Evidence map›Paper›PMID 24881043›Full record

ReviewHaematologica2014

Heme and erythropoieis: more than a structural role.

Deborah Chiabrando, Sonia Mercurio, Emanuela Tolosano

Open access · goldAbstract readReview
In one paragraph

Review in Haematologica, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

99 citing papers in PubMed, 1 synthesis or guideline pooled it, 190 citations in OpenAlex.

  1. Pooled it
  2. Azacitidine, Venetoclax, and Magrolimab in Newly Diagnosed and Relapsed Refractory Acute Myeloid Leukemia: Phase Ib/II Study and Correlative Analysis.Clinical cancer research : an official journal of the American Association for Cancer Research · 2025
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  15. Modulation of Redox Metabolism, CD147, and CD47 Expression with the Maturation of Hematopoietic Stem Cells in Bone Marrow.Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion · 2025
    Article
  16. Article
  17. OATP1B1/1B3 deficiency exacerbates hyperbilirubinemia in erythropoietic protoporphyria.Drug metabolism and disposition: the biological fate of chemicals · 2025
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  18. Review
  19. Review
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39 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Deborah ChiabrandoDepartment of Molecular Biotechnology and Health Sciences and Molecular Biotechnology Center, University of Torino, Italy.
Sonia MercurioDepartment of Molecular Biotechnology and Health Sciences and Molecular Biotechnology Center, University of Torino, Italy.
Emanuela TolosanoDepartment of Molecular Biotechnology and Health Sciences and Molecular Biotechnology Center, University of Torino, Italy emanuela.tolosano@unito.it.
University of Turin · IT

Funding

Telethon GGP12082
6 · The paper itself

Abstract

Erythropoiesis is the biological process that consumes the highest amount of body iron for heme synthesis. Heme synthesis in erythroid cells is finely coordinated with that of alpha (α) and beta (β)-globin, resulting in the production of hemoglobin, a tetramer of 2α- and 2β-globin chains, and heme as the prosthetic group. Heme is not only the structural component of hemoglobin, but it plays multiple regulatory roles during the differentiation of erythroid precursors since it controls its own synthesis and regulates the expression of several erythroid-specific genes. Heme is synthesized in developing erythroid progenitors by the stage of proerythroblast, through a series of eight enzymatic reactions divided between mitochondria and cytosol. Defects of heme synthesis in the erythroid lineage result in sideroblastic anemias, characterized by microcytic anemia associated to mitochondrial iron overload, or in erythropoietic porphyrias, characterized by porphyrin deposition in erythroid cells. Here, we focus on the heme biosynthetic pathway and on human erythroid disorders due to defective heme synthesis. The regulatory role of heme during erythroid differentiation is discussed as well as the heme-mediated regulatory mechanisms that allow the orchestration of the adaptive cell response to heme deficiency.

Indexed as

AnimalsBiosynthetic PathwaysCell DifferentiationErythrocytesErythropoiesisGene Expression RegulationHematologic DiseasesHemeHumansMitochondriaHeme

Identifiers

PMID24881043
PMCPMC4040894
OpenAlexW2049116122

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.