The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding
Open accessAbstract
Protein unfolding, one substrate at a time: Ubiquitin marks proteins for degradation by the proteasome. However, many substrates cannot be directly degraded because they are well folded or are located in cell membranes or in multimeric complexes. These proteins are first unfolded by the Cdc48 adenosine triphosphatase (ATPase), which forms a hexameric assembly that pulls polypeptides through its central pore. Twomey et al. determined structures of Cdc48 at an initiation stage of substrate processing. Surprisingly, a ubiquitin molecule in the substrate-linked polyubiquitin chain could be unfolded simply by binding to the Cdc48 complex. A segment of the unfolded ubiquitin inserts into the ATPase ring and initiates substrate unfolding. This explains why Cdc48 can deal with a broad range of substrates—even ones that are folded. Cooney et al. report the cryo–electron microscopy structure of Cdc48 in complex with an authentic substrate. In contrast to previously reported Cdc48 structures, an asymmetric spiraling assembly wraps around the extended substrate polypeptide. Thus, Cdc48 uses a hand-over-hand mechanism of translocation, which supports a common mechanism for protein substrate unfolding for AAA+ ATPases. Science , this issue p. eaax1033 , p. 502
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.
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
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,828
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 11,626
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E., Armache, J.-P., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,777
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334
CTFFIND4: Fast and accurate defocus estimation from electron micrographs
Rohou, A., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.008 · Cited by 4,913
Recognition of the polyubiquitin proteolytic signal
Thrower, J. S. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,716
Watts, G. D. J., Wymer, J., Kovach, M. J., Mehta, S. G., Mumm, S., Darvish, D., Pestronk, A., Whyte, M. P., & Kimonis, V. E. (2004) · Nature Genetics · doi:10.1038/ng1332 · Cited by 1,391
Exome Sequencing Reveals VCP Mutations as a Cause of Familial ALS
Johnson, J. O., Mandrioli, J., Benatar, M., Abramzon, Y., Van Deerlin, V. M., Trojanowski, J. Q., Gibbs, J. R., Brunetti, M., Gronka, S., Wuu, J., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.036 · Cited by 1,235
Ultrasensitive proteome analysis using paramagnetic bead technology
Hughes, C. S., Foehr, S., Garfield, D. A., Furlong, E. E., Steinmetz, L. M., & Krijgsveld, J. (2014) · Molecular Systems Biology · doi:10.15252/msb.20145625 · Cited by 1,225
Cited by
An expanded lexicon for the ubiquitin code
Dikic, I., & Schulman, B. A. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00543-1 · Cited by 417
The overlapping genetics of amyotrophic lateral sclerosis and frontotemporal dementia
Abramzon, Y. A., Fratta, P., Traynor, B. J., & Chia, R. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00042 · Cited by 244
Mechanisms of substrate recognition by the 26S proteasome
Davis, C., Spaller, B. L., & Matouschek, A. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.010 · Cited by 66
Chu, S., Xie, X., Payan, C., & Stochaj, U. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00639-y · Cited by 58
Multiple UBX proteins reduce the ubiquitin threshold of the mammalian p97-UFD1-NPL4 unfoldase
Fujisawa, R., Polo Rivera, C., & Labib, K. P. (2022) · eLife · doi:10.7554/elife.76763 · Cited by 37
Metadata
- Authors
- Twomey, E. C., Ji, Z., Wales, T. E., Bodnar, N. O., Ficarro, S. B., Marto, J. A., Engen, J. R., & Rapoport, T. A.
- Venue
- Science
- Published
- 2019-08-02
- Volume
- 365
- Issue
- 6452
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2953968681
- Cited by
- 292
- References
- 63
- FWCI
- 11.17
- Type
- journal article
- Language
- en
- Open access
- green
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding. https://app.cochat.ai/papers/10.1126/science.aax1033
- The paper
- Twomey, E. C., Ji, Z., Wales, T. E., Bodnar, N. O., Ficarro, S. B., Marto, J. A., Engen, J. R., & Rapoport, T. A. (2019). Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding. Science. https://doi.org/10.1126/science.aax1033
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.
