Search results for "sequence"

showing 10 items of 4987 documents

Complexity of IL-1β induced gene expression pattern in human articular chondrocytes

1997

The mRNA fingerprinting technique, differential display reverse transcription polymerase chain (DDRT-PCR), was used to detect changes in the overall pattern of gene expression in human articular knee chondrocytes-induced by interleukin-1 beta (IL-1 beta), the prototypical inducer of catabolic responses in degenerate joint diseases. One hundred different primer combinations generated approximately 10,000 different PCR fragments for IL-1 beta treated, as well as for untreated human chondrocytes, cultivated in alginate beads. This represented 53% of all expressed chondrocyte genes as based on statistical considerations. Side by side comparisons of differential display patterns originating from…

Cartilage ArticularDNA ComplementaryMolecular Sequence DataCell Culture TechniquesBiomedical EngineeringBiologyPolymerase Chain ReactionChondrocyteChondrocytesRheumatologyComplementary DNAGene expressionOsteoarthritismedicineHumansOrthopedics and Sports MedicineRNA MessengerGeneAgedDifferential displayDifferential displayIL-1Middle AgedBlotting NorthernMolecular biologyReverse transcriptaseReal-time polymerase chain reactionmedicine.anatomical_structureGene Expression RegulationFemalePrimer (molecular biology)Interleukin-1Osteoarthritis and Cartilage
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Identification and characterisation of the dopamine receptor II from the cat flea Ctenocephalides felis (CfDopRII)

2006

International audience; G protein-coupled receptors (GPCRs) represent a protein family with a wide range of functions. Approximately 30% of human drug targets are GPCRs, illustrating their pharmaceutical relevance. In contrast, the knowledge about invertebrate GPCRs is limited and is mainly restricted to model organisms like Drosophila melanogaster and Caenorhabditis elegans. Especially in ectoparasites like ticks and fleas, only few GPCRs are characterised. From the cat flea Ctenocephalides felis, a relevant parasite of cats and dogs, no GPCRs are known so far. Thus, we performed a bioinformatic analysis of available insect GPCR sequences from the honeybee Apis mellifera, the mosquito Anop…

Cat fleaAnopheles gambiaeMolecular Sequence Dataved/biology.organism_classification_rank.speciesBiochemistryCell LineReceptors DopamineAnimals Genetically ModifiedXenopus laevisAnimalsHumansAmino Acid SequenceCloning MolecularModel organismMolecular BiologyPhylogenyCaenorhabditis elegansCtenocephalides[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]G protein-coupled receptorGeneticsbiologyved/biologyEcologyFelisComputational Biologybiology.organism_classificationDrosophila melanogasterMultigene FamilyInsect ScienceOocytesInsect ProteinsSiphonapteraFemaleRNA Interference[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Drosophila melanogasterSequence Alignment[CHIM.CHEM]Chemical Sciences/Cheminformaticshormones hormone substitutes and hormone antagonistsInsect Biochemistry and Molecular Biology
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Silicateins, the major biosilica forming enzymes present in demosponges: protein analysis and phylogenetic relationship.

2007

Silicateins are enzymes, which are restricted to sponges (phylum Porifera), that mediate the catalytic formation of biosilica from monomeric silicon compounds. The silicatein protein is compartmented in the sponges in the axial filaments which reside in the axial canals of the siliceous spicules. In the present study silicatein has been isolated from the freshwater sponge Lubomirskia baicalensis where it occurs in isoforms with sizes of 23 kDa, 24 kDa and 26 kDa. Since the larger protein is glycosylated we posit that it is a processed form of one of the smaller size forms. The silicatein isoforms are post-translationally modified by phosphorylation; at least four isoforms exist with pI's of…

Cathepsin LMolecular Sequence DataCathepsin LDemospongeCatalytic triadGeneticsAnimalsAmino Acid SequenceGenePeptide sequencePhylogenyCathepsinbiologySequence Homology Amino AcidGeneral MedicineExonsbiology.organism_classificationSilicon DioxideCathepsinsIntronsPoriferaSuberites domunculaSpongeCysteine EndopeptidasesMicroscopy ElectronBiochemistrybiology.proteinGene
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Explicit solutions for a system of coupled Lyapunov differential matrix equations

