<HashMap><database>PAXDB</database><file_versions><headers><Content-Type>application/xml</Content-Type></headers><body><files><Other>http://pax-db.org/downloads/latest/datasets/bioprojects-abundance-files-v4.0.zip</Other></files><type>primary</type></body><statusCode>OK</statusCode><statusCodeValue>200</statusCodeValue></file_versions><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>0</viewCount><searchCount>0</searchCount></scores><additional><omics_type>Proteomics</omics_type><submitter>Christian von Mering</submitter><species>9606</species><full_dataset_link>https://pax-db.org/dataset/9606/1430705385</full_dataset_link><submitter_email>mering@imls.uzh.ch</submitter_email><submitter_affiliation>University of Zurich</submitter_affiliation><sample_protocol></sample_protocol><repository>PAXDB</repository><data_protocol>For the rescaling, the
datasets are first parsed or processed such that the data reflect
proportional abundances of whole protein molecules
(i.e. proportionality to counts of complete, individual protein
molecules, not to molecular weights, protein volumes, or digested
peptides). In the case of spectral counting data protein. The proportional abundances are rescaled linearly to add up
to one million; this means the abundance of each protein of
interest is finally expressed in (parts per million,) relative to
all other proteins in a sample. 
For a given protein abundance dataset, we then compute
the absolute log abundance ratios of all pairs of proteins
annotated to be functionally linked. The median of these absolute
log abundance ratios represents an indirect quality
metric: the closer it is to zero, the better (i.e. the more there
is consistency between abundance values and functional annotations
such as protein complexes or pathways). We then
compute a background expectation for this metric, by permuting
the abundance values in a given dataset randomly,
and recomputing the median log abundance ratios. The permutation
is repeated several times, yielding a distribution of
medians. The actually observed median is then expressed as a
Z-score distance to the random distribution ofmedians—this
distance is termed the interaction consistency score.</data_protocol><pubmed_abstract>Next-generation transcriptome sequencing is increasingly integrated with MS to enhance MS-based protein and peptide identification. Recently, a breakthrough in transcriptome analysis was achieved with the development of ribosome profiling (ribo-seq). This technology is based on the deep sequencing of ribosome-protected mRNA fragments, thereby enabling the direct observation of in vivo protein synthesis at the transcript level. In order to explore the impact of a ribo-seq-derived protein sequence search space on MS/MS spectrum identification, we performed a comprehensive proteome study on a human cancer cell line, using both shotgun and N-terminal proteomics, next to ribosome profiling, which was used to delineate (alternative) translational reading frames. By including protein-level evidence of sample-specific genetic variation and alternative translation, this strategy improved the identification score of 69 proteins and identified 22 new proteins in the shotgun experiment. Furthermore, we discovered 18 new alternative translation start sites in the N-terminal proteomics data and observed a correlation between the quantitative measures of ribo-seq and shotgun proteomics with a Pearson correlation coefficient ranging from 0.483 to 0.664. Overall, this study demonstrated the benefits of ribosome profiling for MS-based protein and peptide identification and we believe this approach could develop into a common practice for next-generation proteomics.</pubmed_abstract><pubmed_title>A proteogenomics approach integrating proteomics and ribosome profiling increases the efficiency of protein identification and enables the discovery of alternative translation start sites.</pubmed_title><pubmed_authors>Koch Alexander A, Gawron Daria D, Steyaert Sandra S, Ndah Elvis E, Crappé Jeroen J, De Keulenaer Sarah S, De Meester Ellen E, Ma Ming M, Shen Ben B, Gevaert Kris K, Van Criekinge Wim W, Van Damme Petra P, Menschaert Gerben G</pubmed_authors><data_synonyms>Add, DmelCG43443, ADD, ADD-87, Hts-RC, data, AU023367, Data Set, protein complex, supply, Proteins, Ovhts, Gene, HtsRC, CG9325, protein, neutral molecular compounds, protein-containing complex, Dmel_CG9325, Xt, Peptide, 1B1, add, Polypeptides, anon-EST:Posey9, protein polypeptide chains, native protein, peptido, htsRC, GLI3-190, natural protein, polypeptide chain, Add-hts, Protein, CG43443, Gene Products, l(2)k14523, Dmel_CG34197, l(2)00634, median, Ovhts-RC, background, supply and distribution, protein