Search results for "alignment"

showing 10 items of 627 documents

Inside the Hsp90 inhibitors binding mode through induced fit docking

2009

Abstract During the last few decades, the development of new anticancer strategies had to face the instability of many tumors, occurring when the genetic plasticity of cells produces new drug-resistant cancers. It has been shown that a chaperone protein, heat shock protein 90 (Hsp90), is one of the fundamental factors involved in the cell response to stresses, and its role in many biochemical pathways has been demonstrated. Thus, the inhibition of Hsp90 represents a new target of antitumor therapy, since it may influence many specific signaling pathways. The natural antibiotic Geldanamycin is the first Hsp90 inhibitor that has been identified. Nevertheless, more potent and water-soluble sma…

Models MolecularStereochemistryLactams MacrocyclicMolecular Sequence DataComputational biologyCrystallography X-RayLigandsHsp90 inhibitorchemistry.chemical_compoundAdenosine TriphosphateHeat shock proteinCatalytic DomainMaterials ChemistryBenzoquinonesAmino Acid SequenceHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistrySpectroscopyInduced fitBinding SitesbiologyMolecular StructureHeat shock proteinDrug discoveryActive siteGeldanamycinRadicicolComputer Graphics and Computer-Aided DesignSmall moleculeHsp90Settore CHIM/08 - Chimica FarmaceuticachemistryDocking (molecular)Molecular dockingbiology.proteinGeldanamicynSequence AlignmentProtein Binding
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Proteomic Analyses Reveal an Acidic Prime Side Specificity for the Astacin Metalloprotease Family Reflected by Physiological Substrates

2011

Astacins are secreted and membrane-bound metalloproteases with clear associations to many important pathological and physiological processes. Yet with only a few substrates described their biological roles are enigmatic. Moreover, the lack of knowledge of astacin cleavage site specificities hampers assay and drug development. Using PICS (proteomic identification of protease cleavage site specificity) and TAILS (terminal amine isotopic labeling of substrates) degradomics approaches >3000 cleavage sites were proteomically identified for five different astacins. Such broad coverage enables family-wide determination of specificities N- and C-terminal to the scissile peptide bond. Remarkably, me…

KeratinocytesModels MolecularProteomicsVascular Endothelial Growth Factor AProteasesmedicine.medical_treatmentProteolysisMolecular Sequence DataBiologyCleavage (embryo)BiochemistryCell LineSubstrate SpecificityAnalytical Chemistry03 medical and health sciencesTandem Mass SpectrometrymedicineHumansAmino Acid SequenceMolecular BiologyPeptide sequencePhylogeny030304 developmental biologyEnzyme Precursors0303 health sciencesProteaseStaining and LabelingEdman degradationmedicine.diagnostic_testResearch030302 biochemistry & molecular biologyTioproninMetalloendopeptidasesTerminal amine isotopic labeling of substratesRecombinant ProteinsKineticsBiochemistryProteolysisKallikreinsAstacinPeptidesSequence AlignmentChromatography LiquidMolecular & Cellular Proteomics
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Cloning and functional analysis of cDNA encoding the hamster Bcl-2 protein.

2000

We have cloned cDNA encoding hamster Bcl-2 protein from total RNA of CHO-9 cells by RT-PCR using oligonucleotide primers sharing homology with the sequence of mouse and rat bcl-2. The fragments spanning the total coding region were cloned into pCR4-TOPO and sequenced for verification. The hamster bcl-2 cDNA has a size of 711 nucleotides and encodes a polypeptide of 236 amino acids. Hamster Bcl-2 shares 95.8 and 88.6% similarity with mouse and human Bcl-2, respectively. Northern blot analysis revealed a single 7.5 kb bcl-2 transcript in hamster (CHO-9), mouse (BK4), and rat (H5) cells and a 8.5 kb bcl-2 mRNA in human (HeLa MR) cells. The bcl-2 cDNA (771 bp) was recloned into pcDNA3 and the r…

MethylnitronitrosoguanidineDNA ComplementaryAlkylationMolecular Sequence DataBiophysicsHamsterBiologyTransfectionBiochemistryCell LineComplementary DNACricetinaeCoding regionAnimalsHumansNorthern blotAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyCloningMessenger RNABase SequenceCell DeathSequence Homology Amino AcidChinese hamster ovary cellCell BiologyTransfectionMolecular biologyProto-Oncogene Proteins c-bcl-2CarcinogensSequence AlignmentBiochemical and biophysical research communications
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Compression-based classification of biological sequences and structures via the Universal Similarity Metric: experimental assessment.

