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Taipale_HSP90_cochaperone_P77_VS3

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 second batch (2012) 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: MSV000078465 | MassIVE | Fri Aug 02 00:00:00 BST 2013

REPOSITORIES: MassIVE

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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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