Search results for "carrier protein"

showing 10 items of 361 documents

Binding of 11-cis retinaldehyde to the partially purified cellular retinaldehyde binding protein from bovine retinal pigment epithelium.

1987

11-cis retinaldehyde binding analysis was performed on a bovine retinal pigment epithelium preparation of cellular retinaldehyde binding protein (CRALBP), whose purity degree was estimated as 75%. Equilibrium binding studies were carried out measuring the replacement of tritium-labeled with unlabeled 11-cis retinaldehyde at 25 degrees C. Analysis of the experimental data both by a direct curve-fitting procedure utilizing a non linear least square regression analysis and by a conventional Scatchard plot revealed a single non-interacting binding site with an apparent equilibrium constant of 0.9 X 10(-7) M. A binding stoichiometry of approximately 1 mol of 11-cis retinaldehyde/mol of binding p…

Apparent Equilibrium ConstantBiologyBinding CompetitiveCellular and Molecular Neurosciencechemistry.chemical_compoundRetinoidsmedicineAnimalsBinding sitePigment Epithelium of EyeMolecular BiologyPharmacologyRetinaRetinal pigment epitheliumBinding proteinRetinalCell BiologyKineticsmedicine.anatomical_structureBiochemistrychemistryCELLULAR RETINALDEHYDE-BINDING PROTEINRetinaldehydeRetinaldehydeMolecular MedicineCattleCarrier ProteinsExperientia
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Fasciola spp: Mapping of the MF6 epitope and antigenic analysis of the MF6p/HDM family of heme-binding proteins

2017

MF6p/FhHDM-1 is a small cationic heme-binding protein which is recognized by the monoclonal antibody (mAb) MF6, and abundantly present in parenchymal cells and secreted antigens of Fasciola hepatica. Orthologs of this protein (MF6p/HDMs) also exist in other causal agents of important foodborne trematodiasis, such as Clonorchis sinensis, Opisthorchis viverrini and Paragonimus westermani. Considering that MF6p/FhHDM-1 is relevant for heme homeostasis in Fasciola and was reported to have immunomodulatory properties, this protein is expected to be a useful target for vaccination. Thus, in this study we mapped the epitope recognized by mAb MF6 and evaluated its antigenicity in sheep. The sequenc…

0301 basic medicineParagonimus westermaniFasciola sppPhysiologyProtein ConformationFlatwormslcsh:MedicineProtein Structure PredictionBiochemistryEpitopeAntigenicEpitopes0302 clinical medicineAnimal CellsImmune PhysiologyMedicine and Health SciencesMacromolecular Structure AnalysisMF6p/HDMEnzyme-Linked Immunoassayslcsh:ScienceMammalsNeuronsImmune System ProteinsMultidisciplinaryFasciolabiologyVaccinationEukaryotaAntibodies MonoclonalRuminantsDendritic StructureVertebratesCellular TypesAntibodyResearch ArticleHemeproteinsProtein StructureAntigenicityFascioliasisHeme bindingImmunology030231 tropical medicineAntibodies HelminthEnzyme-Linked Immunosorbent AssayHemeResearch and Analysis MethodsTrematodesAntibodiesHeme-Binding Proteins03 medical and health sciencesHelminthsparasitic diseasesParasitic DiseasesFasciola hepaticaAnimalsImmunoassaysMolecular BiologySheeplcsh:ROrganismsBiology and Life SciencesProteinsCell BiologyDendritesNeuronal DendritesFasciola hepaticabiology.organism_classificationInvertebratesMolecular biologyFasciola030104 developmental biologyEpitope mappingCellular NeuroscienceAntigens HelminthAmniotesImmunologic Techniquesbiology.proteinlcsh:QCarrier ProteinsEpitope MappingNeuroscience
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Subcellular targeting of multiligand-binding protein gC1qR.

