Cross-linking mass spectrometry for mapping protein complex topologies in situ

Cross-linking mass spectrometry has become an established technology to provide structural information on the topology and dynamics of protein complexes. Readily accessible workflows can provide detailed data on simplified systems, such as purified complexes. However, using this technology to study...

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Podrobná bibliografia
Vydané v:	Essays in biochemistry Ročník 67; číslo 2; s. 215
Hlavní autori:	Lee, Kitaik, O'Reilly, Francis J
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	England 29.03.2023
Predmet:	Cross-Linking Reagents - chemistry Cross-Linking Reagents - metabolism Mass Spectrometry - methods Proteomics - methods Crosslinking proteomics in situ protein-protein interactions
ISSN:	1744-1358, 1744-1358
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Popis
Shrnutí:	Cross-linking mass spectrometry has become an established technology to provide structural information on the topology and dynamics of protein complexes. Readily accessible workflows can provide detailed data on simplified systems, such as purified complexes. However, using this technology to study the structure of protein complexes in situ, such as in organelles, cells, and even tissues, is still a technological frontier. The complexity of these systems remains a considerable challenge, but there have been dramatic improvements in sample handling, data acquisition, and data processing. Here, we summarise these developments and describe the paths towards comprehensive and comparative structural interactomes by cross-linking mass spectrometry.
Bibliografia:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1744-1358 1744-1358
DOI:	10.1042/EBC20220168