Search results for "Base Sequence"

showing 10 items of 1146 documents

Prognostic significance of p16INK4a alterations and 9p21 loss of heterozigosity in locally advanced laryngeal squamous cell carcinoma

2002

The p16INK4a gene, localized within chromosome 9p21, has been identified as a cyclin-dependent kinase inhibitor and may negatively regulate the cell cycle acting as a tumor suppressor. Genetic alterations involving the 9p21 region are common in human cancers. A consecutive series of 64 untreated patients (median of follow up 53 months) undergoing surgical resection for locally advanced laryngeal squamous-cell carcinomas (LSCCs) has been studied prospectively. Our purpose was to investigate p16 alterations (9p21 allelic loss, hypermethylation and point mutations) and their possible association with clinico-pathological data and flow cytometric variables (DNA-ploidy and S-phase fraction (SPF)…

Settore MED/06 - Oncologia MedicaPhysiologyClinical BiochemistryLoss of HeterozygosityBiologyBioinformaticsS PhaseLoss of heterozygosityp16INK4aHumansPoint MutationProspective StudiesLaryngeal NeoplasmsGeneProportional Hazards ModelsUnivariate analysisPloidiesBase SequenceProportional hazards modelGenes p16Point mutationSingle-strand conformation polymorphismDNA NeoplasmCell BiologyDNA MethylationCell cyclePrognosisMultivariate AnalysisDNA methylationCarcinoma Squamous CellCancer researchChromosomes Human Pair 9Journal of Cellular Physiology
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Tumor protein 53-induced nuclear protein 1 expression is repressed by miR-155, and its restoration inhibits pancreatic tumor development.

2007

Pancreatic cancer is a disease with an extremely poor prognosis. Tumor protein 53-induced nuclear protein 1 ( TP53INP1 ) is a proapoptotic stress-induced p53 target gene. In this article, we show by immunohistochemical analysis that TP53INP1 expression is dramatically reduced in pancreatic ductal adenocarcinoma (PDAC) and this decrease occurs early during pancreatic cancer development. TP53INP1 reexpression in the pancreatic cancer-derived cell line MiaPaCa2 strongly reduced its capacity to form s.c., i.p., and intrapancreatic tumors in nude mice. This anti-tumoral capacity is, at least in part, due to the induction of caspase 3-mediated apoptosis. In addition, TP53INP1 −/− mouse embryonic…

Settore MED/06 - Oncologia MedicaTransplantation HeterologousGene ExpressionMice NudeMicePancreatic tumorPancreatic cancerCell Line TumormicroRNAGene expressionmedicineAnimalsHumansRNA NeoplasmNuclear proteinCaspaseHeat-Shock ProteinsMice KnockoutMultidisciplinarybiologyBase Sequenceapoptosis pancreatic cancer ponasterone A tumor suppressor micro RNANuclear ProteinsBiological Sciencesmedicine.diseaseTransplantationPancreatic NeoplasmsMicroRNAsCell Transformation NeoplasticApoptosisCancer researchbiology.proteinTumor Suppressor Protein p53Carrier ProteinsNeoplasm TransplantationCarcinoma Pancreatic DuctalProceedings of the National Academy of Sciences of the United States of America
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The microsomal epoxide hydrolase has a single membrane signal anchor sequence which is dispensable for the catalytic activity of this protein

1994

The microsomal epoxide hydrolase (mEH) catalyses the hydrolysis of reactive epoxides which are formed by the action of cytochromes P-450 from xenobiotics. In addition it has been suggested that mEH might mediate the transport of bile acids. For the mEH it has been shown that it is co-translationally inserted into the endoplasmic reticulum. Here we demonstrate that the N-terminal 20 amino acid residues of this protein serve as its single membrane anchor signal sequence and that the function of this sequence can also be supplied by a cytochrome P-450 (CYP2B1) anchor signal sequence. The evidence supporting this conclusion is as follows: (i) the rat mEH and a CYP2B1-mEH fusion protein, in whic…

Signal peptideDNA ComplementaryCytochromeMolecular Sequence DataProtein Sorting SignalsBiochemistryCatalysisDogsMicrosomesAnimalsAmino Acid SequenceEpoxide hydrolasePancreasMolecular BiologyEpoxide HydrolasesBase SequenceCell-Free SystembiologyChemistryEndoplasmic reticulumCell MembraneTemplates GeneticCell BiologyFusion proteinRatsMembraneBiochemistryProtein BiosynthesisMicrosomal epoxide hydrolaseMicrosomebiology.proteinResearch ArticleBiochemical Journal
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Sequence of the M28 dsRNA: Preprotoxin Is Processed to an α/β Heterodimeric Protein Toxin