1999

Abstract gC1q receptor, a protein originally described as the cell surface receptor for the globular heads of complement factor C1q, has been found to bind human H-kininogen with high affinity and specificity. Therefore, gC1qR has been considered candidate kininogen docking site on the surfaces of platelets, neutrophils and endothelial cells. Recent work demonstrating that gC1qR is an intracellular protein that is tightly associated with mitochondria rather than targeted to the cell surface has challenged this view. To further probe cellular trafficking routes of gC1qR, we overexpressed human gC1qR in a mammalian cell and monitored cell surface exposure of recombinant gC1qR by virtue of its…

CellComplement factor IBiologyLigandsMitochondrial ProteinsCell surface receptormedicineAnimalsHumansBinding siteReceptorPharmacologyBinding SitesMembrane GlycoproteinsBinding proteinComplement C1qBiological TransportTransfectionMolecular biologyCell biologyReceptors Complementmedicine.anatomical_structureHyaluronan ReceptorsCell cultureCOS CellsCarrier ProteinsProtein Processing Post-Translationalcirculatory and respiratory physiologySubcellular FractionsImmunopharmacology
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Human kininogens interact with M protein, a bacterial surface protein and virulence determinant.

1995

Streptococcus pyogenes, the most significant streptococcal species in clinical medicine, expresses surface proteins with affinity for several human plasma proteins. Here we report that kininogens, the precursors to the vasoactive kinins, bind to the surface of S. pyogenes. M protein, a surface molecule and a major virulence factor-in these bacteria, occurs in > 80 different serotypes. Among 49 strains of S. pyogenes, all of different M serotypes, 41 bound radiolabelled kininogens, whereas 6 M protein-negative mutant strains showed no affinity. M protein of most serotypes bind fibrinogen, and among the 55 strains tested, binding of kininogens was closely correlated to fibrinogen bindi…

Kininogen bindingMyeloma proteinStreptococcus pyogenesM1 proteinMolecular Sequence DataEnzyme-Linked Immunosorbent Assaymedicine.disease_causeBiochemistryPeptide MappingAntibodiesBacterial ProteinsmedicineHumansAmino Acid SequenceBinding siteMolecular BiologyKininogenAntigens BacterialBinding SitesbiologyVirulenceKininogensFibrinogen bindingFibrinogenCell BiologyLow-molecular-weight kininogenMolecular biologyStreptococcus pyogenesbiology.proteinCarrier Proteinscirculatory and respiratory physiologyResearch ArticleBacterial Outer Membrane ProteinsProtein Binding
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A lipid transfer protein binds to a receptor involved in the control of plant defence responses

2001

AbstractLipid transfer proteins (LTPs) and elicitins are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defence mechanisms, the biological function of LTP is still an enigma. We show that a wheat LTP1 binds with high affinity sites. Binding and in vivo competition experiments point out that these binding sites are common to LTP1 and elicitins and confirm that they are the biological receptors of elicitins. A mathematical analysis suggests that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits.

Models Molecular0106 biological sciencesTime FactorsProtein ConformationPlasma protein bindingLigands01 natural sciencesBiochemistryProtein structureStructural BiologyReceptorAllosteryTriticumComputingMilieux_MISCELLANEOUSPlant Proteins0303 health sciencesFungal proteinfood and beveragesCell biologyBiochemistryPlant lipid transfer proteinsAllosteric SiteProtein BindingReceptorPhytophthoraLipid transfer proteinAllosteric regulationBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding CompetitiveFungal Proteins03 medical and health sciencesTobaccoGeneticsBinding site[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular Biology030304 developmental biologyBinding SitesDose-Response Relationship DrugAlgal ProteinsCell MembraneElicitinCell BiologyAntigens PlantModels TheoreticalLipid MetabolismElicitinCarrier Proteins010606 plant biology & botanyFEBS Letters
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Human cationic amino acid transporter hCAT-3 is preferentially expressed in peripheral tissues.

2001

At least five distinct carrier proteins form the family of mammalian cationic amino acid transporters (CATs). We have cloned a cDNA containing the complete coding region of human CAT-3. hCAT-3 is glycosylated and localized to the plasma membrane. Transport studies in Xenopus laevis oocytes revealed that hCAT-3 is selective for cationic L-amino acids and exhibits a maximal transport activity similar to other CAT proteins. The apparent substrate affinity and sensitivity to trans-stimulation of hCAT-3 resembles most closely hCAT-2B. This is in contrast to rat and murine CAT-3 proteins that have been reported to display a very low activity and to be inhibited by neutral and anionic L-amino acid…

