Evidence map›Paper›PMID 28316240›Full record

ArticleBiochemistry2017

Heme Gazing: Illuminating Eukaryotic Heme Trafficking, Dynamics, and Signaling with Fluorescent Heme Sensors.

David A Hanna, Osiris Martinez-Guzman, Amit R Reddi

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Key roles of GAPDH, Hsp90, and NO in heme trafficking.Journal of inorganic biochemistry · 2026
    Review
  9. An extended network for regulation of heme homeostasis in cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Mechanisms of heme transport in the mitochondria.Biochemical Society transactions · 2025
    Review
  12. Article
  13. Update on heme biosynthesis, tissue-specific regulation, heme transport, relation to iron metabolism and cellular energy.Liver international : official journal of the International Association for the Study of the Liver · 2024
    Review
  14. Fluorometric Methods to Measure Bioavailable and Total Heme.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  15. Applications of the Whole-Cell System in the Efficient Biosynthesis of Heme.International journal of molecular sciences · 2023
    Review
  16. Article
  17. Article
  18. Heme sensing and trafficking in fungi.Fungal biology reviews · 2023
    Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

David A HannaSchool of Chemistry and Biochemistry and Parker H. Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology , Atlanta, Georgia 30332, United States.
Osiris Martinez-GuzmanSchool of Chemistry and Biochemistry and Parker H. Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology , Atlanta, Georgia 30332, United States.
Amit R ReddiSchool of Chemistry and Biochemistry and Parker H. Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology , Atlanta, Georgia 30332, United States.ORCID 0000-0003-3952-404X
Georgia Institute of Technology · US

Funding

Imaging heme based mitochondrial-cell signaling networks in cell and animal modelR33ES025661 · NIEHS · GEORGIA INSTITUTE OF TECHNOLOGY · PI REDDI, AMIT RAM · 2017 to 2019
$1.7M
The Role of Cu/Zn Superoxide Dismutase (SOD1) in Redox SignalingR01GM118744 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI REDDI, AMIT RAM · 2016 to 2020
$1.6M
Imaging heme based mitochondrial-cell signaling networks in cell and animal models of heavy metal toxicityR21ES025661 · NIEHS · GEORGIA INSTITUTE OF TECHNOLOGY · PI REDDI, AMIT RAM · 2015 to 2016
$416k
NIEHS NIH HHS R21 ES025661NIEHS NIH HHS R33 ES025661NIGMS NIH HHS R01 GM118744
6 · The paper itself

Abstract

Heme (iron protoporphyrin IX) is an essential protein prosthetic group and signaling molecule required for most life on Earth. All heme-dependent processes require the dynamic and rapid mobilization of heme from sites of synthesis or uptake to hemoproteins present in virtually every subcellular compartment. The cytotoxicity and hydrophobicity of heme necessitate that heme mobilization be carefully controlled to mitigate the deleterious effects of this essential toxin. Indeed, a number of disorders, including certain cancers, cardiovascular diseases, and aging and age-related neurodegenerative diseases, are tied to defects in heme homeostasis. However, the molecules and mechanisms that mediate heme transport and trafficking, and the dynamics of these processes, are poorly understood. This is in large part due to the lack of physical tools for probing cellular heme. Herein, we discuss the recent development of fluorescent probes that can monitor and image kinetically labile heme with respect to its mobilization and role in signaling. In particular, we will highlight how heme gazing with these tools can uncover new heme trafficking factors upon being integrated with genetic screens and illuminate the concentration, subcellular distribution, and dynamics of labile heme in various physiological contexts. Altogether, the monitoring of labile heme, along with recent biochemical and cell biological studies demonstrating the reversible regulation of certain cellular processes by heme, is challenging us to reconceptualize heme from being a static cofactor buried in protein active sites to a dynamic and mobile signaling molecule.

Indexed as

Bacterial ProteinsBiological TransportCell LineCytochrome b GroupEscherichia coli ProteinsFluorescence Resonance Energy TransferFluorescent DyesGene ExpressionGenes, ReporterGreen Fluorescent ProteinsHemeHumansLuminescent ProteinsModels, MolecularMolecular ChaperonesProtein Structure, SecondaryBacterial Proteinscytochrome b562, E coliCytochrome b GroupEscherichia coli ProteinsFluorescent DyesGreen Fluorescent ProteinsHemeLuminescent ProteinsMolecular ChaperonesRecombinant Fusion Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID28316240
PMCPMC5629415
OpenAlexW2597299286

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.