Search results for "carrier protein"

showing 10 items of 361 documents

Growth phase-dependent regulation of nuoA-N expression in Escherichia coli K-12 by the Fis protein: upstream binding sites and bioenergetic significa…

2000

The expression of the nuoA-N operon of Escherichia coli K-12, which encodes the proton-pumping NADH dehydrogenase I is modulated by growth phase-dependent regulation. Under respiratory growth conditions, expression was stimulated in early exponential, and to a lesser extent in late exponential and stationary growth phases. The stimulation in the early exponential growth phase was not observed in fis mutants, which are deficient for the growth phase-responsive regulator Fis. Neither the alternative sigma factor RpoS nor the integration host factor (IHF) are involved in growth phase-dependent regulation of this operon. When incubated with nuo promoter DNA, isolated Fis protein formed three re…

DNA BacterialIntegration Host FactorsOperonMutantMolecular Sequence DataBiologymedicine.disease_causeExponential growthBacterial ProteinsFactor For Inversion Stimulation ProteinOperonGeneticsmedicineEscherichia coliBinding sitePromoter Regions GeneticMolecular BiologyEscherichia coliBinding SitesBase SequenceEscherichia coli ProteinsDNase-I FootprintingPromoterMolecular biologyCarrier ProteinsrpoSMoleculargeneral genetics : MGG
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Identification of a third secondary carrier (DcuC) for anaerobic C4-dicarboxylate transport in Escherichia coli: roles of the three Dcu carriers in u…

1996

In Escherichia coli, two carriers (DcuA and DcuB) for the transport of C4 dicarboxylates in anaerobic growth were known. Here a novel gene dcuC was identified encoding a secondary carrier (DcuC) for C4 dicarboxylates which is functional in anaerobic growth. The dcuC gene is located at min 14.1 of the E. coli map in the counterclockwise orientation. The dcuC gene combines two open reading frames found in other strains of E. coli K-12. The gene product (DcuC) is responsible for the transport of C4 dicarboxylates in DcuA-DcuB-deficient cells. The triple mutant (dcuA dcuB dcuC) is completely devoid of C4-dicarboxylate transport (exchange and uptake) during anaerobic growth, and the bacteria are…

DNA BacterialMutantMolecular Sequence DataBiologymedicine.disease_causeMicrobiologyGene productBacterial ProteinsmedicineEscherichia coliDicarboxylic AcidsAmino Acid SequenceAnaerobiosisMolecular BiologyEscherichia coliPeptide sequenceGeneDicarboxylic Acid TransportersBase SequenceSequence Homology Amino AcidEscherichia coli ProteinsChromosome MappingBiological Transportbiology.organism_classificationIsoenzymesOpen reading frameMutagenesis InsertionalBiochemistryC4-dicarboxylate transportCarrier ProteinsBacteriaResearch ArticleJournal of bacteriology
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The long-term cytoskeletal rearrangement induced by rabbit enteropathogenic Escherichia coli is Esp dependent but intimin independent.

1999

Attaching and effacing rabbit enteropathogenic Escherichia coli (REPEC) of the O103 serogroup adhere diffusely on HeLa cells and trigger a slow progressive cytopathic effect (CPE) characterized by the recruitment of vinculin and the assembly of actin stress fibres. In contrast to REPEC O103, the reference human EPEC strain E2348/69 is unable to trigger the CPE. In this study, we have shown first that the fimbrial adhesin AF/R2, which mediates the diffuse adhesion of REPEC O103, was not sufficient to induce the CPE capability upon E2348/69. Non-polar mutants of REPEC O103 for espA, espB, espD and eae were then constructed. The four mutants were unable to induce attaching and effacing lesions…

DNA BacterialMutantMolecular Sequence DataMicrobiologyBacterial AdhesionMicrobiology03 medical and health sciencesBacterial ProteinsEscherichia coliAnimalsHumansEnteropathogenic Escherichia coliCytoskeletonAdhesins BacterialMolecular Biology[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyActinCytoskeleton030304 developmental biologyIntiminCytopathic effect0303 health sciencesAdhesins Escherichia colibiologyBase Sequence030306 microbiologyEscherichia coli ProteinsGenetic Complementation TestREARRANGEMENTbiochemical phenomena metabolism and nutritionVinculinBacterial adhesin[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyGenes Bacterialbiology.proteinRabbitsCarrier ProteinsBacterial Outer Membrane ProteinsHeLa CellsMolecular microbiology
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Myosin VIIa, harmonin and cadherin 23, three Usher I gene products that cooperate to shape the sensory hair cell bundle

