The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes
Open accessAbstract
Significance: Most proteins carry out their function by associating with other proteins in stable or transient complexes. Structural analysis of such complexes, for example by crystallography, is frequently performed to study their function or mode of action. However, many large complexes are refractory to traditional structural biology methods. Alternative methods have been developed that are often combined with computational methods in hybrid structural biology strategies. Among these, the combination of chemical cross-linking and MS (XL-MS) has shown to be particularly informative. Current XL-MS methods mainly rely on the coupling of lysine residues. Here we describe a chemistry to cross-link acidic residues that generates structural information complementary to that obtained by amine-specific cross-linking, thus significantly expanding the scope of XL-MS analyses.
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Cites
Complete subunit architecture of the proteasome regulatory particle
Lander, G. C., Estrin, E., Matyskiela, M. E., Bashore, C., Nogales, E., & Martin, A. (2012) · Nature · doi:10.1038/nature10774 · Cited by 608
Cited by
Grimm, M., Zimniak, T., Kahraman, A., & Herzog, F. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv463 · Cited by 121
“Chemistries targeting acidic amino acids have been successfully introduced (4), however, have not yet led to routine applications.”
BackgroundXL-MS: protein cross-linking coupled with mass spectrometry
Holding, A. N. (2015) · Methods · doi:10.1016/j.ymeth.2015.06.010 · Cited by 107
Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
Oroz, J., Chang, B. J., Wysoczanski, P., Lee, C.-T., Pérez-Lara, Á., Chakraborty, P., Hofele, R. V., Baker, J. D., Blair, L. J., Biernat, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06880-0 · Cited by 100
Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A
Pavic, K., Gupta, N., Omella, J. D., Derua, R., Aakula, A., Huhtaniemi, R., Määttä, J. A., Höfflin, N., Okkeri, J., Wang, Z., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36693-9 · Cited by 36
“The data show that the CIP2A(1-560) residues cross-linked to B56α are located primarily in the N-terminal head domain (K18, K21, E23, E34, K40) with an additional residue at the C-terminus (K490) (Fig.”
BackgroundMethodInfluentialSelf-citationStructural recognition and stabilization of tyrosine hydroxylase by the J-domain protein DNAJC12
Tai, M. D. S., Ochoa, L., Flydal, M. I., Velasco-Carneros, L., Muntaner, J., Santiago, C., Gamiz-Arco, G., Moro, F., Jung-KC, K., Gil-Cantero, D., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57733-6 · Cited by 16
Metadata
- Authors
- Leitner, A., Joachimiak, L. A., Unverdorben, P., Walzthoeni, T., Frydman, J., Förster, F., & Aebersold, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2014-06-17
- Volume
- 111
- Issue
- 26
- Pages
- 9455-9460
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2168248466
- Cited by
- 263
- References
- 1
- FWCI
- 7.48
- Type
- journal article
- Language
- en
- Open access
- bronze
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