Search results for "amino acid sequence"

showing 10 items of 1296 documents

Phosphorylation of the Goodpasture antigen by type A protein kinases.

1995

Collagen IV is the major component of basement membranes. The human alpha 3 chain of collagen IV contains an antigenic domain called the Goodpasture antigen that is the target for the circulating immunopathogenic antibodies present in patients with Goodpasture syndrome. Characteristically, the gene region encoding the Goodpasture antigen generates multiple alternative products that retain the antigen amino-terminal region with a five-residue motif (KRGDS). The serine therein appears to be the major in vitro cAMP-dependent protein kinase phosphorylation site in the isolated antigen and can be phosphorylated in vitro by two protein kinases of approximately 50 and 41 kDa associated with human …

inorganic chemicalsCollagen Type IVAnti-Glomerular Basement Membrane DiseaseMolecular Sequence DataBiochemistryAutoantigensSerineAntigenmedicineSerineGoodpasture syndromeHumansAmino Acid SequencePhosphorylationProtein kinase AMolecular BiologyBasement membranebiologyBase SequenceKinaseCell Biologymedicine.diseaseMolecular biologyCyclic AMP-Dependent Protein Kinasesenzymes and coenzymes (carbohydrates)medicine.anatomical_structureOligodeoxyribonucleotidesbiology.proteinPhosphorylationCollagenAntibodyThe Journal of biological chemistry
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Iron Induces Proliferation and Morphogenesis in Primmorphs from the Marine SpongeSuberites domuncula

2002

Dissociated cells from marine demosponges retain their proliferation capacity if they are allowed to form special aggregates, the primmorphs. On the basis of incorporation studies and septin gene expression, we show that Fe3+ ions are required for the proliferation of cells in primmorphs from Suberites domuncula. In parallel, Fe3+ induced the expression of ferritin and strongly stimulated the synthesis of spicules. This result is supported by the finding that the enzymatic activity of silicatein, converting organosilicon to silicic acid, depends on Fe3+. Moreover, the expression of a scavenger receptor molecule, possibly involved in the morphology of spicules, depends on the presence of Fe3…

inorganic chemicalsIronMolecular Sequence DataMorphogenesisFluorescent Antibody TechniqueSeptinModels BiologicalPolymerase Chain ReactionFungal ProteinsSponge spiculeGene expressionGeneticsAnimalsHistidineAmino Acid SequenceReceptors ImmunologicScavenger receptorMolecular BiologyPhylogenyReceptors LipoproteinReceptors ScavengerSequence Homology Amino AcidbiologyEcologySilicatesMembrane ProteinsDNACell BiologyGeneral MedicineScavenger Receptors Class BBlotting Northernbiology.organism_classificationCathepsinsRecombinant ProteinsPoriferaCell biologySuberites domunculaFerritinSpongeFerritinsbiology.proteinCell DivisionDNA and Cell Biology
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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
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Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes

1998

AbstractPrevious studies directed towards understanding phosphorylation of the chlorophyll a/b binding proteins comprising light harvesting complex II (LHC II) have concentrated on a single phosphorylation site located close to the N-terminus of the mature proteins. Here we show that a series of recombinant pea Lhcb1 proteins, each missing an N-terminal segment including this site, are nevertheless phosphorylated by a protein kinase associated with a photosystem II core complex preparation. An Lhcb1 protein missing the first 58 amino acid residues is not, however, phosphorylated. The results demonstrate that the LHC II proteins are phosphorylated at one or more sites, the implications of wh…

inorganic chemicalsPhotosystem IIMacromolecular SubstancesMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiophysicsmacromolecular substancesBiologyBiochemistryDNA-binding proteinProtein kinaseThylakoid membraneSubstrate Specificitylaw.inventionStructural BiologylawGeneticsProtein phosphorylationAmino Acid SequencePhosphorylationProtein kinase AMolecular BiologyPlant ProteinsKinasePeasPeaPhotosystem II Protein Complexfood and beveragesCell BiologySpinachPeptide FragmentsRecombinant Proteinsenzymes and coenzymes (carbohydrates)BiochemistryThylakoidRecombinant DNALight harvesting proteinPhosphorylationbacteriaCarrier ProteinsProtein KinasesFEBS Letters
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Receptor-mediated uptake of boron-rich neuropeptide y analogues for boron neutron capture therapy.

2014

Peptidic ligands selectively targeting distinct G protein-coupled receptors that are highly expressed in tumor tissue represent a promising approach in drug delivery. Receptor-preferring analogues of neuropeptide Y (NPY) bind and activate the human Y1 receptor subtype (hY1 receptor), which is found in 90% of breast cancer tissue and in all breast-cancer-derived metastases. Herein, novel highly boron-loaded Y1 -receptor-preferring peptide analogues are described as smart shuttle systems for carbaboranes as (10) B-containing moieties. Various positions in the peptide were screened for their susceptibility to carbaborane modification, and the most promising positions were chosen to create a mu…

inorganic chemicalsStereochemistrymedia_common.quotation_subjectMolecular Sequence Datachemistry.chemical_elementPeptideBoron Neutron Capture TherapyBreast NeoplasmsBiochemistrySolid-phase synthesisDrug DiscoveryChlorocebus aethiopsAnimalsHumansNeuropeptide YAmino Acid SequenceGeneral Pharmacology Toxicology and PharmaceuticsReceptorInternalizationBoronBoranesmedia_commonPharmacologychemistry.chemical_classificationChemistryOrganic ChemistryReceptor-mediated endocytosisNeuropeptide Y receptorReceptors Neuropeptide YHEK293 CellsDrug deliveryCOS CellsMolecular MedicineFemaleChemMedChem
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Dissimilar Regulation of Antimicrobial Proteins in the Midgut of Spodoptera exigua Larvae Challenged with Bacillus thuringiensis Toxins or Baculoviru…

