Usher syndrome 1G protein SANS and myomegalin in the retina

2011

Contains fulltext : 96822.pdf (Publisher’s version ) (Closed access) The human Usher syndrome (USH) is the most frequent cause of combined hereditary deaf-blindness. USH is genetically heterogeneous with at least 11 chromosomal loci assigned to 3 clinical types, USH1-3. We have previously demonstrated that all USH1 and 2 proteins in the eye and the inner ear are organized into protein networks by scaffold proteins. This has contributed essentially to our current understanding of the function of USH proteins and explains why defects in proteins of different families cause very similar phenotypes. We have previously shown that the USH1G protein SANS (scaffold protein containing ankyrin repeat…

Scaffold proteinUsher syndromePhosphodiesterase 4D interacting protein (PDE4DIP)Muscle ProteinsPlasma protein bindingMice0302 clinical medicineYeastsChlorocebus aethiopsNuclear proteinCells CulturedGenetics0303 health scienceseducation.field_of_studyNuclear ProteinsCell biologyCOS CellssymbolsPhotoreceptor Cells VertebrateProtein BindingMicrotubule based transportNerve Tissue ProteinsBiologyModels BiologicalRetina03 medical and health sciencessymbols.namesakemedicineAnimalsHumanseducationMolecular BiologyAdaptor Proteins Signal Transducing030304 developmental biologyCell BiologyGlycostation disorders [IGMD 4]Golgi apparatusmedicine.diseaseMacaca mulattaMice Inbred C57BLCytoskeletal ProteinsPhotoreceptor cell functionMyomegalinGenetics and epigenetic pathways of disease Functional Neurogenomics [NCMLS 6]CattleAnkyrin repeatCiliary baseIntracellular transport030217 neurology & neurosurgerySensorineuronal degeneration
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