ArticleBiochemistry2020
Comparison of Cross-Regulation by Different OTUB1:E2 Complexes.
Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 9 citations in OpenAlex.
- Discovery of New OTUB1 Covalent Ligands via Structure-Activity Relationship Studies for Targeted Protein Stabilization.Journal of medicinal chemistry · 2026Article
- An intrinsically disordered region of Ubp10 regulates its binding and activity on ubiquitinated histone substrates.Protein science : a publication of the Protein Society · 2025Article
- Deubiquitinase-Targeting Chimeras (DUBTACs) as a Potential Paradigm-Shifting Drug Discovery Approach.Journal of medicinal chemistry · 2025Review
- Noncanonical and reversible cysteine ubiquitination prevents the overubiquitination of PEX5 at the peroxisomal membrane.PLoS biology · 2024Article
- Circular RNAs in ferroptosis: regulation mechanism and potential clinical application in disease.Frontiers in pharmacology · 2023Review
- Deubiquitinase-targeting chimeras for targeted protein stabilization.Nature chemical biology · 2022Article
- The Deubiquitinase OTUB1 Is a Key Regulator of Energy Metabolism.International journal of molecular sciences · 2022Article
- Modulation of Ubiquitin Signaling in Innate Immune Response by Herpesviruses.International journal of molecular sciences · 2022Review
- The UBE2D ubiquitin conjugating enzymes: Potential regulatory hubs in development, disease and evolution.Frontiers in cell and developmental biology · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
OTUB1 is a highly expressed cysteine protease that specifically cleaves K48-linked polyubiquitin chains. This unique deubiquitinating enzyme (DUB) can bind to a subset of E2 ubiquitin conjugating enzymes, forming complexes in which the two enzymes can regulate one another's activity. OTUB1 can noncatalytically suppress the ubiquitin conjugating activity of its E2 partners by sequestering the charged E2∼Ub thioester and preventing ubiquitin transfer. The same E2 enzymes, when uncharged, can stimulate the DUB activity of OTUB1
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.