The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
Open accessAbstract
The highly conserved AAA ATPase Cdc48/p97 acts on ubiquitylated substrate proteins in cellular processes as diverse as the fusion of homotypic membranes and the degradation of misfolded proteins. The 'Ubiquitin regulatory X' (UBX) domain-containing proteins constitute the so far largest family of Cdc48/p97 cofactors. UBX proteins are involved in substrate recruitment to Cdc48/p97 and in the temporal and spatial regulation of its activity. In combination with UBX-like proteins and other cofactors, they can assemble into a large variety of Cdc48/p97-cofactor complexes possessing distinct cellular functions. This review gives an overview of the different subfamilies of UBX proteins and their functions, and discusses general principles of Cdc48/p97 regulation by these cofactors.
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
The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
Ye, Y., Meyer, H. H., & Rapoport, T. A. (2001) · Nature · doi:10.1038/414652a · Cited by 1,099
Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin
Ramadan, K., Bruderer, R., Spiga, F. M., Popp, O., Baur, T., Gotta, M., & Meyer, H. H. (2007) · Nature · doi:10.1038/nature06388 · Cited by 261
SVIP is a novel VCP/p97-interacting protein whose expression causes cell vacuolation
Nagahama, M., Suzuki, M., Hamada, Y., Hatsuzawa, K., Tani, K., Yamamoto, A., & Tagaya, M. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.02-07-0115 · Cited by 95
Cited by
The emerging complexity of protein ubiquitination
Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821
Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease
Ju, J.-S., Fuentealba, R. A., Miller, S. E., Jackson, E., Piwnica-Worms, D., Baloh, R. H., & Weihl, C. C. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200908115 · Cited by 494
Ubiquitin and membrane protein turnover: from cradle to grave
MacGurn, J. A., Hsu, P.-C., & Emr, S. D. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060210-093619 · Cited by 287
Regulation of Glucose Transporter Translocation in Health and Diabetes
Bogan, J. S. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060109-094246 · Cited by 279
Altun, M., Besche, H. C., Overkleeft, H. S., Piccirillo, R., Edelmann, M. J., Kessler, B. M., Goldberg, A. L., & Ulfhake, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.129718 · Cited by 226
Ritz, D., Vuk, M., Kirchner, P., Bug, M., Schütz, S., Hayer, A., Bremer, S., Lusk, C., Baloh, R. H., Lee, H., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2301 · Cited by 224
Cdc48/p97 mediates UV-dependent turnover of RNA Pol II
Verma, R., Oania, R., Fang, R., Smith, G. T., & Deshaies, R. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.017 · Cited by 196
Lipid droplets as signaling platforms linking metabolic and cellular functions
Arrese, E. L., Saudale, F. Z., & Soulages, J. L. (2014) · Lipid Insights · doi:10.4137/lpi.s11128 · Cited by 54
Rezvani, K., Teng, Y., Pan, Y., Dani, J. A., Lindstrom, J., García Gras, E. A., McIntosh, J. M., & De Biasi, M. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.4723-08.2009 · Cited by 46
Cayli, S., Klug, J., Chapiro, J., Fröhlich, S., Krasteva, G., Orel, L., & Meinhardt, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.037952 · Cited by 31
Veronese, M., Kallabis, S., Kaczmarek, A. T., Das, A., Robers, L., Schumacher, S., Lofrano, A., Brodesser, S., Müller, S., Hofmann, K., et al. (2024) · Life Science Alliance · doi:10.26508/lsa.202402620 · Cited by 8
Metadata
- Authors
- Schuberth, C., & Buchberger, A.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2008-04-26
- Volume
- 65
- Issue
- 15
- Pages
- 2360-2371
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- OpenAlex
- W2011325147
- Cited by
- 277
- References
- 3
- FWCI
- 9.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
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
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.