Search results for "Transporter"

showing 10 items of 676 documents

Real-Time RT-PCR assay to quantify the expression of fum1 and fum19 genes from the Fumonisin-producing Fusarium verticillioides

2007

Fumonisins are a group of mycotoxins produced by Fusarium species of the Gibberella fujikuroi species complex that contaminate food and feed products, and represent a risk for human and animal health. In this work, we have developed a specific real-time reverse transcription-PCR (RT-PCR) assay to quantify the level of expression of two genes of the fumonisin biosynthetic cluster in F. verticillioides: fum1 (that encodes a polyketide synthase enzyme) and the ABC transporter encoding gene fum19. The level of expression of both genes was compared with the amount of fumonisin B(1) (FB(1)), measured by HPLC, produced by several strains of F. verticillioides in liquid culture. The results indicat…

Microbiology (medical)FusariumbiologyReverse Transcriptase Polymerase Chain ReactionFungal geneticsfood and beveragesRNA Fungalbiology.organism_classificationFumonisinsMicrobiologyMicrobiologychemistry.chemical_compoundFusariumchemistryGene Expression Regulation FungalPolyketide synthaseGene expressionFumonisinbiology.proteinGibberella fujikuroiATP-Binding Cassette TransportersMycotoxinPolyketide SynthasesMolecular BiologyGeneJournal of Microbiological Methods
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Conversion of the Sensor Kinase DcuS to the Fumarate Sensitive State by Interaction of the Bifunctional Transporter DctA at the TM2/PAS

2021

The membrane-bound C4-dicarboxylate (C4DC) sensor kinase DcuS of Escherichia coli typically forms a protein complex with the C4DC transporter DctA. The DctA × DcuS complex is able to respond to C4DCs, whereas DcuS without DctA is in the permanent ON state. In DctA, the C-terminal helix 8b (H8b) serves as the site for interaction with DcuS. Here the interaction site in DcuS and the related structural and functional adaptation in DcuS were determined. The Linker connecting transmembrane helix 2 (TM2) and the cytosolic PASC (Per-ARNT-SIM) domain of DcuS, was identified as the major site for interaction with DctA-H8b by in vivo interaction studies. The Linker is known to convert the piston-type…

Microbiology (medical)QH301-705.5sensor complexsensor kinase DcuSmedicine.disease_causeMicrobiologyArticle03 medical and health scienceschemistry.chemical_compoundVirologymedicinestructural co-regulatorBiology (General)BifunctionalEscherichia coli030304 developmental biology0303 health sciences030306 microbiologyKinaseTransporterInteraction studiesTransmembrane domainchemistrybifunctional transporter DctAHelixBiophysicsLinkerMicroorganisms
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Transcriptional expression of selected genes associated with excretion of carboxylic acids from aci mutants of Saccharomyces cerevisiae

2013

Introduction: Saccharomyces cerevisiae is an excellent model organism for studies of transcriptional regulation of metabolic processes in other eukaryotic cells including human cells. Cellular acid-base balance can be disturbed in pathologic situations such as renal acidosis or cancer. The extracellular pH of malignant solid tumors is acidic in the range of 6.5-6.9. EG07 and EG37 aci mutants of Saccharomyces cerevisiae excessively excrete carboxylic acids to glucose-containing media or distilled water. The excreted acids are Krebs and/or glyoxylate cycle intermediates. The genes restoring the wild-type phenotype have function that does not easily explain theAci phenotype.Material/Methods: I…

Microbiology (medical)Transcriptional ActivationSaccharomyces cerevisiae ProteinsCarboxylic acidKrebs and glyoxylate cycleMutantSaccharomyces cerevisiaeCitric Acid CycleGlyoxylate cycleCarboxylic AcidsGene Expressionlcsh:MedicineSaccharomyces cerevisiaeBiologyaci mutantsSpecies SpecificityTranscriptional regulationHumansRNA MessengerGenechemistry.chemical_classificationacid transporterslcsh:RGlyoxylatesMembrane Transport ProteinsBiological Transportbiology.organism_classificationMolecular biologyPhenotypeCitric acid cycleProton-Translocating ATPasesInfectious DiseasesGlucoseBiochemistrychemistryMutationATP-Binding Cassette TransportersPostępy Higieny i Medycyny Doświadczalnej
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Blood-Brain-Barrier Models for the Investigation of Transporter- and Receptor-Mediated Amyloid-β Clearance in Alzheimers Disease

2010

Alzheimer's disease (AD) is the most common form of dementia in the elderly with more than 26 million people worldwide living with the disease. Besides the main neuropathological hallmarks of AD, provoked by the accumulation of amyloid-β (Aβ) and tau hyperphosphorylation, other cells and cellular systems such as microglia and the neurovascular unit establishing the blood-brain-barrier (BBB) have been implicated to play a role in AD etiopathology. Insulating the brain from the blood stream, the BBB facilitates supply and disposal of nutrients and metabolites by the expression of transporters and transcytotic receptors at the polarized endothelial cell (EC) surface. Recently, several proteins…

