Search results for "Amino acid sequence"

showing 10 items of 1296 documents

The endopolygalacturonase 1 from botrytis cinerea activates grapevine defense reactions unrelated to its enzyumatic activity

2003

A purified glycoprotein from Botrytis cinerea(strain T4), identified as endopolygalacturonase 1 (T4BcPG1) by mass spectrometry analysis, has been shown to activate defense reactions in grapevine (Vitis vinifera cv. Gamay). These reactions include calcium influx, production of active oxygen species, activation of two mitogen-activated protein kinases, defense gene transcript accumulation, and phytoalexin production. Most of these defense reactions were also activated in grapevine in response to purified oligogalacturonides (OGA) with a degree of polymerization of 9 to 20. In vivo, these active OGA might be a part of the released products resulting from endopolygalacturonase activity on plan…

elicitor; endopolygalacturonase 1; Botrytis cinerea; plant defenceplant defencePhysiologyMolecular Sequence DataOligosaccharidesBiologyCell wallBotrytis cinereaGene Expression Regulation PlantSequence Homology Nucleic Acid[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyVitisAmino Acid SequencePectinaseendopolygalacturonase 1ComputingMilieux_MISCELLANEOUSBotrytis cinereachemistry.chemical_classificationelicitorBase SequenceSequence Homology Amino AcidKinasePhytoalexinfood and beveragesGeneral MedicineHydrogen Peroxidebiology.organism_classificationImmunity InnateElicitorEnzyme ActivationEnzymePolygalacturonasechemistryBiochemistryCalciumBotrytisMitogen-Activated Protein KinasesGlycoproteinAgronomy and Crop Science
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Identification and characterization of autoantibodies against catalase and α-enolase in patients with primary sclerosing cholangitis

1998

SUMMARY Primary sclerosing cholangitis (PSC) is a chronic cholestatic liver disease of unknown aetiology. Recent studies have shown that genetic factors and both cellular and humoral immunological abnormalities are important in the pathogenesis of PSC. The most prominent autoantibodies in PSC are anti-neutrophil cytoplasmic antibodies (ANCA). The autoepitopes of ANCA in PSC are not well defined. The aim of this study was to identify corresponding ANCA autoantigens in patients with PSC. A biochemical approach with enrichment and partial purification of soluble neutrophil proteins, detection of autoantibodies by Western blot and partial amino acid sequencing were used. Two new autoantigen/aut…

endocrine system diseasesAlpha-enolaseBlotting WesternCholangitis SclerosingMolecular Sequence DataImmunologyAutoimmunityEnzyme-Linked Immunosorbent Assaymedicine.disease_causedigestive systemAutoimmunityPrimary sclerosing cholangitisAntigenWestern blotmedicineHumansImmunology and AllergyAmino Acid SequenceAutoantibodiesAnti-neutrophil cytoplasmic antibodybiologymedicine.diagnostic_testdigestive oral and skin physiologyAutoantibodyOriginal ArticlesCatalasemedicine.diseasedigestive system diseasesPhosphopyruvate HydrataseImmunologybiology.proteinAntibodyClinical and Experimental Immunology
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Type II keratin cDNAs from the rainbow trout: implications for keratin evolution.

2002

From a teleost fish, the rainbow trout Oncorhynchus mykiss, we have cloned and sequenced cDNAs encoding five different type II keratins. The corresponding protein spots, as separated by 2D-PAGE of trout cytoskeletal preparations, have been identified by peptide mass mapping using MALDI mass spectrometry. Three of the sequenced keratins are expressed in the epidermis (subtype IIe), and two in simple epithelia and mesenchymal cells (subtype IIs). The IIs keratins are both orthologs of human K8. This leaves unsequenced only the trace component S3 of the biochemically established trout keratin catalog. A phylogenetic tree has been constructed from a multiple alignment of the rod domains of the …

endocrine systemCancer Researchanimal structuresDNA ComplementaryMolecular Sequence Datamacromolecular substancesPeptide MappingType II keratinEvolution MolecularMesodermSpecies SpecificityAntibody SpecificityKeratinAnimalsHumansProtein IsoformsAmino Acid SequenceCloning MolecularMolecular BiologyZebrafishPhylogenyZebrafishchemistry.chemical_classificationGeneticsMammalsMultiple sequence alignmentintegumentary systembiologyPhylogenetic treeSequence Homology Amino AcidLampreyAntibodies MonoclonalLampreysEpithelial CellsCell Biologybiology.organism_classificationProtein Structure TertiaryTroutchemistryOrgan SpecificityOncorhynchus mykissSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationSharksKeratinsRainbow troutEpidermisSequence AlignmentDevelopmental BiologyDifferentiation; research in biological diversity
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Identification of a Functional Homolog of the Yeast Copper Homeostasis Gene ATX1 from Arabidopsis1

