Search results for "Amino acid sequence"

showing 10 items of 1296 documents

In silico characterization of an Iroquois family-related homeodomain protein.

2005

Homeobox genes have been demonstrated to play important roles during cancer differentiation and embryonic development. The subset of Iroquois-related homeobox genes (IRXs) have furthermore been. demonstrated to be involved in several embryonic developmental processes such as patterning of the anterior-posterior and dorso-ventral axis, as well as specific regions of the central nervous system, and differentiation of the otic vesicle, branchial epithelium, and limbs. We have characterized a novel homeodomain protein and corresponding gene by means of computational biology. Since the protein sequence displayed high similarity to the human IRX proteins, the newly identified homeodomain protein …

TBX1EMX2Molecular Sequence DataHomeobox A1BiologyHomeobox protein Nkx-2.5NKX2-3MiceGene OrderGeneticsAnimalsHumansAmino Acid SequenceRNA MessengerPhylogenyZebrafishExpressed Sequence TagsHomeodomain ProteinsBase SequenceGene Expression ProfilingChromosome MappingComputational BiologyGeneral MedicineExonsZebrafish ProteinsMolecular biologyIntronsGenesPAX4HomeoboxOtic vesicleTranscription FactorsInternational journal of molecular medicine
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Agouti-Related Proteins (AGRPs) and Agouti-Signaling Peptide (ASIP) in Fish and Chicken

2005

We performed an intensive search on sequence databases to identify orthologues of ASIP and AGRP peptides in a number of different species, revealing a number of genomic fragments coding for the C-terminal part of agouti-related motifs, different from annotated peptide sequences, including one fragment from chicken, two from zebrafish, two from Fugu (Takifugu rubripes), and three from Tetraodon (Tetraodon nigroviridis). We have thus shown for the first time that both AGRP and ASIP genes exist in many species in "lower vertebrates" and were most probably present in early stages of vertebrate evolution.

Takifugu rubripesMolecular Sequence DataTetraodon nigroviridisGeneral Biochemistry Genetics and Molecular BiologySpecies SpecificityHistory and Philosophy of Sciencebiology.animalDatabases GeneticAnimalsAgouti-Related ProteinAmino Acid SequenceTetraodonGeneZebrafishPeptide sequencePhylogenyGeneticsbiologyFuguGeneral Neurosciencedigestive oral and skin physiologyFishesProteinsVertebratebiology.organism_classificationAgouti Signaling ProteinIntercellular Signaling Peptides and ProteinsChickensAnnals of the New York Academy of Sciences
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A homolog of the putative tumor suppressor QM in the sponge Suberites domuncula: downregulation during the transition from immortal to mortal (apopto…

1999

Abstract The activation of components of the transcription factors such as AP-1 or c-jun is essential for a physiological response of metazoan cells during aging. The activity of such proto-oncoproteins is under enzymatic control. The function of c-jun is additionally modulated by the QM protein. Here, we studied the expression of the gene, encoding the QM-like protein in the sponge Suberites domuncula . These animals contain high levels of telomerase in their somatic cells. To understand the switch from telomerase-positive immortal cells to telomerase-negative mortal cells which undergo apoptosis, the expression of the QM-like gene was measured in this system. The cDNA, termed QMSD , encod…

TelomeraseMolecular Sequence DataDown-RegulationGene ExpressionApoptosisDownregulation and upregulationComplementary DNAAnimalsHumansAmino Acid SequenceRNA MessengerCloning MolecularTranscription factorGenePhylogenyBase Sequencebiologyc-junProteinsRNA-Binding ProteinsCell BiologyGeneral Medicinebiology.organism_classificationMolecular biologyPoriferaSuberites domunculaOpen reading frameProtein BiosynthesisCarrier ProteinsDevelopmental BiologyTissue and Cell
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Expression of solute carrier 7A4 (SLC7A4) in the plasma membrane is not sufficient to mediate amino acid transport activity.

2002

Member 4 of human solute carrier family 7 (SLC7A4) exhibits significant sequence homology with the SLC7 subfamily of human cationic amino acid transporters (hCATs) [Sperandeo, Borsani, Incerti, Zollo, Rossi, Zuffardi, Castaldo, Taglialatela, Andria and Sebastio (1998) Genomics 49, 230–236]. It is therefore often referred to as hCAT-4 even though no convincing transport activity has been shown for this protein. We expressed SLC7A4 in Xenopus laevis oocytes, but could not detect any transport activity for cationic, neutral or anionic amino acids or for the polyamine putrescine. In addition, human glioblastoma cells stably overexpressing a fusion protein between SLC7A4 and the enhanced green f…

