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MASS, STAT5, Bioenergetic, Protein Gene Products, Gene Proteins, stem cell factor, Pseudomonas polycolor, Energy Metabolisms, KL-1, Replications, MGF, Bacterium aeruginosum, c-Kit ligand, structure, SSKS, KITLG, Autonomous Replications, Eph2, regulation, Bacillus aeruginosus, DNA, fatty acid biosynthesis, SCF, Proteomes, host organism., 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archive~1","varsite~0"],"reanalysis_count":["0"],"submitter_keywords":["Resource Reanalysis"],"citation_count_scaled":["0.0"],"reanalysis_count_scaled":["0.0"],"view_count_scaled":["0.00431832202344232"],"download_count_scaled":["0.0"],"normalized_connections":["1.0"],"additional_accession":[]},"is_claimable":false,"name":"Systematic identification of hypothetical bacteriophage proteins targeting key protein complexes of Pseudomonas aeruginosa.","description":"Data from ProteomeXchange, PXD ID: PXD001199. File: VelosPro0289.mzid_VelosPro0289.MGF. Publsihed as part of J Proteome Res. 2014 Sep 4  . From the Abstract: {{i}} ... In this study, we focused on the composition of important macromolecular complexes of Pseudomonas aeruginosa involved in transcription, DNA replication, fatty acid biosynthesis, RNA regulation, energy metabolism and cell division, during infection with members of seven distinct clades of lytic phages. Using affinity purifications of these host protein complexes coupled to mass spectrometric analyses, 37 host complex-associated phage proteins could be identified. Importantly, eight of these show an inhibitory effect on bacterial growth upon episomal expression, suggesting that these phage proteins are potentially involved in hijacking the host complexes ... {{/i}}","dates":{"submission":"2014-09-09"},"accession":"GPM32320003213","cross_references":{"Pride":["PXD001199"],"pride":[],"Pride Archive":["PXD001199"]}}