ArticleProceedings of the National Academy of Sciences of the United States of America2005
Method for targeting protein destruction by using a ubiquitin-independent, proteasome-mediated degradation pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 47 citations in OpenAlex.
- Regulation of TRIB1 abundance in hepatocyte models in response to proteasome inhibition.Scientific reports · 2023Article
- Current Views on the Interplay between Tyrosine Kinases and Phosphatases in Chronic Myeloid Leukemia.Cancers · 2021Review
- Dynamical Modeling of Optogenetic Circuits in Yeast for Metabolic Engineering Applications.ACS synthetic biology · 2021Article
- A platform for post-translational spatiotemporal control of cellular proteins.Synthetic biology (Oxford, England) · 2021Article
- A Method for Conditional Regulation of Protein Stability in Native or Near-Native Form.Cell chemical biology · 2020Article
- Precision Control of CRISPR-Cas9 Using Small Molecules and Light.Biochemistry · 2019Review
- Article
- Article
- The Eyes Absent Proteins in Developmental and Pathological Angiogenesis.The American journal of pathology · 2016Article
- A safety catch for ornithine decarboxylase degradation.Microbial cell (Graz, Austria) · 2015Article
- Degron protease blockade sensor to image epigenetic histone protein methylation in cells and living animals.ACS chemical biology · 2015Article
- Crim1 maintains retinal vascular stability during development by regulating endothelial cell Vegfa autocrine signaling.Development (Cambridge, England) · 2014Article
- Roles for the ubiquitin-proteasome pathway in protein quality control and signaling in the retina: implications in the pathogenesis of age-related macular degeneration.Molecular aspects of medicine · 2012Review
- Targeted chemical-genetic regulation of protein stability in vivo.Chemistry & biology · 2012Article
- Ligand-switchable substrates for a ubiquitin-proteasome system.The Journal of biological chemistry · 2011Article
- Small-molecule displacement of a cryptic degron causes conditional protein degradation.Nature chemical biology · 2011Article
- Ubiquitin-proteasome pathway and cellular responses to oxidative stress.Free radical biology & medicine · 2011Review
- Targeted protein depletion in Saccharomyces cerevisiae by activation of a bidirectional degron.BMC systems biology · 2010Article
- Targeting proteins for degradation.Nature chemical biology · 2009Review
- In vivo imaging, tracking, and targeting of cancer stem cells.Journal of the National Cancer Institute · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
With the euchromatic portion of several mammalian genomes now sequenced, emphasis has turned to ascertaining the functions of gene products. A method for targeting destruction of selected proteins in mammalian cells is described, based on the ubiquitin-independent mechanism by which ornithine decarboxylase (ODC) is degraded by the 26S proteasome in collaboration with antizyme (AZ). We show that expressing whole proteins, protein domains, or peptide ligands fused to the N terminus of ODC promotes proteasome-dependent degradation of these chimeric fusion proteins and their interacting cellular target proteins. Moreover, the degradation of the interacting (targeted) protein depends on coexpression of AZ in about half of cases, providing an inducible switch for triggering the degradation process. By using 12 pairs of interacting proteins for testing, direct comparisons with several alternative strategies for achieving targeted protein destruction based on the concept of induced ubiquitination revealed advantages of the ODC/AZ system, which does not require posttranslational attachment of ubiquitin to target proteins. As proof of concept, the ODC/AZ system was used to ablate expression of specific endogenous proteins (e.g., TRAF6; Rb), and was shown to create the expected lesions in cellular pathways that require these proteins. Altogether, these findings reveal a strategy for achieving targeted destruction of cellular proteins, thus providing an additional tool for revealing the cellular phenotypes of gene products.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.