Search results for "Amino acid sequence"

showing 10 items of 1296 documents

Cloning and characterization of PRA1, a gene encoding a novel pH-regulated antigen of Candida albicans.

1998

ABSTRACT Candida albicans is an opportunistic fungal pathogen of humans. The cell wall of the organism defines the interface between the pathogen and host tissues and is likely to play an essential and pivotal role in the host-pathogen interaction. The components of the cell wall critical to this interaction are undefined. Immunoscreening of a lambda expression library with sera raised against mycelial cell walls of C. albicans was used to identify genes encoding cell surface proteins. One of the positive clones represented a candidal gene that was differentially expressed in response to changes in the pH of the culture medium. Maximal expression occurred at neutral pH, with no expression d…

Antigens FungalDNA ComplementaryMolecular Sequence DataReceptors Cell SurfaceMicrobiologyFungal ProteinsImmunoscreeningGene Expression Regulation FungalCandida albicansAmino Acid SequenceCloning MolecularCandida albicansMolecular BiologyGenePeptide sequencechemistry.chemical_classificationFungal proteinbiologyBase SequenceSequence Homology Amino AcidHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyCorpus albicansPhenotypeEukaryotic CellschemistryCell fractionationGlycoproteinJournal of bacteriology
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Bioactive peptides as natural antioxidants in food products - A review

2018

Background: Diseases related to oxidative stress and food quality decay are of major concern worldwide as they can lead to economic losses in both public health and food production. The antioxidant peptides, extracted from food proteins, can be explored as natural new drug and food ingredient. Scope and approach Antioxidant peptides are extracted from non-antioxidant precursor proteins from different origin by the activity of either proteolytic microorganisms or isolated enzymes. In the present review, the main sources of bioactive peptides will be discussed. Moreover, the current strategies to obtain these compounds as well as their health benefits and in vivo biological effects will be ev…

Antioxidantfood.ingredientProteolysismedicine.medical_treatmentFood technologyIngredient0404 agricultural biotechnologyfoodmedicinechemistry.chemical_classificationmedicine.diagnostic_testChemistrybusiness.industryFood additiveActive amino acid sequence04 agricultural and veterinary sciencesFood additives040401 food scienceEnzymeBiochemistryOxidative stressProteolysisFood processingbusinessFood qualityFood ScienceBiotechnologyAntioxidant defencesFood quality
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Diversification of CYCLOIDEA-like TCP genes in the basal eudicot families Fumariaceae and Papaveraceae s.str.

2006

CYCLOIDEA-like genes belong to the TCP family of transcriptional regulators and have been shown to control different aspects of shoot development in various angiosperm lineages, including flower monosymmetry in asterids and axillary meristem growth in monocots. Genes related to the CYC gene from ANTIRRHINUM show independent duplications in both asterids and rosids. However, it remains unclear to what extent this affected the evolution of flower symmetry and shoot branching in these and other eudicot lineages. Here, we show that CYC-like genes have also undergone duplications in two related Ranunculales families, Fumariaceae and Papaveraceae s.str. These families exhibit morphological divers…

AquilegiaAsteridsMolecular Sequence DataPlant ScienceFlowersBiologyGenes PlantEvolution MolecularPhylogeneticsPapaveraceaeGene duplicationPapaveraceaeAmino Acid SequenceEcology Evolution Behavior and SystematicsPhylogenyPlant ProteinsGeneticsPhylogenetic treefungiAntirrhinumfood and beveragesGenetic VariationGeneral Medicinebiology.organism_classificationDNA-Binding ProteinsRanunculalesOrgan SpecificityFumariaceaeTranscription FactorsPlant biology (Stuttgart, Germany)
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orthoFind Facilitates the Discovery of Homologous and Orthologous Proteins