MicrogliaTransporterReceptor-mediated endocytosisBiologyBlood–brain barriermedicine.diseaseEndothelial stem cellmedicine.anatomical_structurenervous systemNeurologyIn vivomedicineDementiaNeurology (clinical)ReceptorNeuroscienceCurrent Alzheimer Research
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Modulation of P-glycoprotein activity by novel synthetic curcumin derivatives in sensitive and multidrug-resistant T-cell acute lymphoblastic leukemi…

2016

Abstract Background Multidrug resistance (MDR) and drug transporter P-glycoprotein (P-gp) represent major obstacles in cancer chemotherapy. We investigated 19 synthetic curcumin derivatives in drug-sensitive acute lymphoblastic CCRF–CEM leukemia cells and their multidrug-resistant P-gp-overexpressing subline, CEM/ADR5000. Material and methods Cytotoxicity was tested by resazurin assays. Doxorubicin uptake was assessed by flow cytometry. Binding modes of compounds to P-gp were analyzed by molecular docking. Chemical features responsible for bioactivity were studied by quantitative structure activity relationship (QSAR) analyses. A 7-descriptor QSAR model was correlated with doxorubicin uptak…

Models Molecular0301 basic medicineCurcuminCell SurvivalT cellQuantitative Structure-Activity RelationshipAntineoplastic AgentsPharmacologyPrecursor T-Cell Lymphoblastic Leukemia-LymphomaToxicologyFlow cytometry03 medical and health sciences0302 clinical medicineCell Line TumormedicineHumansDoxorubicinATP Binding Cassette Transporter Subfamily B Member 1CytotoxicityP-glycoproteinPharmacologybiologymedicine.diagnostic_testChemistrymedicine.diseaseDrug Resistance MultipleMultiple drug resistanceLeukemia030104 developmental biologymedicine.anatomical_structureDoxorubicinDrug Resistance NeoplasmCell culture030220 oncology & carcinogenesisbiology.proteinmedicine.drugToxicology and Applied Pharmacology
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Functional cysteine-less subunits of the transporter associated with antigen processing (TAP1 and TAP2) by de novo gene assembly

2002

AbstractWithin the adaptive immune system the transporter associated with antigen processing (TAP) plays a pivotal role in loading of peptides onto major histocompatibility (MHC) class I molecules. As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human TAP subunits by de novo gene synthesis, replacing all 19 cysteines in TAP1 and TAP2. After expression in TAP-deficient human fibroblasts, cysteine-less TAP1 and TAP2 are functional with respect to adenosine triphosphate (ATP)-dependent peptide transport and inhibition by ICP47 from herpes simplex virus. Cysteine-less TAP1 and TAP2 restore maturation and intracellular trafficking of MHC c…

Models MolecularBiophysicsBiological Transport ActiveBiologyMajor histocompatibility complexTransfectionBiochemistryCell Linechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyATP Binding Cassette Transporter Subfamily B Member 3Cysteine-scanning mutagenesisMHC class IGeneticsHumansCysteineATP Binding Cassette Transporter Subfamily B Member 2Molecular BiologyAntigen PresentationAntigen processingHistocompatibility Antigens Class ICell BiologyTransporter associated with antigen processingMolecular biologyRecombinant ProteinsCell biologyProtein SubunitschemistryAmino Acid SubstitutionAntigen processingPeptide transportMembrane proteinbiology.proteinAdenosine triphosphate-binding cassette transporterTAP2ATP-Binding Cassette TransportersTAP1Adenosine triphosphateFEBS Letters
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Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane.

2000

We have studied the membrane insertion of ProW, an Escherichia coli inner membrane protein with seven transmembrane segments and a large periplasmic N-terminal tail, into endoplasmic reticulum (ER)-derived dog pancreas microsomes. Strikingly, significant levels of N-tail translocation is seen only when a minimum of four of the transmembrane segments are present; for constructs with fewer transmembrane segments, the N-tail remains mostly nontranslocated and the majority of the molecules adopt an 'inverted' topology where normally nontranslocated parts are translocated and vice versa. N-tail translocation can also be promoted by shortening of the N-tail and by the addition of positively charg…

