GPMDB00123OtherThayer N, et al.InstrumentNot AvailableNot availableYeastnthayer@fhcrc.orgNot availableBasic Sciences, Fred Hutchinson Cancer Research Center, Seattlehttp://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002698http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002697http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002711http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002710http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002713http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002712http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002715http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002714http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002696http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002717http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002716http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002719http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002718http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002720http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002700http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002722http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002721http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002702http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002701http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002704http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002703http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002706http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002705http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002708http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002707http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320002709Not availableGPMDBProtein Gene Products, Gene Proteins, polypeptide, Identification, asymmetry, long, Protein, asymmetric., Gene Products, Proteins, Identifications (Psychology), Gene, proteins, CellProcedures, AGTBP, determination, Aminosaeure, Procathepsin L, Aminocarbonsaeure, nutrient medium, Gene, baker's yeast, Major excreted protein, high weight, Visible Light, Saccharomyces italicus, Ctsl1, Cathepsin L, method, Method, method used in an experiment, yeast, heavy, Gene Products, Studies, CTSL1, 1190035F06Rik, p39 cysteine proteinase, Cell., light, lager beer yeast, Pulses, Microsomal endopeptidase, Neurotensin endopeptidase, amino acids, CATL, cell, long, Cathepsin L1 light chain, Saccharomyes cerevisiae, CFU-EM, proteins, nkt, present in organism, megakaryocyte/erythroid progenitor cell, Visible, Angiotensin-binding protein, Saccharomyces uvarum var. melibiosus, Study, Candida robusta, Methodological Studies, 3.4.24.16, Cyclic protein 2, Saccharomyces capensis, TR2, brewer's yeast, data, Radiation, Aminokarbonsaeure, Proteins, Light, Procedure, CD258, CFU-MegE, Saccaromyces cerevisiae, Cell, polypeptide, Sccharomyces cerevisiae, LIGHT, Protein, chemical analysis, 3.4.22.15, MEP, Saccharomyces oviformis, Visible Radiations, Radiations, Yeast, Visible Radiation, Meg/E progenitor, HVEML, medium, growth medium, fs, CP-2, Photoradiation, Methodological, Amino, Methodological Study, LTg, Protein Gene Products, plan specification, Gene Proteins, Cathepsin L1 heavy chain, megakaryocyte/erythrocyte progenitor, Photoradiations, EP24.16, MOP, Acids, assay, colony forming unit erythroid megakaryocyte, Proteomes, Mitochondrial oligopeptidase M, Elderly120http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM323200027073dbgap_ncbi~0patentfamilies~0rfam~0merops~0complex-portal~0uniprot~0wormbaseparasite~0embl-covid19~0reactome~0emdb~0wgs_masters~0ebiweb_resources~0opentargets_genetics~0biomodels_all~0ipd-mhc~0ebiweb_teams~0taxonomy~0genome_assembly~0sc-experiments~0ebiweb_people~0enzymeportal_enzymes~0ipd-nhkir~0cellosaurus~0pdbe~0chebi~0patentproteins~0interpro7~0uniref~0chembl~0pdbekb~0gpcrdb~0hgnc~0sc-genes~0intact~0rhea~0ebiweb_training~0alphafold~0imgt-hla~0patentnucleotides~0ensemblroot~0eva_studies~0non-coding~0europepmc~0identifiers_registry~0pdbechem~0hpa-covid19~0eva-variants-covid19~0biosamples~0gwas_catalog~0biotools~0tls_masters~0mesh~0coding~0sra~0opentargets~0efo~0embl-pathogen~0project~0pride~1human_diseases~0geo_datasets~0embl~0treefam~0uniparc~0ols~0dgva~0intenz~0go~0tsa_masters~0biosamples-covid19~0ebiweb_corporate~0omim~0lrg~0earlycause-molecular-sequences~0ipd-kir~0empiar~0rnacentral~0orcid_data_claims~0gpmdb~1lineage-covid19~0metagenomics~0pfam~0pride archive~1varsite~00Resource Reanalysis0.00.00.0037014188772362740.01.0falseIdentification of long-lived proteins retained in cells undergoing repeated asymmetric divisionsData from ProteomeXchange, PXD ID: PXD001251. File: ZN100309_092809_ZN_12.mzml. From ProteomeXchange: {{i}} To identify long-lived proteins that are retained in yeast mother cells, we combined a method developed in our lab with a pulse-chase protocol using total proteome analysis. Cells were initially grown in medium with stable heavy-isotope amino acids to label proteins. The cells were then switched into media containing light-isotope amino acids and cultured for an additional ~18 cell divisions with the MEP engaged. Finally, we determined whether any of the original heavy-labeled proteins were still present in the aged mother cells {{/i}}2014-09-02GPM32320002707PXD001251PXD001251