The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Deciphering post‐translational modification codes
Open accessAbstract
Post‐translational modifications (PTMs) occur on nearly all proteins. Many domains within proteins are modified on multiple amino acid sidechains by diverse enzymes to create a myriad of possible protein species. How these combinations of PTMs lead to distinct biological outcomes is only beginning to be understood. This manuscript highlights several examples of combinatorial PTMs in proteins, and describes recent technological developments, which are driving our ability to understand how PTM patterns may “code” for biological outcomes.
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Cites
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Cited by
Advances in Fmoc solid‐phase peptide synthesis
Behrendt, R., White, P., & Offer, J. (2016) · Journal of Peptide Science · doi:10.1002/psc.2836 · Cited by 760
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Intrinsically disordered proteins play diverse roles in cell signaling
Bondos, S. E., Dunker, A. K., & Uversky, V. N. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00821-7 · Cited by 222
Intrinsically disordered proteins and multicellular organisms
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Metadata
- Authors
- Lothrop, A. P., Torres, M. P., & Fuchs, S. M.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2013-02-09
- Volume
- 587
- Issue
- 8
- Pages
- 1247-1257
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2054590983
- Cited by
- 180
- References
- 13
- FWCI
- 8.14
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Lothrop, A. P., Torres, M. P., & Fuchs, S. M. (2013). Deciphering post‐translational modification codes. FEBS Letters. https://doi.org/10.1016/j.febslet.2013.01.047
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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.
