1997
STEP: a family of brain-enriched PTPs. Alternative splicing produces transmembrane, cytosolic and truncated isoforms.
Bult A, Zhao F, Dirkx R, Raghunathan A, Solimena M, Lombroso P. STEP: a family of brain-enriched PTPs. Alternative splicing produces transmembrane, cytosolic and truncated isoforms. European Journal Of Cell Biology 1997, 72: 337-44. PMID: 9127733.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsBase SequenceBlotting, NorthernBlotting, WesternBrainCalcium-Binding ProteinsCalnexinCHO CellsCricetinaeFemaleFluorescent Antibody Technique, IndirectMembrane ProteinsMolecular Sequence DataProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsSynaptophysinTransfectionConceptsProtein tyrosine phosphataseCatalytic phosphatase domainProtein tyrosine kinase familyHydrophobic amino acid sequenceAlternative splicing mechanismAmino acid sequencePrevious biochemical studiesTyrosine kinase familyStop codon upstreamPhosphatase domainCytosolic variantAlternative splicingMembrane compartmentsTyrosine phosphataseKinase familySplicing mechanismSubcellular localizationCytosolic proteinsAcid sequenceN-terminusInactive variantContinuous sucrose gradientSTEP isoformsPolyproline domainEndoplasmic reticulum
1992
The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine
Kulke R, Horwitz B, Zibello T, DiMaio D. The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine. Journal Of Virology 1992, 66: 505-511. PMID: 1727496, PMCID: PMC238311, DOI: 10.1128/jvi.66.1.505-511.1992.Peer-Reviewed Original ResearchConceptsHydrophobic amino acidsAmino acidsE5 proteinRandom hydrophobic sequencesHydrophobic domainRodent fibroblast cell linesCentral hydrophobic domainHydrophobic amino acid sequenceCarboxyl-terminal amino acidsMouse C127 cellsAmino acid sequenceClasses of mutantsAbsence of glutamineBovine papillomavirus E5Mutant proteinsTransforming proteinDefective mutantsHydrophobic sequenceFibroblast cell lineProtein stabilityAcid sequenceC127 cellsHomodimer formationEfficient transformationProtein
1989
Transforming activity of a 16-amino-acid segment of the bovine papillomavirus E5 protein linked to random sequences of hydrophobic amino acids
Horwitz B, Weinstat D, DiMaio D. Transforming activity of a 16-amino-acid segment of the bovine papillomavirus E5 protein linked to random sequences of hydrophobic amino acids. Journal Of Virology 1989, 63: 4515-4519. PMID: 2552136, PMCID: PMC251082, DOI: 10.1128/jvi.63.11.4515-4519.1989.Peer-Reviewed Original ResearchConceptsE5 proteinAmino acidsWild-type E5 proteinBovine papillomavirus E5 proteinAmino acid sequence requirementsHydrophobic amino acid sequenceCarboxyl-terminal amino acidsMouse C127 cellsAmino acid sequenceBovine papillomavirus type 1Carboxyl-terminal portionWild-type onesHydrophobic amino acidsPapillomavirus type 1Hydrophobic sequenceDifferent amino acidsAcid sequenceC127 cellsSequence requirementsE5 geneCell transformationFoci formationSubstitution mutationsCell membraneProtein
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