Search results for "Peptide sequence"

showing 10 items of 330 documents

The fnr Gene of Bacillus licheniformis and the Cysteine Ligands of the C-Terminal FeS Cluster

1998

Many of the O2-responsive gene regulators of bacteria are members of the fumarate nitrate reductase-cyclic AMP receptor protein family of transcriptional regulators (12, 13, 15, 17) with predicted structures similar to those of the cyclic AMP receptor protein (11). The Fnr (stands for fumarate nitrate reductase regulator) protein from Escherichia coli (FnrEc) controls the expression of a variety of genes, mainly of anaerobic respiration and metabolism (5, 13). It contains a N-terminal cluster of three essential cysteine residues which are supposed to bind together with Cys122 a [4Fe 4S]2+ cluster which is required for O2 sensing (4, 7, 8, 10, 16). A wide variety of gram-negative bacteria co…

inorganic chemicalsIron-Sulfur ProteinsMolecular Sequence DataRestriction MappingMutantBacillusGenetics and Molecular BiologySequence alignmentmacromolecular substancesBacillus subtilisLigandsNitrate reductaseenvironment and public healthMicrobiologyBacterial ProteinsAmino Acid SequenceCysteineBacillus licheniformisMolecular BiologyPeptide sequenceBacillus megateriumSequence Homology Amino AcidbiologyEscherichia coli ProteinsGene Expression Regulation Bacterialbiology.organism_classificationenzymes and coenzymes (carbohydrates)KineticsBiochemistryBacillus megateriumbacteriaSequence AlignmentBacillus subtilisTranscription FactorsCysteineJournal of Bacteriology
researchProduct

Activation of a murine autoreactive B cell by immunization with human recombinant autoantigen La/SS-B: Characterization of the autoepitope

1995

Immunization of Balb/c mice with a homogeneously purified recombinant human La/SS-B protein resulted in activation of an autoreactive B cell secreting a novel monoclonal anti-La antibody termed La4B6. La4B6 reacted with La protein from a variety of sources including human, bovine, rat and mouse. ATP blocked the binding of La4B6 to recombinant La protein. The human epitope was identified as consisting of the amino acid sequence SKGRRFKGKGKGN, which includes the proposed ATP-binding site of the La protein. In the human and bovine La protein, the epitope exists as a continuous amino acid sequence. In rat and mouse the epitope was found to consist of the amino acid sequence SKG interrupted by a…

medicine.drug_classRecombinant Fusion ProteinsImmunologyMolecular Sequence DataAutoimmunityBiologyMonoclonal antibodyAutoantigensPC12 CellsEpitopelaw.inventionCell LineMiceAdenosine TriphosphatelawmedicineImmunology and AllergyAnimalsHumansElméleti orvostudományokAmino Acid SequenceGeneralLiterature_REFERENCE(e.g.dictionariesencyclopediasglossaries)Peptide sequencechemistry.chemical_classificationB-LymphocytesMicroscopy ConfocalLinear epitopeOrvostudományok3T3 CellsMolecular biologyAmino acidRatschemistryMicroscopy FluorescenceRibonucleoproteinsRecombinant DNAbiology.proteinCattleImmunizationAntibodyEpitope MappingGene DeletionConformational epitope
researchProduct

Modulation of type II collagen-induced arthritis in DBA/1 mice by intravenous application of a peptide from the C1q-A chain.

1992

In this report we are able to show that intravenous (i.v.) application (day 0) of a nonapeptide (residues 26-34) from the human C1q A-chain (designated peptide A-C1q) prior to intradermal (i.d.) administration of chicken type II collagen (CII) in arthritis-susceptible DBA/1 mice (H2q), leads to abrogation of polymorphonuclear neutrophil (PMN) invasion into the joints. This nonapeptide exhibits epitope characteristics and high homology to residues 137-147 of CB11 (a cyanogen bromide fragment of chicken CII, known to contain both arthritis inducing and suppressing determinants). Arthritis index was lowest in animals pretreated i.v. with CII (as internal control), though animals pretreated i.v…

musculoskeletal diseasesMaleInjections IntradermalImmunologyMolecular Sequence DataType II collagenArthritischemical and pharmacologic phenomenaPeptideEpitopechemistry.chemical_compoundMiceAntigenAdjuvants ImmunologicmedicineImmunology and AllergyAnimalsAmino Acid Sequenceskin and connective tissue diseasesPeptide sequencechemistry.chemical_classificationbiologyArthritisComplement C1qHematologymedicine.diseaseMolecular biologyPeptide FragmentschemistryMice Inbred DBAImmunologyAntibody FormationInjections Intravenousbiology.proteinCyanogen bromideCollagenAntibodyOligopeptidesImmunobiology
researchProduct