aggregate, all_pairs, molecule, Bph, molecula, Random selection by shearing, oligonucleotide random primer, proportion, HTS-R1, HTS, Hts, molecules, peptides, l(2)k06121, adducin, GLI3FL, distribution, AI854843, proportionality, add-like, HTS-RC, rate, proteins, Molekuel, Pdn, sample population, introduction, Protein Gene Products, Gene Proteins, Adducin, RANDOM, 10^[-6], ppm, sample, supply., quotient, Peptid, peptidos, Polypeptide, Attention Deficit Hyperactivity Disorder, l(2)01103, EST D, CG34197, HtsF, ratio</data_synonyms><description_synonyms>HCT-116 cell, HCT116 cell, HCT-116, HCT 116., HCT116</description_synonyms><pubmed_title_synonyms>Translation Profiling, protein translation, Profiling, protein anabolism, protein biosynthetic process, Footprintings, ARTSeq, Peptidomics, Researchs, protein complex, Capture, Ribosome Profilings, Proteins, Proteogenomic Profiling, ribosome profiling, Gene, protein, active mRNA translation sequencing, protein-containing complex, Productivity, Translation, protein synthesis., Translation Profilings, protein polypeptide chains, Ribosome-Bound tRNA, native protein, natural protein, polypeptide chain, Ribosome Footprinting, Ribo-Seq, Protein, Gene Products, protein formation, Footprinting, protein biosynthesis, Proteogenomic Research, Analysis, Profilings, tRNA Captures, Ribosome Bound tRNA Capture, protein aggregate, Translating Ribosome Affinity Purification, Ribosome, Ribosome-Bound tRNA Captures, Research, Proteogenomic Analysis, Ribosome-Bound tRNA Capture, proteins, tRNA Capture, Ribosome-Bound, Ribosome Footprintings, Protein Gene Products, Gene Proteins, Proteogenomic, Captures, ribosome footprinting</pubmed_title_synonyms><name_synonyms>Line, Peptidomics., Cell Lines, HCT-116 cell, HCT116 cell, HCT-116, HCT116, HCT 116, Cell, Lines</name_synonyms><pubmed_abstract_synonyms>protein translation, human being, single-organism developmental process, Footprintings, determination, Transcriptome Profile, Peptidomics, Ribo-seq, Capture, postnatal development, number, Gene Expression Profile, Gene, ribosomal RNA, growth and development, Profiles, protein, protein-containing complex, Ximpact, Reading Frame, presence, Human, Frames, peptide, Translation, Polypeptides, protein polypeptide chains, Translation Profilings, peptido, polypeptide chain, Homo sapiens, Messenger, Ribosome Footprinting, Ribo-Seq, Gene Products, Profilings, protein aggregate, Non Polyadenylated, Man, study, Frame, Ribosome-Bound tRNA Captures, Diversity, Man (Taxonomy), Genetic, peptides, MS2, Profile, Polyadenylated Messenger, Ribosome-Bound tRNA Capture, messenger RNA, proteins, tRNA Capture, man, Signatures, template RNA, Expression Signature, sample, Transcriptomes, peptidos, Variation, Translation Profiling, Genetic Variations, Peptidomics., Profiling, RNA, protein anabolism, data, lumen, Transcriptome, protein biosynthetic process, Variations, ARTSeq, Polyadenylated, protein complex, Ribosome Profilings, space, Arts, Modern, Expression Profiles, Proteins, ribosome profiling, Messenger RNA, total expressed protein, Diversities, active mRNA translation sequencing, INSDC_feature:misc_RNA, Peptide, impact-a, whole transcriptome, Gene Expression, polypeptide, development, count in organism, Ribosome-Bound tRNA, Experiment, native protein, natural protein, Poly(A)+ mRNA, Expression Signatures, Gene Expression Signatures, Protein, chemical analysis, Genetic Diversities, protein formation, Footprinting, INSDC_feature:mRNA, sequence, ribosomal profiling, protein biosynthesis, Gene Expression Signature, Polyadenylated RNA, tRNA Captures, Ribosome Bound tRNA Capture, anatomical spaces, Translating Ribosome Affinity Purification, membrane bound ribosome, Expression Profile, tandem MS, Transcriptome Profiles, free ribosome, Polyadenylated Messenger RNA, Ribosome, lumen space, Industrial, Poly(A)+ RNA, Non Polyadenylated mRNA, Industrial Arts, protein_coding_transcript, mRNA, Poly(A) Tail, MS/MS, postnatal growth, Non-Polyadenylated, common, Genetic Diversity, Ribosome-Bound, Ribosome Footprintings, Non-Polyadenylated mRNA, primary structure of sequence macromolecule, human, sample population, Protein Gene Products, Gene Proteins, protein synthesis, Gene Expression Profiles, Modern Man, Captures, ribosome footprinting, Reading, Peptid, Polypeptide, assay, Signature, Ribo-seq assay, Polyadenylated mRNA, E430016J11Rik, growth, Poly(A) RNA, Proteomes, RWDD5</pubmed_abstract_synonyms><citation_count>0</citation_count></additional><is_claimable>false</is_claimable><name>H.sapiens - Cell line, Hct116 (Koch,proteomics,2014)</name><description>abundance based on MAPPED_BY_AUTHORS, HCT116, Interaction consistency score: 4.6, Coverage: 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