ReviewBioEssays : news and reviews in molecular, cellular and developmental biology2025
Ubiquitin C-Terminal Hydrolase L1 (UCHL1), Beyond Hydrolysis.
Review in BioEssays : news and reviews in molecular, cellular and developmental biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Tied to Work: Topologically Knotted SPOUT Methyltransferases and UCH Deubiquitinases in Cellular Biochemistry.Journal of cellular biochemistry · 2026Review
- UCH-L1 in Alzheimer's Disease: A Crucial Player in Dementia-Associated Mechanisms.International journal of molecular sciences · 2025Review
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.
Funding
Abstract
Ubiquitin C-terminal hydrolase L1 (UCHL1) is a component of the ubiquitin-proteasome system (UPS) linked to neurodegeneration. Despite its exceptionally high abundance in neurons, UCHL1's precise role remains unclear. This review critically examines the proposed functions of UCHL1 and the challenges to understanding its role in neuronal cells. While UCHL1 hydrolyzes small adducts from the C-terminus of ubiquitin, its occluded active site limits the range of possible substrates and restricts its activity as an efficient deubiquitinase (DUB). These constraints, alongside the paucity of identified substrates, challenge the centrality of this proposed role. We also explore the potential of UCHL1 acting as a ubiquitin ligase and its nonenzymatic role in stabilizing mono-ubiquitin by preventing its lysosomal degradation. By highlighting the unresolved complexities surrounding UCHL1, this perspective proposes several approaches to elucidate UCHL1's significance in the brain.
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.