1987

This paper is concerned with the problem of obtaining explicit expressions of solutions of a system of coupled Lyapunov matrix differential equations of the typewhere Fi, Ai(t), Bi(t), Ci(t) and Dij(t) are m×m complex matrices (members of ℂm×m), for 1≦i, j≦N, and t in the interval [a,b]. When the coefficient matrices of (1.1) are timeinvariant, Dij are scalar multiples of the identity matrix of the type Dij=dijI, where dij are real positive numbers, for 1≦i, j≦N Ci, is the transposed matrix of Bi and Fi = 0, for 1≦i≦N, the Cauchy problem (1.1) arises in control theory of continuous-time jump linear quadratic systems [9–11]. Algorithms for solving the above particular case can be found in [1…

Cauchy problemLyapunov functionSequenceDifferential equationGeneral MathematicsMathematical analysisIdentity matrixsymbols.namesakeMatrix (mathematics)symbolsInitial value problemApplied mathematicsBoundary value problemMathematicsProceedings of the Edinburgh Mathematical Society
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Exact treatment of operator difference equations with nonconstant and noncommutative coefficients

2013

We study a homogeneous linear second-order difference equation with nonconstant and noncommuting operator coefficients in a vector space. We build its exact resolutive formula consisting of the explicit noniterative expression of a generic term of the unknown sequence of vectors. Some nontrivial applications are reported in order to show the usefulness and the broad applicability of the result.

Cauchy problemSequenceDifferential equationGeneral MathematicsOperator (physics)Mathematical analysisGeneral EngineeringExpression (computer science)Term (logic)Noncommutative geometrySettore FIS/03 - Fisica Della MateriaCauchy problem Noncommuting operators Operator difference equationsMathematicsVector space
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Expression of M-cadherin protein in myogenic cells during prenatal mouse development and differentiation of embryonic stem cells in culture.

1994

Molecules regulating morphogenesis by cell-cell interactions are the cadherins, a class of calcium-dependent adhesion molecules. One of its members, M-cadherin, has been isolated from a myoblast cell line (Donalies et al. [1991] Proc. Natl. Acad. Sci. U.S.A. 88:8024—8028). In mouse development, expression of M-cadherin mRNA first appears at day 8.5 of gestation (E8.5) in somites and has been postulated to be down-regulated in developing muscle masses (Moore and Walsh [1993] Development 117:1409—1420). Affinity-purified polyclonal M-cadherin antibodies, detecting a protein of approximately 120 kDa, were used to study the cell expression pattern of M-cadherin protein. It was first visualized …

Cell Adhesion Molecules NeuronalRecombinant Fusion ProteinsMolecular Sequence DataMorphogenesisFluorescent Antibody TechniqueGestational AgeBiologyEmbryonic and Fetal DevelopmentMiceLamininPregnancyMyocyteAnimalsAmino Acid SequenceRNA MessengerMuscle SkeletalCells CulturedDNA PrimersMice Inbred BALB CBase SequenceCadherinCell adhesion moleculeStem CellsCell MembraneGene Expression Regulation DevelopmentalCadherinsEmbryonic stem cellMolecular biologyCell culturebiology.proteinDesminFemaleDevelopmental BiologyDevelopmental dynamics : an official publication of the American Association of Anatomists
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Cloning of a rat-specific long PCP4/PEP19 isoform

2007

We report the identification of a cDNA that encodes a putative protein of 94 amino acids and expected molecular weight of 10.7 kDa, the C-terminal half of which is identical to that of PEP19, a small, brain-specific protein involved in Ca++/calmodulin signaling. The novel rat-specific protein, tentatively named long PEP19 isoform (LPI), is the product of alternative splicing of the rat PCP4 gene encoding PEP19. We found that antibodies raised against the first 13 N-terminal amino acids of LPI, not present in PEP19, recognize a protein enriched in the developing rat brain.

