Search results for "Tubule"

showing 10 items of 308 documents

The Usher syndrome 1G protein SANS participates in the transport of ciliary cargo in photoreceptor cells

2012

Human Usher syndrome (USH) is the most common form of combined deaf-blindness, characterized by profound congenital deafness, constant vestibular dysfunction and pre-pubertal onset of retinitis pigmentosa. The USH1G protein SANS (scaffold protein containing ankyrin repeats and SAM domain) is associated with microtubules and mediates a transport related periciliary protein network in photoreceptor cells. Here we aim to enlighten the involvement of SANS in ciliary transport of photoreceptor cells by identifying proteins associated with SANS in transport complexes. In Y2H screen of retinal cDNA library we identified the direct binding of SANS to dynactin-1 (p150Glued), a subunit of the dynacti…

Scaffold proteinRetinal degenerationGeneticsOpsinlcsh:CytologyProtein subunitCiliumCell BiologyBiologymedicine.diseaseOpsin transportCell biologyMicrotubuleRetinitis pigmentosaPoster Presentationmedicinesense organslcsh:QH573-671Cilia
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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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A survey on tubulin and arginine methyltransferase families sheds light on p. lividus embryo as model system for antiproliferative drug development

2019

Tubulins and microtubules (MTs) represent targets for taxane-based chemotherapy. To date, several lines of evidence suggest that effectiveness of compounds binding tubulin often relies on different post-translational modifications on tubulins. Among them, methylation was recently associated to drug resistance mechanisms impairing taxanes binding. The sea urchin is recognized as a research model in several fields including fertilization, embryo development and toxicology. To date, some &alpha

Sea urchinPRMTSettore BIO/11 - Biologia MolecolareDrug actionmacromolecular substancesBiologyCatalysisCatalysilcsh:ChemistryInorganic ChemistryMicrotubuleArginine methylationTubulinbiology.animalGene familyPhysical and Theoretical ChemistrySea urchinlcsh:QH301-705.5Molecular BiologySpectroscopyEchinodermechinodermsOrganic ChemistryEmbryoComputer Science Applications1707 Computer Vision and Pattern RecognitionGeneral MedicineMethylationComputer Science ApplicationsCell biologyTubulinDrug developmentlcsh:Biology (General)lcsh:QD1-999embryonic structuresbiology.proteinPost-translational modification
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The colocalizations of pulp neural stem cells markers with dentin matrix protein-1, dentin sialoprotein and dentin phosphoprotein in human denticle (…

2021

Abstract Background The primary dentin, secondary dentin, and reactive tertiary dentin are formed by terminal differentiated odontoblasts, whereas atubular reparative tertiary dentin is formed by odontoblast-like cells. Odontoblast-like cells differentiate from pulpal stem cells, which express the neural stem cell markers nestin, S100β, Sox10, and P0. The denticle (pulp stone) is an unique mineralized extracellular matrix that frequently occurs in association with the neurovascular structures in the dental pulp. However, to date, the cellular origin of denticles in human dental pulp is unclear. In addition, the non-collagenous extracellular dentin matrix proteins dentin matrix protein 1 (DM…

SialoglycoproteinsMatrix (biology)Neural Stem Cellsstomatognathic systemDentinmedicineHumansDental PulpExtracellular Matrix ProteinsOdontoblastsChemistryCell DifferentiationGeneral MedicinePhosphoproteinsDentin phosphoproteinDMP1Cell biologystomatognathic diseasesmedicine.anatomical_structureDentinal TubuleOdontoblastDentinDental Pulp CalcificationPulp (tooth)AnatomyDentin sialoproteinDevelopmental BiologyAnnals of Anatomy - Anatomischer Anzeiger
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The adaptation of mechanically softened gutta-percha to the canal walls in the presence or absence of smear layer: a scanning electron microscopic st…

1995

Summary The objective of this study was to compare the adaptation of mechanically softened gutta-percha to the root canal wall in the presence and absence of smear layer. The root canals of 20 freshly extracted human maxillary incisors were cleaned and shaped. Prior to obturation, 10 root canals were irrigated with 20 ml of 50% citric acid followed by 20 ml of 5.25% sodium hypochlorite. All canals were obturated with mechanical compaction of gutta-percha and AH-26 sealer. After 72h, each tooth was fractured in half. Scanning electron microscopy demonstrated that the sealer had formed a continuous layer in contact with the canal walls, becoming progressively thinner towards the apex. The sea…

