The DOI matches its Crossref record; 115 of the 115 references it cites were found in a registry or an index.
Crosslinking and Mass Spectrometry: An Integrated Technology to Understand the Structure and Function of Molecular Machines
Open accessAbstract
In recent years, chemical crosslinking of protein complexes and the identification of crosslinked residues by mass spectrometry (XL-MS; sometimes abbreviated as CX-MS) has become an important technique bridging mass spectrometry (MS) and structural biology. By now, XL-MS is well established and supported by publicly available resources as a convenient and versatile part of the structural biologist's toolbox. The combination of XL-MS with cryo-electron microscopy (cryo-EM) and/or integrative modeling is particularly promising to study the topology and structure of large protein assemblies. Among the targets studied so far are proteasomes, ribosomes, polymerases, chromatin remodelers, and photosystem complexes. Here we provide an overview of recent advances in XL-MS, the current state of the field, and a cursory outlook on future challenges.
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Cites
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Cited by
Mass-spectrometric exploration of proteome structure and function
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Complex‐centric proteome profiling by SEC‐SWATH‐MS
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Metadata
- Authors
- Leitner, A., Faini, M., Stengel, F., & Aebersold, R.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2016-01
- Volume
- 41
- Issue
- 1
- Pages
- 20-32
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2183276865
- Cited by
- 355
- References
- 115
- FWCI
- 1.76
- Type
- journal article
- Language
- en
- Open access
- green
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- Leitner, A., Faini, M., Stengel, F., & Aebersold, R. (2016). Crosslinking and Mass Spectrometry: An Integrated Technology to Understand the Structure and Function of Molecular Machines. Trends in Biochemical Sciences. https://doi.org/10.1016/j.tibs.2015.10.008
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