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IBench Ground Truth Validation Tool

ABSTRACT: iBench is an open-source tool that provides enhanced validation of Mass Spectrometry identification methods. For this project, iBench was applied to Percolator rescored results from Mascot searches from a tryptic digestion of the K562 proteome, HLA-I immunopeptidome experiment, and synthetic peptide libraries. Here we provide the Mascot search results which were benchmarked as well as the original searches used to generate the ground truth identifications. These search results were generated by reprocessing RAW data from the PXD031709, PXD034056 and PXD031812 repositories.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Michele Mishto

LAB HEAD: Michele Mishto, Juliane Liepe

PROVIDER: PXD034968 | Pride | 2022-10-11

REPOSITORIES: Pride

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inSPIRE Spectral Rescoring Tool

Project description:inSPIRE is an open-source tool for spectral rescoring of mass spectrometry search results. For this project, inSPIRE was applied to MaxQuant, PEAKS DB, and Mascot search results from a tryptic digestion of the K562 proteome. Here we provide the RAW files and search results using MaxQuant, PEAKS DB, and Mascot. We also reprocessed RAW data from the PXD031709 and PXD031812 repositories for which we provide the search result files. Additionally, we provide PEAKS search results from RAW files from the PXD015489 repository which was used as training data for a predictor used within inSPIRE. Michele Mishto, Head of the research group Molecular Immunology at King’s College London and the Francis Crick Institute, London (UK). Email: michele.mishto@kcl.ac.uk,

2022-10-26 | PXD034056 | Pride

Reanalysis of Data-dependent acquisition based proteomic datasets of Mycobacterium abscessus

Project description:Detection of species-specific proteotypic peptides for accurate and easy characterization of infectious non-tuberculous mycobacteria such as Mycobacterium abscessus is essential. Therefore, we carried out reanalysis of publicly available M. abscessus proteomic dataset MSV000085363, PXD015680 and PXD022644 by proteome database search and followed by spectral library generation. The raw DDA data were searched against the M. abscessus proteome database using Proteome Discoverer and FragPipe. The resulting peptide spectrum matches were converted into a spectral library using BiblioSpec.

2024-03-07 | PXD045930 | Pride

Reanalysis of Data-dependent acquisition based proteomic datasets of Mycobacterium avium subsp. paratuberculosis, Mycobacterium marinum and Mycobacterium vaccae

Project description:Detection of species-specific proteotypic peptides for accurate and easy characterization of infectious non-tuberculous mycobacteria such as Mycobacterium avium subsp. paratuberculosis, Mycobacterium marinum and Mycobacterium vaccae is essential. Therefore, we carried out reanalysis of publicly available M. avium subsp. paratuberculosis, M. marinum and M. vaccae proteomic dataset PXD027444, PXD003766 and PASS00954 by proteome database search and followed by spectral library generation. The raw DDA data were searched against their respective reference proteome databases using Proteome Discoverer and FragPipe. The resulting peptide spectrum matches were converted into a spectral library using BiblioSpec.

2024-03-07 | PXD045965 | Pride

Nipped in the bud: a microbial effector destabilizes MADS-domain transcription factors

Project description:Eluates from pull down experiments were separated on an SDS gel, and bands isolated for in gel trypsin digestion. Digested samples were analysed by LCMSMS on an Orbitrap. Peaklists were generated using MaxQuant 1.3.0.5 and database searches performed using Mascot Server 2.4. Data from all gel slices from one sample were merged in one Mascot search, and the results were imported into Scaffold 4.0.4.

2014-05-21 | PXD000223 | Pride

Global Identification of Protein PTMs in a Single-pass Database Search

Project description:Bottom-up proteomics database search algorithms used for peptide identification cannot comprehensively identify posttranslational modifications (PTMs) in a single-pass because of high false discovery rates (FDRs). A new approach to database searching enables Global PTM (G-PTM) identification by exclusively looking for curated PTMs, thereby avoiding the FDR penalty experienced during conventional variable modification searches. We identified nearly 2500 unique, high-confidence modified peptides comprising 31 different PTM types in single-pass database searches.

