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Taipale_HSP90_cochaperone_P77_VS1

ABSTRACT: This submission is part of the mass spectrometry datasets for the manuscript by Taipale et al. (HSP90 cochaperone interaction network). This submission contains files for the first batch (2011) of the files included in the manuscript, all acquired on a 5600 TripleTOF mass spectrometer. See the README file within "Methods and Protocols" and the accompanying File description.

PROVIDER: MSV000078466 | MassIVE | Fri Aug 02 00:00:00 BST 2013

REPOSITORIES: MassIVE

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Publications

A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.

Taipale Mikko M Tucker George G Peng Jian J Krykbaeva Irina I Lin Zhen-Yuan ZY Larsen Brett B Choi Hyungwon H Berger Bonnie B Gingras Anne-Claude AC Lindquist Susan S

Cell 20140701 2

Chaperones are abundant cellular proteins that promote the folding and function of their substrate proteins (clients). In vivo, chaperones also associate with a large and diverse set of cofactors (cochaperones) that regulate their specificity and function. However, how these cochaperones regulate protein folding and whether they have chaperone-independent biological functions is largely unknown. We combined mass spectrometry and quantitative high-throughput LUMIER assays to systematically charac ...[more]

PMID: 25036637

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Taipale_HSP90_cochaperone_P77_VS6

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Taipale_HSP90_cochaperone_P77_VS5

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2014-04-02 | MSV000078574 | MassIVE

Raj_nSR100_interactions_P36_V21_P105_V17

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2014-04-23 | MSV000078609 | MassIVE

Model data for the evaluation of dependent-peptide visualisation tools

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ATR phosphoproteomics - substrate validation

Project description:ATR phosphoproteomics - Validation of ATR substrates as identified in phosphoproteomics screen. Sample Processing Protocol: Samples were processed as detailed in the accompanying manuscript. Data Processing Protol: Data were processed as detailed in the accompanying manuscript and the attached R script files.

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DIA-Umpire: comprehensive computational framework for data independent acquisition proteomics

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