ArticleThe Journal of biological chemistry2018
An unlikely heme chaperone confirmed at last.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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.
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.
Who cites it
6 citing papers in PubMed.
- Bottom-Up Model Suggesting Membrane Localization of Heme Oxygenase‑1 Contributes to Heme Selection for Degradation.ACS omega · 2026Article
- Heme allocation in eukaryotic cells relies on mitochondrial heme export through FLVCR1b to cytosolic GAPDH.Nature communications · 2025Article
- Molecular insights into the role of heme in the transcriptional regulatory system AppA/PpsR.Biophysical journal · 2022Article
- GAPDH is involved in the heme-maturation of myoglobin and hemoglobin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Review
- Heme cytotoxicity is the consequence of endoplasmic reticulum stress in atherosclerotic plaque progression.Scientific reports · 2021Observational
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Labile heme, as opposed to heme that is tightly bound within proteins, is thought to require a chaperone to be trafficked within the cell due to its cytotoxicity, but the identity of this chaperone was not known. A new study reveals that an unlikely protein, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), is a heme chaperone that binds and transfers labile heme to downstream target proteins. These results provide a new framework for understanding heme homeostasis and raise intriguing questions regarding the intersection of heme transport, carbohydrate metabolism, and intracellular signaling.
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Registered trials
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.