Evidence map›Paper›PMID 29971218›Full record

ReviewFrontiers in cellular and infection microbiology2018

From Host Heme To Iron: The Expanding Spectrum of Heme Degrading Enzymes Used by Pathogenic Bacteria.

Kristin V Lyles, Zehava Eichenbaum

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cellular and infection microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

37 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Biochemical and functional characterization ofFrontiers in microbiology · 2026
    Article
  5. Key roles of GAPDH, Hsp90, and NO in heme trafficking.Journal of inorganic biochemistry · 2026
    Review
  6. Frontiers in microbiology · 2026
    Article
  7. Exploring the Terra incognita of AI-based domain classifications.Protein science : a publication of the Protein Society · 2025
    Article
  8. Review
  9. Article
  10. Heme alters biofilm formation inMicrobiology spectrum · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Endogenously produced HMicrobiology spectrum · 2024
    Article
  18. Review
  19. Review
  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

2 authors at 1 institution in 1 country.

Kristin V LylesBiology, Georgia State University, Atlanta, GA, United States.
Zehava EichenbaumBiology, Georgia State University, Atlanta, GA, United States.
Georgia State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Iron is an essential nutrient for many bacteria. Since the metal is highly sequestered in host tissues, bound predominantly to heme, pathogenic bacteria often take advantage of heme uptake and degradation mechanisms to acquire iron during infection. The most common mechanism of releasing iron from heme is through oxidative degradation by heme oxygenases (HOs). In addition, an increasing number of proteins that belong to two distinct structural families have been implicated in aerobic heme catabolism. Finally, an enzyme that degrades heme anaerobically was recently uncovered, further expanding the mechanisms for bacterial heme degradation. In this analysis, we cover the spectrum and recent advances in heme degradation by infectious bacteria. We briefly explain heme oxidation by the two groups of recognized HOs to ground readers before focusing on two new types of proteins that are reported to be involved in utilization of heme iron. We discuss the structure and enzymatic function of proteins representing these groups, their biological context, and how they are regulated to provide a more complete look at their cellular role.

Indexed as

BacteriaBacterial InfectionsBacterial ProteinsHemeHeme Oxygenase (Decyclizing)Host Microbial InteractionsIronProtein ConformationBacterial ProteinsHemeHeme Oxygenase (Decyclizing)Ironheme bindingheme degradationheme oxygenaseiron regulationpathogenic bacteria

Identifiers

PMID29971218
PMCPMC6018153
OpenAlexW2807683109

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.