Search results for "carrier protein"

showing 10 items of 361 documents

Cystinuria subtype and nephrolithiasis

1999

GeneticsMembrane glycoproteinsBiochemistryNephrologyCarrier proteinMutation (genetic algorithm)biology.proteinmedicineCystinuriaBiologymedicine.diseaseKidney International
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Membrane-insertion fragments of Bcl-xL, Bax, and Bid.

2004

Apoptosis regulators of the Bcl-2 family associate with intracellular membranes from mitochondria and the endoplasmic reticulum, where they perform their function. The activity of these proteins is related to the release of apoptogenic factors, sequestered in the mitochondria, to the cytoplasm, probably through the formation of ion and/or protein transport channels. Most of these proteins contain a C-terminal putative transmembrane (TM) fragment and a pair of hydrophobic alpha helices (alpha5-alpha6) similar to the membrane insertion fragments of the ion-channel domain of diphtheria toxin and colicins. Here, we report on the membrane-insertion properties of different segments from antiapopt…

GlycosylationStereochemistryRecombinant Fusion ProteinsMolecular Sequence Databcl-X ProteinBcl-xLApoptosisBiochemistryProtein Structure SecondaryMembrane LipidsMiceProtein structureBcl-2-associated X proteinPredictive Value of TestsProto-Oncogene ProteinsProtein Interaction MappingAnimalsHumansAmino Acid SequencePeptide sequencebcl-2-Associated X ProteinbiologyIntracellular MembranesTransmembrane proteinPeptide FragmentsTransport proteinProtein TransportProto-Oncogene Proteins c-bcl-2Multigene FamilyHelixbiology.proteinBiophysicsCarrier ProteinsHydrophobic and Hydrophilic InteractionsAlpha helixBH3 Interacting Domain Death Agonist ProteinBiochemistry
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2015

Bacterial infections remain a serious health concern, in particular causing life-threatening infections of hospitalized and immunocompromised patients. The situation is exacerbated by the rise in antibacterial drug resistance, and new treatments are urgently sought. In this endeavour, accurate structures of molecular targets can support early-stage drug discovery. Here, crystal structures, in three distinct forms, of recombinantPseudomonas aeruginosaβ-ketoacyl-(acyl-carrier-protein) synthase II (FabF) are presented. This enzyme, which is involved in fatty-acid biosynthesis, has been validated by genetic and chemical means as an antibiotic target in Gram-positive bacteria and represents a po…

Gram-negative bacteriabiologyAcyl carrier protein synthaseStereochemistryDrug discoveryPlatensimycinBiophysicsActive sitePlasma protein bindingCondensed Matter Physicsbiology.organism_classificationLigand (biochemistry)Biochemistry3. Good healthchemistry.chemical_compoundchemistryBiochemistryStructural BiologyGeneticsbiology.proteinBinding siteActa Crystallographica Section F Structural Biology Communications
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Sequence-Specific Repression of Cotranslational Translocation of the Hepatitis B Virus Envelope Proteins Coincides with Binding of Heat Shock Protein…

1997

AbstractThe large L envelope protein of the hepatitis B virus has the peculiar capacity to adopt two transmembrane topologies. The N-terminal preS domain of L initially remains in the cytosol while the S domain is cotranslationally inserted into the endoplasmic reticulum membrane. The preS region of about half of the L molecules is posttranslationally translocated to the lumenal space. We now demonstrate that the repression of cotranslational translocation of preS is conferred by a preS1-specific sequence. By analysis of L deletion mutants, the cytosolic anchorage determinant was mapped to amino acid sequence 70 to 94 of L. The intrinsic potential of this determinant to suppress cotranslati…

Hepatitis B virusHSC70 Heat-Shock ProteinsRecombinant Fusion ProteinsPlasma protein bindingBiologyGenes envCytosolViral Envelope ProteinsHeat shock proteinVirologyHumansHSP70 Heat-Shock ProteinsBinding sitePromoter Regions GeneticPeptide sequenceBinding SitesBase SequenceCell-Free SystemEndoplasmic reticulumHSC70 Heat-Shock ProteinsOligonucleotides AntisenseMolecular biologyTransmembrane proteinChaperone (protein)Protein Biosynthesisbiology.proteinMutagenesis Site-DirectedMetallothioneinCarrier ProteinsProtein BindingVirology
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Chaperones Involved in Hepatitis B Virus Morphogenesis

