Proteomics

Dataset Information

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Mablango_ClpP_HYTANE_P124_Lumos


ABSTRACT: This dataset consists of 6 raw MS files, acquired on Thermo Fusion Lumos mass spectrometer operated in Data Dependent Acquisition mode. Samples were generated by Keith Wong. Sample processing and mass spectrometry acquisition was performed by Cassandra Wong. Data analysis was performed by Cassandra Wong, Shen Zhang and Keith Wong. The files are associated with a manuscript submitted for publication by Mark Mabanglo et al. The main goal of this paper was to demonstrate the use of novel imipridone derived compounds to induce selective cancer cell lethality via dysregulation of ClpP in cancer cells. Walid Houry is the corresponding author of the manuscript (walid.houry@utoronto.ca); Anne-Claude Gingras should be contacted for questions on this dataset (gingras@lunenfeld.ca) This submission is associated with 4 Supplementary Files (in addition to this README file) Metadata describes the composition of this dataset. Peptides lists all peptide identification evidence. Proteins lists all protein identification evidence. Pvalue_peptides lists all p-values calculated between conditions for peptides.

INSTRUMENT(S): Orbitrap Fusion Lumos

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

SUBMITTER: Anne-Claude Gingras  

PROVIDER: MSV000089642 | MassIVE | Mon Jun 13 11:16:00 BST 2022

REPOSITORIES: MassIVE

Dataset's files

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Publications

Potent ClpP agonists with anticancer properties bind with improved structural complementarity and alter the mitochondrial N-terminome.

Mabanglo Mark F MF   Wong Keith S KS   Barghash Marim M MM   Leung Elisa E   Chuang Stephanie H W SHW   Ardalan Afshan A   Majaesic Emily M EM   Wong Cassandra J CJ   Zhang Shen S   Lang Henk H   Karanewsky Donald S DS   Iwanowicz Andrew A AA   Graves Lee M LM   Iwanowicz Edwin J EJ   Gingras Anne-Claude AC   Houry Walid A WA  

Structure (London, England : 1993) 20221230 2


The mitochondrial ClpP protease is responsible for mitochondrial protein quality control through specific degradation of proteins involved in several metabolic processes. ClpP overexpression is also required in many cancer cells to eliminate reactive oxygen species (ROS)-damaged proteins and to sustain oncogenesis. Targeting ClpP to dysregulate its function using small-molecule agonists is a recent strategy in cancer therapy. Here, we synthesized imipridone-derived compounds and related chemical  ...[more]

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