Search results for "Recombinant protein"

showing 10 items of 707 documents

Alternate methods to prevent protease use as a masking agent in sport.

2010

Doping in SportsCommunicationProteasebusiness.industrymedicine.medical_treatmentPhysical Therapy Sports Therapy and RehabilitationUrinalysisRecombinant ProteinsHuman–computer interactionMedicineHumansOrthopedics and Sports MedicinebusinessErythropoietinMasking agentPeptide HydrolasesJournal of science and medicine in sport
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Molecular interaction of artemisinin with translationally controlled tumor protein (TCTP) of Plasmodium falciparum

2012

Malaria causes millions of death cases per year. Since Plasmodium falciparum rapidly develops drug resistance, it is of high importance to investigate potential drug targets which may lead to novel rational therapy approaches. Here we report on the interaction of translationally controlled tumor protein of P. falciparum (PfTCTP) with the anti-malarial drug artemisinin. Furthermore, we investigated the crystal structure of PfTCTP. Using mass spectrometry, bioinformatic approaches and surface plasmon resonance spectroscopy, we identified novel binding sites of artemisinin which are in direct neighborhood to amino acids 19-46, 108-134 and 140-163. The regions covered by these residues are know…

Drugmedia_common.quotation_subjectPlasmodium falciparumProtozoan ProteinsDrug resistanceBiologyCrystallography X-RayBiochemistryAntimalarialsparasitic diseasesTranslationally-controlled tumor proteinBiomarkers TumormedicineHumansComputer SimulationBinding siteArtemisininmedia_commonPharmacologychemistry.chemical_classificationBinding SitesMolecular StructureTumor Protein Translationally-Controlled 1Plasmodium falciparumSurface Plasmon Resonancebiology.organism_classificationArtemisininsRecombinant ProteinsAmino acidMolecular Docking SimulationchemistryBiochemistryFunction (biology)Protein Bindingmedicine.drugBiochemical Pharmacology
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Interferon-alpha 2a increases serum concentration of hyaluronic acid and type III procollagen aminoterminal propeptide in patients with chronic hepat…

1994

Interferon-alpha (IFN-alpha) has become an important drug for the treatment of chronic viral liver diseases. However, the action of IFN-alpha remains unclear. We investigated whether human recombinant IFN-alpha modulates serum concentrations of hyaluronic acid (HA) and type III procollagen aminoterminal propeptide (P-III-NP) in 56 patients with chronic hepatitis-B under IFN-alpha therapy. IFN-alpha increased the HA serum level in 44 of 46 patients and, after cessation of treatment, HA serum levels returned to the pretherapy levels. The increase of HA serum level was higher in patients with active cirrhosis (aC) than in patients with chronic persistent hepatitis (CPH) and in patients with se…

Drugmedicine.medical_specialtyCirrhosisPhysiologymedia_common.quotation_subjectBiopsyInterferon alpha-2Viruslaw.invention03 medical and health scienceschemistry.chemical_compound0302 clinical medicinelawInternal medicineHyaluronic acidMedicineHumansHyaluronic AcidProtein precursor030304 developmental biologymedia_commonHepatitis Chronic0303 health sciencesbusiness.industryGastroenterologyInterferon-alphaHepatologymedicine.diseaseHepatitis BPeptide FragmentsRecombinant Proteins3. Good healthProcollagen peptidaseEndocrinologychemistry030220 oncology & carcinogenesisImmunologyChronic DiseaseRecombinant DNAbusinessProcollagenFollow-Up StudiesDigestive diseases and sciences
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Atomic Structures of Two Novel Immunoglobulin-like Domain Pairs in the Actin Cross-linking Protein Filamin

2009

Filamins are actin filament cross-linking proteins composed of an N-terminal actin-binding domain and 24 immunoglobulin-like domains (IgFLNs). Filamins interact with numerous proteins, including the cytoplasmic domains of plasma membrane signaling and cell adhesion receptors. Thereby filamins mechanically and functionally link the cell membrane to the cytoskeleton. Most of the interactions have been mapped to the C-terminal IgFLNs 16–24. Similarly, as with the previously known compact domain pair of IgFLNa20–21, the two-domain fragments IgFLNa16–17 and IgFLNa18–19 were more compact in small angle x-ray scattering analysis than would be expected for two independent domains. Solution state NM…

