2000
Physical Association of Eukaryotic Initiation Factor 4G (eIF4G) with eIF4A Strongly Enhances Binding of eIF4G to the Internal Ribosomal Entry Site of Encephalomyocarditis Virus and Is Required for Internal Initiation of Translation
Lomakin I, Hellen C, Pestova T. Physical Association of Eukaryotic Initiation Factor 4G (eIF4G) with eIF4A Strongly Enhances Binding of eIF4G to the Internal Ribosomal Entry Site of Encephalomyocarditis Virus and Is Required for Internal Initiation of Translation. Molecular And Cellular Biology 2000, 20: 6019-6029. PMID: 10913184, PMCID: PMC86078, DOI: 10.1128/mcb.20.16.6019-6029.2000.Peer-Reviewed Original ResearchConceptsInternal ribosomal entry siteEMCV internal ribosomal entry siteEIF4GAdditional amino-terminal sequenceEukaryotic initiation factor 4GRNA recognition motifEukaryotic initiation factor 4GIInternal ribosomal entryEntry siteComplex formationBeta-globin mRNAAmino-terminal sequenceEncephalomyocarditis virus internal ribosomal entry siteRibosomal entryRecognition motifLike domainMutational analysisPhysical associationInternal initiationHigh-affinity bindingBinding fragmentSpecific interactionsRNASimilar affinitySpecific high-affinity bindingOne Polypeptide with Two Aminoacyl-tRNA Synthetase Activities
Stathopoulos C, Li T, Longman R, Vothknecht U, Becker H, Ibba M, Söll D. One Polypeptide with Two Aminoacyl-tRNA Synthetase Activities. Science 2000, 287: 479-482. PMID: 10642548, DOI: 10.1126/science.287.5452.479.Peer-Reviewed Original ResearchConceptsProlyl-tRNA synthetaseProtein synthesisCysteinyl-tRNA synthetase activityAmino-terminal sequenceSynthetase activityAminoacyl-tRNA synthetase activityCertain archaeaEvolutionary originMethanococcus jannaschiiGenome sequenceSubstrate specificityGenetic analysisSuch organismsMessenger RNARNA synthetasesSynthetaseSequenceArchaeaJannaschiiSynthetasesRNAOrganismsPolypeptideProlylProtein
1992
GAP‐43 as a plasticity protein in neuronal form and repair
Strittmatter S, Vartanian T, Fishman M. GAP‐43 as a plasticity protein in neuronal form and repair. Developmental Neurobiology 1992, 23: 507-520. PMID: 1431834, DOI: 10.1002/neu.480230506.Peer-Reviewed Original ResearchConceptsGrowth cone membraneShort amino-terminal sequenceG proteinsCone membranePlasticity proteinsSpecific cellular domainsAmino-terminal sequenceMembrane localizationG-protein activityGAP-43Cellular domainsProtein activityCell shapeIntracellular proteinsActin filamentsBeta subunitRemarkable plasticityNeural developmentSuch plasticityTerminal sequenceProteinNeurite extensionGuanine nucleotidesNeurite growthAxonal extension
1990
Alternate splicing in a parvoviral nonstructural gene links a common amino-terminal sequence to downstream domains which confer radically different localization and turnover characteristics
Cotmore S, Tattersall P. Alternate splicing in a parvoviral nonstructural gene links a common amino-terminal sequence to downstream domains which confer radically different localization and turnover characteristics. Virology 1990, 177: 477-487. PMID: 2142555, DOI: 10.1016/0042-6822(90)90512-p.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAphidicolinBase SequenceCapsidCell DivisionChromosome MappingDiterpenesFluorescent Antibody TechniqueGenes, ViralL CellsMiceMinute virus of miceMolecular Sequence DataMolecular WeightParvoviridaeRNA SplicingRNA, ViralSequence Homology, Nucleic AcidViral Core ProteinsViral Nonstructural ProteinsViral Structural ProteinsConceptsCommon amino-terminal domainAmino-terminal domainNS-1 moleculesCommon amino-terminal sequenceNS-1 polypeptideAmino-terminal sequenceSodium dodecyl sulfate gel electrophoresisNS-1Dodecyl sulfate gel electrophoresisUnphosphorylated formInternal exonsAlternate splicingGene productsSulfate gel electrophoresisA9 cellsNonstructural genesSpliced formsPhosphorylated formDownstream domainContiguous sequencesNonstructural proteinsSpecies migratePeptide-specific antibodiesMinute virusTurnover characteristics
1989
Amino-terminal sequences of prosomatostatin direct intracellular targeting but not processing specificity
Sevarino K, Stork P, Ventimiglia R, Mandel G, Goodman R. Amino-terminal sequences of prosomatostatin direct intracellular targeting but not processing specificity. Cell 1989, 57: 11-19. PMID: 2564811, DOI: 10.1016/0092-8674(89)90167-0.Peer-Reviewed Original ResearchConceptsEndocrine cell linesRat preprosomatostatinCarboxy-terminal thirdDistinct cell typesAmino-terminal sequenceCell linesHybrid proteinLeader sequenceIntracellular targetingRegulated pathwayPreprosomatostatin 1Cellular factorsExpression vectorCell typesPattern of processingProcessing siteBioactive peptidesAnglerfish isletsSequenceDifferential processingPeptidesProteinResiduesPathwayHigh levels
1986
Organization of nonstructural genes of the autonomous parvovirus minute virus of mice
Cotmore S, Tattersall P. Organization of nonstructural genes of the autonomous parvovirus minute virus of mice. Journal Of Virology 1986, 58: 724-732. PMID: 2939261, PMCID: PMC252977, DOI: 10.1128/jvi.58.3.724-732.1986.Peer-Reviewed Original ResearchConceptsOpen reading frameAutonomous parvovirus minute virusParvovirus minute virusSimilar proteinsFusion proteinCommon amino-terminal sequenceSingle open reading frameNonstructural protein NS-1Rabbit reticulocyte lysate translation systemViral genomeReticulocyte lysate translation systemAlternative open reading framesNS-2 proteinsCarboxy-terminal halfNS-1 proteinNS-1Amino acid sequenceBacterial fusion proteinLysate translation systemMinute virusAmino-terminal sequenceProcaryotic expression vectorR2 transcriptsReading frameAcid sequence
1978
STUDIES OF THE STRUCTURE OF THE HUMAN Ia-LIKE ANTIGEN11This research is supported by grants from the U.S. Public Health Service (AI-10736 and AI-09576).
Springer T, Kaufman J, Terhorst C, Strominger J. STUDIES OF THE STRUCTURE OF THE HUMAN Ia-LIKE ANTIGEN11This research is supported by grants from the U.S. Public Health Service (AI-10736 and AI-09576). 1978, 229-234. DOI: 10.1016/b978-0-12-483260-2.50029-x.Peer-Reviewed Original Research
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