SilverMaterials scienceScanning electron microscopeRoot canalSmear layerDentistryRoot Canal Filling Materialschemistry.chemical_compoundstomatognathic systemRoot Canal ObturationmedicineHumansMethenamineGeneral DentistryTitaniumRoot Canal ObturationbiologyEpoxy Resinsbusiness.industryDental Marginal AdaptationGutta-perchabiology.organism_classificationDrug Combinationsmedicine.anatomical_structureDentinal TubulechemistrySmear LayerSodium hypochloriteDentinMicroscopy Electron ScanningDental Pulp CavityGutta-PerchabusinessBismuthLayer (electronics)Root Canal PreparationInternational Endodontic Journal
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Design and synthesis of pironetin analogue/colchicine hybrids and study of their cytotoxic activity and mechanisms of interaction with tubulin

2014

We here report the synthesis of a series of 12 hybrid molecules composed of a colchicine moiety and a pironetin analogue fragment. The two fragments are connected through an ester-amide spacer of variable length. The cytotoxic activities of these compounds and their interactions with tubulin have been investigated. Relations between the structure and activity are discussed. Since the spacer is not long enough to permit a simultaneous binding of the hybrid molecules to the colchicine and pironetin sites on tubulin, a further feature investigated was whether these molecules would interact with the latter through the pironetin end (irreversible covalent binding) or through the colchicine end (…

StereochemistryChemical structureCellsFluorescent Antibody TechniqueAntineoplastic AgentsLigandsMicrotubulespironetinStructure-Activity Relationshipchemistry.chemical_compoundChemical structureTubulinNeoplasmsDrug DiscoveryTumor Cells CulturedHumansColchicineMoietyMoleculeStructure–activity relationshipBinding siteCell ProliferationPharmacologyBinding SitesDrug effectsMolecular StructurebiologyToxicityCell growthMoleculesTubulinchemistryPyronesDrug Designbiology.proteinMolecular MedicineColchicineJournal of Medicinal Chemistry
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Synthesis and biological evaluation of 2-(3',4',5'-trimethoxybenzoyl)-3-N,N-dimethylamino benzo[b]furan derivatives as inhibitors of tubulin polymeri…

2008

Molecules that target microtubules have an important role in the treatment of cancer. A new class of inhibitors of tubulin polymerization based on the 2-(3,4,5-trimethoxybenzoyl)-2-dimethylamino-benzo[b]furan molecular skeleton was synthesized and evaluated for antiproliferative activity, inhibition of tubulin polymerization, and cell cycle effects. The most promising compound in this series was 2-(3,4,5-trimethoxybenzoyl)-3-dimethylamino-6-methoxy-benzo[b]furan, which inhibits cancer cell growth at nanomolar concentrations and interacts strongly with tubulin by binding to the colchicine site.

StereochemistryClinical BiochemistryPharmaceutical Sciencemacromolecular substancesAntimitotic AgentsBiochemistryChemical synthesisArticlechemistry.chemical_compoundInhibitory Concentration 50MiceStructure-Activity RelationshipMicrotubuleFuranCell Line TumorDrug Discoverypolycyclic compoundsTumor Cells CulturedStructure–activity relationshipAnimalsHumansMolecular BiologyBenzofuransCell ProliferationCombretastatin A-4biologyTubulin ModulatorsOrganic ChemistryTubulin ModulatorsTubulinchemistrybiology.proteinMolecular MedicineBioisostereProtein Binding
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Water-soluble isoindolo[2,1-a]quinoxalin-6-imines: In vitro antiproliferative activity and molecular mechanism(s) of action

2015

Abstract Water-soluble isoindoloquinoxalin (IIQ) imines and the corresponding acetates were conveniently prepared from the key intermediates 2-(2′-aminophenyl)-2H-isoindole-1-carbonitriles obtained by a Strecker reaction between substituted 1,2-dicarbaldehydes and 1,2-phenylenediamines. Both series were screened by the National Cancer Institute (Bethesda, MD) and showed potent antiproliferative activity against a panel of 60 human tumor cell lines. Several of the novel compounds showed GI50 values at a nanomolar level on the majority of the tested cell lines. Among IIQ derivatives, methoxy substituents at positions 3 and 8 or/and 9 were especially effective in impairing cell cycle progressi…

