Evidence map›Paper›PMID 19720833›Full record

ArticleThe Journal of biological chemistry2009

Direct Fe2+ sensing by iron-responsive messenger RNA:repressor complexes weakens binding.

Mateen A Khan, William E Walden, Dixie J Goss, Elizabeth C Theil

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

23 citing papers in PubMed, 50 citations in OpenAlex.

  1. FeInternational journal of molecular sciences · 2025
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  8. Iron metabolism, ferroptosis, and lncRNA in cancer: knowns and unknowns.Journal of Zhejiang University. Science. B · 2022
    Review
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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

4 authors at 3 institutions in 1 country.

Mateen A KhanDepartment of Chemistry, Hunter College, City University of New York, New York, New York 10065, USA.
William E Walden
Dixie J Goss
Elizabeth C Theil
Hunter College · USUniversity of California, Berkeley · USUniversity of Illinois Chicago · US

Funding

RED CELL FERRITIN: ONTOGENETIC CONTROLR01DK020251 · NIDDK · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI GOSS, DIXIE J, THEIL, ELIZABETH C · 1986 to 2010
$5.1M
REGULATION OF IRON METABOLISM GENES IN EUKARYOTESR01DK047281 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI WALDEN, WILLIAM EDWARD · 1995 to 2010
$2.4M
Ferritin: Protein/mRNA/DNA in Fe/O Regulation/MetabolismR56DK020251 · NIDDK · CHILDREN'S HOSPITAL & RES CTR AT OAKLAND · PI GOSS, DIXIE J, THEIL, ELIZABETH C · 2008 to 2008
$120k
RED CELL FERRITIN MRNA AND PROTEIN-STRUCTURE/FUNCTIONR37DK020251 · NIDDK · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI THEIL, ELIZABETH C · 1987 to 1994
–
NIDDK NIH HHS DK20251NIDDK NIH HHS DK47281NIDDK NIH HHS R01 DK020251NIDDK NIH HHS R01 DK047281NIDDK NIH HHS R56 DK020251
6 · The paper itself

Abstract

Fe(2+) is now shown to weaken binding between ferritin and mitochondrial aconitase messenger RNA noncoding regulatory structures ((iron-responsive element) (IRE)-RNAs) and the regulatory proteins (IRPs), which adds a direct role of iron to regulation that can complement the well known regulatory protein modification and degradative pathways related to iron-induced mRNA translation. We observe that the K(d) value increases 17-fold in 5'-untranslated region IRE-RNA:repressor complexes; Fe(2+), is studied in the absence of O(2). Other metal ions, Mn(2+) and Mg(2+) have similar effects to Fe(2+) but the required Mg(2+) concentration is 100 times greater than for Fe(2+) or Mn(2+). Metal ions also weaken ethidium bromide binding to IRE-RNA with no effect on IRP fluorescence, using Mn(2+) as an O(2)-resistant surrogate for Fe(2+), indicating that metal ions bound IRE-RNA but not IRP: Fe(2+) decreases IRP repressor complex stability of ferritin IRE-RNA 5-10 times compared with 2-5 times for mitochondrial aconitase IRE-RNA, over the same concentration range, suggesting that differences among IRE-RNA structures contribute to the differences in the iron responses observed in vivo. The results show the IRE-RNA:repressor complex literally responds to Fe(2+), selectively for each IRE-mRNA.

Indexed as

Regulatory Sequences, Nucleic AcidAnimalsIronMagnesiumManganeseRabbitsRanidaeRepressor ProteinsResponse ElementsRNA, MessengerIronMagnesiumManganeseRepressor ProteinsRNA, Messenger

Identifiers

PMID19720833
PMCPMC2781567
OpenAlexW2150861947

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.