The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Measuring protein structural changes on a proteome-wide scale using limited proteolysis-coupled mass spectrometry
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Cites
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855
Skyline: an open source document editor for creating and analyzing targeted proteomics experiments
MacLean, B., Tomazela, D. M., Shulman, N., Chambers, M., Finney, G. L., Frewen, B., Kern, R., Tabb, D. L., Liebler, D. C., & MacCoss, M. J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq054 · Cited by 4,697
L-Arginine Modulates T Cell Metabolism and Enhances Survival and Anti-tumor Activity
Geiger, R., Rieckmann, J. C., Wolf, T., Basso, C., Feng, Y., Fuhrer, T., Kogadeeva, M., Picotti, P., Meissner, F., Mann, M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.09.031 · Cited by 1,775
Self-citationSelected reaction monitoring–based proteomics: workflows, potential, pitfalls and future directions
Picotti, P., & Aebersold, R. (2012) · Nature Methods · doi:10.1038/nmeth.2015 · Cited by 1,302
Self-citationSpectroscopic Methods for Analysis of Protein Secondary Structure
Pelton, J. T., & McLean, L. R. (2000) · Analytical Biochemistry · doi:10.1006/abio.1999.4320 · Cited by 1,195
Tracking cancer drugs in living cells by thermal profiling of the proteome
Savitski, M. M., Reinhard, F. B. M., Franken, H., Werner, T., Savitski, M. F., Eberhard, D., Molina, D. M., Jafari, R., Dovega, R. B., Klaeger, S., et al. (2014) · Science · doi:10.1126/science.1255784 · Cited by 1,187
Choi, M., Chang, C.-Y., Clough, T., Broudy, D., Killeen, T., MacLean, B., & Vitek, O. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu305 · Cited by 1,035
Hydrogen exchange mass spectrometry for studying protein structure and dynamics
Konermann, L., Pan, J., & Liu, Y.-H. (2011) · Chem. Soc. Rev. · doi:10.1039/c0cs00113a · Cited by 838
OpenMS: a flexible open-source software platform for mass spectrometry data analysis
Röst, H. L., Sachsenberg, T., Aiche, S., Bielow, C., Weisser, H., Aicheler, F., Andreotti, S., Ehrlich, H.-C., Gutenbrunner, P., Kenar, E., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3959 · Cited by 693
Michalski, A., Cox, J., & Mann, M. (2011) · Journal of Proteome Research · doi:10.1021/pr101060v · Cited by 685
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Thermal proteome profiling for interrogating protein interactions
Mateus, A., Kurzawa, N., Becher, I., Sridharan, S., Helm, D., Stein, F., Typas, A., & Savitski, M. M. (2020) · Molecular Systems Biology · doi:10.15252/msb.20199232 · Cited by 258
Zhou, M., Lantz, C., Brown, K. A., Ge, Y., Paša-Tolić, L., Loo, J. A., & Lermyte, F. (2020) · Chemical Science · doi:10.1039/d0sc04392c · Cited by 146
Bamberger, C., Pankow, S., Martínez-Bartolomé, S., Ma, M., Diedrich, J., Rissman, R. A., & Yates, J. R. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00912 · Cited by 70
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Metadata
- Authors
- Schopper, S., Kahraman, A., Leuenberger, P., Feng, Y., Piazza, I., Müller, O., Boersema, P. J., & Picotti, P.
- Venue
- Nature Protocols
- Published
- 2017-10-26
- Volume
- 12
- Issue
- 11
- Pages
- 2391-2410
- ISSN
- 1750-2799 (ISSN-L)
- 1754-2189
- OpenAlex
- W2765241646
- Cited by
- 288
- References
- 46
- FWCI
- 5.25
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Measuring protein structural changes on a proteome-wide scale using limited proteolysis-coupled mass spectrometry. https://app.cochat.ai/papers/10.1038/nprot.2017.100
- The paper
- Schopper, S., Kahraman, A., Leuenberger, P., Feng, Y., Piazza, I., Müller, O., Boersema, P. J., & Picotti, P. (2017). Measuring protein structural changes on a proteome-wide scale using limited proteolysis-coupled mass spectrometry. Nature Protocols. https://doi.org/10.1038/nprot.2017.100
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