Cytotoxic necrotizing factor type 2 produced by virulent Escherichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin s…

1994

Cytotoxic necrotizing factor type 2 (CNF2) produced by Escherichia coli strains isolated from intestinal and extraintestinal infections is a dermonecrotic toxin of 110 kDa. We cloned the CNF2 gene from a large plasmid carried by an Escherichia coli strain isolated from a lamb with septicemia. Hydropathy analysis of the deduced amino acid sequence revealed a largely hydrophilic protein with two potential hydrophobic transmembrane domains. The N-terminal half of CNF2 showed striking homology (27% identity and 80% conserved residues) to the N-terminal portion of Pasteurella multocida toxin. Methylamine protection experiments and immunofluorescence studies suggested that CNF2 enters the cytosol…

rho GTP-Binding ProteinsBacterial ToxinsMolecular Sequence DataRestriction Mapping[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyIn Vitro TechniquesSEQUENCE GENIQUEmedicine.disease_causeCell LineGTP-binding protein regulatorsGTP-Binding ProteinsmedicineEscherichia coliHumansCloning MolecularCytoskeletonEscherichia coliPeptide sequence[SDV.BC] Life Sciences [q-bio]/Cellular BiologyActinAdenosine Diphosphate RiboseMultidisciplinaryBase SequenceSequence Homology Amino AcidCytotoxinsBinding proteinEscherichia coli ProteinsMolecular biologyActinsCytosolTransmembrane domainActin CytoskeletonBiochemistryGenes BacterialFACTEUR CYTOTOXIQUE NECROSANTSequence AlignmentResearch Article
researchProduct

Synthesis and Biological Evaluation of a Multiantigenic Tn/TF-Containing Glycopeptide Mimic of the Tumor-Related MUC1 Glycoprotein

2006

solid-phase synthesisMolecular Sequence DataBreast Neoplasms010402 general chemistrymedicine.disease_cause01 natural sciencesBiochemistryantitumor agentsSolid-phase synthesisAntigenAntigens NeoplasmantigensCell Line TumorDrug DiscoverymedicineHumansAmino Acid SequenceGeneral Pharmacology Toxicology and PharmaceuticsPeptide sequenceMUC1Pharmacologychemistry.chemical_classification010405 organic chemistryMolecular MimicryMucin-1Organic ChemistryTransferringlycopeptidesoxime chemical ligationGlycopeptide0104 chemical sciencesMolecular mimicrychemistryBiochemistryTransferrinMolecular MedicineFemaleGlycoproteinChemMedChem
researchProduct

Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymati…

1997

The NS5B protein of the hepatitis C virus (HCV) is an RNA-dependent RNA polymerase (RdRp) (S.-E. Behrens, L. Tomei, and R. De Francesco, EMBO J. 15:12-22, 1996) that is assumed to be required for replication of the viral genome. To further study the biochemical and structural properties of this enzyme, an NS5B-hexahistidine fusion protein was expressed with recombinant baculoviruses in insect cells and purified to near homogeneity. The enzyme was found to have a primer-dependent RdRp activity that was able to copy a complete in vitro-transcribed HCV genome in the absence of additional viral or cellular factors. Filter binding assays and competition experiments showed that the purified enzym…

virusesImmunologyMolecular Sequence DataRNA-dependent RNA polymeraseSequence alignmentRNA-binding proteinHepacivirusViral Nonstructural ProteinsMicrobiologychemistry.chemical_compoundStructure-Activity RelationshipVirologyRNA polymeraseNS5BPeptide sequencePolymerasebiologyBase SequenceSequence Homology Amino AcidRNARNA-Binding ProteinsTemplates GeneticRNA-Dependent RNA PolymeraseMolecular biologyRecombinant ProteinschemistryAmino Acid SubstitutionInsect Sciencebiology.proteinRNA ViralSequence AlignmentResearch Article
researchProduct

Impact of VP1-Specific Protein Sequence Motifs on Adeno-Associated Virus Type 2 Intracellular Trafficking and Nuclear Entry

2012

ABSTRACT Adeno-associated virus type 2 (AAV2) has gained much interest as a gene delivery vector. A hallmark of AAV2-mediated gene transfer is an intracellular conformational change of the virus capsid, leading to the exposure of infection-relevant protein domains. These protein domains, which are located on the N-terminal portion of the structural proteins VP1 and VP2, include a catalytic phospholipase A 2 domain and three clusters of basic amino acids. We have identified additional protein sequence motifs located on the VP1/2 N terminus that also proved to be obligatory for virus infectivity. These motifs include signals that are known to be involved in protein interaction, endosomal sort…

virusesImmunologyProtein domainAmino Acid MotifsMolecular Sequence DataSequence alignmentBiologyMicrobiologyVirusCell LineParvoviridae InfectionsVirologyHumansAmino Acid SequenceAdeno-Associated Virus Type 2Peptide sequenceCell NucleusDependovirusMolecular biologyTransport proteinCell biologyVirus-Cell InteractionsProtein TransportCapsidInsect ScienceCapsid ProteinsSequence motifSequence Alignment
researchProduct

In vitro studies on the activation of the hepatitis C virus NS3 proteinase by the NS4A cofactor.