1995

The killer and immunity phenotypes of K28 killer strains of Saccharomyces cerevisiae are determined by the 1.75-kb M28 dsRNA virus. In the plus strand, M28p, the K28 preprotoxin gene, comprises bases 13-1047 and is followed, after an additional 85 bases, by a 63-bp poly(A) sequence and a 553-base 3'-sequence. This 3'-sequence contains two potential stem-loop structures predicted to bind the L-A encoded cap-pol protein, initiating encapsidation; high-level expression results in curing of M1 dsRNA. Expression of M28p confers the complete K28 killer and immunity phenotype on a cell lacking M28 dsRNA. K28 toxin is a disulfide-bonded heterodimer of alpha (10.5 kDa) and beta (11 kDa) components w…

Signal peptideDNA ComplementaryGlycosylationSaccharomyces cerevisiae ProteinsGlycosylationMolecular Sequence DataMutantCarboxypeptidasesSaccharomyces cerevisiaeBiologymedicine.disease_causeCleavage (embryo)Fungal Proteinschemistry.chemical_compoundGene Expression Regulation FungalVirologyEndopeptidasesmedicineSecretionAmino Acid SequenceSubtilisinsGeneDNA PrimersRNA Double-StrandedBase SequenceToxinSerine EndopeptidasesMembrane ProteinsRNA FungalMycotoxinsMolecular biologyKiller Factors YeastRNA silencingchemistryProprotein ConvertasesProtein Processing Post-TranslationalVirology
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Structure, organization and expression of two clustered cuticle protein genes during the metamorphosis of an insect, Tenebrio molitor.

1998

A 4-kb DNA segment of Tenebrio molitor (Insecta, Coleoptera) genomic DNA containing two larval-pupal cuticular genes has been cloned and sequenced. These genes, transcribed in opposite directions, are related in DNA sequence and the proteins encoded are very similar. Each of them contains a single intron located inside the sequence encoding the signal peptide, and a conserved sequence at -200 bp from the mRNA start position. These similarities in sequence suggest that these genes have evolved by duplication followed by diversification and that they are members of a family of genes with a common ancestry. They are the first example of clustered genes in Tenebrio molitor.

Signal peptideDNA ComplementaryMolecular Sequence DataGenes InsectBiologyBiochemistryDNA sequencingConserved sequenceEvolution MolecularGene duplicationAnimalsAmino Acid SequenceTenebrioPeptide sequenceGeneIn Situ HybridizationGeneticsBase SequenceSequence Homology Amino AcidfungiIntronMetamorphosis BiologicalGene Expression Regulation DevelopmentalIntronsgenomic DNAMultigene FamilyInsect ProteinsEuropean journal of biochemistry
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Molecular cloning and primary structure of a Rhesus (Rh)-like protein from the marine sponge Geodia cydonium

1997

In humans, the 30,000 M(r) Rhesus (Rh) polypeptide D (RhD) is a dominant antigen (Ag) of the Rh blood group system. To date, an Rh-like protein has been found in chimpanzees, gorillas, gibbons, and rhesus monkeys. Related to the 30,000 M(r) Rh Ag protein are two polypeptides of 50,000 M(r), the human 50,000 M(r) Rh Ag and the RhD-like protein from Caenorhabditis elegans. The function of all these proteins is not sufficiently known. Here we characterize a cDNA clone (GCRH) encoding a putative 57,000 M(r) polypeptide from the marine sponge Geodia cydonium, which shares sequence similarity both to the RhD Ag and the Rh50 glycoprotein. The sponge Rh-like protein comprises 523 aa residues; hydro…

Signal peptideDNA ComplementaryMolecular Sequence DataImmunologyMolecular cloningGeneticsAnimalsHumansAmino Acid SequenceCloning MolecularCaenorhabditis elegansGlycoproteinschemistry.chemical_classificationRh-Hr Blood-Group SystemBase SequenceSequence Homology Amino AcidbiologyProtein primary structurebiology.organism_classificationMolecular biologyPoriferaSpongeTransmembrane domainchemistryGlycoproteinRh blood group systemImmunogenetics
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Complete sequence, expression and evolution of two members of the hexamerin protein family during the larval development of the rice moth, Corcyra ce…

2002

Three distinct types of storage hexamerins are expressed in the "last-instar" larvae of the rice moth, Corcyra cephalonica. A cDNA expression library was constructed from fat body-RNA and screened with a polyclonal antibody raised against purified hexamerin (SP2) of Corcyra cephalonica. Two slightly different "full-length" hexamerin cDNA clones (Hex2a and Hex2b) were isolated and sequenced. Both include open reading frames of 2109 bp which are translated into polypeptides of 703 amino acids with 92.5% identity. Signal peptides of 19 amino acids are present at the N-termini. The 684 amino acids native proteins have a high content of aryl groups (17.6%). According to both the criteria for ami…

