The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry
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Citations
Cites
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,995
Self-citationOng, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
Self-citationTranscriptional regulation by histone ubiquitination and deubiquitination
Zhang, Y. (2003) · Genes & Development · doi:10.1101/gad.1156403 · Cited by 425
Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics
Kirkpatrick, D. S., Denison, C., & Gygi, S. P. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-750 · Cited by 209
Overalkylation of a Protein Digest with Iodoacetamide
Boja, E. S., & Fales, H. M. (2001) · Analytical Chemistry · doi:10.1021/ac0103423 · Cited by 190
Dahl, K. H., & McKinley-McKee, J. S. (1981) · Bioorganic Chemistry · doi:10.1016/0045-2068(81)90012-2 · Cited by 25
Cited by
Protein Analysis by Shotgun/Bottom-up Proteomics
Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491
SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
Ikeda, F., Deribe, Y. L., Skånland, S. S., Stieglitz, B., Grabbe, C., Franz-Wachtel, M., van Wijk, S. J. L., Goswami, P., Nagy, V., Terzic, J., et al. (2011) · Nature · doi:10.1038/nature09814 · Cited by 745
Chemical Modification of Proteins at Cysteine: Opportunities in Chemistry and Biology
Chalker, J. M., Bernardes, G. J. L., Lin, Y. A., & Davis, B. G. (2009) · Chemistry – An Asian Journal · doi:10.1002/asia.200800427 · Cited by 649
Atypical ubiquitylation — the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
Kulathu, Y., & Komander, D. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3394 · Cited by 619
Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
Plechanovová, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H., & Hay, R. T. (2012) · Nature · doi:10.1038/nature11376 · Cited by 521
Metadata
- Authors
- Nielsen, M. L., Vermeulen, M., Bonaldi, T., Cox, J., Moroder, L., & Mann, M.
- Venue
- Nature Methods
- Published
- 2008-06
- Volume
- 5
- Issue
- 6
- Pages
- 459-460
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W2081736950
- Cited by
- 286
- References
- 6
- FWCI
- 6.20
- Type
- journal article
- Language
- en
- Open access
- closed
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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Data sources
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.
