Dataset Information

Szewczyk_InhibitionOfPRMT7_P36_2020

ABSTRACT: This dataset consists of 16 raw MS files, acquired on Orbitrap Fusion Lumos Tribrid mass spectrometer operated in Data Dependent Acquisition (DDA) mode for the 8 input files and DDA with simultaneous parallel reaction monitoring (targeted masses; 599.33, 604.33, 608.23, 606.33, 407.89, 403.22, 651.35, 657.29, 656.02, 652.62, and 611.34) for the 8 mono-methyl arginine immunoprecipitation files. Samples were generated by Magdalena M Szewczyk and mass spectrometric acquisition was performed by Amber L Couzens. Analysis was performed by Amber L Couzens, Suzanne Ackloo, and David Dilworth The files are associated with a manuscript submitted for publication by Magdalena M Szewczyk et al. The main goal of this paper was to enable further discovery of PRMT7 biology and to explore its potential as a therapeutic target. Dalia Barsyte-Lovejoy (d.barsyte@utoronto.ca) and Hiroshi Nara (nara@pharm.or.jp) are the corresponding authors of the manuscript; Anne-Claude Gingras should be contacted for questions on this dataset (gingras@lunenfeld.ca). This submission is associated with 1 Supplementary Files (in addition to this README file) MassIVE_Table 1 describes the composition of this dataset

INSTRUMENT(S): Orbitrap Fusion Lumos

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

SUBMITTER: Anne-Claude Gingras

PROVIDER: MSV000084773 | MassIVE | Wed Jan 08 08:53:00 GMT 2020

REPOSITORIES: MassIVE

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Publications

Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response.

Szewczyk Magdalena M MM Ishikawa Yoshinori Y Organ Shawna S Sakai Nozomu N Li Fengling F Halabelian Levon L Ackloo Suzanne S Couzens Amber L AL Eram Mohammad M Dilworth David D Fukushi Hideto H Harding Rachel R Dela Seña Carlo C CC Sugo Tsukasa T Hayashi Kozo K McLeod David D Zepeda Carlos C Aman Ahmed A Sánchez-Osuna Maria M Bonneil Eric E Takagi Shinji S Al-Awar Rima R Tyers Mike M Richard Stephane S Takizawa Masayuki M Gingras Anne-Claude AC Arrowsmith Cheryl H CH Vedadi Masoud M Brown Peter J PJ Nara Hiroshi H Barsyte-Lovejoy Dalia D

Nature communications 20200514 1

Protein arginine methyltransferases (PRMTs) regulate diverse biological processes and are increasingly being recognized for their potential as drug targets. Here we report the discovery of a potent, selective, and cell-active chemical probe for PRMT7. SGC3027 is a cell permeable prodrug, which in cells is converted to SGC8158, a potent, SAM-competitive PRMT7 inhibitor. Inhibition or knockout of cellular PRMT7 results in drastically reduced levels of arginine monomethylated HSP70 family stress-as ...[more]

PMID: 32409666

Dataset Information

Szewczyk_InhibitionOfPRMT7_P36_2020

Dataset's files

Publications

Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response.

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