Evidence map›Paper›PMID 23177986›Full record

ReviewCurrent topics in membranes2012

H(+)-coupled divalent metal-ion transporter-1: functional properties, physiological roles and therapeutics.

Ali Shawki, Patrick B Knight, Bryan D Maliken, Eric J Niespodzany, Bryan Mackenzie

Abstract readReview
In one paragraph

Review in Current topics in membranes, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
16.5field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Dietary Iron Absorption: Biochemical and Nutritional Aspects.Advances in experimental medicine and biology · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The Endolysosomal Transporter DMT1 is Required for Morphine Regulation of Neuronal Ferritin Heavy Chain.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2023
    Article
  18. Article
  19. Review
  20. Review
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

5 authors at 1 institution in 1 country.

Ali ShawkiDepartment of Molecular & Cellular Physiology, University of Cincinnati College of Medicine, Cincinnati, Ohio, USA.
Patrick B Knight
Bryan D Maliken
Eric J Niespodzany
Bryan Mackenzie
University of Cincinnati Medical Center · US

Funding

Short Term Medical Student Training GrantT35DK060444 · NIDDK · UNIVERSITY OF CINCINNATI · PI JASON T BLACKARD · 2002 to 2026
$2.3M
Divalent metal-ion transporter DMT1 and its role in intestinal metal-ion uptakeR01DK080047 · NIDDK · UNIVERSITY OF CINCINNATI · PI MACKENZIE, BRYAN · 2008 to 2012
$1.5M
NIDDK NIH HHS DK060444NIDDK NIH HHS R01 DK080047NIDDK NIH HHS T35 DK060444
6 · The paper itself

Abstract

Divalent metal-ion transporter-1 (DMT1) is a widely expressed, iron-preferring membrane transport protein. Animal models establish that DMT1 plays indispensable roles in intestinal nonheme-iron absorption and iron acquisition by erythroid precursor cells. Rare mutations in human DMT1 result in severe microcytic-hypochromic anemia. When we express DMT1 in RNA-injected Xenopus oocytes, we observe rheogenic Fe(2+) transport that is driven by the proton electrochemical potential gradient. In that same preparation, DMT1 also transports cadmium and manganese but not copper. Whether manganese metabolism relies upon DMT1 remains unclear but DMT1 contributes to the effects of overexposure to cadmium and manganese in some tissues. There exist at least four DMT1 isoforms that arise from variant transcription of the SLC11A2 gene. Whereas these isoforms display identical functional properties, N- and C-terminal variations contain cues that direct the cell-specific targeting of DMT1 isoforms to discrete subcellular compartments (plasma membrane, endosomes, and lysosomes). An iron-responsive element (IRE) in the mRNA 3'-untranslated region permits the regulation of some isoforms by iron status, and additional mechanisms by which DMT1 is regulated are emerging. Natural-resistance-associated macrophage protein-1 (NRAMP1)-the only other member of the mammalian SLC11 gene family-contributes to antimicrobial function by extruding from the phagolysosome divalent metal ions (e.g. Mn(2+)) that may be essential cofactors for bacteria-derived enzymes or required for bacterial growth. The principal or only intestinal nonheme-iron transporter, DMT1 is a validated therapeutic target in hereditary hemochromatosis (HHC) and other iron-overload disorders.

Indexed as

AnimalsCation Transport ProteinsHemochromatosisHumansIronIron OverloadIron-Regulatory ProteinsManganeseModels, AnimalMutationRNA, MessengerSolute Carrier Family 11, Member 2Structure-Activity RelationshipXenopusCation Transport ProteinsIronIron-Regulatory ProteinsManganeseRNA, MessengerSolute Carrier Family 11, Member 2

Identifiers

PMID23177986
PMCPMC7027397
OpenAlexW103117919

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.