1998

Abstract A cDNA clone encoding a homolog of the yeast (Saccharomyces cerevisiae) gene Anti-oxidant 1(ATX1) has been identified from Arabidopsis. This gene, referred to as CopperCHaperone(CCH), encodes a protein that is 36% identical to the amino acid sequence of ATX1 and has a 48-amino acid extension at the C-terminal end, which is absent from ATX1 homologs identified in animals. ATX1-deficient yeast (atx1) displayed a loss of high-affinity iron uptake. Expression of CCH in the atx1 strain restored high-affinity iron uptake, demonstrating thatCCH is a functional homolog of ATX1. When overexpressed in yeast lacking the superoxide dismutase geneSOD1, both ATX1 and CCHprotected the cell from t…

endocrine systemDNA ComplementarySaccharomyces cerevisiae ProteinsPhysiologyMolecular Sequence DataSaccharomyces cerevisiaeSOD1ArabidopsisGene ExpressionSaccharomyces cerevisiaePlant ScienceFungal ProteinsGene productSuperoxide dismutaseOzoneCopper Transport ProteinsComplementary DNAArabidopsisGene expressionGeneticsHomeostasisAmino Acid SequenceCation Transport ProteinsBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsGenetic Complementation Testbiology.organism_classificationYeastOxidative StressBiochemistrybiology.proteinCarrier ProteinsCopperResearch ArticlePlant Physiology
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Origin of Insulin Receptor-Like Tyrosine Kinases in Marine Sponges

1999

One autapomorphic character restricted to all Metazoa including Porifera [sponges] is the existence of transmembrane receptor tyrosine kinases (RTKs). In this study we screened for molecules from one subfamily within the superfamily of the insulin receptors. The subfamily includes the insulin receptors (InsR), the insulin-like growth factor I receptors, and the InsR-related receptors--all found in vertebrates--as well as the InsR-homolog from Drosophila melanogaster. cDNAs encoding putative InsRs were isolated from the hexactinellid sponge Aphrocallistes vastus, the demosponge Suberites domuncula, and the calcareous sponge Sycon raphanus. Phylogenetic analyses of the catalytic domains of th…

endocrine systemDNA ComplementarySubfamilyMolecular Sequence DataReceptor tyrosine kinaseEvolution MolecularMiceDemospongeCatalytic DomainBotanyAnimalsHumansAmino Acid SequenceSycon raphanusCloning MolecularPhylogenyCephalochordateBase SequenceSequence Homology Amino Acidbiologygeodia cydonium; adhesion receptors; evolutionnutritional and metabolic diseasesSequence Analysis DNAbiology.organism_classificationReceptor InsulinPoriferaRatsSuberites domunculaInsulin receptorSpongeBiochemistrybiology.proteinGeneral Agricultural and Biological Scienceshormones hormone substitutes and hormone antagonistsThe Biological Bulletin
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A mutation in the second intracellular loop of the pituitary adenylate cyclase activating polypeptide type I receptor confers constitutive receptor a…

2000

AbstractThe pituitary adenylate cyclase activating polypeptide (PACAP) type I receptor belongs to the glucagon/secretin/vasoactive intestinal polypeptide (VIP) receptor family. We mutated and deleted an amino acid residue (E261) which is located within the second intracellular loop of the rat PACAP type I receptor and which is highly conserved among the receptor family. The wild-type receptor and the mutant receptors were efficiently expressed at the surface of COS-7 cells at nearly the same level and revealed the same high affinity for the agonist PACAP-27. The cAMP contents of COS cells transfected with the E261A, E261Q, and the deletion mutant receptor were 4.6-, 5.7-, and 6.7-fold highe…

endocrine systemGrowth-hormone-releasing hormone receptorMolecular Sequence DataReceptors Pituitary Adenylate Cyclase-Activating PolypeptideBiophysicsGlutamic AcidSignal transductionTransfectionBiochemistryBeta-1 adrenergic receptorConstitutive activityStructural BiologycAMPCyclic AMPGeneticsEnzyme-linked receptorAnimals5-HT5A receptorAmino Acid SequenceReceptors Pituitary HormoneMolecular BiologySequence DeletionPeptide hormone receptorSite-directed mutagenesisPituitary adenylate cyclase activating polypeptideChemistryLiver receptor homolog-1Cell BiologyMolecular biologyRatsInterleukin-21 receptorCOS CellsMutagenesis Site-DirectedEstrogen-related receptor gammaSequence AlignmentGlucagon receptor familyhormones hormone substitutes and hormone antagonistsAdenylyl CyclasesReceptors Pituitary Adenylate Cyclase-Activating Polypeptide Type IFEBS Letters
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New biological aspects of Chromogranin A-derived peptides: Focus on vasostatins

