Search results for "Protein Interaction Domains and Motifs"

showing 2 items of 42 documents

Prediction of Specific TCR-Peptide Binding From Large Dictionaries of TCR-Peptide Pairs

2019

Abstract The T cell repertoire is composed of T cell receptors (TCR) selected by their cognate MHC-peptides and naive TCR that do not bind known peptides. While the task of distinguishing a peptide-binding TCR from a naive TCR unlikely to bind any peptide can be performed using sequence motifs, distinguishing between TCRs binding different peptides requires more advanced methods. Such a prediction is the key for using TCR repertoires as disease-specific biomarkers. We here used large scale TCR-peptide dictionaries with state-of-the-art natural language processing (NLP) methods to produce ERGO (pEptide tcR matchinG predictiOn), a highly specific classifier to predict which TCR binds to which…

lcsh:Immunologic diseases. AllergyComputer scienceevaluation methodsT-LymphocytesT cellImmunologyReceptors Antigen T-CellEpitopes T-LymphocyteTarget peptidePeptide bindingPeptidechemical and pharmacologic phenomenaComputational biologyLigandsSoftware implementationautoencoder (AE)AntigenEvaluation methodsmedicineImmunology and AllergyHumansProtein Interaction Domains and MotifsEpitope specificityAntigensDatabases ProteinOriginal Researchchemistry.chemical_classificationBinding SitesT cell repertoireChemistryRepertoirelong short-term memory (LSTM)T-cell receptorepitope specificitydeep learninghemic and immune systemsmedicine.anatomical_structuremachine learningPeptidesSequence motiflcsh:RC581-607SoftwareProtein BindingSignal TransductionTCR repertoire analysisFrontiers in Immunology
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α-secretase mediated conversion of the amyloid precursor protein derived membrane stub C99 to C83 limits Aβ generation

2009

The Swedish mutation within the amyloid precursor protein (APP) causes early-onset Alzheimer's disease due to increased cleavage of APP by BACE1. While beta-secretase shedding of Swedish APP (APPswe) largely results from an activity localized in the late secretory pathway, cleavage of wild-type APP occurs mainly in endocytic compartments. However, we show that liberation of Abeta from APPswe is still dependent on functional internalization from the cell surface. Inspite the unchanged overall beta-secretase cleaved soluble APP released from APP(swe) secretion, mutations of the APPswe internalization motif strongly reduced C99 levels and substantially decreased Abeta secretion. We point out t…

medicine.medical_specialtymedia_common.quotation_subjectEndocytic cycleCHO CellsTransfectionBiochemistryAmyloid beta-Protein PrecursorCellular and Molecular NeuroscienceCricetulusCricetinaeInternal medicinemental disordersmedicineAmyloid precursor proteinAnimalsHumansBiotinylationProtein Interaction Domains and MotifsSecretionInternalizationSecretory pathwaymedia_commonAmyloid beta-PeptidesbiologyChemistryP3 peptidePeptide FragmentsCell biologyEndocrinologyGene Expression RegulationAlpha secretaseMutationbiology.proteinAmyloid Precursor Protein SecretasesAmyloid precursor protein secretaseJournal of Neurochemistry
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