Cell ExtractsGene isoformProtein isoformDNA ComplementaryCalmodulinMolecular Sequence DataNerve Tissue ProteinsAntibodiesRats Sprague-DawleyMiceExonComplementary DNAGeneticsAnimalsHumansProtein IsoformsAmino Acid SequenceRNA MessengerCloning MolecularPeptide sequencechemistry.chemical_classificationBase SequencebiologyGene Expression ProfilingAlternative splicingBrainGene Expression Regulation DevelopmentalRNA-Binding ProteinsExonsGeneral MedicineMolecular biologyIntronsRatsAmino acidchemistryBiochemistrybiology.proteinCalmodulin-Binding ProteinsPeptidesInternational Journal of Molecular Medicine
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Termination of transcription in an ‘in vitro’ system is dependent on a polyadenylation sequence

1991

Using HeLa cell nuclear extract as a source of the different transcription and polyadenylation factors and reverse transcription to analyze the levels of RNA 5' and 3' to the cleavage-polyadenylation site, an in vitro assay has been established to study polyadenylation coupled to transcription directed by different adenovirus promoters. The levels of transcription 5' and 3' to the cleavage site in the L3 polyadenylation region are practically the same as described previously, however, the level of transcription 3' to the cleavage site in the SV40 early polyadenylation region decreases immediately after the cleavage site indicating a termination of the transcription.

Cell ExtractsTranscription GeneticPolyadenylationMolecular Sequence DataRNA polymerase IISimian virus 40BiologyCleavage (embryo)AdenoviridaeTranscription (biology)GeneticsRNA MessengerPromoter Regions GeneticBase SequenceRNARNA-Directed DNA PolymerasePromoterMolecular biologyReverse transcriptasebiology.proteinRNA Polymerase IIChromosome DeletionPoly ACytokinesisHeLa CellsPlasmidsNucleic Acids Research
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Nuclear receptors modulate the interaction of Sp1 and GC-rich DNA via ternary complex formation

2000

Binding sites for transcription factor Sp1have been implicated in the transcriptional regulation of several genes by hormones or vitamins, and here we show that a GC-rich element contributes to the retinoic acid response of the interleukin 1β promoter. To explain such observations, it has been proposed that nuclear receptors can interact with Sp1 bound to GC-rich DNA. However, evidence supporting this model has remained indirect. So far, nuclear receptors have not been detected in a complex with Sp1 and GC-rich DNA, and the expected ternary complexes in non-denaturing gels were not seen. In search for these missing links we found that nuclear receptors [retinoic acid receptor (RAR), thyroid…

Cell ExtractsTranscriptional ActivationReceptors Retinoic AcidSp1 Transcription FactorRecombinant Fusion ProteinsReceptors Cytoplasmic and NuclearTretinoinRetinoic acid receptor betaBiologyRetinoid X receptorLigandsResponse ElementsTransfectionModels BiologicalBiochemistryAntibodiesCell LineSubstrate SpecificityAnimalsPromoter Regions GeneticMolecular BiologyNuclear receptor co-repressor 1Nuclear receptor co-repressor 2Binding SitesReceptors Thyroid HormoneDNACell BiologyRetinoic acid receptor gammaRetinoid X receptor gammaGC Rich SequenceProtein Structure TertiaryNuclear receptor coactivator 1Retinoic acid receptorDrosophila melanogasterEcdysteroneRetinoid X ReceptorsOligodeoxyribonucleotidesBiochemistryReceptors CalcitriolThermodynamicsResearch ArticleInterleukin-1Protein BindingTranscription FactorsBiochemical Journal
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Streptolysin O: the C-terminal, tryptophan-rich domain carries functional sites for both membrane binding and self-interaction but not for stable oli…

2001

AbstractStreptolysin O belongs to the class of thiol-activated toxins, which are single chain, four-domain proteins that bind to membranes containing cholesterol and then assemble to form large oligomeric pores. Membrane binding involves a conserved tryptophan-rich sequence motif located within the C-terminally located domain 4. In contrast, sites involved in oligomerization and pore formation have been assigned to domains 1 and 3, respectively. We here examined the functional properties of domain 4, which was recombinantly expressed with an N-terminal histidine tag for purification and an additional cysteine residue for covalent labeling. The fluorescently labeled fragment readily bound to…

Cell Membrane PermeabilityMembrane bindingProtein ConformationBiophysicsPlasma protein bindingBiochemistryThiol-activated toxinStructure-Activity RelationshipProtein structureBacterial ProteinsProtein oligomerizationHumansProtein oligomerizationBinding sitePore-forming toxinBinding SitesChemistryErythrocyte MembraneCell BiologyMembraneBiochemistryMutationStreptolysinsBiophysicsPore-forming toxinFluoresceinStreptolysinSequence motifProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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