2015-07-31 | GSE59956 | GEO

System-level analysis of cancer and stomal cell specific proteomes reveals extensive reprogramming of phosphorylation networks by tumor microenvironment

Project description:DLD-1 cells and mouse were treated with DMSO, GDC0941 and CAL101 for 2 hours. Proteins were digested with trypsin and phospho peptides were enriched using TiO2. Enriched phosphopeptides and peptides were analysed by LTQ Orbitrap Velos mass spectrometer. (MS/MS data were converted to mgf files using Mascot Distiller (version 2.2) and searched against the UniProt-TrEMBL and UniProt SwissProt databases (release March 2012) and a decoy database using the Mascot search engine (version 2.2). The data was searched twice, restricting searches against human or mouse specific sequences in each separate search. For phosphoproteomics, tolerance windows were 3 p.p.m. and 600 mmu for parent and fragment ions, respectively. For proteomics, these were 5 p.p.m. and 50 mmu for parent and fragment ions, respectively. Allowed variable modifications were methionine oxidation, pyroglutamate at the N-terminus and phosphorylation of serine, threonine and tyrosine residues. Significance of peptide identification was assessed by comparing results returned by searches against random and forward databases. The probability of correct phosphorylation site assignment was determined by the Mascot delta score approach. Ambiguous phosphorylation site assignments are reported as gene name followed by start and end of the amino acid sequence

2014-04-02 | PXD000218 | Pride

Reanalysis of Data-dependent acquisition based proteomic datasets of Mycobacterium smegmatis

Project description:Detection of species-specific proteotypic peptides for accurate and easy characterization of infectious non-tuberculous mycobacteria such as Mycobacterium smegmatis is essential. Therefore, we carried out reanalysis of publicly available M. smegmatis proteomic dataset PXD003303, PXD004197, PXD010020, PXD016241, PXD017602, PXD027848, PXD027855 and PXD029588 by proteome database search and followed by spectral library generation. The raw DDA data were searched against their respective reference proteome databases using Proteome Discoverer and FragPipe. The resulting peptide spectrum matches were converted into a spectral library using BiblioSpec.

2024-03-07 | PXD046063 | Pride

Metastasis-repressive CircRNA MASCOT Regulates Distribution of the Splicing Factor hnRNP M

Project description:Alternative splicing (AS) diversifies the transcriptome complexity and is usually hijacked by cancer cells. Here, we identified heterogeneous nuclear ribonucleoprotein M (hnRNP M) as an indispensable contributor to EMT-related AS reprogramming, whose sub-nuclear distribution of hnRNP M is altered in metastatic tumors. Upon TGFβ stimulation, hnRNP M trends to disassociate with a circRNA called MASCOT (hnRNP M-ASsociated Circular RNA Of TGFβ) that demonstrated an impressive inhibitory effect on EMT process and tumor metastasis. Mechanistically, the anti-metastatic effect of MASCOT is attributed to not only its competition with U2 RNA splicing factors to recruit hnRNP M in the nucleoplasm, but also the anchorage of hnRNP M with nucleolin into the nucleolus to cause a temporospatial separation of hnRNP M from spliceosome. Moreover, the correlation between MASCOT expression and hnRNP M sub-nuclear localization was validated in clinical specimens. Our study deciphers the regulatory codes controlling AS networks and highlights MASCOT as a promising therapeutic to treat metastasis.

2022-09-20 | GSE213677 | GEO

Metastasis-repressive CircRNA MASCOT Regulates Distribution of the Splicing Factor hnRNP M

2022-09-10 | GSE165576 | GEO

Npro protein interaction partners

Project description:The N-terminal protease Npro from pestiviruses has been shown to rapidly dismantle the innate immune response by targeting IRF3 for degradation, resulting in inhibition of apoptosis and interferon production. To understand it’s role in these different responses, we have identified multiple cellular factors that interact with this viral protein using mass spectrometry and proteomic analysis. Pull-down experiments were performed with Npro, and the samples were run on an SDS gel. Each lane was cut into 5-6 sclices and the slices were digested with trypsin. Peptides were extracted and analysed by LX-MSMS on an LTQ-Orbitrap (Thermo). Data were processed with MaxQuant (1.3.0.5) and searches performed with Mascot on the Sptrembl database (taxonomy human). All gel slices from one sample were merged in one Mascot search. Mascot results were imported into Scaffold 3.6.5.

2016-12-22 | PXD000115 | Pride

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