2007

Abstract Background Similarity of sequences is a key mathematical notion for Classification and Phylogenetic studies in Biology. It is currently primarily handled using alignments. However, the alignment methods seem inadequate for post-genomic studies since they do not scale well with data set size and they seem to be confined only to genomic and proteomic sequences. Therefore, alignment-free similarity measures are actively pursued. Among those, USM (Universal Similarity Metric) has gained prominence. It is based on the deep theory of Kolmogorov Complexity and universality is its most novel striking feature. Since it can only be approximated via data compression, USM is a methodology rath…

Computer scienceAlgorismesPrediction by partial matchingCompression dissimilaritycomputer.software_genreBiochemistryProtein Structure SecondaryPhylogenetic studiesStructural BiologySequence Analysis ProteinDatabases Proteinlcsh:QH301-705.5Biological dataNCDApplied MathematicsGenomicsClassificationCDComputer Science ApplicationsBenchmarking:Informàtica::Informàtica teòrica [Àrees temàtiques de la UPC]Universal compression dissimilarityArea Under CurveMetric (mathematics)lcsh:R858-859.7Data miningAlgorithmsData compressionResearch Article:Informàtica::Aplicacions de la informàtica::Bioinformàtica [Àrees temàtiques de la UPC]Normalization (statistics)lcsh:Computer applications to medicine. Medical informaticsBioinformatics Sequence Alignment AlgorithmsSet (abstract data type)Similarity (network science)Normalized compression sissimilarityData compression (Computer science)AnimalsHumansAmino Acid SequenceMolecular BiologyBiologyDades -- Compressió (Informàtica)USMUniversal similarity metricProteinsUCDProtein Structure TertiaryData setGenòmicaStatistical classificationlcsh:Biology (General)ROC CurvecomputerSequence AlignmentSoftwareBMC bioinformatics
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Caspase-mediated apoptosis in sponges: cloning and function of the phylogenetic oldest apoptotic proteases from Metazoa

2003

AbstractSponges (phylum Porifera) represent the phylogenetically oldest metazoan phylum. These animals have complex cell adhesion and powerful immune systems which allow the formation of a distinct body plan. Consequently, an apoptotic machinery has to be predicted that allows sponges to eliminate unwanted cells accumulating during development. With the marine sponge Geodia cydonium, it is shown that allografts of these animals undergo apoptosis as demonstrated by apoptotic DNA fragmentation. Extracts from allografts contain an enzymic activity characteristic for caspases; as substrate to determine the cleavage activity, Ac-DEVD-AMC was applied. cDNAs encoding predicted caspase-3-related pr…

Molecular Sequence DataApoptosisCaspase 3SpongeCoumarinsEndopeptidasesAnimalsInvertebrateAmino Acid SequenceCloning MolecularEnzyme InhibitorsMolecular BiologyPhylogenyCaspasebiologyCaspase 3Cell adhesion moleculeAlternative splicingApoptotic DNA fragmentationPotential proapoptotic molecule DD2Cell BiologyBcl-2 homologous proteinbiology.organism_classificationSuberites domunculaCaspaseCaspase InhibitorsPoriferaCell biologyIsoenzymesSuberites domunculaSpongeApoptosisCaspasesbiology.proteinOligopeptidesSequence AlignmentBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Life cycle of Renylaima capensis, a brachylaimid trematode of shrews and slugs in South Africa: two-host and three-host transmission modalities sugge…

2012

Abstract Background The life cycle of the brachylaimid trematode species Renylaima capensis, infecting the urinary system of the shrew Myosorex varius (Mammalia: Soricidae: Crocidosoricinae) in the Hottentots Holland Nature Reserve, South Africa, has been elucidated by a study of its larval stages, epizootiological data in local snails and mammals during a 34-year period, and its verification with mtDNA sequencing. Methods Parasites obtained from dissected animals were mounted in microscope slides for the parasitological study and measured according to standardized methods. The mitochondrial DNA cox 1 gene was sequenced by the dideoxy chain-termination method. Results The slugs Ariostralis …

MaleAriostralis nebulosaGastropodaMolecular Sequence DataMyosorex variusZoologyHelminth geneticsTrematode InfectionsDNA Mitochondriallcsh:Infectious and parasitic diseasesElectron Transport Complex IVSouth Africabiology.animalGastropodaAnimalslcsh:RC109-216Urinary TractArionidaeLife Cycle StagesLarvaBase SequencebiologyResearchShrewsShrewSequence Analysis DNADNA Helminthbiology.organism_classificationInfectious DiseasesMutationFemaleParasitologyTrematodaTrematodaSequence AlignmentParasites & Vectors
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Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29

2002

Abstract ERp29 is a soluble protein localized in the endoplasmic reticulum (ER) of eukaryotic cells, which is conserved in all mammalian species. The N-terminal domain of ERp29 displays sequence and structural similarity to the protein disulfide isomerase despite the lack of the characteristic double cysteine motif. Although the exact function of ERp29 is not yet known, it was hypothesized that it may facilitate folding and/or export of secretory proteins in/from the ER. ERp29 is induced by ER stress, i.e. accumulation of unfolded proteins in the ER. To gain an insight into the mechanisms regulating ERp29 expression we have cloned and characterized the rat ERp29 gene and studied in details …

