Search results for " Homology"

showing 10 items of 633 documents

Wheat amylase trypsin inhibitors drive intestinal inflammation via activation of toll-like receptor 4

2012

Ingestion of wheat, barley, or rye triggers small intestinal inflammation in patients with celiac disease. Specifically, the storage proteins of these cereals (gluten) elicit an adaptive Th1-mediated immune response in individuals carrying HLA-DQ2 or HLA-DQ8 as major genetic predisposition. This well-defined role of adaptive immunity contrasts with an ill-defined component of innate immunity in celiac disease. We identify the α-amylase/trypsin inhibitors (ATIs) CM3 and 0.19, pest resistance molecules in wheat, as strong activators of innate immune responses in monocytes, macrophages, and dendritic cells. ATIs engage the TLR4–MD2–CD14 complex and lead to up-regulation of maturation markers a…

GliadinMice0302 clinical medicineHEK293 CellImmunology and AllergyTriticumPlant Proteins2. Zero hungerMice Knockout0303 health sciencesToll-like receptorMice Inbred C3Hfood and beveragesPlant ProteinU937 CellsAcquired immune system3. Good health030211 gastroenterology & hepatologymedicine.symptomTrypsin InhibitorsHumanSignal TransductionImmunologyMolecular Sequence DataInflammationBiologyProinflammatory cytokineCell Line03 medical and health sciencesImmune systemImmunitymedicineAnimalsHumansAmino Acid Sequence030304 developmental biologyInnate immune systemSequence Homology Amino AcidAnimalBIO/13 - BIOLOGIA APPLICATAnutritional and metabolic diseasesHordeumImmunity InnateToll-Like Receptor 4Mice Inbred C57BLCeliac DiseaseHEK293 CellsImmunologyMyeloid Differentiation Factor 88TLR4Trypsin Inhibitor
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The inhibition of glycerol permeation through aquaglyceroporin-3 induced by mercury(II)

2016

Mercurial compounds are known to inhibit water permeation through aquaporins (AQPs). Although in the last years some hypotheses were proposed, the exact mechanism of inhibition is still an open question and even less is known about the inhibition of the glycerol permeation through aquaglyceroporins. Molecular dynamics (MD) simulations of human aquaporin-3 (AQP3) have been performed up to 200 ns in the presence of Hg2+ ions. For the first time, we have observed the unbiased passage of a glycerol molecule from the extracellular to cytosolic side. Moreover, the presence of Hg2+ ions covalently bound to Cys40 leads to a collapse of the aromatic/arginine selectivity filter (ar/R SF), blocking th…

Glycerol0301 basic medicineMolecular dynamicCell Membrane PermeabilityBiochemistryProtein Structure Secondarychemistry.chemical_compoundGLPFCOORDINATIONCRYSTALEscherichia coli ProteinsPermeationBiochemistryCovalent bondSettore CHIM/03 - Chimica Generale E InorganicaPhosphatidylcholinesCOMPLEXESProtein BindingSTRUCTURAL BASISCations DivalentPlasmodium falciparumAquaporinCYSTEINE-189Molecular Dynamics SimulationMolecular dynamicsAquaporinsWATER CHANNELInorganic Chemistry03 medical and health sciencesEscherichia coliGlycerolExtracellularHumansMoleculePERMEABILITYProtein Structure QuaternaryAquaporin 3Binding SitesAQUAPORIN INHIBITIONWaterBiological TransportMembranes ArtificialAquaglyceroporinMercurySIMULATIONSProtein Structure TertiaryCytosolWater permeation030104 developmental biologyAquaglyceroporinschemistryStructural Homology ProteinBiophysicsGlycerol permeationJournal of Inorganic Biochemistry
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The shell-forming proteome of Lottia gigantea reveals both deep conservations and lineage-specific novelties

2013

19 pages; International audience; Proteins that are occluded within the molluscan shell, the so-called shell matrix proteins (SMPs), are an assemblage of biomolecules attractive to study for several reasons. They increase the fracture resistance of the shell by several orders of magnitude, determine the polymorph of CaCO(3) deposited, and regulate crystal nucleation, growth initiation and termination. In addition, they are thought to control the shell microstructures. Understanding how these proteins have evolved is also likely to provide deep insight into events that supported the diversification and expansion of metazoan life during the Cambrian radiation 543 million years ago. Here, we p…

Glycoside Hydrolasesmedicine.medical_treatmentproteomeGastropodaMolecular Sequence DataBiologyBiochemistrymollusc shell matrix proteinsTranscriptomeCyclophilins03 medical and health sciencesPaleontologyLineage specificAnimal ShellsSequence Analysis ProteinTandem Mass Spectrometry[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]evolutionmedicineAnimalsAmino Acid Sequence14. Life underwaterMantle (mollusc)[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyCarbonic Anhydrases030304 developmental biologyExtracellular Matrix Proteins0303 health sciencesProteaseEpidermal Growth FactorSequence Homology Amino AcidLimpet030302 biochemistry & molecular biologyCell Biologybiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsbiomineralizationPeptide FragmentsProtein Structure TertiaryPeroxidasesEvolutionary biology[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomeLottia giganteaElectrophoresis Polyacrylamide GelmantleBiomineralization
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Identification of a positively evolving putative binding region with increased variability in posttranslational motifs in zonadhesin MAM domain 2.

