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Evaluating protein interactions through cross-linking mass spectrometry

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New bioinformatics tools enable the recognition of neighboring amino acids in protein complexes.

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Figure 1: CXMS complements other techniques that characterize protein interactions and structure.

References

  1. Walzthoeni, T. et al. Nat. Methods 9, 901–903 (2012).

    Article  CAS  Google Scholar 

  2. Yang, B. et al. Nat. Methods 9, 904–906 (2012).

    Article  CAS  Google Scholar 

  3. Li, D. et al. Bioinformatics 13, 3049–3050 (2005).

    Article  Google Scholar 

  4. Fields, S. & Song, O. Nature 340, 245–246 (1989).

    Article  CAS  Google Scholar 

  5. Elion, E.A. Curr. Protoc. Mol. Biol. 70, 20.5 (2006).

    Google Scholar 

  6. Leitner, A. et al. Mol. Cell. Proteomics 9, 1634–1649 (2010).

    Article  CAS  Google Scholar 

  7. Trester-Zedlitz, M. et al. J. Am. Chem. Soc. 125, 2416–2425 (2003).

    Article  CAS  Google Scholar 

  8. Wang, J., Pérez-Santiago, J., Katz, J.E., Mallick, P. & Bandeira, N. Mol. Cell. Proteomics 9, 1476–1485 (2010).

    Article  CAS  Google Scholar 

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Correspondence to David L Tabb.

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Tabb, D. Evaluating protein interactions through cross-linking mass spectrometry. Nat Methods 9, 879–881 (2012). https://doi.org/10.1038/nmeth.2139

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