Proteomics

Dataset Information

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Poirson_TPD_timsTOFPro2_VS13_14


ABSTRACT: This dataset consists of 18 raw DDA MS files and associated peak lists and results files, acquired on timsTOF Pro2 mass spectrometer operated in Data Dependent Acquisition-PASEF (Parallel accumulation-serial fragmentation) mode. It also consists of 18 raw DIA MS files acquired in Data Independent-PASEF mode on timsTOF Pro2 mass spectrometer. Samples were generated by Juline Poirson. Sample processing and mass spectrometry acquisition was performed by Cassandra Wong. Analysis was performed by Cassandra Wong and Juline Poirson. The files are associated with a manuscript submitted for publication by Juline Poirson et al. The main goal of this paper was to establish a synthetic proteome-scale platform to identify human proteins that promote degradation or stabilization of a target protein in a proximity-dependent manner. Mikko Taipale is the corresponding author of the manuscript (mikko.taipale@utoronto.ca); Anne-Claude Gingras should be contacted for questions on this dataset (gingras@lunenfeld.ca) This submission is associated with 3 Supplementary Files (in addition to this README file) Table 1 describes the composition of this dataset Table 2 lists all the peptide identification evidence (as per iProphet) Table 3 lists the protein intensity values

INSTRUMENT(S): timsTOF Pro 2

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Anne-Claude Gingras  

PROVIDER: MSV000093202 | MassIVE | Thu Oct 26 09:32:00 BST 2023

SECONDARY ACCESSION(S): PXD046426

REPOSITORIES: MassIVE

Dataset's files

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Publications


Targeted protein degradation and stabilization are promising therapeutic modalities because of their potency, versatility and their potential to expand the druggable target space<sup>1,2</sup>. However, only a few of the hundreds of E3 ligases and deubiquitinases in the human proteome have been harnessed for this purpose, which substantially limits the potential of the approach. Moreover, there may be other protein classes that could be exploited for protein stabilization or degradation<sup>3-5<  ...[more]

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