Evidence map›Paper›PMID 27515257›Full record

ReviewThe Biochemical journal2016

Ubiquitin C-terminal hydrolase L1 (UCH-L1): structure, distribution and roles in brain function and dysfunction.

Paul Bishop, Dan Rocca, Jeremy M Henley

Abstract readReview
In one paragraph

Review in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 180 papers, 5 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
180citing papers in PubMed, 5 pooled it
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

180 citing papers in PubMed, 5 syntheses or guidelines pooled it.

  1. Pooled it
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  6. Review
  7. Impact of routine use of the GFAP and UCH-L1 TBI blood test for management of mild TBI on patient care in a European emergency department.European journal of trauma and emergency surgery : official publication of the European Trauma Society · 2026
    Article
  8. Article
  9. Interpreting p-tau217 on the ward: frailty and plasma biomarkers in acutely admitted older adults.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
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  12. Tightly Knotted Enzymes Inhibit Protein-Protein Aggregation.bioRxiv : the preprint server for biology · 2026
    Article
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120 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Paul BishopSchool of Biochemistry, Centre for Synaptic Plasticity, Biomedical Sciences Building, University of Bristol, Bristol BS8 1TD, U.K.
Dan RoccaSchool of Biochemistry, Centre for Synaptic Plasticity, Biomedical Sciences Building, University of Bristol, Bristol BS8 1TD, U.K.
Jeremy M HenleySchool of Biochemistry, Centre for Synaptic Plasticity, Biomedical Sciences Building, University of Bristol, Bristol BS8 1TD, U.K. j.m.henley@bristol.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/K014358/1Biotechnology and Biological Sciences Research Council PG/14/60/31014British Heart Foundation PG/14/60/31014Medical Research Council MR/L003791/1
6 · The paper itself

Abstract

Ubiquitin C-terminal hydrolase L1 (UCH-L1) is an extremely abundant protein in the brain where, remarkably, it is estimated to make up 1-5% of total neuronal protein. Although it comprises only 223 amino acids it has one of the most complicated 3D knotted structures yet discovered. Beyond its expression in neurons UCH-L1 has only very limited expression in other healthy tissues but it is highly expressed in several forms of cancer. Although UCH-L1 is classed as a deubiquitinating enzyme (DUB) the direct functions of UCH-L1 remain enigmatic and a wide array of alternative functions has been proposed. UCH-L1 is not essential for neuronal development but it is absolutely required for the maintenance of axonal integrity and UCH-L1 dysfunction is implicated in neurodegenerative disease. Here we review the properties of UCH-L1, and how understanding its complex structure can provide new insights into its roles in neuronal function and pathology.

Indexed as

AnimalsBrainHumansHydrophobic and Hydrophilic InteractionsProtein ConformationUbiquitin ThiolesteraseUbiquitin ThiolesteraseUCHL1 protein, humanaxonneuritesubiquitin C-terminal hydrolase L1 (UCH-L1)ubiquitin ligasesubiquitin proteasome system

Identifiers

PMID27515257
PMCPMC4980807

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.