The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
NEDD8 and ubiquitin ligation by cullin-RING E3 ligases
Open accessAbstract
RING E3s comprise the largest family of ubiquitin (UB) and ubiquitin-like protein (UBL) ligases. RING E3s typically promote UB or UBL transfer from the active site of an associated E2 enzyme to a distally-recruited substrate. Many RING E3s - including the cullin-RING ligase family - are multifunctional, interacting with various E2s (or other E3s) to target distinct proteins, transfer different UBLs, or to initially modify substrates with UB or subsequently elongate UB chains. Here we consider recent structures of cullin-RING ligases, and their partner E2 enzymes, representing ligation reactions. The studies collectively reveal multimodal mechanisms - interactions between ancillary E2 or E3 domains, post-translational modifications, or auxiliary binding partners - directing cullin-RING E3-E2 enzyme active sites to modify their specific targets.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“ubiquitin E3 ligases serve as scaffolds between a target protein and an activated ubiquitin E2 conjugating enzyme charged with a ubiquitin molecule (E2–Ub), by binding both molecules, then catalysing the transfer of ubiquitin from the active site cysteine of the E2 onto a lysine side chain of a target protein104–107.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [107]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex
Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507
Self-citationProteolysis-Targeting Chimeras as Therapeutics and Tools for Biological Discovery
Burslem, G. M., & Crews, C. M. (2020) · Cell · doi:10.1016/j.cell.2019.11.031 · Cited by 1,079
Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., & Schulman, B. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.022 · Cited by 767
Self-citationStructural basis of lenalidomide-induced CK1α degradation by the CRL4CRBN ubiquitin ligase
Petzold, G., Fischer, E. S., & Thomä, N. H. (2016) · Nature · doi:10.1038/nature16979 · Cited by 620
Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism
Cappadocia, L., & Lima, C. D. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00737 · Cited by 581
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
Orlicky, S. M., Tang, X., Willems, A. R., Tyers, M., & Sicheri, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00034-5 · Cited by 515
Structure of the E6/E6AP/p53 complex required for HPV-mediated degradation of p53
Martinez-Zapien, D., Ruiz, F. X., Poirson, J., Mitschler, A., Ramirez, J., Forster, A., Cousido-Siah, A., Masson, M., Pol, S. V., PODJARNY, A. D., et al. (2016) · Nature · doi:10.1038/nature16481 · Cited by 512
Insights into E3 ligase activity revealed by a SUMO–RanGAP1–Ubc9–Nup358 complex
Reverter, D., & Lima, C. D. (2005) · Nature · doi:10.1038/nature03588 · Cited by 493
Cited by
Sorted by citations
PROTAC targeted protein degraders: the past is prologue
Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395
Structural basis of human transcription–DNA repair coupling
Kokić, G., Wagner, F., Chernev, A., Urlaub, H., & Cramer, P. (2021) · Nature · doi:10.1038/s41586-021-03906-4 · Cited by 139
An E3 ligase guide to the galaxy of small-molecule-induced protein degradation
Jevtić, P., Haakonsen, D. L., & Rapé, M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.002 · Cited by 147
Riching, K. M., Caine, E. A., Urh, M., & Daniels, D. L. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00339b · Cited by 107
Chemoproteomics-enabled discovery of a covalent molecular glue degrader targeting NF-κB
King, E. A., Cho, Y. J., Hsu, N. T., Dovala, D., McKenna, J. M., Tallarico, J. A., Schirle, M., & Nomura, D. K. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.02.008 · Cited by 105
Metadata
- Authors
- Baek, K., Scott, D. C., & Schulman, B. A.
- Affiliations
- Max Planck Institute of Biochemistry (DE)
- St. Jude Children's Research Hospital (US)
- Corresponding author
- Schulman, Brenda A
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2021-04
- Volume
- 67
- Pages
- 101-109
- ISSN
- 0959-440X (ISSN-L)
- PMC
- PMC8096640
- OpenAlex
- W3096018906
- Cited by
- 152
- References
- 50
- Citations by year
- 2026: 21 · 2025: 21 · 2024: 34 · 2023: 28 · 2022: 33 · 2021: 15
- FWCI
- 1.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Current Opinion in Structural Biology (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (R01CA247365, P30CA021765)
- European Research Council (789016-NEDD8Activate)
- Deutsche Forschungsgemeinschaft (SCHU 3196/1-1)
- American Lebanese Syrian Associated Charities
- Horizon 2020
- Max-Planck-Gesellschaft
- St. Jude Children's Research Hospital
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- NEDD8, Cullin-RING E3 ligases, ubiquitin-like proteins, ubiquitination, post-translational modification, ubiquitin chain elongation
- MeSH terms
- Ubiquitins, Catalytic Domain, Ubiquitin, Ubiquitin-Protein Ligases, Cullin Proteins, Ubiquitination
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