TeratocarcinomaAmino Acid Transport System y+Recombinant Fusion ProteinsGreen Fluorescent ProteinsMolecular Sequence DataRetinoic acidBiologyArginineBiochemistryPolymerase Chain ReactionGreen fluorescent proteinchemistry.chemical_compoundXenopus laevisTumor Cells CulturedAnimalsHumansAmino acid transporterAmino Acid SequenceAmino AcidsMolecular BiologyPeptide sequenceDNA Primerschemistry.chemical_classificationMammalsSequence Homology Amino AcidCell MembraneCell BiologySubcellular localizationFusion proteinAmino acidSolute carrier familyKineticsLuminescent ProteinschemistryBiochemistryGlioblastomaSequence AlignmentResearch Article
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Glucosylation of Rho proteins by Clostridium difficile toxin B.

1995

TOXIN A and B, the major virulence factors of Clostridium difficile, are the causative agents of antibiotic-associated pseudomembran-ous colitis. In cultured cell lines their potent cytotoxicity results from their ability to induce disaggregation of the microfilament cytoskeleton1,2. Toxin B acts on the low-molecular-mass GTPase Rho A3,4, which is involved in the regulation of the actin cytoskeleton. We report here that toxin B catalyses the incorporation of up to one mole of glucose per mole of RhoA at the amino acid thre-onine at position 37. The modification was identified and localized by tandem electrospray mass spectrometry. UDP-glucose selectively serves as cosubstrate for the monogl…

ThreonineRHOAGlycosylationBacterial ToxinsMolecular Sequence DataClostridium difficile toxin AClostridium difficile toxin Bmacromolecular substancesmedicine.disease_causeMicrofilamentCatalysisMass SpectrometryGTP PhosphohydrolasesBacterial ProteinsGTP-Binding ProteinsmedicineTumor Cells CulturedAnimalsAmino Acid SequenceCytoskeletonActinCells CulturedCytoskeletonMultidisciplinarybiologyToxinClostridioides difficileActin cytoskeletonActinsRecombinant ProteinsRatsGlucoseMarsupialiaBiochemistryGlucosyltransferasesbiology.proteinrhoA GTP-Binding ProteinNature
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Bradykinin-induced Internalization of the Human B2Receptor Requires Phosphorylation of Three Serine and Two Threonine Residues at Its Carboxyl Tail

1999

The binding of bradykinin (BK) to B2 receptor triggers the internalization of the agonist-receptor complex. To investigate the mechanisms and the receptor structures involved in this fundamental process of receptor regulation, the human B2 receptor was mutated within its cytoplasmic tail by complementary strategies of truncation, deletion, and amino acid substitution. Ligand binding, signal transduction, internalization as well as phosphorylation were studied for the mutated receptors expressed in COS, CHO, and HEK 293 cells. Truncation of 44 out of 55 amino acid residues of the receptor's cytoplasmic tail corresponding to positions 321-364 did not alter the kinetics of BK binding and the r…

ThreonineReceptor Bradykinin B2media_common.quotation_subjectMolecular Sequence DataCHO CellsBiologyBradykininTransfectionBiochemistryCell LineSerineCricetinaeSerineAnimalsHumans5-HT5A receptorAmino Acid SequencePhosphorylationInternalizationReceptorMolecular BiologyPeptide sequenceDNA Primersmedia_commonBase SequenceReceptors BradykininCoated Pits Cell-MembraneCell BiologyInterleukin-13 receptorClathrinEndocytosisRecombinant ProteinsCell biologyKineticsBiochemistryCOS CellsPhosphorylationSignal transductionJournal of Biological Chemistry
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Ras, Rap, and Rac Small GTP-binding Proteins Are Targets for Clostridium sordellii Lethal Toxin Glucosylation

1996

Lethal toxin (LT) from Clostridium sordellii is one of the high molecular mass clostridial cytotoxins. On cultured cells, it causes a rounding of cell bodies and a disruption of actin stress fibers. We demonstrate that LT is a glucosyltransferase that uses UDP-Glc as a cofactor to covalently modify 21-kDa proteins both in vitro and in vivo. LT glucosylates Ras, Rap, and Rac. In Ras, threonine at position 35 was identified as the target amino acid glucosylated by LT. Other related members of the Ras GTPase superfamily, including RhoA, Cdc42, and Rab6, were not modified by LT. Incubation of serum-starved Swiss 3T3 cells with LT prevents the epidermal growth factor-induced phosphorylation of m…