1996

AbstractProteolytic processing of the nonstructural proteins of the hepatitis C virus (HCV) is mediated by two viral proteinases: the NS2-3 proteinase cleaving at the NS2/3 junction and the NS3 serine-type proteinase responsible for processing at the NS3/4A, NS4A/B, NS4B/5A, and NS5A/B sites. Activity of the NS3 proteinase is modulated by NS4A. In the absence of this cofactor processing at the NS3-dependent sites does not occur or, in the case of the NS5A/B junction, is poor but increased when NS4A is present. Although recent studies demonstrated that proteinase activation requires direct interaction between NS3 and NS4A, the mechanism by which NS4A exerts the activation function is not kno…

virusesMolecular Sequence DataHepacivirusBiologyViral Nonstructural ProteinsCell LineEnzyme activatorProteinase 3VirologyCricetinaeMicrosomesAnimalsHumansAmino Acid SequenceBinding siteNS5APeptide sequenceSequence Deletionchemistry.chemical_classificationNS3Binding SitesBase Sequencevirus diseasesIntracellular Membranesbiochemical phenomena metabolism and nutritionMolecular biologyIn vitrodigestive system diseasesAmino acidEnzyme ActivationBiochemistrychemistryDNA ViralPeptidesHeLa CellsVirology
researchProduct

Single amino acid substitutions in the glycoprotein B carboxy terminus influence the fusion from without property of herpes simplex virus type 1.

1995

Syncytial mutations of herpes simplex virus type 1 (HSV-1) strains ANG, ANG path, HFEM, tsB5 and HSZP cause extensive cell fusion and were mapped to the cytoplasmic domain of glycoprotein B (gB), within the syn 3 locus. These strains are so far the only ones which show the phenotype ‘fusion from without’ (FFWO): 60 min after infection with high m.o.i., cells in a tissue culture are fused without transcription and translation of the viral genome. In this report we detected, using the recombinants 27/III and K-7, that an amino acid exchange from Ala to Val at aa position 854 of gB is the main determinant for FFWO activity of strains ANG, ANG path and recombinant K-7. The transfer of this muta…

virusesMutantRestriction MappingEnzyme-Linked Immunosorbent AssayHerpesvirus 1 HumanBiologymedicine.disease_causeKidneylaw.inventionCell FusionCytopathogenic Effect ViralViral Envelope ProteinslawVirologyCyclosporin aCricetinaeChlorocebus aethiopsmedicineBaby hamster kidney cellAnimalsAmino Acid SequenceAmino AcidsPeptide sequenceVero CellsRecombination GeneticCell fusionAlanineValineVirologyHerpes simplex virusPhenotypeRecombinant DNAVero cellThe Journal of general virology
researchProduct

SARS-CoV-2 envelope protein topology in eukaryotic membranes

2020

Coronavirus E protein is a small membrane protein found in the virus envelope. Different coronavirus E proteins share striking biochemical and functional similarities, but sequence conservation is limited. In this report, we studied the E protein topology from the new SARS-CoV-2 virus both in microsomal membranes and in mammalian cells. Experimental data reveal that E protein is a single-spanning membrane protein with the N-terminus being translocated across the membrane, while the C-terminus is exposed to the cytoplasmic side (Nt lum /Ct cyt ). The defined membrane protein topology of SARS-CoV-2 E protein may provide a useful framework to understand its interaction with other viral and ho…

virusescoronavirusmedicine.disease_causeViral Envelope Proteinsmembrane insertionPeptide sequencelcsh:QH301-705.5Topology (chemistry)PhylogenyCoronavirusMutationChemistryGeneral NeuroscienceProteïnes de membranaEukaryotavirus diseases129Recombinant ProteinsCell biologysars-cov-2MembraneProtein topologyCoronavirus InfectionsResearch Article1001topologyPneumonia ViralImmunologySequence alignmentBiologyTopologiaVirusGeneral Biochemistry Genetics and Molecular BiologyBetacoronavirusCoronavirus Envelope ProteinsViral envelopeMicrosomesmedicineHumansAmino Acid SequencePandemicsResearchCell MembraneCOVID-1915envelope proteinMembrane proteinlcsh:Biology (General)CytoplasmMutationSequence AlignmentOpen Biology
researchProduct