2002

Deaf-blindness in three distinct genetic forms of Usher type I syndrome (USH1) is caused by defects in myosin VIIa, harmonin and cadherin 23. Despite being critical for hearing, the functions of these proteins in the inner ear remain elusive. Here we show that harmonin, a PDZ domain-containing protein, and cadherin 23 are both present in the growing stereocilia and that they bind to each other. Moreover, we demonstrate that harmonin b is an F-actin-bundling protein, which is thus likely to anchor cadherin 23 to the stereocilia microfilaments, thereby identifying a novel anchorage mode of the cadherins to the actin cytoskeleton. Moreover, harmonin b interacts directly with myosin VIIa, and i…

DNA ComplementaryCadherin Related ProteinsCell Cycle Proteinsmacromolecular substancesMyosinsBiologyTransfectionMicrofilamentGeneral Biochemistry Genetics and Molecular BiologyCell LineMiceCDH23Two-Hybrid System TechniquesHair Cells Auditoryotorhinolaryngologic diseasesmedicineAnimalsHumansProtein IsoformsRats WistarMolecular BiologyActinAdaptor Proteins Signal TransducingGene LibraryGeneral Immunology and MicrobiologyCadherinGeneral NeuroscienceStereociliaDyneinsCell DifferentiationArticlesCadherinsActin cytoskeletonActinsProtein Structure TertiaryRatsCell biologyCytoskeletal ProteinsMicroscopy Electronmedicine.anatomical_structureMicroscopy FluorescenceMyosin VIIasense organsCarrier ProteinsTip linkPCDH15HeLa CellsProtein BindingThe EMBO Journal
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Key Disulfide Bonds in an Insect Hormone Binding Protein: cDNA Cloning of a Juvenile Hormone Binding Protein of Heliothis virescens and Ligand Bindin…

1995

The hemolymph juvenile hormone binding protein (JHBP) from the early fifth instar larvae of Heliothis virescens (Lepidoptera, Noctuidae) has been purified, and three cDNA clones for this protein have been isolated from a fat body cDNA library constructed in bacteriophage λZAP XR. The deduced amino acid sequence of the full-length clone predicts a mature protein consisting of 224 residues, a molecular mass of 24 976 Da, and a p/ of 5.29. Comparison of the amino acid sequence to that of the previously described JHBP from Manduca sexta shows 51 % overall identity with highly conserved N- and C-terminal regions. One of the three clones bound photoactivatable analogs of juvenile hormones with mu…

DNA ComplementaryPhotochemistryphenylalanineMolecular Sequence DataMutantcomplementary DNAMothsBiochemistryHemolymphComplementary DNAAnimalsAmino Acid SequenceDisulfidesCloning MolecularcysteinePeptide sequencehormone binding proteinhormone analogHormone binding proteinBase SequencePhotoaffinity labelingMolecular massjuvenile hormoneChemistrycDNA libraryAffinity LabelsMolecular biologyJuvenile HormonesBiochemistryLarvaJuvenile hormoneMutagenesis Site-DirectedInsect ProteinsalanineCarrier ProteinsBiochemistry
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Identification of fatty acid binding proteins as markers associated with the initiation and/or progression of renal cell carcinoma

2005

Renal cell carcinoma (RCC) representing the most common neoplasia of the kidney in Western countries is a histologic diverse disease with an often unpredictable course. The prognosis of RCC is worsened with the onset of metastasis, and the therapies currently available are of limited success for the treatment of metastatic RCC. Although gene expression analyses and other methods are promising tools clarifying and standardizing the pathological classification of RCC, novel innovative molecular markers for the diagnosis, prognosis, and for the monitoring of this disease during therapy as well as potential therapeutic targets are urgently needed. Using proteome-based strategies, a number of RC…

DiseaseBiologyFatty Acid-Binding ProteinsKidneyurologic and male genital diseasesmedicine.disease_causeBiochemistryMetastasisReference ValuesRenal cell carcinomaCell Line TumorBiomarkers TumormedicineCarcinomaHumansElectrophoresis Gel Two-DimensionalUrotheliumCarcinoma Renal CellneoplasmsMolecular BiologyDNA PrimersKidneyReverse Transcriptase Polymerase Chain ReactionPrognosismedicine.diseaseImmunohistochemistryKidney Neoplasmsfemale genital diseases and pregnancy complicationsGene Expression Regulation Neoplasticmedicine.anatomical_structureImmunologyDisease ProgressionCancer researchUrotheliumCarrier ProteinsCarcinogenesisKidney diseasePROTEOMICS
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Mpdz is a quantitative trait gene for drug withdrawal seizures

2004

Physiological dependence and associated withdrawal episodes can constitute a powerful motivational force that perpetuates drug use and abuse. Using robust behavioral models of drug physiological dependence in mice, positional cloning, and sequence and expression analyses, we identified an addiction-relevant quantitative trait gene, Mpdz. Our findings provide a framework to define the protein interactions and neural circuit by which this gene's product (multiple PDZ domain protein) affects drug dependence, withdrawal and relapse.

