Evidence map›Paper›PMID 29259115›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Structure of the human monomeric NEET protein MiNT and its role in regulating iron and reactive oxygen species in cancer cells.

Colin H Lipper, Ola Karmi, Yang Sung Sohn, Merav Darash-Yahana, Heiko Lammert, Luhua Song, Amy Liu, Ron Mittler, Rachel Nechushtai, José N Onuchic and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Ferroptosis in cancer: revealing the multifaceted functions of mitochondria.Cellular and molecular life sciences : CMLS · 2025
    Review
  7. Article
  8. Review
  9. CISD3/MiNT is required for complex I function, mitochondrial integrity, and skeletal muscle maintenance.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Viruses traverse the human proteome through peptide interfaces that can be biomimetically leveraged for drug discovery.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Review
  14. Paramagnetic NMR to study iron sulfur proteins:Journal of biomolecular NMR · 2023
    Article
  15. Article
  16. PINK1 and Parkin regulate IPNature communications · 2023
    Article
  17. 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

11 authors at 5 institutions in 2 countries.

Colin H LipperDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093.
Ola KarmiThe Alexander Silberman Institute of Life Science, Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, Jerusalem 91904, Israel.
Yang Sung SohnThe Alexander Silberman Institute of Life Science, Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, Jerusalem 91904, Israel.
Merav Darash-YahanaThe Alexander Silberman Institute of Life Science, Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, Jerusalem 91904, Israel.
Heiko LammertCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005.
Luhua SongDepartment of Biological Sciences, University of North Texas, Denton, TX 76203.
Amy LiuDepartment of Biological Sciences, University of North Texas, Denton, TX 76203.
Ron MittlerDepartment of Biological Sciences, University of North Texas, Denton, TX 76203.
Rachel NechushtaiThe Alexander Silberman Institute of Life Science, Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, Jerusalem 91904, Israel.
José N OnuchicCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005; jonuchic@rice.edu pajennings@ucsd.edu.
Patricia A JenningsDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093; jonuchic@rice.edu pajennings@ucsd.edu.
Hebrew University of Jerusalem · ILUniversity of North Texas · USUniversity of California, San Diego · USCenter for Theoretical Biological Physics · USRice University · US

Funding

The New Family of NEET Proteins: 2Fe-2S Protein Mediated Health and DiseaseR01GM101467 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JENNINGS, PATRICIA A · 2012 to 2015
$1.3M
NIGMS NIH HHS R01 GM101467
6 · The paper itself

Abstract

The NEET family is a relatively new class of three related [2Fe-2S] proteins (CISD1-3), important in human health and disease. While there has been growing interest in the homodimeric gene products of CISD1 (mitoNEET) and CISD2 (NAF-1), the importance of the inner mitochondrial CISD3 protein has only recently been recognized in cancer. The CISD3 gene encodes for a monomeric protein that contains two [2Fe-2S] CDGSH motifs, which we term mitochondrial inner NEET protein (MiNT). It folds with a pseudosymmetrical fold that provides a hydrophobic motif on one side and a relatively hydrophilic surface on the diametrically opposed surface. Interestingly, as shown by molecular dynamics simulation, the protein displays distinct asymmetrical backbone motions, unlike its homodimeric counterparts that face the cytosolic side of the outer mitochondrial membrane/endoplasmic reticulum (ER). However, like its counterparts, our biological studies indicate that knockdown of MiNT leads to increased accumulation of mitochondrial labile iron, as well as increased mitochondrial reactive oxygen production. Taken together, our study suggests that the MiNT protein functions in the same pathway as its homodimeric counterparts (mitoNEET and NAF-1), and could be a key player in this pathway within the mitochondria. As such, it represents a target for anticancer or antidiabetic drug development.

Indexed as

Cell Line, TumorCrystallography, X-RayHumansIronIron-Sulfur ProteinsKineticsMitochondrial MembranesMitochondrial ProteinsMolecular Dynamics SimulationMutationNeoplasmsProtein DomainsProtein FoldingReactive Oxygen SpeciesRNA InterferenceCISD3 protein, humanIronIron-Sulfur ProteinsMitochondrial ProteinsReactive Oxygen Speciescanceriron homeostasisiron-sulfur proteinsmitochondriaNEET proteins

Identifiers

PMID29259115
PMCPMC5777063
OpenAlexW2779852721

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.