ArticleStructure (London, England : 1993)2020
Getting Close: Insight into the Structure and Function of K11/K48-Branched Ubiquitin Chains.
Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed.
- Ubiquitin-Modifying Enzymes as Cell-Fate Regulators in Intestinal Inflammation.International journal of biological sciences · 2026Review
- The Ubiquitin Script: writing protein fates in chains.Essays in biochemistry · 2025Review
- Modulation of the tumor microenvironment by the ubiquitin-proteasome system in colorectal cancer.Journal of translational medicine · 2025Review
- USP39 at the crossroads of cancer immunity: regulating immune evasion and immunotherapy response through RNA splicing and ubiquitin signaling.Frontiers in immunology · 2025Review
- Autophagy/Mitophagy Regulated by Ubiquitination: A Promising Pathway in Cancer Therapeutics.Cancers · 2023Review
- Role of circRNA in E3 Modification under Human Disease.Biomolecules · 2022Review
- Post-translational modifications on the retinoblastoma protein.Journal of biomedical science · 2022Review
- Deubiquitinase PSMD14 promotes ovarian cancer progression by decreasing enzymatic activity of PKM2.Molecular oncology · 2021Article
- Review
- The role of ubiquitination and deubiquitination in cancer metabolism.Molecular cancer · 2020Review
Corrections and comments
- Comment on
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
K11/K48-branched ubiquitin chains are proteasomal priority signals that elicit the rapid elimination of mitotic regulators and aggregation-prone proteins. Indicative of an intriguing signaling mode, Boughton et al. (2019) unravel an interaction between distal subunits of K11/K48-branched ubiquitin trimers that could provide a combined surface for recognition by the proteasomal receptor RPN1.
Indexed as
Identifiers
31951536What 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.