Mardakheh Faraz K FK

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Proteomics (17)
Multiomics (1)

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Homo sapiens (8)
Mus musculus (7)
Danio rerio (1)

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pride (16)
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Cell culture (15)
Permanent cell line cell (13)
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Carcinoma (5)
Colon cancer (5)
Breast cancer (2)
Pancreatic cancer (2)
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Mass Spectrometry (16)
Shotgun proteomics (10)
Affinity purification coupled with mass spectrometry proteomics (5)
Top-down proteomics (1)

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LTQ Orbitrap Velos (1)

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2023 (7)
2026 (3)
2020 (3)
2016 (2)
2021 (2)

Lab affiliation

Centre for Cancer Cell & Molecular Biology, Barts Cancer Institute, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, UK. (5)
Centre for Cancer Cell & Molecular Biology Barts Cancer Institute Queen Mary University of London Charterhouse Square London EC1M 6BQ U.K. (2)
Barts Cancer Institute, Queen Mary University of London, Chareterhouse square, London EC1M 6BQ, UK. (1)
Barts Cancer Institute, Queen Mary University of London, Charterhouse square, London EC1M 6BQ. (1)
Barts Cancer Institute, Queen Mary University of London. (1)
Centre for Cancer Cell & Molecular Biology Barts Cancer Institute Queen Mary University of London John Vane Science Centre Charterhouse Square London EC1M 6BQ UK (1)
Centre for Cancer Cell & Molecular Biology Barts Cancer Institute Queen Mary University of London Charterhouse Square London EC1M 6BQ UK. (1)
Centre for Cancer Cell & Molecular Biology Barts Cancer Institute Queen Mary University of London John Vane Science Centre Charterhouse Square London EC1M 6BQ UK (1)
Centre for Cancer Cell & Molecular Biology, Barts Cancer Institute, Queen Mary University of London, John Vane Science Centre, Charterhouse Square, London EC1M 6BQ, UK (1)
Centre for Cancer Cell and Molecular Biology, Barts Cancer Institute, Queen Mary University of London, Charterhouse square, London EC1M 6BQ, United Kingdom. (1)
Division of Cancer Biology, Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, The United Kingdom. (1)

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Analysis of FAM65A interactions

We identified FAM65A as a novel interactor of RHOA. To reveal other binding partners of FAM65A, we carried out a quantitative IP-MS, using SILAC labelled HeLa cells ectopically expressing GFP-FAM65A or GFP alone as control. Experiments were performed in duplicate with switched labelling and specific...

ORGANISM(S): Homo sapiens (Human)

2016-11-01 | PXD004933 | Pride

Intensity-based absolute quantification (iBAQ) of proteins in MDA-MB231

To determine the absolute copy number of proteins in MDA-MB231 breast cancer cells, we employed IBAQ mediated absolute quantification of proteins based on (Schwanhäusser et al., Nature, 2011), with some modifications. Maqquant calculated iBAQ values were calibrated using spike-in standards, and used...

ORGANISM(S): Homo sapiens (Human)

2021-05-14 | PXD024139 | Pride

Ibaq absolute protein quantification breast cancer mda-mb231

Interactome analysis of human RBMS1 protein in SW480 cells.

To identify protein binding partners of endogenous RBMS1, it was immunoprecipicated in triplicate, vs. IgG control, from SW480 colon adenocarcinoma cells, and subjected to MS analysis on an Q-exactive plus Orbitrap mass spectrometer. Raw files 13, 14, and 15 correspond to biological replicate IPs of...

ORGANISM(S): Homo sapiens (Human)

2020-06-10 | PXD019479 | Pride

Ip-ms rbms1 lc-ms/ms

Analysis of the impact of Nucleolin phospho-mutants on the proteome of pancreatic ductal adenocarcinoma cells.

To reveal the impact of Nucleolin (Ncl) phosphorylation on oncogenic KRAS-induced changes in the proteome of Pancreatic Ductal Adenocarcinoma (PDAC) cells, we carried out a quantitative proteomic analysis on tumour cells isolated from an inducible mouse model of PDAC (iKras PDAC) (Ying et al., 2012)...