Evidence map›Paper›PMID 21640720›Full record

ArticleExperimental and molecular pathology2011

Delta-aminolevulinic dehydratase is a proteasome interacting protein.

Fawzia Bardag-Gorce, Samuel W French

Open access · greenAbstract read
In one paragraph

Article in Experimental and molecular pathology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
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  9. The Remarkable Character of Porphobilinogen Synthase.Accounts of chemical research · 2016
    Article
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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

2 authors at 1 institution in 1 country.

Fawzia Bardag-GorceHarbor UCLA Medical Center, Torrance, CA 90502, USA. fgorce@ucla.edu
Samuel W French
Harbor–UCLA Medical Center · US

Funding

PATHOGENESIS OF EXPERIMENTAL ALCOHOLIC LIVER DISEASER01AA008116 · NIAAA · UNIVERSITY OF OTTAWA · PI FRENCH, SAMUEL WILLIAM · 1990 to 2010
$2.9M
NIAAA NIH HHS R01 AA008116PHS HHS NIAAA8116
6 · The paper itself

Abstract

The proteasome interacts with a large number of proteins which regulate specific cellular functions. The focus of this study is to examine the proteasome interaction with Delta-aminolevulinate dehydratase (ALAD). ALAD is involved in the heme biosynthesis pathway and was co-isolated, with the 20S proteasome using several chromatographic purification steps. The MALDI-TOF mass spectrometry analysis identified this proteasome co-isolated protein as ALAD. When the proteasome was isolated using density-gradient centrifugation, ALAD was also found in the 26S proteasome fractions. It co-isolated with the 20S more than with the 26S proteasome. Furthermore, immunoprecipitated ALAD stained positive with antibodies to proteasome subunits. These results indicate that ALAD might interact with the proteasome. It is possible that ALAD is involved in modulating proteasome activity. When purified proteasomes were incubated with ALAD it was found that ALAD changes proteasome activity in a dose dependent manner. This indicates that ALAD may play a significant role in regulating proteasome activity. The data supports the hypothesis that ALAD, an important enzyme for heme synthesis, is also important as a proteasome interacting protein.

Indexed as

Amino Acid SequenceAnimalsChromatographyHumansImmunoprecipitationMiceMolecular Sequence DataPorphobilinogen SynthaseProteasome Endopeptidase ComplexRatsPorphobilinogen SynthaseProteasome Endopeptidase Complex

Identifiers

PMID21640720
PMCPMC3185203
OpenAlexW2087139038

What OpenQuestion holds

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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.