1999

Little is known about host cell factors necessary for hepatitis B virus (HBV) assembly which involves envelopment of cytosolic nucleocapsids by the S, M and L transmembrane viral envelope proteins and subsequent budding into intraluminal cisternae. Central to virogenesis is the L protein that mediates hepatocyte receptor binding and envelopment of capsids. To serve these topologically conflicting roles, L protein exhibits an unusual dual membrane topology, disposing its N-terminal preS domain inside and outside of the virion lipid envelope. The mixed topology is achieved by posttranslational preS translocation of about half of the L protein molecules across a post-endoplasmic reticulum memb…

Hepatitis B virusProtein FoldingCalnexinHSC70 Heat-Shock ProteinsClinical BiochemistryBiochemistryViral Matrix ProteinsCytosolViral Envelope ProteinsViral envelopeCalnexinMorphogenesisAnimalsHumansHSP70 Heat-Shock ProteinsProtein PrecursorsMolecular BiologyHepatitis B Surface AntigensViral matrix proteinbiologyChemistryCalcium-Binding ProteinsHSC70 Heat-Shock ProteinsBiological TransportVirologyTransmembrane proteinCell biologyProtein BiosynthesisMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein foldingCarrier ProteinsMolecular ChaperonesBiological Chemistry
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Human hepatic cell uptake of resveratrol: involvement of both passive diffusion and carrier-mediated process

2004

This work reports significant advances on the transport in hepatic cells of resveratrol, a natural polyphenol with potent protective properties. First, we describe a new simple technique to qualitatively follow resveratrol cell uptake and intracellular distribution, based on resveratrol fluorescent properties. Second, the time-course study and the quantification of (3)H-labelled resveratrol uptake have been performed using human hepatic derived cells (HepG2 tumor cells) and hepatocytes. The temperature-dependence of the kinetics of uptake as well as the cis-inhibition experiments agree with the involvement of a carrier-mediated transport in addition to passive diffusion. The decrease of pas…

HepatoblastomaMetabolic Clearance RateCellBiophysicsBiological AvailabilityBiological Transport ActiveResveratrolBiochemistryCell LineDiffusionchemistry.chemical_compoundResveratrol bindingCell Line TumorStilbenesmedicineHumansDistribution (pharmacology)Tissue DistributionMolecular BiologyTemperaturefood and beveragesCell BiologyBlood proteinsmedicine.anatomical_structurechemistryBiochemistryResveratrolCell cultureHepatocytesHepatic stellate cellBiophysicsCarrier ProteinsIntracellularBiochemical and Biophysical Research Communications
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A role for the 2-oxoglutarate carrier in glutathione transport into hepatocyte mitochondria?

2004

HepatologybiologyMembrane transport proteinGlutathioneMitochondrionGPX4chemistry.chemical_compoundmedicine.anatomical_structurechemistryBiochemistryCarrier proteinHepatocyteGlutathione transportmedicinebiology.protein2-OxoglutarateHepatology
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Apoptosis induced by (E)-5-(2-bromovinyl)-2'-deoxyuridine in varicella zoster virus thymidine kinase-expressing cells is driven by activation of c-Ju…

2003

The molecular mode of cell killing by the antiviral drug (E)-5-(2-bromovinyl-2'-deoxyuridine (BVDU) was studied in Chinese hamster ovary (CHO) cells stably transfected with the thymidine kinase gene (tk) of varicella zoster virus (CHO-VZVtk). The colony-forming ability of the cells was reduced to <1% at a concentration of approximately 1 microM BVDU, whereas for nontransfected cells or cells transfected with tk gene of herpes simplex virus type 1 (CHO-HSVtk), a 1000-fold higher dose was required to achieve the same response. BVDU inhibited thymidylate synthase in CHO-VZVtk but not in CHO-HSVtk and control cells. On the other hand, the drug was incorporated into DNA of VZVtk- and HSVtk-expre…

