Evidence map›Paper›PMID 18790052›Full record

ReviewBiochimica et biophysica acta2008

The ubiquitin-proteasome system in spongiform degenerative disorders.

Brandi R Whatley, Lian Li, Lih-Shen Chin

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

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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.

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

Funding

Pathogenic Mechanisms of Environmental Toxicants in Parkinson's DiseaseR01ES015813 · NIEHS · EMORY UNIVERSITY · PI LI, LIAN · 2008 to 2012
$1.7M
Characterization of a neuronal ubiquitination machineryR01NS047199 · NINDS · EMORY UNIVERSITY · PI LI, LIAN · 2004 to 2008
$1.7M
Molecular analysis of DJ-1 function and dysfunctionR01NS050650 · NINDS · EMORY UNIVERSITY · PI CHIN, LIH-SHEN · 2006 to 2010
$1.7M
Mechanisms of Endosome-to-Lysosome Trafficking in BrainR01NS047575 · NINDS · EMORY UNIVERSITY · PI LI, LIAN · 2004 to 2007
$1.1M
A novel E3 ligase in modulation of mitochondrial function and neurodegenerationF31NS055468 · NINDS · EMORY UNIVERSITY · PI WHATLEY, BRANDI R · 2007 to 2008
$52k
NIEHS NIH HHS ES015813NIEHS NIH HHS R01 ES015813NINDS NIH HHS F31 NS055468NINDS NIH HHS NS047199NINDS NIH HHS NS047575NINDS NIH HHS NS050650NINDS NIH HHS NS055468NINDS NIH HHS R01 NS047199NINDS NIH HHS R01 NS047575NINDS NIH HHS R01 NS050650
6 · The paper itself

Abstract

Spongiform degeneration is characterized by vacuolation in nervous tissue accompanied by neuronal death and gliosis. Although spongiform degeneration is a hallmark of prion diseases, this pathology is also present in the brains of patients suffering from Alzheimer's disease, diffuse Lewy body disease, human immunodeficiency virus (HIV) infection, and Canavan's spongiform leukodystrophy. The shared outcome of spongiform degeneration in these diverse diseases suggests that common cellular mechanisms must underlie the processes of spongiform change and neurodegeneration in the central nervous system. Immunohistochemical analysis of brain tissues reveals increased ubiquitin immunoreactivity in and around areas of spongiform change, suggesting the involvement of ubiquitin-proteasome system dysfunction in the pathogenesis of spongiform neurodegeneration. The link between aberrant ubiquitination and spongiform neurodegeneration has been strengthened by the discovery that a null mutation in the E3 ubiquitin-protein ligase mahogunin ring finger-1 (Mgrn1) causes an autosomal recessively inherited form of spongiform neurodegeneration in animals. Recent studies have begun to suggest that abnormal ubiquitination may alter intracellular signaling and cell functions via proteasome-dependent and proteasome-independent mechanisms, leading to spongiform degeneration and neuronal cell death. Further elucidation of the pathogenic pathways involved in spongiform neurodegeneration should facilitate the development of novel rational therapies for treating prion diseases, HIV infection, and other spongiform degenerative disorders.

Indexed as

AnimalsHumansNeurodegenerative DiseasesPrion DiseasesProteasome Endopeptidase ComplexUbiquitinProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID18790052
PMCPMC2612938
OpenAlexW2129661920

What OpenQuestion holds

Textmetadata
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.