2015

Finding homologous and orthologous protein sequences is often the first step in evolutionary studies, annotation projects, and experiments of functional complementation. Despite all currently available computational tools, there is a requirement for easy-to-use tools that provide functional information. Here, a new web application called orthoFind is presented, which allows a quick search for homologous and orthologous proteins given one or more query sequences, allowing a recurrent and exhaustive search against reference proteomes, and being able to include user databases. It addresses the protein multidomain problem, searching for homologs with the same domain architecture, and gives a si…

Architecture domainScienceBrute-force searchSequence alignmentComputational biologyBiologyAnnotationDatabases GeneticHomologous chromosomeAnimalsHumansWeb applicationAmino Acid SequenceGeneticsInternetMultidisciplinarySequence Homology Amino Acidbusiness.industryQRProteinsSequence homologyProteomeMedicinebusinessSequence AlignmentSoftwareResearch ArticlePLOS ONE
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Arginine-rich peptides are blockers of VR-1 channels with analgesic activity

2000

Vanilloid receptors (VRs) play a fundamental role in the transduction of peripheral tissue injury and/or inflammation responses. Molecules that antagonize VR channel activity may act as selective and potent analgesics. We report that synthetic arginine-rich hexapeptides block heterologously expressed VR-1 channels with submicromolar efficacy in a weak voltage-dependent manner, consistent with a binding site located near/at the entryway of the aqueous pore. Dynorphins, natural arginine-rich peptides, also blocked VR-1 activity with micromolar affinity. Notably, synthetic and natural arginine-rich peptides attenuated the ocular irritation produced by topical capsaicin application onto the eye…

ArginineReceptors DrugBiophysicsTRPV Cation ChannelsPainDynorphinPharmacologyArginineEyeDynorphinsBiochemistryInhibitory Concentration 50MiceXenopus laevisDynorphinchemistry.chemical_compoundStructural BiologyNon-competitive antagonistGeneticsAnimalsChannel blockerAmino Acid SequenceBinding siteReceptorMolecular BiologyNon-competitive antagonistAnalgesicsChemistryElectric ConductivityNociceptorCell BiologyCapsaicinIonic poreOocytesNociceptorCapsaicinPeptidesFEBS Letters
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Activation of nitric oxide signaling by the rheumatoid arthritis shared epitope

2006

Objective. Susceptibility to rheumatoid arthritis (RA) is closely associated with HLA–DRB1 alleles encoding a shared epitope (SE) in positions 70–74 of the HLA–DR chain. The mechanistic basis for this association is unknown. Given the proposed pathogenic role of nitric oxide (NO) in RA, this study was undertaken to examine whether the SE can trigger NO signaling events. Methods. The intracellular levels of NO were measured with the fluorescent NO probe 4,5diaminofluorescein diacetate and by the 2,3diaminonaphthalene method. NO synthase activity was determined by measuring the rate of conversion of radioactive arginine to citrulline. Levels of cGMP were measured with a commercial enzyme-link…

ArginineT-LymphocytesMolecular Sequence DataImmunologyCellBiologyNitric OxideEpitopeCell LineNitric oxideArthritis Rheumatoidchemistry.chemical_compoundRheumatologymedicineCitrullineHumansImmunology and AllergyPharmacology (medical)Amino Acid SequenceB cellB-LymphocytesLymphoblastHLA-DR1 AntigenFibroblastsMolecular biologyChromium Radioisotopesmedicine.anatomical_structurechemistryImmunologyEpitopes B-LymphocyteFluoresceinIndicators and ReagentsSignal transductionSignal TransductionArthritis & Rheumatism
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Bacterial sensor kinases using Fe–S cluster binding PAS or GAF domains for O2sensing

2012

[4Fe-4S](2+) clusters are used by very diverse types of bacterial sensors for response to oxygen, including DNA-binding proteins of the CRP/FNR family and sensor kinases like NreB. In NreB the cluster is bound by an input domain of the PAS type. The [4Fe-4S](2+) cluster of NreB responds to O(2) by degradation to a [2Fe-2S](2+) cluster which is labile and decomposes. NreB constitutes together with AirS the NreB/AirS family of bacterial sensor kinases that contain PAS or GAF domains for binding of [4Fe-4S](2+) or [2Fe-2S](2+) clusters and oxygen sensing. The NreB/AirS family is related to the FixL sensor kinases that use hemeB binding PAS domains for oxygen sensing.