Herpesvirus 3 HumanFas Ligand ProteinFas-Associated Death Domain ProteinApoptosisCHO CellsBiologyTransfectionAntiviral AgentsThymidine KinaseFas ligandchemistry.chemical_compoundNecrosisCricetinaeCytotoxic T cellAnimalsSimplexvirusAdaptor Proteins Signal TransducingPharmacologyCaspase 8GenomeMembrane GlycoproteinsChinese hamster ovary cellCell CycleJNK Mitogen-Activated Protein KinasesTransfectionDNAThymidylate SynthaseMolecular biologyCaspase 9Transcription Factor AP-1Cell killingchemistryBromodeoxyuridineApoptosisThymidine kinaseCaspasesMolecular MedicineMitogen-Activated Protein KinasesCarrier ProteinsBromodeoxyuridineMolecular pharmacology
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Inhibition of ubiquitin-dependent proteolysis by a synthetic glycine-alanine repeat peptide that mimics an inhibitory viral sequence.

2002

AbstractThe glycine–alanine repeat (GAr) of the Epstein–Barr virus nuclear antigen-1 is a cis-acting transferable element that inhibits ubiquitin/proteasome-dependent proteolysis in vitro and in vivo. We have here examined the effect of a synthetic 20-mer GAr oligopeptide on the degradation of iodinated or biotin labeled lysozyme in a rabbit reticulocyte lysates in vitro assay. Micromolar concentrations of the GA-20 peptide inhibited the hydrolysis of lysozyme without significant effect on ubiquitination. Addition of the peptide did not inhibit the hydrolysis of fluorogenic substrate by purified proteasomes and did not affect the ubiquitination of lysozyme. An excess of the peptide failed t…

Herpesvirus 4 HumanProteasome Endopeptidase ComplexGly–Ala repeatPolymersProteolysisMolecular Sequence DataBiophysicsGlycineBiotinPeptideBiochemistryIodine Radioisotopeschemistry.chemical_compoundS5aUbiquitinStructural BiologyMultienzyme ComplexesGeneticsmedicineAnimalsAmino Acid SequenceEnzyme InhibitorsMolecular BiologyPeptide sequenceUbiquitinsEpstein–Barr virus nuclear antigen-1Alaninechemistry.chemical_classificationOligopeptideAlaninebiologymedicine.diagnostic_testProteasomeMolecular MimicryUbiquitinationCell BiologyCysteine EndopeptidasesBiochemistryProteasomechemistryEpstein-Barr Virus Nuclear AntigensIsotope Labelingbiology.proteinMuramidaseRabbitsLysozymeCarrier ProteinsPeptidesOligopeptidesFEBS letters
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Identification of a novel compound heterozygote SCO2 mutation in cytochrome c oxidase deficient fatal infantile cardioencephalomyopathy

2006

UNLABELLED Fatal infantile cardioencephalomyopathy (OMIM No. 604377) is a disorder of the mitochondrial respiratory chain and is characterised by neonatal progressive muscular hypotonia and cardiomyopathy because of severe Cytochrome c oxidase deficiency. Here we report a novel mutation in the Cytochrome c oxidase assembly gene SCO2 in an infant with fatal infantile cardioencephalomyopathy despite normal initial metabolic screening. CONCLUSION In newborns with unexplained muscular hypotonia and cardiomyopathy genetic testing of mitochondrial respiratory chain disorders might be helpful to establish a final diagnosis and guide treatment decisions.

Heterozygotemedicine.medical_specialtyPathologyCardiomyopathyCytochrome-c Oxidase DeficiencyCompound heterozygositymedicine.disease_causeMitochondrial ProteinsFatal OutcomeMitochondrial EncephalomyopathiesInternal medicinemedicineHumansCytochrome c oxidaseGeneGenetic testingMutationMuscular hypotoniamedicine.diagnostic_testbiologybusiness.industryInfantGeneral Medicinemedicine.diseaseEndocrinologyMitochondrial respiratory chainMutationPediatrics Perinatology and Child Healthbiology.proteinFemaleCardiomyopathiesCarrier ProteinsbusinessMolecular ChaperonesActa Paediatrica
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