Proteomics

Dataset Information

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Mitochondria cross-linking mass spectrometry


ABSTRACT: We performed cross-linking mass spectrometry experiments on intact mitochondria isolated from mouse heart in two conditions, native-state and high-salt treatment to disrupt electrostatic interactions. Both conditions were provided in biological replicates.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Mus musculus  

TISSUE(S): Heart

DISEASE(S): Not Available

SUBMITTER: Fan Liu  

LAB HEAD: Albert J.R. Heck

PROVIDER: PXD006816 | Pride | 2017-12-11

REPOSITORIES: pride

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Publications

The interactome of intact mitochondria by cross-linking mass spectrometry provides evidence for coexisting respiratory supercomplexes.

Liu Fan F   Lössl Philip P   Rabbitts Beverley M BM   Balaban Robert S RS   Heck Albert J R AJR  

Molecular & cellular proteomics : MCP 20171208 2


Mitochondria exert an immense amount of cytophysiological functions, but the structural basis of most of these processes is still poorly understood. Here we use cross-linking mass spectrometry to probe the organization of proteins in native mouse heart mitochondria. Our approach provides the largest survey of mitochondrial protein interactions reported so far. In total, we identify 3,322 unique residue-to-residue contacts involving half of the mitochondrial proteome detected by bottom-up proteom  ...[more]

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