GPMDB00463OtherBenevento M, et al.InstrumentNot AvailableNot availableHuman_adenovirus_c_uid14518, Humanm.benevento@uu.nlNot availableBiomolecular Mass Spectrometry and Proteomics, Bijvoet Centre for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrechthttp://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210027817http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210027822http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210027821http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210027819Not availableGPMDBpeptidolysis, count in organism, presence or absence in organism., Degradations, count, Proteolyses, ATP-dependent proteolysis, Digestion, structure, content, Protein, Protein Digestions, Degradation, number, composition, quantitative, compositionality, Protein Degradations, Protein Digestion, composed of, Digestions, Protein Degradation, presenceGene., APR, protease activity, data, SeptD1, Viral, JCAP, LRP, Slpa, Eseptin, Proteins, FNZ, APOER, FINC, Normalcy, HAPO, LETS, CIG, peptide, polypeptide, Viral Gene Proteins, SINT1, CD91, Protein, Gene Products, TGFBR5, PNUTL4, ED-B, Sint1, AF17q25, Normalities, NAPB, average, SZP, FN, Normality, NOXA, CACP, present in organism, proteins, Viral Gene Products, peptide hydrolase activity, Protein Gene Products, MSF, Msf, Gene Proteins, Health, A2MR, proteinase activity, LRP1A, GFND2, GFND, MSF1, acting on peptide bonds, hydrolase, IGFBP3R460http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM112100278213dbgap_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 Reanalysis0.00.00.014188772362739050.01.0falseAdenovirus composition, proteolysis, and disassembly studied by in-depth qualitative and quantitative proteomics.Data from ProteomeXchange, PXD ID: PXD000591. File: HAdV_LysN_OrbiXL.msf. Published as part of J Biol Chem. 2014 Apr 18;289(16):11421-30 . From the Abstract: {{i}} Using high-resolution MS-based proteomics in combination with multiple protease digestion, we profiled, with on average 90% sequence coverage, all 13 viral proteins present in an human adenovirus (HAdV) vector. This in-depth profile provided multiple peptide-based evidence on intrinsic protease activity affecting several HAdV proteins. {{/i}}2014-06-09GPM11210027821PXD000591PXD000591