Search results for " AMINO"

showing 10 items of 789 documents

Molecular cloning and evolution of lobster hemocyanin.

2001

In the American lobster, Homarus americanus, oxygen is transported by a hemocyanin that is composed 2 x 6 subunits. N-terminal sequencing show the presence of three distinct subunit types (alpha, beta and gamma). We cloned the cDNA of one of these subunits that belong to the alpha-type. It encodes a hemocyanin subunit of 654 amino acids with a molecular mass of 84.8 kDa, which is synthesized in the hepatopancreas. Phylogenetic analyses of the crustacean hemocyanin sequences show two well-separated clades, which correspond to the alpha and gamma-type subunits. Sequences of beta-type subunits are still unknown. The gamma-sequences have evolved about 15% faster than the alpha-subunits, consist…

Protein subunitmedicine.medical_treatmentMolecular Sequence DataBiophysicsMolecular cloningBiochemistryEvolution MolecularComplementary DNAmedicineAnimalsTissue DistributionAmino Acid SequenceRNA MessengerCloning MolecularMolecular clockMolecular BiologyPhylogenyHomarusMolecular massbiologySequence Homology Amino AcidHemocyaninCell BiologyAmerican lobsterbiology.organism_classificationMolecular biologyNephropidaeProtein SubunitsHemocyaninsBiochemical and biophysical research communications
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Assessing the low complexity of protein sequences via the low complexity triangle.

2020

Background Proteins with low complexity regions (LCRs) have atypical sequence and structural features. Their amino acid composition varies from the expected, determined proteome-wise, and they do not follow the rules of structural folding that prevail in globular regions. One way to characterize these regions is by assessing the repeatability of a sequence, that is, calculating the local propensity of a region to be part of a repeat. Results We combine two local measures of low complexity, repeatability (using the RES algorithm) and fraction of the most frequent amino acid, to evaluate different proteomes, datasets of protein regions with specific features, and individual cases of proteins…

ProteomeProteomesComputer scienceProtein SequencingBiochemistryDatabase and Informatics MethodsSequence Analysis ProteinProtein methodsPeptide sequencechemistry.chemical_classification0303 health sciencesSequenceMultidisciplinary030302 biochemistry & molecular biologyQRGenomicsAmino acidTandem RepeatsProteomeAmino Acid AnalysisMedicineSequence AnalysisResearch ArticleRepetitive Sequences Amino AcidBioinformaticsSequence analysisScienceResearch and Analysis MethodsGenome Complexity03 medical and health sciencesProtein DomainsAmino Acid Sequence AnalysisTandem repeatGeneticsHumansFraction (mathematics)Repeated SequencesAmino Acid SequenceMolecular Biology TechniquesSequencing TechniquesRepresentation (mathematics)Molecular Biology030304 developmental biologyMolecular Biology Assays and Analysis Techniquesbusiness.industryBiology and Life SciencesProteinsComputational BiologyPattern recognitionchemistryGlobular ProteinsArtificial intelligencebusinessPLoS ONE
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TrpM, a Small Protein Modulating Tryptophan Biosynthesis and Morpho-Physiological Differentiation in Streptomyces coelicolor A3(2).

2016

In the model actinomycete Streptomyces coelicolor A3(2), small open reading frames encoding proteins with unknown functions were identified in several amino acid biosynthetic gene operons, such as SCO2038 (trpX) in the tryptophan trpCXBA locus. In this study, the role of the corresponding protein in tryptophan biosynthesis was investigated by combining phenotypic and molecular analyses. The 2038KO mutant strain was characterized by delayed growth, smaller aerial hyphae and reduced production of spores and actinorhodin antibiotic, with respect to the WT strain. The capability of this mutant to grow on minimal medium was rescued by tryptophan and tryptophan precursor (serine and/or indole) su…