EGF-like domainFilaminsMolecular Sequence DataMolecular ConformationImmunoglobulinsmacromolecular substancesPlasma protein bindingBiologyFilaminModels BiologicalBiochemistryCell membraneHAMP domain03 medical and health sciencesContractile Proteins0302 clinical medicineddc:570Cell AdhesionmedicineHumansScattering RadiationAmino Acid SequenceCytoskeletonCell adhesionMolecular BiologyCytoskeletonActin030304 developmental biology0303 health sciencesMicrofilament ProteinsCell BiologyActinsRecombinant ProteinsProtein Structure Tertiary3. Good healthCell biologyCross-Linking Reagentsmedicine.anatomical_structureProtein Structure and Folding030217 neurology & neurosurgeryProtein BindingJournal of Biological Chemistry
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A peptide inhibiting the collagen binding function of integrin alpha2I domain.

1999

Integrin alpha2 subunit forms in the complex with the beta1 subunit a cell surface receptor binding extracellular matrix molecules, such as collagens and laminin-1. It is a receptor for echovirus-1, as well. Ligands are recognized by the special "inserted" domain (I domain) in the integrin alpha2 subunit. Venom from a pit viper, Bothrops jararaca, has been shown to inhibit the interaction of platelet alpha2beta1 integrin with collagen because of the action of a disintegrin/metalloproteinase named jararhagin. The finding that crude B. jararaca venom could prevent the binding of human recombinant ralpha2I domain to type I collagen led us to study jararhagin further. Synthetic peptides represe…

EGF-like domainIntegrinIntegrin alpha2PeptideBiologyBiochemistryPeptides CyclicEuropiumAntigens CDCrotalid VenomsDisintegrinHumansAmino Acid SequenceMolecular BiologyRGD motifDNA Primerschemistry.chemical_classificationBase SequenceCell MembraneMetalloendopeptidasesCell BiologyCyclic peptideRecombinant ProteinsBiochemistrychemistryJararhaginbiology.proteinCollagenBinding domainThe Journal of biological chemistry
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Crystal structure of human gamma-butyrobetaine hydroxylase.

2010

Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0A resolution. The GBBH monomer consists of a catalytic double-stranded beta-helix (DBSH) domai…

EGF-like domainStereochemistrygamma-Butyrobetaine DioxygenaseBiophysicsDrug designBiochemistryHydroxylationchemistry.chemical_compoundDioxygenaseCatalytic DomainHumansEnzyme InhibitorsMolecular BiologyHistidinechemistry.chemical_classificationCrystallographybiologyActive siteCell BiologyRecombinant ProteinsZincEnzymeBiochemistrychemistryCyclic nucleotide-binding domainDrug Designbiology.proteinProtein MultimerizationMethylhydrazinesBiochemical and biophysical research communications
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Characterization of murine monoclonal antibodies against the Ro52 autoantigen

1997

SUMMARY Immunization of BALB/c mice with purified recombinant human Ro52 protein resulted in three anti-Ro52 MoAbs termed 2E7, 4C6 and 4F11. All anti-Ro52 MoAbs specifically reacted with recombinant human Ro52 protein, and also with Ro52 protein in total extracts of all human cell lines analysed, including the epithelial cell line HeLa, the B cell line Raji, the bladder carcinoma cell line RT112, and a fibroblast cell line derived from patients with xeroderma pigmentosum. The anti-Ro52 MoAbs were able to immunoprecipitate the recombinant human Ro52 protein expressed in wheat germ extract, but failed to precipitate hY RNAs from cell extracts. The staining pattern of the MoAbs strongly differ…

Editorial Reviewmedicine.drug_classMolecular Sequence DataImmunologyCellMonoclonal antibodyAutoantigensEpitopelaw.inventionHeLaMiceAntibody SpecificitylawRNA Small CytoplasmicmedicineAnimalsHumansImmunology and AllergyAmino Acid SequencebiologyAntibodies Monoclonalbiology.organism_classificationMolecular biologyRecombinant ProteinsStainingEpitope mappingmedicine.anatomical_structureRibonucleoproteinsImmunologybiology.proteinRecombinant DNAAntibodySequence AlignmentEpitope MappingGene DeletionClinical and Experimental Immunology
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IL-6 stimulates annexin 1 expression and translocation and suggests a new biological role as class II acute phase protein.

