2016
DOI: 10.1016/j.chembiol.2016.05.012
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In Vivo Conformational Dynamics of Hsp90 and Its Interactors

Abstract: Summary Hsp90 belongs to a family of some of the most highly expressed heat shock proteins that function as molecular chaperones to protect the proteome not only from the heat shock, but from other misfolding events. As many client proteins of Hsp90 are involved in oncogenesis, this chaperone has been in focus of intense research efforts. Yet, we lack structural information for how Hsp90 interacts with co-chaperones and client proteins. Here, we develop a mass spectrometry based approach that allows quantitati… Show more

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Cited by 76 publications
(143 citation statements)
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“…Chemical cross-linking provides evidence of proximal solventaccessible sites on proteins in vivo and is a means to predict and assemble models of protein structures (34,35,39). It is important to note that the chemical cross-linking workflow in this study was performed on whole, functional mitochondria.…”
Section: Resultsmentioning
confidence: 99%
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“…Chemical cross-linking provides evidence of proximal solventaccessible sites on proteins in vivo and is a means to predict and assemble models of protein structures (34,35,39). It is important to note that the chemical cross-linking workflow in this study was performed on whole, functional mitochondria.…”
Section: Resultsmentioning
confidence: 99%
“…Functional, respiring mitochondria were cross-linked in situ using a PIR cross-linker, biotin-aspartate proline-PIR n-hydroxyphthalimide (BDP-NHP) (33)(34)(35)39), and were assembled into an interactome consisting of 2,427 nonredundant cross-linked peptide pairs across 11 individual murine samples (Dataset S1). We identified 327 unique mitochondrial proteins, 31.3% of the murine mitochondrial proteome (327 of 1,042 proteins; MitoCarta 2.0) (Fig.…”
Section: Resultsmentioning
confidence: 99%
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