2007

Chromogranin A (CgA), one component of the granin family, represents the major soluble protein co-stored and co-released with catecholamines, within chromaffin cells secretory granules. It is considered a diagnostic and prognostic marker of several diseases, including a variety of tumours and cardiac heart failure. It also represents a precursor of biologically active fragments, generated after proteolytic cleavage at the level of the multiple pairs of dibasic sites which enrich its sequence. CgA, and its derived fragments show an old evolutionary history being ubiquitously present throughout the animal word, from mammals to invertebrates. Their biological functions include control of hormo…

endocrine systemPhysiologyMolecular Sequence DataBiologyModels BiologicalBiochemistryParacrine signallingChromogranine AAnimalsHumansAmino Acid SequenceAutocrine signallingMolecular BiologyPeptide sequencePhylogenyInnate immune systemSettore BIO/16 - Anatomia UmanaGraninChromogranin APeptide FragmentsBiochemistrybiology.proteinChromogranin AParathyroid hormone secretionNeuroendocrine tumorsCalreticulinHomeostasisComparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology
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Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors.

1999

The assembly of signalling molecules into macromolecular complexes (transducisomes) provides specificity, sensitivity and speed in intracellular signalling pathways. Rod photoreceptors in the eye contain an unusual set of glutamic-acid-rich proteins (GARPs) of unknown function. GARPs exist as two soluble forms, GARP1 and GARP2, and as a large cytoplasmic domain (GARP' part) of the beta-subunit of the cyclic GMP-gated channel. Here we identify GARPs as multivalent proteins that interact with the key players of cGMP signalling, phosphodiesterase and guanylate cyclase, and with a retina-specific ATP-binding cassette transporter (ABCR), through four, short, repetitive sequences. In electron mic…

genetic structuresPhosphodiesterase InhibitorsMolecular Sequence DataCyclic Nucleotide-Gated Cation ChannelsGlutamic AcidNerve Tissue ProteinsPlasma protein bindingBiologyIn Vitro TechniquesRetinal Rod Photoreceptor CellsAnimalsAmino Acid SequenceTransducinEye ProteinsPeptide sequenceCyclic GMPMultidisciplinaryPhosphoric Diester HydrolasesPhosphodiesteraseProteinsTransporterGlutamic acidRod Cell Outer SegmentRecombinant ProteinsCell biologyBiochemistryCytoplasmGuanylate CyclaseATP-Binding Cassette TransportersCattleTransducinSignal transductionProtein BindingSignal TransductionNature
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AMPA Receptor Auxiliary Proteins of the CKAMP Family

2019

α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors are assembled of four core subunits and several additional interacting proteins. Cystine-knot AMPA receptor-modulating proteins (CKAMPs) constitute a family of four proteins that influence the trafficking, subcellular localization and function of AMPA receptors. The four CKAMP family members CKAMP39/shisa8, CKAMP44/shisa9, CKAMP52/shisa6 and CKAMP59/shisa7 differ in their expression profile and their modulatory influence on AMPA receptor function. In this review, I report about recent findings on the differential roles of CKAMP family members.

glutamate receptorhippocampusGene ExpressionReviewAMPA receptorBiologySynaptic TransmissionCatalysisCell Linelcsh:ChemistryInorganic ChemistryLong term plasticitylateral geniculate nucleusAnimalsHumansAmino Acid SequenceReceptors AMPAAMPA receptorPhysical and Theoretical Chemistrysynaptic functionReceptorlcsh:QH301-705.5Molecular BiologySpectroscopyNeuronal Plasticitymusculoskeletal neural and ocular physiologyOrganic ChemistryGlutamate receptorGeniculate BodiesGeneral MedicineSubcellular localizationlong-term plasticityComputer Science ApplicationsCell biologyProtein TransportSynaptic functionlcsh:Biology (General)lcsh:QD1-999nervous systemauxiliary subunitMultigene FamilySynapsesCarrier ProteinsIon Channel Gatingshort-term plasticityFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Redox modulation of Rubisco conformation and activity through its cysteine residues

2008

Treatment of purified Rubisco with agents that specifically oxidize cysteine-thiol groups causes catalytic inactivation and increased proteolytic sensitivity of the enzyme. It has been suggested that these redox properties may sustain a mechanism of regulating Rubisco activity and turnover during senescence or stress. Current research efforts are addressing the structural basis of the redox modulation of Rubisco and the identification of critical cysteines. Redox shifts result in Rubisco conformational changes as revealed by the alteration of its proteolytic fragmentation pattern upon oxidation. In particular, the augmented susceptibility of Rubisco to proteases is due to increased exposure…

inorganic chemicalsChloroplastsbiologyPhysiologyCatabolismCysteamineRibulose-Bisphosphate CarboxylasefungiRuBisCOMutagenesisfood and beveragesChlamydomonas reinhardtiiPlant ScienceOxidative phosphorylationPlantsbiology.organism_classificationRedoxChloroplastBiochemistryPlant Cellsbiology.proteinAmino Acid SequenceOxidation-ReductionCysteineJournal of Experimental Botany
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