5' Flanking RegionRecombinant Fusion ProteinsMolecular Sequence DataCHO CellsBiologyCell LineMiceCricetinaeSequence Homology Nucleic AcidGene expressionTumor Cells CulturedGeneticsAnimalsHumansRNA MessengerLuciferasesPromoter Regions GeneticProtein disulfide-isomeraseGeneHeat-Shock ProteinsPhylogenyBase SequenceGene Expression ProfilingEndoplasmic reticulumPromoter3T3 CellsDNAExonsSequence Analysis DNAGeneral MedicineMolecular biologyIntronsRatsHousekeeping geneSecretory proteinGenesUnfolded protein responseFemaleTranscription Initiation SiteSequence AlignmentHeLa CellsGene
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Gene within gene configuration and expression of the Drosophila melanogaster genes lethal(2) neighbour of tid [l(2)not] and lethal(2) relative of tid…

1997

In this paper, we describe the structure and temporal expression pattern of the Drosophila melanogaster genes l(2)not and l(2)rot located at locus 59F5 vis a vis the tumor suppressor gene l(2)tid described previously and exhibiting a gene within gene configuration. The l(2)not protein coding region, 1530 nt, is divided into two exons by an intron, 2645 nt, harboring the genes l(2)rot, co-transcribed from the same DNA strand, and l(2)tid, co-transcribed from the opposite DNA strand, located vis a vis. To determine proteins encoded by the genes described in this study polyclonal rabbit antibodies (Ab), anti-Not and anti-Rot, were generated. Immunostaining of developmental Western blots with t…

Embryo NonmammalianTranscription GeneticMolecular Sequence DataRestriction MappingGenes Insectmacromolecular substancesBiologyMannosyltransferasesAntibodiesExonTranscription (biology)GeneticsAnimalsDrosophila ProteinsNorthern blotAmino Acid SequenceMicroscopy ImmunoelectronGeneBody PatterningRegulation of gene expressionBase SequenceSequence Homology Amino Acidtechnology industry and agricultureIntronRNAGene Expression Regulation DevelopmentalMembrane ProteinsGeneral MedicineExonsMolecular biologyIntronsPeptide FragmentsAntisense RNADrosophila melanogasterGene Expression RegulationInsect ProteinsRabbitsSequence AlignmentGene
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Measurement of high order Kerr refractive index of major air components: erratum

2010

A clarification is missing concerning the high order Kerr non-linearities deduced from our experimental data published in [Opt. Express 17, 13429-13434 (2009)]. Here, we rectify this omission by making explicit the distinction between cross-Kerr and Kerr effects, and by extrapolating the value of the nonlinear refractive index for the last effect. Since the occurrence of sign inversion in the Kerr effect is not affected, the overall report in [Opt. Express 17, 13429-13434] remains valid.

Kerr effect[ PHYS.PHYS.PHYS-ATOM-PH ] Physics [physics]/Physics [physics]/Atomic Physics [physics.atom-ph](320.2250) Femtosecond phenomena; (350.5400) Plasmas; (190.7110) Ultrafast nonlinear optics; (260.5950) Self-focusing01 natural sciences010309 opticsOptics0103 physical sciencesZ-scan techniqueHigh order[PHYS.PHYS.PHYS-ATOM-PH] Physics [physics]/Physics [physics]/Atomic Physics [physics.atom-ph]010306 general physicsfemtosecondLaser beamsplasmaPhysics[PHYS.PHYS.PHYS-ATOM-PH]Physics [physics]/Physics [physics]/Atomic Physics [physics.atom-ph]Molecular alignmentbusiness.industrySelf-focusingNonlinear refractive indexPolarization (waves)Atomic and Molecular Physics and Opticslaser filamentationbusinessRefractive index) Ultrafast nonlinear optics
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Phobalysin, a Small β-Pore-Forming Toxin of Photobacterium damselae subsp. damselae

2015

ABSTRACT Photobacterium damselae subsp. damselae , an important pathogen of marine animals, may also cause septicemia or hyperaggressive necrotizing fasciitis in humans. We previously showed that hemolysin genes are critical for virulence of this organism in mice and fish. In the present study, we characterized the hlyA gene product, a putative small β-pore-forming toxin, and termed it phobalysin P (PhlyP), for “photobacterial lysin encoded on a plasmid.” PhlyP formed stable oligomers and small membrane pores, causing efflux of K + , with no significant leakage of lactate dehydrogenase but entry of vital dyes. The latter feature distinguished PhlyP from the related Vibrio cholerae cytolysin…

ErythrocytesBacterial ToxinsMolecular Sequence DataImmunologyVirulencemedicine.disease_causeHemolysin ProteinsHemolysisMicrobiologyBacterial AdhesionMicrobiologyHemolysin ProteinsmedicineAnimalsHumansAmino Acid SequencePore-forming toxinbiologyPhotobacteriumEpithelial CellsHemolysinPhotobacteriumbiology.organism_classificationMolecular PathogenesisInfectious DiseasesPhotobacterium damselaeVibrio choleraeParasitologyRabbitsCytolysinSequence AlignmentInfection and Immunity
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