The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.
Probing Native Protein Structures by Chemical Cross-linking, Mass Spectrometry, and Bioinformatics
Open accessAbstract
Chemical cross-linking of reactive groups in native proteins and protein complexes in combination with the identification of cross-linked sites by mass spectrometry has been in use for more than a decade. Recent advances in instrumentation, cross-linking protocols, and analysis software have led to a renewed interest in this technique, which promises to provide important information about native protein structure and the topology of protein complexes. In this article, we discuss the critical steps of chemical cross-linking and its implications for (structural) biology: reagent design and cross-linking protocols, separation and mass spectrometric analysis of cross-linked samples, dedicated software for data analysis, and the use of cross-linking data for computational modeling. Finally, the impact of protein cross-linking on various biological disciplines is highlighted.
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Cites
Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., & Aebersold, R. (1999) · Nature Biotechnology · doi:10.1038/13690 · Cited by 4,683 · cited 1×
“The introduction of affinity tags into protein chemistry re-agents has found widespread use for quantitative proteomics as well as for the characterization of post-translational modifications (15, 16).”
BackgroundBioorthogonal Chemistry: Fishing for Selectivity in a Sea of Functionality
Sletten, E. M., & Bertozzi, C. R. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200900942 · Cited by 3,165
ChIP–seq: advantages and challenges of a maturing technology
Park, P. J. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2641 · Cited by 2,217
Gray, J. J., Moughon, S., Wang, C., Schueler-Furman, O., Kuhlman, B., Rohl, C. A., & Baker, D. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00670-3 · Cited by 1,127
Fragmentation pathways of protonated peptides
Paizs, B., & Suhai, S. (2005) · Mass Spectrometry Reviews · doi:10.1002/mas.20024 · Cited by 1,118
Calculation of Protein-Ligand Binding Affinities
Gilson, M. K., & Zhou, H.-X. (2007) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.36.040306.132550 · Cited by 966
The minimum information about a proteomics experiment (MIAPE)
Taylor, C. F., Paton, N. W., Lilley, K. S., Binz, P.-A., Julian, R. K., Jones, A. R., Zhu, W., Apweiler, R., Aebersold, R., Deutsch, E. W., et al. (2007) · Nature Biotechnology · doi:10.1038/nbt1329 · Cited by 766
Self-citationAnalysis of protein complexes using mass spectrometry
Gingras, A.-C., Gstaiger, M., Raught, B., & Aebersold, R. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2208 · Cited by 708
Self-citationSinz, A. (2006) · Mass Spectrometry Reviews · doi:10.1002/mas.20082 · Cited by 648
Kuo, M.-H., & Allis, C. D. (1999) · Methods · doi:10.1006/meth.1999.0879 · Cited by 602
Cited by
Next-generation proteomics: towards an integrative view of proteome dynamics
Altelaar, A. F. M., Munoz, J., & Heck, A. J. R. (2013) · Nature Reviews Genetics · doi:10.1038/nrg3356 · Cited by 782
Quantitative, High-Resolution Proteomics for Data-Driven Systems Biology
Cox, J., & Mann, M. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061308-093216 · Cited by 685
Rappsilber, J. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.10.014 · Cited by 422
Herzog, F., Kahraman, A., Boehringer, D., Mak, R., Bracher, A., Walzthoeni, T., Leitner, A., Beck, M., Hartl, F.-U., Ban, N., et al. (2012) · Science · doi:10.1126/science.1221483 · Cited by 371
Self-citationPredicting Protein–Protein Interactions from the Molecular to the Proteome Level
Keskin, O., Tuncbag, N., & Gursoy, A. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00683 · Cited by 369
Metadata
- Authors
- Leitner, A., Walzthoeni, T., Kahraman, A., Herzog, F., Rinner, O., Beck, M., & Aebersold, R.
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2010-08
- Volume
- 9
- Issue
- 8
- Pages
- 1634-1649
- ISSN
- 1535-9476 (ISSN-L)
- OpenAlex
- W2026507477
- Cited by
- 458
- References
- 74
- FWCI
- 19.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Leitner, A., Walzthoeni, T., Kahraman, A., Herzog, F., Rinner, O., Beck, M., & Aebersold, R. (2010). Probing Native Protein Structures by Chemical Cross-linking, Mass Spectrometry, and Bioinformatics. Molecular & Cellular Proteomics. https://doi.org/10.1074/mcp.r000001-mcp201
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