ThreonineUridine Diphosphate GlucoseRHOABacterial ToxinsMolecular Sequence DataClostridium sordelliimacromolecular substancesCDC42GTPaseBiologyCell morphologyBiochemistryGTP PhosphohydrolasesProto-Oncogene Proteins p21(ras)MiceGTP-binding protein regulatorsGTP-Binding ProteinsAnimalsHumansAmino Acid SequenceMolecular BiologyClostridiumEpidermal Growth FactorKinase3T3 CellsCell Biologybiology.organism_classificationMolecular biologyActinsrac GTP-Binding ProteinsActin CytoskeletonKineticsGlucoserap GTP-Binding ProteinsGlucosyltransferasesCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinPhosphorylationGuanosine TriphosphateHeLa CellsJournal of Biological Chemistry
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Cholesterol Modulates the Interaction of β-Amyloid Peptide with Lipid Bilayers

2009

The interaction of an amphiphilic, 40-amino acid beta-amyloid (Abeta) peptide with liposomal membranes as a function of sterol mole fraction (X(sterol)) was studied based on the fluorescence anisotropy of a site-specific membrane sterol probe, dehydroergosterol (DHE), and fluorescence resonance energy transfer (FRET) from the native Tyr-10 residue of Abeta to DHE. Without Abeta, peaks or kinks in the DHE anisotropy versus X(sterol) plot were detected at X(sterol) approximately 0.25, 0.33, and 0.53. Monomeric Abeta preserved these peaks/kinks, but oligomeric Abeta suppressed them and created a new DHE anisotropy peak at X(sterol) approximately 0.38. The above critical X(sterol) values coinci…

Time FactorsLipid BilayersMolecular Sequence DataBiophysicsPeptideFluorescence Polarization7. Clean energy03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAlzheimer DiseaseErgosterolFluorescence Resonance Energy TransferAmino Acid SequenceLipid bilayer030304 developmental biologychemistry.chemical_classification0303 health sciencesLiposomeAmyloid beta-PeptidesChemistryCholesterolSterolPeptide FragmentsCrystallographyFörster resonance energy transferMembraneCholesterolCell BiophysicsTyrosinelipids (amino acids peptides and proteins)030217 neurology & neurosurgeryFluorescence anisotropyProtein BindingBiophysical Journal
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Selective labelling of melittin with a fluorescent dansylcadaverine probe using guinea-pig liver transglutaminase

1991

Abstract Melittin, a C-terminal peptide, incorporated the fluorescent probe monodansylcadaverine (DNC) when catalysed by guinea-pig liver transglutaminase and Ca2+, as determined by thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC). A 1:1 adduct DNC-melittin was identified in which a single glutamine residue out of two, i.e. Gln25, acts as acyl donor. Incubation of melittin with transglutaminase in the absence of DNC originated high molecular mass complexes indicative that the peptide lysine residue can act as an acyl acceptor. The DNC-melittin was about 3 times more active in the lysis of red cell membranes than native melittin. Fluorescence study of the lab…

Tissue transglutaminaseGuinea PigsMolecular Sequence DataBiophysicsFluorescence spectrometryPeptideHemolysiscomplex mixturesBiochemistryHigh-performance liquid chromatographyCatalysisMelittinAdductchemistry.chemical_compoundResidue (chemistry)Structural BiologyCadaverineDansyl-labellingGeneticsAnimalsHumansAmino Acid SequenceMolecular BiologyChromatography High Pressure LiquidFluorescent Dyeschemistry.chemical_classificationTransglutaminasesChromatographybiologyChemistrytechnology industry and agricultureMelittinCell BiologyBuffer solutionTransglutaminaseMelittenLiverbiology.proteinCalciumlipids (amino acids peptides and proteins)Chromatography Thin LayerHPLCFEBS Letters
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Addressing substrate glutamine requirements for tissue transglutaminase using substance P analogues

1999

AbstractWe have investigated the effect on the substrate requirements for guinea pig liver (tissue) transglutaminase of a set of 11 synthetic glutamine substitution analogues making up the full sequence of the naturally occurring tissue transglutaminase substrate substance P. While a number of peptide sequences derived from proteins that are well-recognized as tissue transglutaminase substrates have been studied, the enzyme activity using substitution analogues of full-length natural substrates has not been investigated as thoroughly. Thus, our set of substance P analogues only differs from one to other by one amino acid mutation while the length (of the peptide) is maintained as in the nat…

Tissue transglutaminaseStereochemistryGlutamineGuinea PigsMolecular Sequence DataBiophysicsPeptideSubstance PBiochemistrySubstance P analogueSubstrate SpecificityResidue (chemistry)Structural BiologyGeneticsAnimalsAmino Acid SequenceMolecular Biologychemistry.chemical_classificationTransglutaminasesbiologySubstrate (chemistry)Cell BiologyTransglutaminasePeptide FragmentsEnzyme assayMultiple peptide synthesisAmino acidGlutamineEnzymeLiverchemistryBiochemistryMutationbiology.proteinFEBS Letters
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