DrugGenotypePositional cloningmedia_common.quotation_subjectMolecular Sequence DataQuantitative Trait LociPDZ domainGene ExpressionQuantitative trait locusBiologyProtein–protein interactionMiceMice CongenicDrug withdrawalSeizuresmedicineAnimalsGenetic Predisposition to DiseaseCloning MolecularGenemedia_commonGeneticsBehavior AnimalEthanolGeneral NeuroscienceChromosome MappingMembrane ProteinsEmbryo Mammalianmedicine.diseaseSubstance Withdrawal SyndromeMice Inbred C57BLCarrier ProteinsNeuroscienceNature Neuroscience
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Polymer therapeutics—polymers as drugs, drug and protein conjugates and gene delivery systems: Past, present and future opportunities

2006

As the 21st century begins we are witnessing a paradigm shift in medical practice. Whereas the use of polymers in biomedical materials applications, for example as prostheses, medical devices, cont...

Drugchemistry.chemical_classificationPolymersbusiness.industrymedia_common.quotation_subjectPharmaceutical ScienceMedical practiceNanotechnologyGenetic TherapyPolymerModels TheoreticalPharmacologyGene deliveryTransfectionDrug Delivery SystemsPharmaceutical PreparationschemistryHumansMedicineCarrier Proteinsbusinessmedia_commonJournal of Drug Targeting
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Mechanism of the Citrate Transporters in Carbohydrate and Citrate Cometabolism in Lactococcus and Leuconostoc Species

1998

ABSTRACT Citrate metabolism in the lactic acid bacterium Leuconostoc mesenteroides generates an electrochemical proton gradient across the membrane by a secondary mechanism (C. Marty-Teysset, C. Posthuma, J. S. Lolkema, P. Schmitt, C. Divies, and W. N. Konings, J. Bacteriol. 178:2178–2185, 1996). Reports on the energetics of citrate metabolism in the related organism Lactococcus lactis are contradictory, and this study was performed to clarify this issue. Cloning of the membrane potential-generating citrate transporter (CitP) of Leuconostoc mesenteroides revealed an amino acid sequence that is almost identical to the known sequence of the CitP of Lactococcus lactis . The cloned gene was exp…

EXPRESSIONLactococcusMolecular Sequence DataApplied Microbiology and BiotechnologyCitric AcidMicrobiologyACID BACTERIAchemistry.chemical_compoundBacterial ProteinsNUCLEOTIDE-SEQUENCELactococcusLeuconostocAmino Acid SequenceCloning MolecularElectrochemical gradientchemistry.chemical_classificationEcologybiologySymportersLACTATE EFFLUXLactococcus lactisfood and beveragesMETABOLIC ENERGYMembrane transportHydrogen-Ion Concentrationbiology.organism_classificationENERGY GENERATIONLACTIS BIOVAR DIACETYLACTISAmino acidchemistryBiochemistryLeuconostoc mesenteroidesESCHERICHIA-COLIFood MicrobiologyCarbohydrate MetabolismbacteriaKLEBSIELLA-PNEUMONIAECitric acidCarrier ProteinsLeuconostocFood ScienceBiotechnologyMEMBRANE-VESICLESApplied Environmental Microbiology
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Innate immunity but not NLRP3 inflammasome activation correlates with severity of stable COPD.

2014

Background In models of COPD, environmental stressors induce innate immune responses, inflammasome activation and inflammation. However, the interaction between these responses and their role in driving pulmonary inflammation in stable COPD is unknown. Objectives To investigate the activation of innate immunity and inflammasome pathways in the bronchial mucosa and bronchoalveolar lavage (BAL) of patients with stable COPD of different severity and control healthy smokers and non-smokers. Methods Innate immune mediators (interleukin (IL)-6, IL-7, IL-10, IL-27, IL-37, thymic stromal lymphopoietin (TSLP), interferon γ and their receptors, STAT1 and pSTAT1) and inflammasome components (NLRP3, NA…

EXPRESSIONMaleINTERLEUKIN-6InflammasomesCOPD PathologyChronic Obstructive Pulmonary DiseaseRespiratory SystemImmunity NLRP3 COPDBronchiReceptors Cell SurfaceRespiratory MucosaPULMONARYInterferon-gammaPulmonary Disease Chronic ObstructiveMARKERSThymic Stromal LymphopoietinSPUTUMNLR Family Pyrin Domain-Containing 3 ProteinCytokine Receptor gp130Humans1506HMGB1 ProteinAdaptor Proteins Signal TransducingAgedScience & TechnologyRECEPTORInterleukinsSmoking1103 Clinical SciencesMiddle AgedInterleukin-1 Receptor-Like 1 ProteinImmunity InnateInnate Immunityrespiratory tract diseasesANTIINFLAMMATORY CYTOKINESTAT1 Transcription FactorCase-Control StudiesT-CELLSASTHMACytokinesFemaleCOPD Pathology Innate ImmunityCarrier ProteinsLife Sciences & BiomedicineBronchoalveolar Lavage FluidSMOKERSThorax
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