Search results for "FRAGMENTS"

showing 10 items of 422 documents

Influence of the C-terminus of the glycophorin A transmembrane fragment on the dimerization process

2000

The monomer-dimer equilibrium of the glycophorin A (GpA) transmembrane (TM) fragment has been used as a model system to investigate the amino acid sequence requirements that permit an appropriate helix-helix packing in a membrane‐mimetic environment. In particular, we have focused on a region of the helix where no crucial residues for packing have been yet reported. Various deletion and replacement mutants in the C‐terminal region of the TM fragment showed that the distance between the dimerization motif and the flanking charged residues from the cytoplasmic side of the protein is important for helix packing. Furthermore, selected GpA mutants have been used to illustrate the rearrangement o…

Models MolecularStereochemistryProtein ConformationMutantMolecular Sequence DataBiochemistryProtein structureGlycophorinAmino Acid SequenceGlycophorinsMolecular BiologyProtein secondary structurePeptide sequencebiologyChemistryC-terminusProteïnes de membranaMembrane ProteinsTransmembrane proteinPeptide FragmentsBiochemistryMembrane proteinbiology.proteinDimerizationResearch Article
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A molecular assembly system that renders antigens of choice highly repetitive for induction of protective B cell responses.

2002

Virus like particles (VLPs) are known to induce potent B cell responses in the absence of adjuvants. Moreover, epitope-specific antibody responses may be induced by VLPs that contain peptides inserted in their immunodominant regions. However, due to steric problems, the size of the peptides capable of being incorporated into VLPs while still permitting capsid assembly, is rather limited. While peptides genetically fused to either the N- or C-terminus of VLPs present fewer assembly problems, the immune responses obtained against such epitopes are often limited, most likely because the epitopes are not optimally exposed. In addition, such particles may be less stable in vivo. Here, we show th…

Models MolecularViral Hepatitis VaccinesHepatitis B virusMacromolecular SubstancesProtein ConformationvirusesRecombinant Fusion ProteinsProtozoan ProteinsAntigens ProtozoanBiologyProtein EngineeringEpitopePhospholipases AInclusion Bodies ViralViral Matrix ProteinsMiceImmune systemAntigenVirus-like particlemedicineAnimalsB cellB-LymphocytesMice Inbred BALB CVaccines SyntheticGeneral VeterinaryGeneral Immunology and MicrobiologyImmunodominant EpitopesImmunogenicityVaccinationPublic Health Environmental and Occupational HealthMolecular biologyHepatitis B Core AntigensPeptide FragmentsCell biologyProtein Structure TertiaryHBcAgBee VenomsInfectious Diseasesmedicine.anatomical_structureCross-Linking ReagentsCapsidDrug DesignMolecular MedicineFemaleImmunizationPeptidesOligopeptidesVaccine
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Subunit organization of the abalone Haliotis tuberculata hemocyanin type 2 (HtH2), and the cDNA sequence encoding its functional units d, e, f, g and…

1999

We have developed a HPLC procedure to isolate the two different hemocyanin types (HtH1 and HtH2) of the European abalone Haliotis tuberculata. On the basis of limited proteolytic cleavage, two-dimensional immunoelectrophoresis, PAGE, N-terminal protein sequencing and cDNA sequencing, we have identified eight different 40-60-kDa functional units (FUs) in HtH2, termed HtH2-a to HtH2-h, and determined their linear arrangement within the elongated 400-kDa subunit. From a Haliotis cDNA library, we have isolated and sequenced a cDNA clone which encodes the five C-terminal FUs d, e, f, g and h of HtH2. As shown by multiple sequence alignments, defg of HtH2 correspond structurally to defg from Octo…

Models Molecularfood.ingredientDNA ComplementarySequence analysismedicine.medical_treatmentMolecular Sequence DataOctopodiformesMegathura crenulataBiochemistryEvolution MolecularfoodSequence Analysis ProteinComplementary DNAmedicineAnimalsHaliotisAmino Acid SequenceCloning MolecularProtein Structure QuaternaryPeptide sequenceImmunoelectrophoresisbiologySequence Homology Amino AcidcDNA libraryHelix SnailsProtein primary structureHemocyaninAnatomySequence Analysis DNAbiology.organism_classificationPeptide FragmentsBiochemistryMolluscaHemocyaninsEuropean journal of biochemistry
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The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended

2012

Filamins are large proteins that cross-link actin filaments and connect to other cellular components. The C-terminal rod 2 region of FLNa (filamin A) mediates dimerization and interacts with several transmembrane receptors and intracellular signalling adaptors. SAXS (small-angle X-ray scattering) experiments were used to make a model of a six immunoglobulin-like domain fragment of the FLNa rod 2 (domains 16–21). This fragment had a surprising three-branched structural arrangement, where each branch was made of a tightly packed two-domain pair. Peptides derived from transmembrane receptors and intracellular signalling proteins induced a more open structure of the six domain fragment. Mutagen…