2005

Positive selection has been shown to be pervasive in sex-related proteins of many metazoan taxa. However, we are only beginning to understand molecular evolutionary processes on the lineage to humans. To elucidate the evolution of proteins involved in human reproduction, we studied the sequence evolution of MAM domains of the sperm-ligand zonadhesin in respect to single amino acid sites, solvent accessibility, and posttranslational modification. GenBank-data were supplemented by new cDNA-sequences of a representative non-human primate panel. Solvent accessibility predictions identified a probably exposed fragment of 30 amino acids belonging to MAM domain 2 (i.e., MAM domain 3 in mouse). The…

GlycosylationGlycosylationMolecular Sequence DataBiologyProtein Serine-Threonine Kinaseschemistry.chemical_compoundMiceN-linked glycosylationGenetic variationGeneticsAnimalsAmino Acid SequenceBinding sitePhosphorylationSelection GeneticMolecular BiologyPeptide sequenceEcology Evolution Behavior and SystematicsBinding selectivitychemistry.chemical_classificationGeneticsBinding SitesBase SequenceSequence Homology Amino AcidGenetic VariationMembrane ProteinsAmino acidRepressor ProteinsSperm MaturationchemistryMultigene FamilyPhosphorylationProtein Processing Post-TranslationalTranscription FactorsMolecular phylogenetics and evolution
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Probing suggested catalytic domains of glycosyltransferases by site-directed mutagenesis.

2003

The plant enzyme arbutin synthase isolated from cell suspension cultures of Rauvolfia serpentina and heterologously expressed in Escherichia coli is a member of the NRD1beta family of glycosyltransferases. This enzyme was used to prove, by site-directed mutagenesis, suggested catalytic domains and reaction mechanisms proposed for enzyme-catalyzed glycosylation. Replacement of amino acids far from the NRD domain do not significantly affect arbutin synthase activity. Exchange of amino acids at the NRD site leads to a decrease of enzymatic activity, e.g. substitution of Glu368 by Asp. Glu368, which is a conserved amino acid in glycosyltransferases located at position 2 and is important for enz…

GlycosylationStereochemistryMolecular Sequence DataBiologyBiochemistryPolymerase Chain ReactionGene Expression Regulation EnzymologicRauwolfiaSubstrate Specificitychemistry.chemical_compoundCatalytic DomainGlycosyltransferaseEscherichia coliAmino Acid SequenceSite-directed mutagenesisConserved SequenceDNA Primerschemistry.chemical_classificationBinding SitesATP synthaseSequence Homology Amino AcidMutagenesisArbutinGlycosyltransferasesEnzyme assayRecombinant ProteinsAmino acidEnzymechemistryBiochemistryAmino Acid Substitutionbiology.proteinMutagenesis Site-DirectedEuropean journal of biochemistry
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Polymorphism in the immunoglobulin-like domains of the receptor tyrosine kinase from the sponge Geodia cydonium.

1996

Sponges [Porifera] are the phylogenetically oldest phylum of the Metazoa. They are provided with both cellular and humoral allorecognition systems. The underlying molecules are not yet known. To study allorecognition in sponges we first determined the frequency of graft rejection in a natural population of the marine sponge Geodia cydonium. We then determined, for the first time at the molecular level, the degree of sequence polymorphism in segments of one molecule which may be related to sponge allorecognition and host defense: the Ig-like domains from the receptor tyrosine kinase [RTK]. Thirty six pairs of auto- and allografts were assayed, either by parabiotic attachment or insertion of …

Graft RejectionDNA ComplementaryGeodia cydoniumMolecular Sequence DataImmunoglobulinsPolymerase Chain ReactionReceptor tyrosine kinaseMolecular levelSequence Homology Nucleic AcidAnimalsGeodiaAmino Acid SequenceAllorecognitionGene LibraryPolymorphism GeneticGraft rejectionbiologyBase SequenceSequence Homology Amino AcidReceptor Protein-Tyrosine KinasesGeneral MedicineAnatomySequence Analysis DNAbiology.organism_classificationCell biologyPoriferaSpongesurgical procedures operativebiology.proteinAntibodyCell adhesion and communication
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Suppression of allograft rejection in the sponge Suberites domuncula by FK506 and expression of genes encoding FK506-binding proteins in allografts.