Models MolecularBioquímicaGlycosylationChromosomal translocationBiologyEndoplasmic ReticulumBiochemistryBacterial ProteinsMembranes (Biologia)MicrosomesEscherichia coliAnimalsInner membranePancreasMolecular BiologyEscherichia coli ProteinsEndoplasmic reticulumMembrane ProteinsSTIM1Periplasmic spaceCell BiologyMolecular biologyTransmembrane proteinCell biologyMembrane proteinMutationCatsMicrosomeATP-Binding Cassette TransportersProteïnesJournal of Biological Chemistry
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Cytotoxicity of Novel Sulfanilamides Towards Sensitive and Multidrugresistant Leukemia Cells

2014

Novel sulfa Schiff bases were synthesized and characterized by a reaction between aromatic sulfonamides and aromatic aldehydes or heterocyclic ketones in equimolar ratios. Their cytotoxicity was evaluated by the resazurin assay towards human sensitive CCRF-CEM and multidrug-resistant CEM/ADR5000 leukemia cells. Three of the tested compounds viz., 4-(anthracen-9-ylmethyleneamino)-N-(pyrimidin-2-yl)benzenesulfonamide (4), 4-(anthracen-9- ylmethyleneamino)benzenesulfonamide, (5) and 4-((3-phenylallylidene)amino)benzene-sulfonamide, (6) were cytotoxic (IC 50 values: 5.38-19.96 µM). CEM/ADR5000 cells were not cross-resistant to these compounds, indicating activity against otherwise drug-resistan…

Models MolecularCell SurvivalStereochemistryBiochemistrychemistry.chemical_compoundSulfanilamideCell Line TumorSulfanilamidesDrug DiscoverymedicineHumansCytotoxic T cellDoxorubicinATP Binding Cassette Transporter Subfamily B Member 1Homology modelingCytotoxicityPharmacologyLeukemiaChemistryOrganic ChemistryResazurinSulfanilamidemedicine.diseaseProtein Structure TertiaryLeukemiaDoxorubicinDrug Resistance NeoplasmMolecular MedicineVerapamilmedicine.drugCurrent Medicinal Chemistry
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Copper(II)-Induced Restructuring of ZnuD, a Zinc(II) Transporter from Neisseria meningitidis.

2019

Cluster 2 (288HDDDNAHAHTH298) from Neisseria meningitidis ZnuD is a flexible loop that captures zinc(II) ions, acting as a "fishing net". We describe its Zn(II) and Cu(II) binding capabilities, focusing on the thermodynamics of such interactions and comparing them with the complexes of the 1MAHHHHHHL9-NH2 region. Copper(II) complexes with the studied ZnuD regions are thermodynamically more stable than the zinc(II) ones-Cu(II) complexes dominate in solution even in close to physiological ratios of the studied metal ions (a 10-fold excess of Zn(II) over Cu(II)). While the binding of native Zn(II) has no significant impact on the structure of its transporter, Cu(II) binding induces a conformat…

Models MolecularConformational changeMetal ions in aqueous solutionchemistry.chemical_elementZincNeisseria meningitidis010402 general chemistry01 natural sciencesInorganic ChemistryBacterial ProteinsHumansProlineAmino Acid SequencePhysical and Theoretical ChemistryCation Transport ProteinsPolyproline helix010405 organic chemistryTransporterCopper0104 chemical sciencesMeningococcal InfectionsCrystallographyZincchemistryHelixThermodynamicsCopperProtein BindingInorganic chemistry
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The Nature of the Stimulus and of the Fumarate Binding Site of the Fumarate Sensor DcuS of Escherichia coli

2005

DcuS is a membrane-associated sensory histidine kinase of Escherichia coli specific for C(4) -dicarboxylates. The nature of the stimulus and its structural prerequisites were determined by measuring the induction of DcuS-dependent dcuB'-'lacZ gene expression. C(4)-dicarboxylates without or with substitutions at C2/C3 by hydrophilic (hydroxy, amino, or thiolate) groups stimulated gene expression in a similar way. When one carboxylate was replaced by sulfonate, methoxy, or nitro groups, only the latter (3-nitropropionate) was active. Thus, the ligand of DcuS has to carry two carboxylate or carboxylate/nitro groups 3.1-3.8 A apart from each other. The effector concentrations for half-maximal i…

Models MolecularMagnetic Resonance SpectroscopyHistidine KinaseRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeBiochemistryCitric AcidStructure-Activity Relationshipchemistry.chemical_compoundFumaratesEscherichia colimedicineDicarboxylic AcidsAmino Acid SequenceCarboxylatePhosphorylationBinding siteKinase activityTartratesMolecular BiologyEscherichia coliPeptide sequenceDicarboxylic Acid TransportersBinding SitesChemistryEscherichia coli ProteinsAutophosphorylationHistidine kinaseGene Expression Regulation BacterialCell BiologyNitro CompoundsPeptide FragmentsEnzyme ActivationLac OperonBiochemistryMutagenesis Site-DirectedPropionatesProtein KinasesSequence AlignmentBinding domainJournal of Biological Chemistry
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