StereochemistryStrecker amino acid synthesisAntineoplastic AgentsApoptosisIsoindolo[21-a]quinoxalin-6-imineTopoisomerase I inhibitorsTopoisomerase-I InhibitorMicrotubulesTubulinCell Line TumorQuinoxalinesDrug DiscoveryHumansCytotoxic T cellCell ProliferationPharmacologyTopoisomerase I inhibitorChemistryAntitubulin agents; G-quadruplex interaction; Isoindolo[2; 1-a]quinoxalin-6-imines; Topoisomerase I inhibitors; Drug Discovery3003 Pharmaceutical Science; Organic Chemistry; PharmacologyAntitubulin agentsDrug Discovery3003 Pharmaceutical ScienceCell CycleOrganic ChemistryWaterGeneral MedicineSettore CHIM/08 - Chimica FarmaceuticaIn vitroTelomereAntitubulin agentAntitubulin agents; G-quadruplex interaction; Isoindolo[21-a]quinoxalin-6-imines; Topoisomerase I inhibitors; Drug Discovery3003 Pharmaceutical Science; Organic Chemistry; Pharmacology1-a]quinoxalin-6-iminesDNA Topoisomerases Type ISolubilityBiochemistryCell cultureApoptosisIsoindolo[2Cancer cellIminesG-quadruplex interactionDrug Screening Assays Antitumor
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Functionalized lipid tubules as tools for helical crystallization of proteins

1997

The development of functional supramolecular devices built by self-assembly of elementary molecules and with bioactive properties arouses considerable interest in the field of nanotechnology and new materials. We report here the formation of a new class of lipid tubules exhibiting both properties of molecular recognition and crystal formation for the protein streptavidin. These lipid tubules, made of biotin-containing dioctadecylamine molecules, are straight hollow cylinders with a constant diameter of 27 nm and variable length up to several micrometers. They are unilamellar with an inner diameter of about 16 nm, as shown by cryoelectron microscopy. Streptavidin binds to the biotinylated tu…

StreptavidinliposomesSupramolecular chemistryTWO-DIMENSIONAL CRYSTALSMEMBRANESCatalysisACETYLCHOLINE-RECEPTORVESICLESlipidschemistry.chemical_compoundTOXIN B-SUBUNITMolecular recognition2-DIMENSIONAL CRYSTALLIZATIONELECTRON-MICROSCOPYLiposomeChemistryVesicleOrganic Chemistrytechnology industry and agricultureCHOLERA-TOXINGeneral ChemistryCrystallographyMembranehelical structuresRESOLUTIONBiotinylationSelf-assemblyself-assembly tubulesMICROSTRUCTURESChemistry – A European Journal
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Topotecan triggers apoptosis in p53-deficient cells by forcing degradation of XIAP and survivin thereby activating caspase-3-mediated Bid cleavage.

2009

The topoisomerase I inhibitor topotecan (TPT) is used in the therapy of different tumors including high-grade gliomas. We previously showed that TPT-induced apoptosis depends on p53 with p53 wild-type (wt) cells being more resistant because of p53-controlled degradation of topoisomerase I. Here, we show that p53-deficient (p53(-/-)) fibroblasts undergo excessive mitochondrial apoptosis featuring H2AX phosphorylation, Bcl-x(L) decline, cytochrome c release, caspase-9/-3/-2 activation, and cleavage of Bid. In wt and apaf-1(-/-) cells, caspase-2 did not become activated and Bid was not cleaved. In addition, p53(-/-) cells cotreated with TPT and caspase-3 inhibitor showed neither caspase-2 acti…

SurvivinBlotting WesternDown-RegulationCaspase 3ApoptosisX-Linked Inhibitor of Apoptosis ProteinBiologyTopoisomerase-I InhibitorInhibitor of apoptosisTransfectionInhibitor of Apoptosis ProteinsHistonesMiceCell Line TumorSurvivinAnimalsHumansPhosphorylationRNA Small InterferingPharmacologyMice KnockoutCaspase 3Caspase 2TransfectionFibroblastsFlow CytometryMolecular biologyXIAPMice Inbred C57BLRepressor ProteinsApoptotic Protease-Activating Factor 1ApoptosisCancer researchMolecular MedicineApoptosomeTopoisomerase I InhibitorsTumor Suppressor Protein p53TopotecanMicrotubule-Associated ProteinsBH3 Interacting Domain Death Agonist ProteinThe Journal of pharmacology and experimental therapeutics
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