Proteomics0301 basic medicineProtein ExtractionMutantlcsh:MedicineStreptomyces coelicolor A3(2)Settore BIO/19 - Microbiologia GeneraleBiochemistrySerinechemistry.chemical_compoundAromatic Amino AcidsSmall ProteinAntibioticsTRPMMicrobial PhysiologyMedicine and Health SciencesBacterial PhysiologyAmino Acidslcsh:ScienceProtein MetabolismExtraction TechniquesMultidisciplinarybiologyOrganic CompoundsAntimicrobialsStreptomyces coelicolorTryptophanDrugsChemistryBiochemistryPhysical SciencesPhysiological DifferentiationResearch ArticleTryptophan BiosynthesiSmall Protein; Biosynthesis; Morpho-Physiological Differentiation: Streptomyces coelicolorBiosynthesisResearch and Analysis MethodsMicrobiologyStreptomycesActinorhodin03 medical and health sciencesBiosynthesisMicrobial ControlBacterial SporesPharmacology030102 biochemistry & molecular biologyOrganic Chemistrylcsh:RChemical CompoundsTryptophanTrpM; Small Protein; Tryptophan Biosynthesis; Morphological Differentiation; Physiological Differentiation; Streptomyces coelicolor A3(2); ProteomicsBiology and Life SciencesProteinsBacteriologybiology.organism_classificationAmino Acid MetabolismMetabolism030104 developmental biologychemistrylcsh:QMorphological DifferentiationTrpM
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General Statistical Framework for Quantitative Proteomics by Stable Isotope Labeling

2014

Pedro J. Navarro et al.

ProteomicsSaccharomyces cerevisiae ProteinsProteomeQuantitative proteomicsGene Expressionstable isotope labelingSaccharomyces cerevisiaeyeastOxygen Isotopescomputer.software_genreBiochemistryStatistical powerInterpretation (model theory)statistical analysisStable isotope labeling by amino acids in cell cultureQuantitative proteomicsData MiningModels StatisticalChromatographyChemistryMolecular Sequence AnnotationHydrogen PeroxideGeneral ChemistryVariance (accounting)Isotope LabelingStable Isotope LabelingBiological systemNull hypothesiscomputerData integrationJournal of Proteome Research
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CiliaCarta: An integrated and validated compendium of ciliary genes

2019

The cilium is an essential organelle at the surface of mammalian cells whose dysfunction causes a wide range of genetic diseases collectively called ciliopathies. The current rate at which new ciliopathy genes are identified suggests that many ciliary components remain undiscovered. We generated and rigorously analyzed genomic, proteomic, transcriptomic and evolutionary data and systematically integrated these using Bayesian statistics into a predictive score for ciliary function. This resulted in 285 candidate ciliary genes. We generated independent experimental evidence of ciliary associations for 24 out of 36 analyzed candidate proteins using multiple cell and animal model systems (mouse…

ProteomicsSensory ReceptorsNematodaSocial SciencesCiliopathiesBiochemistrySensory disorders Donders Center for Medical Neuroscience [Radboudumc 12]Transcriptome0302 clinical medicineAnimal CellsPsychologyRETINAL PHOTORECEPTOR CELLSExomeNeurons0303 health sciences030302 biochemistry & molecular biologyEukaryotaGenomicsPRIMARY CILIUMthecilium3. Good healthNucleic acidsGenetic interferenceOsteichthyesMedicineEpigeneticsCellular Structures and OrganellesCellular Typesproteomic databasesSensory Receptor CellsScienceeducationCiliary genesLEBER CONGENITAL AMAUROSISGenomics03 medical and health sciencesGeneticsCiliaCaenorhabditis elegansIDENTIFICATIONMUTATIONSEmbryosciliaOrganismsBiology and Life SciencesBayes TheoremMolecular Sequence Annotationmedicine.diseaseInvertebratesFishciliary proteomeAnimal StudiesCaenorhabditisGene expressionembryos030217 neurology & neurosurgeryDevelopmental BiologyNeurosciencePhotoreceptorsCandidate geneEmbryologyOligonucleotidesMorpholinoDatabase and Informatics MethodsRNA interferenceBayesian classifierTRANSITION ZONEZebrafishAntisense OligonucleotidesZebrafishGeneticsMultidisciplinarySpectrometric Identification of ProteinsProteomic DatabasesNucleotidesCiliumQStable Isotope Labeling by Amino Acids in Cell CultureRphotoreceptorsMetabolic Disorders Radboud Institute for Molecular Life Sciences [Radboudumc 6]Animal ModelsPhenotypeINTRAFLAGELLAR TRANSPORTDIFFERENTIATIONPhenotypeExperimental Organism SystemsCaenorhabditis ElegansVertebratesSensory PerceptionResearch ArticleSignal TransductionEXPRESSIONStable isotope labeling by amino acids in cell cultureComputational biologyBiologyResearch and Analysis MethodsSOLUTE-CARRIER-PROTEINModel OrganismsmedicineAnimalsdata integration030304 developmental biologyAfferent NeuronsReproducibility of ResultsCell Biologyzebrafishbiology.organism_classificationCiliopathyRenal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11]Biological DatabasesCellular NeuroscienceRNAOSCP1CiliaCartaPLoS ONE
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Antagonists and agonists at the glycine site of the NMDA receptor for therapeutic interventions.