Signal peptideDNA ComplementaryProtein familyBlotting WesternMolecular Sequence DataMothsBiochemistryEvolution MolecularComplete sequenceComplementary DNAEscherichia coliAnimalsAmino Acid SequenceMolecular BiologyGenePhylogenychemistry.chemical_classificationBase SequenceSequence Homology Amino AcidbiologyfungiBlotting Northernbiology.organism_classificationRecombinant ProteinsAmino acidOpen reading framechemistryBiochemistryRice mothLarvaInsect ScienceInsect ProteinsInsect Biochemistry and Molecular Biology
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A novel cell wall protein specific to the mycelial form of Yarrowia lipolytica.

1996

A cDNA clone specifying a cell wall protein was isolated from a Yarrowia lipolytica cDNA library. The cDNA library was constructed in the expression vector lambda gt 11, with the RNA isolated from actively growing mycelial cells. The deduced amino acid sequence shows that the encoded protein contains an N-terminal hydrophobic signal peptide. We have designated this protein YWP1 for Yarrowia lipolytica cell Wall Protein. Northern hybridization identified YWP1 transcript only when Y. lipolytica was growing in the mycelial form. The encoded protein seems to be covalently bound to the glucan cell wall since it is not released from the cell walls by sodium dodecyl sulphate extraction, but it is …

Signal peptideDNA ComplementaryTranscription GeneticHydrolasesBlotting WesternGenetic VectorsMolecular Sequence DataRestriction MappingBioengineeringApplied Microbiology and BiotechnologyBiochemistryCell wallFungal ProteinsOpen Reading FramesTransformation GeneticCell WallComplementary DNAGene Expression Regulation FungalYeastsGeneticsEscherichia coliAmino Acid SequenceCloning MolecularFluorescent Antibody Technique IndirectPeptide sequenceAntibodies FungalGene LibraryExpression vectorbiologyBase SequencecDNA libraryRNASodium Dodecyl SulfateYarrowiaRNA Fungalbiology.organism_classificationBlotting NorthernBlotting SouthernBiochemistrySaccharomycetalesElectrophoresis Polyacrylamide GelBiotechnologyYeast (Chichester, England)
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The nucleotide and deduced amino acid structures of sheep and pig fetuin. Common structural features of the mammalian fetuin family

1992

This study was initiated to gain further insight into the structural features of the mammalian fetuin family. The cDNA structures of sheep and pig fetuin were determined. The cDNA insert encoding sheep (pig) fetuin comprised 1550 (1470) nucleotides, including 54 (46) nucleotides encoding a signal peptide of 18 (15) residues and 1038 (1041) nucleotides encoding the 346 (347) amino acids of the mature plasma protein. The predicted amino-terminal sequence of the mature pig fetuin was confirmed by the amino-terminal sequence of the purified protein. However, two alternative sheep amino-terminal sequences were found in fetuin purified from the plasma of a single sheep fetus; the minor product wa…

Signal peptideGlycosylationSwineBlotting WesternMolecular Sequence DataSequence alignmentBiologyBiochemistrySequence Homology Nucleic AcidComplementary DNAEndopeptidasesAnimalsHumansAmino Acid SequenceCloning MolecularPeptide sequenceMammalschemistry.chemical_classificationSheepBase SequenceSerine EndopeptidasesStructural geneNucleic acid sequenceMembrane ProteinsDNAMolecular biologyFetuinAmino acidBiochemistrychemistryElectrophoresis Polyacrylamide Gelalpha-FetoproteinsEuropean Journal of Biochemistry
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Molecular characterization of hemoglobin from the honeybee Apis mellifera

2005

Due to the prevailing importance of the tracheal system for insect respiration, hemoglobins had been considered rare exceptions in this arthropod subphylum. Here we report the identification, cloning and expression analysis of a true hemoglobin gene in the honeybee Apis mellifera (Hymenoptera). The deduced amino acid sequence covers 171 residues (19.5 kDa) and harbors all globin-typical features, including the proximal and the distal histidines. The protein has no signal peptide for transmembrane transport and was predicted to localize in the cytoplasm. The honeybee hemoglobin gene shows an ancient structure, with introns in positions B12.2 and G7.0, while most other insect globins have div…

Signal peptideInsectaPhysiologymedia_common.quotation_subjectMolecular Sequence DataInsectBiologyHemoglobinsPhylogeneticsBotanyAnimalsAmino Acid SequenceRNA MessengerGlobinGenePeptide sequencemedia_commonGeneticsBase SequencefungiIntronSequence Analysis DNABeesBiological EvolutionInsect ScienceHemoglobinJournal of Insect Physiology
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