2001

SUMMARY Porifera (sponges) are, evolutionarily, the oldest metazoan phylum. Recent molecular data suggest that these animals possess molecules similar to and homologous with those of the innate and adaptive immune systems of higher Metazoa. Applying the biological system of parabiosis and the technique of differential display of mRNA, two cDNAs encoding putative FK506-binding proteins were isolated. FK506 is successfully used in clinics as a drug to prevent allograft rejection and is toxic to Suberites domuncula cells in vitro at doses above 100ng ml−1. Autograft fusion of transplants from S. domuncula was not affected by FK506. Allograft non-fusion was not affected by FK506 at toxic doses;…

Graft RejectionDNA ComplementaryPhysiologyParabiosisMolecular Sequence DataGene ExpressionSequence HomologyAquatic SciencePolymerase Chain ReactionTacrolimusTacrolimus Binding ProteinsImmune systempolycyclic compoundsHomologous chromosomeAnimalsTransplantation HomologousAmino Acid SequenceCloning MolecularMolecular BiologyGeneEcology Evolution Behavior and SystematicsGene LibraryMessenger RNADifferential displaybiologyAnatomybiology.organism_classificationIn vitroCell biologyPoriferaSuberites domunculaInsect ScienceAnimal Science and ZoologyThe Journal of experimental biology
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Increased expression of the potential proapoptotic molecule DD2 and increased synthesis of leukotriene B4 during allograft rejection in a marine spon…

2000

Sponges (Porifera) are a classical model to study the events during tissue transplantation. Applying the 'insertion technique' autografts from the marine sponge Geodia cydonium fuse within 5 days. In contrast, allografts are rejected and destroyed. Here we show that during allograft rejection the cells in the grafts undergo apoptosis; 5 days after transplantation 46% of the cells show signs of apoptosis. In a previous study it was shown that during this process a tumor necrosis factor-like molecule is induced in allo- and xenografts. Molecules grouped to the superfamily of tumor necrosis factor receptors and a series of associated adapter molecules contain the characteristic death domain. T…

Graft RejectionLeukotriene B4Molecular Sequence DataGene ExpressionApoptosisLeukotriene B4Transplantation Autologouschemistry.chemical_compoundDownregulation and upregulationGene expressionAnimalsHumansTransplantation HomologousAmino Acid SequenceCloning MolecularReceptorMolecular BiologyDeath domainSequence Homology Amino AcidChemistryCell BiologyMolecular biologyPoriferaTransplantationAlcohol Oxidoreductasessurgical procedures operativeApoptosisTumor necrosis factor alphaPeptidesCell Death & Differentiation
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European Congress of Mathematics Kraków, 2 – 7 July, 2012

2013

Persistent homology is a recent grandchild of homology that has found use in science and engineering as well as in mathematics. This paper surveys the method as well as the applications, neglecting completeness in favor of highlighting ideas and directions. 2010 Mathematics Subject Classification. Primary 55N99; Secondary 68W30.

GrandchildPersistent homologyMathematics Subject ClassificationScience and engineeringHomology (mathematics)EpistemologySingular homology
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N-terminal myristoylation-dependent masking of neutralizing epitopes in the preS1 attachment site of hepatitis B virus

2011

The N-terminally myristoylated preS1 domain of the large hepatitis B surface protein (LHBs) mediates specific attachment of hepatitis B virus (HBV) to hepatocytes. Its B-cell epitopes leading to neutralization of infectivity are not yet characterized.We inserted C- and N-terminal preS1 peptides into the most immunogenic region of HBV core particles, therewith immunized Balb/c mice and determined binding properties and neutralization potential of resulting antibodies in vitro.The particles with preS1 inserts were highly immunogenic and the corresponding anti-preS antibodies strongly bound to HBV particles from chronic carriers infected with different HBV genotypes A-F. However, antibodies bi…

Hepatitis B virusHBsAgGenotypeMolecular Sequence DataIn Vitro TechniquesBiologymedicine.disease_causeMyristic AcidNeutralizationEpitopeMice03 medical and health sciencesHepatitis B Chronic0302 clinical medicinemedicineAnimalsHumansHepatitis B VaccinesAmino Acid SequenceHepatitis B AntibodiesProtein Precursors030304 developmental biologyHepatitis B virusInfectivityMice Inbred BALB C0303 health sciencesBinding SitesHepatitis B Surface AntigensSequence Homology Amino AcidHepatologyHepatitis Bmedicine.diseaseAntibodies NeutralizingVirology3. Good healthEpitope mappingbiology.proteinEpitopes B-Lymphocyte030211 gastroenterology & hepatologyAntibodyEpitope MappingJournal of Hepatology
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