2015

Antimicrobial peptides (AMPs) and lysozymes are the main effectors of the insect immune system, and they are involved in both local and systemic responses. Among local responses, midgut immune reaction plays an important role in fighting pathogens that reach the insect body through the oral route, as do many microorganisms used in pest control. Under this point of view, understanding how insects defend themselves locally during the first phases of infections caused by food-borne pathogens is important to further improve microbial control strategies. In the present study, we analyzed the transcriptional response of AMPs and lysozymes in the midgut of Spodoptera exigua (Lepidoptera: Noctuidae…

media_common.quotation_subjectAntimicrobial peptidesMolecular Sequence DataBacillus thuringiensislcsh:MedicineInsectSpodopteraSpodopteraMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaHemolymphAnimalsAmino Acid SequencePest Control Biologicallcsh:SciencePhylogenymedia_commonMultidisciplinarybiologyBacillus thuringiensis ToxinsSequence Homology Amino AcidMonophenol Monooxygenasefungilcsh:RMidgutbiology.organism_classificationEndotoxinsSettore AGR/11 - ENTOMOLOGIA GENERALE E APPLICATALarvaNoctuidaeInsect ProteinsMuramidaselcsh:QBaculoviridaeDigestive SystemAntimicrobial Cationic PeptidesResearch ArticlePLoS ONE
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In vivo evaluation of the interaction between the Escherichia coli IGP synthase subunits using the Bacterial Two-Hybrid system

2020

ABSTRACT Histidine biosynthesis is one of the most characterized metabolic routes for its antiquity and its central role in cellular metabolism; indeed, it represents a cross-road between nitrogen metabolism and de novo synthesis of purines. This interconnection is due to the activity of imidazole glycerol phosphate synthase, a heterodimeric enzyme constituted by the products of two his genes, hisH and hisF, encoding a glutamine amidotransferase and a cyclase, respectively. Despite their interaction was suggested by several in vitro experiments, their in vivo complex formation has not been demonstrated. On the contrary, the analysis of the entire Escherichia coli interactome performed using…

medicine.disease_causeMicrobiologyInteractomeCyclase03 medical and health scienceschemistry.chemical_compoundBiosynthesisAminohydrolasesTwo-Hybrid System TechniquesEscherichia coliGeneticsmedicineHistidineAmino Acid SequencePurine metabolismMolecular BiologyEscherichia coliHistidine030304 developmental biologyGlutamine amidotransferase0303 health sciencesATP synthasebiologyEscherichia coli Proteins030302 biochemistry & molecular biologyProtein SubunitschemistryBiochemistrybiology.proteinProtein BindingFEMS Microbiology Letters
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The C-terminal antibody binding domain ofCandida albicansmp58 represents a protective epitope during candidiasis

2003

The 58-kDa surface mannoprotein of Candida albicans (mp58) elicits strong antibody responses during infection. Epitope mapping with sera from patients with candidiasis and control individuals indicated the presence of multiple IgG-reactive continuous epitopes on the protein, expanding both the amino- and carboxy-terminal domains and several internal regions. These immunoreactive regions were similar to the ones previously identified using sera from immunized animals. Two of the epitopic regions (including the C-terminal domain) showed increased reactivity with antibodies present in sera from patients with candidiasis as compared to control individuals. Patients who survived the infection di…

medicine.drug_classEnzyme-Linked Immunosorbent AssayMonoclonal antibodyMicrobiologyEpitopeImmunoglobulin GFungal ProteinsEpitopesMiceCandida albicansGeneticsmedicineAnimalsAmino Acid SequenceCandida albicansMolecular BiologyMice Inbred BALB CMembrane GlycoproteinsbiologyCandidiasisAntibodies Monoclonalbiology.organism_classificationDisseminated CandidiasisVirologyCorpus albicansProtein Structure TertiaryEpitope mappingbiology.proteinFemaleAntibodyEpitope MappingFEMS Microbiology Letters
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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
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Analysis of type-restricted and cross-reactive epitopes on virus-like particles of human papillomavirus type 33 and in infected tissues using monoclo…

1994

A panel of six monoclonal antibodies recognizing at least three different antigenic regions has been raised against the L1 major capsid protein of human papillo-mavirus type 33 (HPV-33), which is associated with cervical carcinoma. The antigenic sites defined by these antibodies have been mapped and classified as type-restricted or broadly cross-reactive using bacterially expressed L1 fusion proteins of a variety of HPV types. Conformational and linear epitopes have been distinguished using native and denatured virus-like particles. HPV infection of genital lesions has been analysed using both monoclonal antibodies and DNA amplification by PCR. The antibodies obtained should be useful to pr…

medicine.drug_classRecombinant Fusion ProteinsMolecular Sequence DataUterine Cervical NeoplasmsCross ReactionsAntibodies ViralMonoclonal antibodyEpitopeVirusCapsidAntigenAntibody SpecificityVirologyEscherichia colimedicineHumansAmino Acid SequenceCloning MolecularAntigens ViralPapillomaviridaeBase SequencebiologyVirionHPV infectionAntibodies MonoclonalUterine Cervical Dysplasiamedicine.diseaseFusion proteinVirologyMolecular biologyCapsidCondylomata AcuminataDNA Viralbiology.proteinFemaleAntibodySequence AlignmentEpitope MappingJournal of General Virology
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