Evidence map›Paper›PMID 24728987›Full record

ArticleNucleic acids research2014

Rapid kinetics of iron responsive element (IRE) RNA/iron regulatory protein 1 and IRE-RNA/eIF4F complexes respond differently to metal ions.

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

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

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  10. Approaches for measuring the dynamics of RNA-protein interactions.Wiley interdisciplinary reviews. RNA · 2020
    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

6 authors at 4 institutions in 1 country.

Mateen A KhanDepartment of Chemistry and Biochemistry, Hunter College, City University of New York, New York, NY 10065, USA.
Jia MaDepartment of Chemistry and Biochemistry, Hunter College, City University of New York, New York, NY 10065, USA.
William E WaldenDepartment of Microbiology and Immunology, University of Illinois at Chicago, Chicago, IL 60612-7334, USA.
William C MerrickDepartment of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Elizabeth C TheilChilderen's Hospital Oakland Research Institute, Oakland, CA 94609, USA.
Dixie J GossDepartment of Chemistry and Biochemistry, Hunter College, City University of New York, New York, NY 10065, USA dgoss@hunter.cuny.edu.
City University of New York · USCase Western Reserve University · USHunter College · 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 DK47281
6 · The paper itself

Abstract

Metal ion binding was previously shown to destabilize IRE-RNA/IRP1 equilibria and enhanced IRE-RNA/eIF4F equilibria. In order to understand the relative importance of kinetics and stability, we now report rapid rates of protein/RNA complex assembly and dissociation for two IRE-RNAs with IRP1, and quantitatively different metal ion response kinetics that coincide with the different iron responses in vivo. kon, for FRT IRE-RNA binding to IRP1 was eight times faster than ACO2 IRE-RNA. Mn(2+) decreased kon and increased koff for IRP1 binding to both FRT and ACO2 IRE-RNA, with a larger effect for FRT IRE-RNA. In order to further understand IRE-mRNA regulation in terms of kinetics and stability, eIF4F kinetics with FRT IRE-RNA were determined. kon for eIF4F binding to FRT IRE-RNA in the absence of metal ions was 5-times slower than the IRP1 binding to FRT IRE-RNA. Mn(2+) increased the association rate for eIF4F binding to FRT IRE-RNA, so that at 50 µM Mn(2+) eIF4F bound more than 3-times faster than IRP1. IRP1/IRE-RNA complex has a much shorter life-time than the eIF4F/IRE-RNA complex, which suggests that both rate of assembly and stability of the complexes are important, and that allows this regulatory system to respond rapidly to change in cellular iron.

Indexed as

Regulatory Sequences, Ribonucleic AcidAconitate HydrataseAnimalsEukaryotic Initiation Factor-4FFerritinsIronIron Regulatory Protein 1KineticsManganesePotassiumRabbitsRNA, MessengerAconitate HydrataseEukaryotic Initiation Factor-4FFerritinsIronIron Regulatory Protein 1ManganesePotassiumRegulatory Sequences, Ribonucleic AcidRNA, Messenger

Identifiers

PMID24728987
PMCPMC4041422
OpenAlexW2164220737

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.