The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Ubiquitin: structures, functions, mechanisms
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Cites
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HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
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“This proposal was confirmed by structures of a hydroxylated HIF-1a peptide bound to VHL [130,131].”
BackgroundInfluentialIn Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
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A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., & Varshavsky, A. (1989) · Science · doi:10.1126/science.2538923 · Cited by 1,535
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
Joazeiro, C. A. P., & Weissman, A. M. (2000) · Cell · doi:10.1016/s0092-8674(00)00077-5 · Cited by 1,249
Molecular dissection of autophagy: two ubiquitin-like systems
Ohsumi, Y. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056522 · Cited by 1,240 · cited 2×
“(The only known exceptions are Atg8 and Atg12, which share the same E1 [15].”
BackgroundInteraction of the Fanconi Anemia Proteins and BRCA1 in a Common Pathway
Garcia-Higuera, I., Taniguchi, T., Ganesan, S., Meyn, M. S., Timmers, C., Hejna, J., Grompe, M., & D'Andrea, A. D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00173-3 · Cited by 1,198
Masson, N., Willam, C., Maxwell, P. H., Pugh, C. W., & Ratcliffe, P. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5197 · Cited by 1,014 · cited 10×
“This proposal was confirmed by structures of a hydroxylated HIF-1a peptide bound to VHL [130,131].”
BackgroundInfluentialHIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation
Yu, F., White, S. B., Zhao, Q., & Lee, F. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181341498 · Cited by 796
Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL
Hon, W.-C., Wilson, M. I., Harlos, K., Claridge, T. D. W., Schofield, C. J., Pugh, C. W., Maxwell, P. H., Ratcliffe, P. J., Stuart, D. I., & Jones, E. Y. (2002) · Nature · doi:10.1038/nature00767 · Cited by 751
CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
Petrucelli, L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh083 · Cited by 723 · cited 1×
“CHIP substrates that conform to this paradigm include the cystic fibrosis transmembrane receptor [112], the glucocorticoid receptor [113], and tau [114,115].”
BackgroundRegulation and Destabilization of HIF-1α by ARD1-Mediated Acetylation
Jeong, J.-W., Bae, M.-K., Ahn, M.-Y., Kim, S.-H., Sohn, T.-K., Bae, M.-H., Yoo, M.-A., Song, E. J., Lee, K.-J., & Kim, K.-W. (2002) · Cell · doi:10.1016/s0092-8674(02)01085-1 · Cited by 716
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Inhibition of HIF2α Is Sufficient to Suppress pVHL-Defective Tumor Growth
Kondo, K., Kim, W. Y., Lechpammer, M., & Kaelin, W. G. (2003) · PLoS Biology · doi:10.1371/journal.pbio.0000083 · Cited by 611
Cited by
A genomic and functional inventory of deubiquitinating enzymes.
Nijman, S. M. B., Luna-Vargas, M. P. A., Velds, A., Brummelkamp, T. R., Dirac, A. M. G., Sixma, T. K., & Bernards, R. (2005) · Cell · doi:10.1016/j.cell.2005.11.007 · Cited by 1,854
Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.
Reyes-Turcu, F. E., Ventii, K. H., & Wilkinson, K. D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.082307.091526 · Cited by 1,396
Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling
Mukhopadhyay, D., & Riezman, H. (2007) · Science · doi:10.1126/science.1127085 · Cited by 1,221
Structural insights into the catalysis and regulation of E3 ubiquitin ligases
Buetow, L., & Huang, D. T. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.91 · Cited by 679
RETRACTED: hnRNP K: An HDM2 Target and Transcriptional Coactivator of p53 in Response to DNA Damage
Moumen, A., Masterson, P., O'Connor, M. J., & Jackson, S. P. (2005) · Cell · doi:10.1016/j.cell.2005.09.032 · Cited by 350
Retracted
Metadata
- Authors
- Pickart, C. M., & Eddins, M. J.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2004-11
- Volume
- 1695
- Issue
- 1-3
- Pages
- 55-72
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2166440816
- Cited by
- 1,407
- References
- 16
- FWCI
- 17.71
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
