Evidence map›Paper›PMID 22811913›Full record

ArticleBiochemistry research international2012

Ubiquitin C-terminal hydrolase l1 in tumorigenesis.

Jennifer Hurst-Kennedy, Lih-Shen Chin, Lian Li

Open access · goldAbstract read
In one paragraph

Article in Biochemistry research international, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.1field-weighted citation impact, top 12% of its field
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

43 citing papers in PubMed, 77 citations in OpenAlex.

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  20. Deubiquitinase Activity Profiling Identifies UCHL1 as a Candidate Oncoprotein That Promotes TGFβ-Induced Breast Cancer Metastasis.Clinical cancer research : an official journal of the American Association for Cancer Research · 2020
    Article
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 at 1 institution in 1 country.

Jennifer Hurst-KennedyDepartment of Pharmacology and Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, GA 30322, USA.
Lih-Shen Chin
Lian Li
Emory University · US

Funding

IRACDA Fellowships in Research and Science Training (FIRST)K12GM000680 · NIGMS · EMORY UNIVERSITY · PI BROWN, LOU ANN S, MCCARTY, NAEL A · 2000 to 2024
$41.2M
Pathogenic Mechanisms of Environmental Toxicants in Parkinson's DiseaseR01ES015813 · NIEHS · EMORY UNIVERSITY · PI LI, LIAN · 2008 to 2012
$1.7M
Molecular analysis of DJ-1 function and dysfunctionR01NS050650 · NINDS · EMORY UNIVERSITY · PI CHIN, LIH-SHEN · 2006 to 2010
$1.7M
A Novel Ubiquitin-Dependent Pathogenic Pathway in Spongiform NeurodegenerationR01AG034126 · NIA · EMORY UNIVERSITY · PI CHIN, LIH-SHEN · 2009 to 2013
$1.5M
The PINK1 Mitochondrial Signaling PathwayR01GM082828 · NIGMS · EMORY UNIVERSITY · PI LI, LIAN · 2008 to 2011
$1.4M
NIA NIH HHS R01 AG034126NIEHS NIH HHS R01 ES015813NIGMS NIH HHS K12 GM000680NIGMS NIH HHS R01 GM082828NINDS NIH HHS R01 NS050650
6 · The paper itself

Abstract

Ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1, aka PGP9.5) is an abundant, neuronal deubiquitinating enzyme that has also been suggested to possess E3 ubiquitin-protein ligase activity and/or stabilize ubiquitin monomers in vivo. Recent evidence implicates dysregulation of UCH-L1 in the pathogenesis and progression of human cancers. Although typically only expressed in neurons, high levels of UCH-L1 have been found in many nonneuronal tumors, including breast, colorectal, and pancreatic carcinomas. UCH-L1 has also been implicated in the regulation of metastasis and cell growth during the progression of nonsmall cell lung carcinoma, colorectal cancer, and lymphoma. Together these studies suggest UCH-L1 has a potent oncogenic role and drives tumor development. Conversely, others have observed promoter methylation-mediated silencing of UCH-L1 in certain tumor subtypes, suggesting a potential tumor suppressor role for UCH-L1. In this paper, we provide an overview of the evidence supporting the involvement of UCH-L1 in tumor development and discuss the potential mechanisms of action of UCH-L1 in oncogenesis.

Identifiers

PMID22811913
PMCPMC3395355
OpenAlexW2145280442

What OpenQuestion holds

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LicenceCC BY
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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.