Evidence map›Paper›PMID 16680451›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2006

Superoxide dismutase 1 modulates expression of transferrin receptor.

Ruth Danzeisen, Tilmann Achsel, Ulrich Bederke, Mauro Cozzolino, Claudia Crosio, Alberto Ferri, Malte Frenzel, Edith Butler Gralla, Lea Huber, Albert Ludolph and 4 more

Registry-linked trialOpen access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT02164253 (Feasibility and Safety Pilot Therapeutic Study of the Iron Chelator Deferiprone in Amyotrophic Lateral Sclerosis), which is not on this map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.9field-weighted citation impact, top 10% 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.

NCT02164253 phase2completednot on this mapstarted 2013, after this paper: background citation

Feasibility and Safety Pilot Therapeutic Study of the Iron Chelator Deferiprone in Amyotrophic Lateral Sclerosis

TypeinterventionalSponsorUniversity Hospital, LilleRan2013 to 2016Enrolled23ConditionsALS (Amyotrophic Lateral Sclerosis), Iron OverloadArmsDeferiprone
3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  3. Review
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  8. Review
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  12. Flightless flies: Drosophila models of neuromuscular disease.Annals of the New York Academy of Sciences · 2010
    Review
  13. Article
  14. Dysregulation of iron homeostasis in the CNS contributes to disease progression in a mouse model of amyotrophic lateral sclerosis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  15. Article
  16. 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

14 authors at 6 institutions in 3 countries.

Ruth DanzeisenDepartment of Neurology, University of Ulm, Ulm, Germany.
Tilmann Achsel
Ulrich Bederke
Mauro Cozzolino
Claudia Crosio
Alberto Ferri
Malte Frenzel
Edith Butler Gralla
Lea Huber
Albert Ludolph
Monica Nencini
Giuseppe Rotilio
Joan Selverstone Valentine
Maria Teresa Carrì
Universität Ulm · DEFondazione Santa Lucia · ITIstituti di Ricovero e Cura a Carattere Scientifico · ITUniversity of California, Los Angeles · USUniversity of Rome Tor Vergata · ITUniversity of Sassari · IT

Funding

FUNCTIONAL STUDIES OF CYTOSOLIC ANTIOXIDANT PROTEINSR01DK046828 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI VALENTINE, JOAN SELVERSTONE · 1993 to 2010
$3.0M
NIDDK NIH HHS DK46828
6 · The paper itself

Abstract

Copper-zinc superoxide dismutase (SOD1) plays a protective role against the toxicity of superoxide, and studies in Saccharomyces cerevisiae and in Drosophila have suggested an additional role for SOD1 in iron metabolism. We have studied the effect of the modulation of SOD1 levels on iron metabolism in a cultured human glial cell line and in a mouse motoneuronal cell line. We observed that levels of the transferrin receptor and the iron regulatory protein 1 were modulated in response to altered intracellular levels of superoxide dismutase activity, carried either by wild-type SOD1 or by an SOD-active amyotrophic lateral sclerosis (ALS) mutant enzyme, G93A-SOD1, but not by a superoxide dismutase inactive ALS mutant, H46R-SOD1. Ferritin expression was also increased by wild-type SOD1 overexpression, but not by mutant SOD1s. We propose that changes in superoxide levels due to alteration of SOD1 activity affect iron metabolism in glial and neuronal cells from higher eukaryotes and that this may be relevant to diseases of the nervous system.

Indexed as

ActinsAnimalsBlotting, WesternCell LineCell Line, TumorFerritinsHumansMiceMutationProtein BiosynthesisReceptors, TransferrinRNA InterferenceSuperoxide DismutaseSuperoxide Dismutase-1TransfectionActinsFerritinsReceptors, TransferrinSOD1 protein, humanSod1 protein, mouseSuperoxide DismutaseSuperoxide Dismutase-1

Identifiers

PMID16680451
OpenAlexW1981215411

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.