2003

For decades neuroreceptor research has focused on the development of NMDA glycine-site antagonists, after Johnson and Ascher found out in 1987 about the co-agonistic character of this achiral amino acid at the NMDA receptor. Contrary to the inhibitory glycine receptor (glycine(A)) the glycine binding site on the NMDA receptor (glycine(B)) is strychnine-insensitive. A great diversity of diseases showing a disturbed glutamate neurotransmission have been linked to the NMDA receptor. Glycine site antagonists have been investigated for acute diseases like stroke and head trauma as well as chronic ones like dementia and chronic pain.

PsychosisGlycinePainPharmacologyNeurotransmissionInhibitory postsynaptic potentialReceptors N-Methyl-D-AspartateGlycine bindingMemantineDrug DiscoverymedicineAnimalsHumansReceptorGlycine receptorPharmacologychemistry.chemical_classificationBinding SitesEpilepsyOrganic ChemistryGlutamate receptorGeneral Medicinemedicine.diseaseAmino acidStrokeNeuroprotective AgentsBiochemistrychemistryGlycineSchizophreniaNMDA receptorAnticonvulsantsDementiaExcitatory Amino Acid AntagonistsEuropean journal of medicinal chemistry
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Changes in enzymes involved in photosynthesis and other metabolic processes in the fruit of Opuntia ficus-indica during growth and ripening

2011

The aim of this study was to investigate changes in the abundance of a number of enzymes in the peel, core and seeds of fruits of Opuntia ficus-indica (L.) Miller during development. The enzymes studied were phosphoenolpyruvate carboxylase (PEPC; EC: 4.1.1.31), ribulose-1,5-bisphosphate carboxylase/oxygenase (RUBISCO; EC: 4.1.1.39), aldolase (EC: 4.1.2.13), pyruvate, orthophosphate dikinase (PPDK; EC: 2.7.9.1), phosphoenolpyruvate carboxykinase (PEPCK; EC: 4.1.1.49) and aspartate aminotransferase (AspAT; EC: 2.6.1.1). To detect these enzymes, antibodies specific for each enzyme were used to probe Western blots of sodium dodecyl sulphate polyacrylamide gels. Fruit weight increased throughout…

PyruvateOxygenaseOpuntia ficus-indica (L) Miller; Fruit metabolism; Phosphoenolpyruvate carboxylase; Phosphoenolpyruvate carboxykinase; Pyruvate orthophosphate dikinase; Aspartate aminotransferase; Aldolase; Ribulose-15-bisphosphate carboxylase/oxygenaseHorticultureAspartate aminotransferasePhosphoenolpyruvate carboxylaseAldolaseOpuntia ficus-indica (L.) Miller Fruit metabolism Phosphoenolpyruvate carboxylase Phosphoenolpyruvate carboxykinase Pyruvate orthophosphatedikinase Aspartate aminotransferase Aldolase Ribulose-15-bisphosphatecarboxylase/oxygenaseorthophosphate dikinasebiologyRuBisCOAldolase Afood and beveragesRipeningFruit metabolismPyruvate carboxylaseRibulose-1Settore AGR/03 - Arboricoltura Generale E Coltivazioni ArboreeOpuntia ficus-indica (L) MillerPhosphoenolpyruvate carboxykinaseBiochemistrybiology.protein5-bisphosphate carboxylase/oxygenaseCrassulacean acid metabolismPhosphoenolpyruvate carboxykinasePhosphoenolpyruvate carboxylaseScientia Horticulturae
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Evolutionary plasticity of SH3 domain binding by Nef proteins of the HIV-1/SIVcpz lentiviral lineage

2021

The accessory protein Nef of human and simian immunodeficiency viruses (HIV and SIV) is an important pathogenicity factor known to interact with cellular protein kinases and other signaling proteins. A canonical SH3 domain binding motif in Nef is required for most of these interactions. For example, HIV-1 Nef activates the tyrosine kinase Hck by tightly binding to its SH3 domain. An archetypal contact between a negatively charged SH3 residue and a highly conserved arginine in Nef (Arg77) plays a key role here. Combining structural analyses with functional assays, we here show that Nef proteins have also developed a distinct structural strategy—termed the "R-clamp”—that favors the formation …