BacteriaKinaseStereochemistryChemistryIronOxygen metabolismMolecular Sequence DataPhosphotransferasesO2 sensingBioinformaticsProtein Structure TertiaryOxygenInorganic ChemistryProtein structureCluster (physics)Amino Acid SequencePeptide sequenceOxygen sensingSulfurDalton Trans.
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Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins.

1996

Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin are well-studied prototypes of pore-forming bacterial cytotoxins. Each is produced as a water-soluble single-chain polypeptide that inserts into target membranes to form aqueous transmembrane pores. This review will compare properties of the three toxin prototypes, highlighting the similarities and also the differences in their structure, mode of binding, mechanism of pore formation, and the responses they elicit in target cells. Pore-forming toxins represent the most potent and versatile weapons with which invading microbes damage the host macroorganism.

Bacterial ToxinsLipid BilayersMolecular Sequence Datamedicine.disease_causeBiochemistryMicrobiologyMicrobiologyHemolysin ProteinsBacterial ProteinsEscherichiaGeneticsmedicineAnimalsHumansAmino Acid SequenceMolecular BiologyEscherichia colibiologyToxinEscherichia coli ProteinsCell MembraneHemolysinGeneral Medicinebiology.organism_classificationEnterobacteriaceaeBiochemistryStreptolysinsStreptolysinCytolysinExotoxinArchives of microbiology
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Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus…

1992

The homologous C-terminal repeats of Clostridium difficile toxins (ToxA and ToxB) and streptococcal glucosyltransferases appear to mediate protein-carbohydrate interactions at cellular binding sites with sugar moieties as substrates. A consensus sequence of 134 repeating units from gram-positive bacteria indicates that these repeats have a modular design with (i) a stretch of aromatic amino acids proposed to be involved in the primary carbohydrate-protein interaction, (ii) an amplification of this interaction by repetition of the respective sequences, and (iii) a second domain, not characterized, that is responsible for carbohydrate specificity.

Bacterial ToxinsMolecular Sequence DataEnterotoxinMicrobiologyMicrobiologyStreptococcus mutanschemistry.chemical_compoundEnterotoxinsGlucosyltransferasesBacterial ProteinsGlycosyltransferaseConsensus SequenceConsensus sequenceAromatic amino acidsAmino Acid SequenceBinding siteMolecular BiologyPeptide sequenceBinding SitesbiologySequence Homology Amino AcidClostridioides difficileCytotoxinsClostridium difficilechemistryBiochemistryGlucosyltransferasesbiology.proteinCarbohydrate MetabolismResearch ArticleJournal of bacteriology
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Shared Binding Sites in Lepidoptera for Bacillus thuringiensis Cry1Ja and Cry1A Toxins

2001

ABSTRACT Bacillus thuringiensis toxins act by binding to specific target sites in the insect midgut epithelial membrane. The best-known mechanism of resistance to B. thuringiensis toxins is reduced binding to target sites. Because alteration of a binding site shared by several toxins may cause resistance to all of them, knowledge of which toxins share binding sites is useful for predicting cross-resistance. Conversely, cross-resistance among toxins suggests that the toxins share a binding site. At least two strains of diamondback moth ( Plutella xylostella ) with resistance to Cry1A toxins and reduced binding of Cry1A toxins have strong cross-resistance to Cry1Ja. Thus, we hypothesized that…

Bacterial ToxinsMolecular Sequence DataSpodopteraBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsAmino Acid SequenceBinding siteBinding SitesDiamondback mothBacillus thuringiensis ToxinsEcologybiologyHeliothis virescensfungibiology.organism_classificationEndotoxinsLepidopteraPlutellidaeCry1AcLarvaNoctuidaeFood ScienceBiotechnologyApplied and Environmental Microbiology
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