The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Structural and Functional Insights to Ubiquitin-Like Protein Conjugation
Open accessAbstract
Attachment of ubiquitin (Ub) and ubiquitin-like proteins (Ubls) to cellular proteins regulates numerous cellular processes including transcription, the cell cycle, stress responses, DNA repair, apoptosis, immune responses, and autophagy, to name a few. The mechanistically parallel but functionally distinct conjugation pathways typically require the concerted activities of three types of protein: E1 Ubl-activating enzymes, E2 Ubl carrier proteins, and E3 Ubl ligases. E1 enzymes initiate pathway specificity for each cascade by recognizing and activating cognate Ubls, followed by catalyzing Ubl transfer to cognate E2 protein(s). Under certain circumstances, the E2 Ubl complex can direct ligation to the target protein, but most often requires the cooperative activity of E3 ligases. Reviewed here are recent structural and functional studies that improve our mechanistic understanding of E1-, E2-, and E3-mediated Ubl conjugation.
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Cites
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Cited by
Swatek, K. N., & Komander, D. (2016) · Cell Research · doi:10.1038/cr.2016.39 · Cited by 2,081
E3 ubiquitin ligases: styles, structures and functions
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Drugging the undruggables: exploring the ubiquitin system for drug development
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The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery
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Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
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Metadata
- Authors
- Streich, F. C., & Lima, C. D.
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2014-05-06
- Volume
- 43
- Issue
- 1
- Pages
- 357-379
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- OpenAlex
- W2157574579
- Cited by
- 164
- References
- 14
- FWCI
- 1.15
- Type
- journal article
- Language
- en
- Open access
- bronze
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