The DOI matches its Crossref record; 21 of the 23 references it cites were found in a registry or an index.
Harnessing the Ubiquitination Machinery to Target the Degradation of Specific Cellular Proteins
Open accessAbstract
The functional characterization of a specific gene, or its protein product, often relies on assessing the consequences of its elimination, usually accomplished by gene knockout, ribozyme, antisense, or RNA-mediated interference (RNAi) technologies. The selective degradation of cellular proteins is mediated primarily by the ubiquitin-proteasome pathway. Manipulation of the ubiquitin-dependent proteolytic machinery to eliminate specific gene products at the protein level has been previously attempted with some success in vitro; however, the in vivo efficacy of this approach has not yet been achieved. Here we report successful engineering of the substrate receptor of a major ubiquitin-proteolytic machinery to direct the degradation of otherwise stable cellular proteins both in yeast and in mammalian cells.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“Zhou et al.210 described some of the earliest chimeric bioPROTACs, including a fusion consisting of full-length β-TRCP protein and an N-terminal peptide of the E7 protein of human papillomavirus type 16 (HPV-16) that degraded retinoblastoma protein (RB1) in a human osteosarcoma cell line.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [210]
In the citing paper
“These studies demonstrated that the SCF E3 ligase could be redirected to degrade non-SCF targets.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [210]
Citations
Cites
A simplified system for generating recombinant adenoviruses
He, T., Zhou, S., da Costa, L. T., Yu, J., Kinzler, K. W., & Vogelstein, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2509 · Cited by 3,209
The human papilloma virus-16 E7-oncoprotein is able to bind to the retinoblastoma gene product
Dyson, N., Howley, P. M., Münger, K., & Harlow, E. (1989) · Science · doi:10.1126/science.2537532 · Cited by 3,017
Self-citationUBIQUITIN-DEPENDENT PROTEIN DEGRADATION
Hochstrasser, M. (1996) · Annual Review of Genetics · doi:10.1146/annurev.genet.30.1.405 · Cited by 1,706
Bai, C., Sen, P., Hofmann, K., Ma, L., Goebl, M. G., Harper, J. W., & Elledge, S. J. (1996) · Cell · doi:10.1016/s0092-8674(00)80098-7 · Cited by 1,421
SCF and Cullin/RING H2-Based Ubiquitin Ligases
Deshaies, R. J. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.435 · Cited by 1,238
Münger, K., Werness, B. A., Dyson, N. J., Phelps, W. C., Harlow, E. E., & Howley, P. M. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08594.x · Cited by 1,204
Self-citationRegulation of retinoblastoma protein functions by ectopic expression of human cyclins
Hinds, P. W., Mittnacht, S., Dulić, V., Arnold, A., Reed, S. I., & Weinberg, R. A. (1992) · Cell · doi:10.1016/0092-8674(92)90249-c · Cited by 998
Feldman, R. M. R., Correll, C. C., Kaplan, K. B., & Deshaies, R. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80404-3 · Cited by 820
CDC20 and CDH1 : A Family of Substrate-Specific Activators of APC-Dependent Proteolysis
Visintin, R., Prinz, S., & Amon, A. (1997) · Science · doi:10.1126/science.278.5337.460 · Cited by 812
Margottin-Goguet, F., Bour, S. P., Durand, H., Selig, L., Bénichou, S., Richard, V., Thomas, D., Strebel, K., & Bénarous, R. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80056-8 · Cited by 670
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
Sakamoto, K. M., Kim, K. B., Kumagai, A., Mercurio, F., Crews, C. M., & Deshaies, R. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141230798 · Cited by 2,609
An auxin-based degron system for the rapid depletion of proteins in nonplant cells
Nishimura, K., Fukagawa, T., Takisawa, H., Kakimoto, T., & Kanemaki, M. (2009) · Nature Methods · doi:10.1038/nmeth.1401 · Cited by 1,663
Themes and variations on ubiquitylation
Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,507
Drug discovery in the ubiquitin–proteasome system
Nalepa, G., Rolfe, M., & Harper, J. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2056 · Cited by 635
Metadata
- Authors
- Zhou, P., Bogacki, R., McReynolds, L., & Howley, P. M.
- Affiliations
- Harvard University (US)
- Corresponding author
- Zhou, Pengbo
- Howley, Peter M.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2000-09
- Volume
- 6
- Issue
- 3
- Pages
- 751-756
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2034414781
- Cited by
- 164
- References
- 23
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 7 · 2023: 9 · 2022: 8 · 2021: 3 · 2020: 8 · 2019: 6 · 2018: 5 · 2017: 5 · 2016: 7 · 2015: 6 · 2014: 9 · 2013: 6 · 2012: 2
- FWCI
- 2.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R01CA064888, R01-CA64888-06)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- ubiquitination, protein degradation, ubiquitin-proteasome system, selective protein degradation, proteasome, RNA interference, yeast, mammalian cells
- MeSH terms
- F-Box-WD Repeat-Containing Protein 7, Animals, Uterine Cervical Neoplasms, Female, Humans, Ligases, Mammals, Molecular Biology, Nuclear Proteins, Plasmids, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Osteosarcoma, Substrate Specificity, Tumor Cells, Cultured, Ubiquitins, Gene Expression Regulation, Enzymologic, Retinoblastoma Protein, Cell Cycle Proteins, GTP-Binding Proteins, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligases, F-Box Proteins, beta-Transducin Repeat-Containing Proteins, Retinoblastoma-Like Protein p107
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