Models Moleculargenetics [Receptors Dopamine D3]metabolism [Recombinant Proteins]Protein Conformationgenetics [Antigens CD18]chemistry [Recombinant Proteins]Plasma protein bindingCrystallography X-RayLigandsFilaminmetabolism [Antigens CD18]metabolism [Cytoskeletal Proteins]BiochemistryfilaminsContractile ProteinsProtein structuremetabolism [Peptide Fragments]FLNAchemistry [Antigens CD18]genetics [Cell Adhesion Molecules]Small-angle X-ray scatteringMicrofilament Proteinsgenetics [Contractile Proteins]Recombinant Proteinschemistry [Receptors Dopamine D3]FBLIM1 protein humanddc:540Domain (ring theory)DimerizationProtein Bindingchemistry [Contractile Proteins]FilaminsAntigens CD18metabolism [Cell Adhesion Molecules]BiologyScattering Small Anglemetabolism [Receptors Dopamine D3]Humanschemistry [Microfilament Proteins]Protein Interaction Domains and Motifsmetabolism [Mutant Proteins]DRD3 protein humanMolecular Biologymetabolism [Contractile Proteins]Actingenetics [Cytoskeletal Proteins]Cryoelectron MicroscopyMutagenesista1182Receptors Dopamine D3metabolism [Microfilament Proteins]Cell Biologychemistry [Cell Adhesion Molecules]genetics [Peptide Fragments]Peptide FragmentsCytoskeletal ProteinsCrystallographychemistry [Mutant Proteins]chemistry [Peptide Fragments]CD18 AntigensBiophysicschemistry [Cytoskeletal Proteins]Mutant Proteinsgenetics [Microfilament Proteins]Cell Adhesion MoleculesBiochemical Journal
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Assay for O6-alkylguanine-DNA-alkyltransferase using oligonucleotides containing O6-methylguanine in a BamHI recognition site as substrate

1992

Abstract Double-stranded oligonucleotides, 40 bases in length containing an O 6 -methylguanine in a Bam HI restriction site, were developed as substrates for the determination of human O 6 -alkylguanine-DNA-alkyltransferase (AGT). The assay proved highly sensitive and quantitative. After incubation of the 5′-end-labeled oligonucleotides with cell homogenates of peripheral blood lymphocytes, the DNA was digested with Bam HI. Cleavage with this restriction enzyme did not occur in the O 6 -methylguanine-containing oligonucleotide unless the fragment was repaired. The cleaved oligonucleotide was separated from the intact parent oligonucleotide by reverse-phase high-performance liquid chromatogr…

Molecular Sequence DataOligonucleotidesBiophysicsBiologyCleavage (embryo)Sensitivity and SpecificityBiochemistryHigh-performance liquid chromatographyO(6)-Methylguanine-DNA Methyltransferasechemistry.chemical_compoundHumansLymphocytesMolecular BiologyChromatography High Pressure LiquidBase SequenceOligonucleotideSubstrate (chemistry)MethyltransferasesCell BiologyMolecular biologyPeptide FragmentsRestriction siteRestriction enzymeBiochemistrychemistryBamHIPhosphorus RadioisotopesDNAAnalytical Biochemistry
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Mapping of a binding site for ATP within the extracellular region of the Torpedo nicotinic acetylcholine receptor beta-subunit.

1997

Using 2,8,5'-[H-3]ATP as a direct photoaffinity label for membrane-bound nicotinic acetylcholine receptor (nAChR) from Torpedo marmorata, we have identified a binding site for ATP in the extracellular region of the beta-subunit of the receptor. Photolabeling was completely inhibited in the presence of saturating concentrations of nonradioactive ATP, whereas neither the purinoreceptor antagonists suramin, theophyllin, and caffeine nor the nAChR antagonists alpha-bungarotoxin and d-tubocurarine affected the labeling reaction. Competitive and noncompetitive nicotinic agonists and Ca2+ increased the yield of the photoreaction by up to 50%, suggesting that the respective binding sites are allost…

Molecular Sequence DataPhotoaffinity LabelsReceptors NicotinicTorpedoTritiumBiochemistryPeptide Mappingchemistry.chemical_compoundGanglion type nicotinic receptorAdenosine TriphosphateAdenine nucleotideAnimalsChymotrypsinTrypsinAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisCell MembranePeptide FragmentsNicotinic acetylcholine receptorNicotinic agonistBiochemistrychemistrybiology.proteinAlpha-4 beta-2 nicotinic receptorExtracellular SpaceAdenosine triphosphateSequence AnalysisATP synthase alpha/beta subunitsBiochemistry
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Two Antigenic Peptides from Genes m123 and m164 of Murine Cytomegalovirus Quantitatively Dominate CD8 T-Cell Memory in the H-2 d Haplotype

2001

ABSTRACT The importance of CD8 T cells for the control of cytomegalovirus (CMV) infection has raised interest in the identification of immunogenic viral proteins as candidates for vaccination and cytoimmunotherapy. The final aim is to determine the viral “immunome” for any major histocompatibility complex class I molecule by antigenicity screening of proteome-derived peptides. For human CMV, there is a limitation to this approach: the T cells used as responder cells for peptide screening are usually memory cells that have undergone in vivo selection. On this basis, pUL83 (pp65) and pUL123 (IE1 or pp68 to -72) were classified as immunodominant proteins. It is an open question whether this li…