MaleDNA ComplementaryGene ExpressionThymus GlandIn Vitro TechniquesBiochemistryCell LineMiceXenopus laevisComplementary DNACoding regionAnimalsHumansTissue DistributionAmino acid transporterAmino Acid SequenceCationic Amino Acid Transporterschemistry.chemical_classificationCATSBase SequenceChemistryCationic polymerizationBrainMembrane ProteinsAmino acidRatsBiochemistryCarrier proteinOocytesAmino Acid Transport Systems BasicFemaleCarrier ProteinsBiochemistry
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Molecular partners of hNOT/ALG3, the human counterpart of the Drosophila NOT and yeast ALG3 gene, suggest its involvement in distinct cellular proces…

2018

This study provides first insights into the involvement of hNOT/ALG3, the human counterpart of the Drosophila Neighbour of TID and yeast ALG3 gene, in various putative molecular networks. HNOT/ALG3 encodes two translated transcripts encoding precursor proteins differing in their N-terminus and showing 33% identity with the yeast asparagine-linked glycosylation 3 (ALG3) protein. Experimental evidence for the functional homology of the proteins of fly and man in the N-glycosylation has still to be provided. In this study, using the yeast two-hybrid technique we identify 17 molecular partners of hNOT-1/ALG3-1. We disclose the building of hNOT/ALG3 homodimers and provide experimental evidence f…

0301 basic medicineGlycosylationSaccharomyces cerevisiae ProteinsRNA-binding proteinSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumMannosyltransferases03 medical and health scienceschemistry.chemical_compoundCongenital Disorders of GlycosylationNeoplasmsNuclear Receptor Subfamily 4 Group A Member 2GeneticsAnimalsDrosophila ProteinsHumansMolecular BiologyTranscription factorOSBPGeneGenetics (clinical)Cellular compartmentEndoplasmic reticulumMembrane ProteinsRNA-Binding ProteinsGeneral MedicineLRP1Cell biology030104 developmental biologychemistryNerve DegenerationDrosophilaCarrier ProteinsHuman molecular genetics
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Altered lipid metabolism in a Drosophila model of Friedreich's ataxia

2010

13 páginas, 5 figuras.-- et al.

MaleAtaxiaCell SurvivalLipid Metabolism Disordersmedicine.disease_causeNervous SystemAnimals Genetically ModifiedLipid peroxidationchemistry.chemical_compoundDownregulation and upregulationIron-Binding ProteinsLipid dropletGeneticsmedicineAnimalsDrosophila ProteinsHumansMolecular BiologyGenetics (clinical)Membrane GlycoproteinsbiologyCélulas glialesFatty AcidsLipid metabolismArticlesGeneral MedicineCell biologyDisease Models AnimalOxidative Stressmedicine.anatomical_structurechemistryBiochemistryFriedreich AtaxiaFrataxinbiology.proteinNeurogliaDrosophilaLipid Peroxidationmedicine.symptomCarrier ProteinsNeurogliaOxidative stress
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Recurrence of pleomorphic adenoma of the parotid gland-predictive value of cadherin-11 and fascin

2008

The predictive value of cadherin-11, tenascin, fascin, and mucin-1 as markers for the likelihood of recurrence in pleomorphic adenoma of the parotid gland was examined. In this retrospective study we analysed 20 tumours from16 patients by immunohistochemistry. Staining intensities were measured using a semiquantitative scoring approach; localisation (tumour centre vs border) as well as clinical data were analysed and correlated with follow-up. Cadherin-11 was increased in recurrent tumours. However, no changes of fascin, tenascin or mucin-1 were observed. Cadherin-11 and fascin were increased in primary tumours of patients with later recurrence, with fascin upregulation restricted to the tu…

AdultMaleMicrobiology (medical)Pathologymedicine.medical_specialtyAdolescentAdenoma PleomorphicTenascinmacromolecular substancesPathology and Forensic MedicinePleomorphic adenomaDownregulation and upregulationBiomarkers TumormedicineHumansParotid GlandImmunology and AllergyRetrospective StudiesFascinbiologyCadherinMicrofilament ProteinsMucin-1MucinTenascinGeneral MedicineMiddle AgedCadherinsPrognosismedicine.diseaseImmunohistochemistryParotid NeoplasmsParotid glandmedicine.anatomical_structurebiology.proteinImmunohistochemistryFemaleNeoplasm Recurrence LocalCarrier ProteinsAPMIS
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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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