RNA virusesviruksetvirusesSimian Acquired Immunodeficiency SyndromeHIV InfectionsPathology and Laboratory MedicineSH3 domainWhite Blood CellsImmunodeficiency VirusesAnimal CellsMedicine and Health SciencesBiology (General)MammalsGenetics11832 Microbiology and virology0303 health sciencesKinase030302 biochemistry & molecular biologyEukaryotavirus diseasesTransfection3. Good healthSIVMedical MicrobiologyViral PathogensViral evolutionVirusesVertebratesProto-Oncogene Proteins c-hckApesSimian Immunodeficiency VirusPathogensCellular TypesTyrosine kinaseResearch ArticlePrimateskinaasitEvolutionary ImmunologyLineage (genetic)QH301-705.5Immune CellsImmunologyevoluutioBiologyTransfectionResearch and Analysis MethodsHIV-tartuntaMicrobiologyViral EvolutionEvolution Molecularsrc Homology Domains03 medical and health sciencesVirologyRetrovirusesGeneticsAnimalsHumansLuciferaseAmino Acid Sequencenef Gene Products Human Immunodeficiency VirusChimpanzeesMolecular Biology TechniquesMicrobial PathogensMolecular Biology030304 developmental biologyEvolutionary BiologyBlood CellsSequence Homology Amino AcidMacrophagesLentivirusOrganismsBiology and Life SciencesHIVCell BiologyRC581-607Organismal Evolution3121 General medicine internal medicine and other clinical medicineMicrobial EvolutionAmniotesHIV-1ParasitologySalt bridgeproteiinitImmunologic diseases. AllergyZoology
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Pseudouridine: Still mysterious, but never a fake (uridine)!

2014

International audience; Pseudouridine () is the most abundant of >150 nucleoside modifications in RNA. Although was discovered as the first modified nucleoside more than half a century ago, neither the enzymatic mechanism of its formation, nor the function of this modification are fully elucidated. We present the consistent picture of synthases, their substrates and their substrate positions in model organisms of all domains of life as it has emerged to date and point out the challenges that remain concerning higher eukaryotes and the elucidation of the enzymatic mechanism.

RNA MitochondrialSaccharomyces cerevisiaeReviewBiologyModified nucleosidesPseudouridine03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA modificationEscherichia coliHumansRNA Processing Post-Transcriptional[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Intramolecular TransferasesUridineMolecular Biology030304 developmental biology0303 health sciencesRNACell BiologyRNA Transfer Amino Acid-SpecificRibonucleoproteins Small NuclearUridineIsoenzymeschemistryBiochemistryRNA Ribosomal030220 oncology & carcinogenesisTransfer RNANucleic Acid ConformationRNARibosomesNucleosidePseudouridineSmall nuclear RNA[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyRNA Guide Kinetoplastida
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RepeatsDB in 2021: improved data and extended classification for protein tandem repeat structures

2020

The RepeatsDB database (URL: https://repeatsdb.org/) provides annotations and classification for protein tandem repeat structures from the Protein Data Bank (PDB). Protein tandem repeats are ubiquitous in all branches of the tree of life. The accumulation of solved repeat structures provides new possibilities for classification and detection, but also increasing the need for annotation. Here we present RepeatsDB 3.0, which addresses these challenges and presents an extended classification scheme. The major conceptual change compared to the previous version is the hierarchical classification combining top levels based solely on structural similarity (Class > Topology > Fold) with two new lev…

Repetitive Sequences Amino AcidAcademicSubjects/SCI00010BiologíaStatistics as TopicProtein Data Bank (RCSB PDB)Computational biologyBiologyRepetitive SequencesGene Ontology; HEK293 Cells; HeLa Cells; Humans; Proteins; Reproducibility of Results; Statistics as Topic; User-Computer Interface; Databases Protein; Repetitive Sequences Amino Acid; Tandem Repeat SequencesDatabases03 medical and health sciencesAnnotationUser-Computer InterfaceProtein structureSimilarity (network science)Tandem repeatGeneticsDatabase IssueHumansDatabases ProteinCiencias Exactasdatabase030304 developmental biology0303 health sciencesHierarchy (mathematics)Protein030302 biochemistry & molecular biologyProteinsReproducibility of Resultscomputer.file_formatProtein Data BankClass (biology)proteinsAmino AcidComputingMethodologies_PATTERNRECOGNITIONGene OntologyHEK293 CellsclassificationTandem Repeat Sequencesprotein tandem repeat structures[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]computerHeLa CellsNucleic Acids Research
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