Evidence map›Paper›PMID 20637515›Full record

ReviewTrends in biotechnology2010

Genome-wide approaches to systematically identify substrates of the ubiquitin-proteasome pathway.

Chang Liu, Vitnary Choe, Hai Rao

Abstract readReview
In one paragraph

Review in Trends in biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

6 citing papers in PubMed, 7 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.

Chang LiuInstitute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245, USA.
Vitnary Choe
Hai Rao
The University of Texas Health Science Center at San Antonio · US

Funding

Targeting ubiquitylated proteins to the proteasomeR01GM078085 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI RAO, HAI · 2007 to 2011
$1.3M
NIGMS NIH HHS GM 078085NIGMS NIH HHS R01 GM078085
6 · The paper itself

Abstract

The ubiquitin-proteasome system handles the majority of controlled proteolysis in eukaryotes. Defects in the ubiquitin-proteasome system have been implicated in diseases ranging from cancers to neurodegenerative disorders. However, the precise role of ubiquitin-proteasome-mediated degradation in health and disease is far from clear. A major challenge is to link specific substrates directly to a particular degradation pathway. Here, we review genome-wide approaches that have been developed in recent years to comprehensively identify ubiquitylated substrates of a particular pathway. Components of the ubiquitin-proteasome system are attractive drug targets, as illustrated by the efficacy of some proteasome inhibitors in the treatment of multiple myeloma. Information that has emerged from these studies could reveal novel drug targets and strategies for treating human diseases.

Indexed as

Fungal ProteinsGenomicsHumansMetabolic Networks and PathwaysProteasome Endopeptidase ComplexProtein BindingUbiquitin-Protein Ligase ComplexesFungal ProteinsProteasome Endopeptidase ComplexUbiquitin-Protein Ligase Complexes

Identifiers

PMID20637515
PMCPMC2926183
OpenAlexW2069787719

What OpenQuestion holds

Textmetadata
LicenceTDM
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.