MuromegalovirusAdoptive cell transferAntigenicityImmunologyCD8-Positive T-LymphocytesBiologymedicine.disease_causeMajor histocompatibility complexMicrobiologyImmediate-Early ProteinsViral Matrix ProteinsMiceOpen Reading FramesViral ProteinsImmune systemVirologymedicineAnimalsCytotoxic T cellAntigens ViralMice Inbred BALB CH-2 AntigensCytomegalovirusHerpesviridae InfectionsPhosphoproteinsVirologyPeptide FragmentsHaplotypesInsect ScienceProteomeImmunologybiology.proteinPathogenesis and ImmunityFemaleImmunologic MemorySpleenCD8Journal of Virology
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Processing and Presentation of Murine Cytomegalovirus pORFm164-Derived Peptide in Fibroblasts in the Face of All Viral Immunosubversive Early Gene Fu…

2002

ABSTRACTCD8 T cells are the principal effector cells in the resolution of acute murine cytomegalovirus (mCMV) infection in host organs. This undoubted antiviral and protective in vivo function of CD8 T cells appeared to be inconsistent with immunosubversive strategies of the virus effected by early (E)-phase genesm04,m06, andm152. The so-called immune evasion proteins gp34, gp48, and gp37/40, respectively, were found to interfere with peptide presentation at different steps in the major histocompatibility complex (MHC) class I pathway of antigen processing and presentation in fibroblasts. Accordingly, they were proposed to prevent recognition and lysis of infected fibroblasts by cytolytic T…

MuromegalovirusImmunologyAntigen presentationMajor histocompatibility complexMicrobiologyImmediate-Early ProteinsMiceOpen Reading FramesViral ProteinsImmune systemAntigenVirologyMHC class IAnimalsCytotoxic T cellAntigens ViralGenes Immediate-EarlyCells CulturedAntigen PresentationMice Inbred BALB CMembrane GlycoproteinsbiologyAntigen processingFibroblastsVirologyPeptide FragmentsCTL*Insect Sciencebiology.proteinPathogenesis and ImmunityFemaleT-Lymphocytes CytotoxicJournal of Virology
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Identification of a Kd-restricted antigenic peptide encoded by murine cytomegalovirus early gene M84

2000

The two sister cytomegaloviruses (CMVs), human and murine CMV, have both evolved immune evasion functions that interfere with the major histocompatibility complex class I (MHC-I) pathway of antigen processing and presentation and are effectual in the early (E) phase of virus gene expression. However, studies on murine CMV have shown that E-phase immune evasion is leaky. An E-phase protein involved in immune evasion, namely m04-gp34, was found to simultaneously account for an antigenic peptide presented by the MHC-I molecule Dd. Recent work has demonstrated the induction of protective immunity specific for the E-phase protein M84-p65, one of two murine CMV homologues of the human CMV matrix …

MuromegalovirusPeptideBiologyMajor histocompatibility complexImmediate-Early ProteinsMiceOpen Reading FramesImmune systemVirologyAnimalsAmino Acid SequenceLymphocyte CountAntigens ViralGenes Immediate-EarlyGeneAntigenic peptidechemistry.chemical_classificationMice Inbred BALB CViral matrix proteinAntigen processingH-2 AntigensVirologyMolecular biologyPeptide FragmentschemistryCytomegalovirus earlybiology.proteinImmunologic MemoryT-Lymphocytes CytotoxicJournal of General Virology
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Beta-amyloid monomers are neuroprotective

2009

The 42-aa-long β-amyloid protein—Aβ1-42—is thought to play a central role in the pathogenesis of Alzheimer's disease (AD) (Walsh and Selkoe, 2007). Data from AD brain (Shankar et al., 2008), transgenic APP (amyloid precursor protein)-overexpressing mice (Lesné et al., 2006), and neuronal cultures treated with synthetic Aβ peptides (Lambert et al., 1998) indicate that self-association of Aβ1-42monomers into soluble oligomers is required for neurotoxicity. The function of monomeric Aβ1-42is unknown. The evidence that Aβ1-42is present in the brain and CSF of normal individuals suggests that the peptide is physiologically active (Shoji, 2002). Here we show that synthetic Aβ1-42monomers support …

N-MethylaspartateStimulationPeptideNeuroprotectionNeuro-degenerative diseasePathogenesismental disordersNitrilesmedicineAmyloid precursor proteinButadienesExcitatory Amino Acid AgonistsAnimalsEnzyme InhibitorsReceptorCells CulturedPodophyllotoxinchemistry.chemical_classificationCerebral CortexNeuronsAnalysis of VarianceAmyloid beta-PeptidesbiologyCell DeathDose-Response Relationship DrugGeneral NeuroscienceNeurodegenerationβ-Amyloid proteinNeurotoxicityself-assemblyTyrphostinsmedicine.diseaseEmbryo MammalianPeptide FragmentsCell biologyRatsNeuroprotective Agentschemistrybiology.proteinBrief CommunicationsNeuroscienceβ-Amyloid protein; Neuro-degenerative diseases; self-assembly
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