1998

Annexin 1 (Ax 1), a protein whose synthesis and secretion are induced during the inflammatory response, has been proposed as a mediator of the anti-inflammatory action of glucocorticoids. To gain insight into a broader role of Ax 1 during the inflammatory response, the authors have investigated how pro-inflammatory cytokines [interleukin 1 (IL-1), IL-6 and tumour necrosis factor alpha (TNF-alpha)] affect Ax 1 expression and regulation at transcriptional and translational levels. The authors show that induction of the Ax 1 protein and its translocation to the cell membrane are stimulated by interleukin 6. However neither IL-1 nor TNF-alpha display these effects. Analysis of 5'-deletion mutan…

ElectrophoresisImmunologyAdenocarcinomaBiochemistryDexamethasoneMediatorAnnexinTumor Cells CulturedImmunology and AllergyHumansSecretionRNA MessengerCloning MolecularInterleukin 6Promoter Regions GeneticMolecular BiologyAnnexin A1Reporter genebiologyInterleukin-6Acute-phase proteinInterleukinNuclear ProteinsHematologyMolecular biologyRecombinant ProteinsDNA-Binding ProteinsGene Expression Regulation NeoplasticMifepristonebiology.proteinCCAAT-Enhancer-Binding ProteinsMutagenesis Site-DirectedTumor necrosis factor alphaAcute-Phase ProteinsTranscription FactorsCytokine
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Cloning of Several Genes Coding for Retinoic Acid Nuclear Receptors in the Mouse Embryonal Carcinoma Cell Line PCC7–MZ1

1993

Mouse embryonal carcinoma cell line PCC7-Mz1 can be induced by retinoic acid (RA) to differentiate into several well defined phenotypes of neuroectodermal origin (Lang, E. et al. (1989) J. Cell. Biol. 109, 2481-2493). Several subclones of the cell line (clonal variants) differ from each other in their developmental potential. To test whether these differences in cellular fate are due to somatic mutations in specific genes of these cells, we have cloned full length cDNAs coding for the alpha 1 and beta 2 isoforms, and partial length cDNAs coding for the alpha 2, beta 1 and beta 3 isoforms of the retinoic acid nuclear receptor (RAR). The cloned cDNAs did not differ in sequence from those of n…

Embryonal Carcinoma Stem CellsReceptors Retinoic AcidSomatic cellCellular differentiationMolecular Sequence DataRetinoic acidTretinoinBiologyEmbryonal carcinomaMicechemistry.chemical_compoundTumor Cells CulturedmedicineAnimalsHumansAmino Acid SequenceCloning MolecularPromoter Regions GeneticGenePharmacologyCloningBase SequenceNuclear ProteinsEmbryonal Carcinoma Stem CellsCell DifferentiationDNAmedicine.diseaseMolecular biologyRecombinant ProteinsRetinoic acid receptorchemistryNeoplastic Stem CellsCarrier ProteinsJournal of Receptor Research
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Derivatives of Erythropoietin That Are Tissue Protective But Not Erythropoietic

2004

Erythropoietin (EPO) is both hematopoietic and tissue protective, putatively through interaction with different receptors. We generated receptor subtype–selective ligands allowing the separation of EPO's bioactivities at the cellular level and in animals. Carbamylated EPO (CEPO) or certain EPO mutants did not bind to the classical EPO receptor (EPOR) and did not show any hematopoietic activity in human cell signaling assays or upon chronic dosing in different animal species. Nevertheless, CEPO and various nonhematopoietic mutants were cytoprotective in vitro and conferred neuroprotection against stroke, spinal cord compression, diabetic neuropathy, and experimental autoimmune encephalomyeli…

Encephalomyelitis Autoimmune ExperimentalEncephalomyelitiscarbamylated erythropoietinApoptosisPharmacologyLigandsNeuroprotectionRats Sprague-DawleyMiceStructure-Activity RelationshipDiabetic Neuropathiesddc:570hemic and lymphatic diseasesReceptors ErythropoietinmedicineAnimalsHumansErythropoiesisReceptorErythropoietinCells CulturedNeuronsMice Inbred C3HBinding SitesMultidisciplinaryChemistryExperimental autoimmune encephalomyelitisErythropoietin; erythropoietin receptor; carbamylated erythropoietin; neuroprotective agentsmedicine.diseaseRecombinant ProteinsRatsErythropoietin receptorStrokeNeuroprotective AgentsErythropoietin Erythropoietin derivative NeuroprotectionHematocritMutagenesisErythropoietinDrug DesignImmunologyErythropoiesisFemaleNervous System DiseasesSignal transductionerythropoietin receptorSpinal Cord CompressionSignal Transductionmedicine.drugScience
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