Evidence map›Paper›PMID 27714045›Full record

ReviewMetallomics : integrated biometal science2016

Mammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20.

N Maio, T A Rouault

Open access · greenAbstract readReview
In one paragraph

Review in Metallomics : integrated biometal science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Pulling back the mitochondria's iron curtain.npj metabolic health and disease · 2025
    Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. The indispensable role of mammalian iron sulfur proteins in function and regulation of multiple diverse metabolic pathways.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2019
    Review
  14. Review
  15. Iron-sulfur clusters: from metals through mitochondria biogenesis to disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  16. Review
  17. Article
  18. Iron-sulfur cluster biogenesis and trafficking in mitochondria.The Journal of biological chemistry · 2017
    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.

N MaioMolecular Medicine Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, 9000 Rockville Pike, 20892 Bethesda, MD, USA. rouault@mail.nih.gov.
T A RouaultMolecular Medicine Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, 9000 Rockville Pike, 20892 Bethesda, MD, USA. rouault@mail.nih.gov.
Eunice Kennedy Shriver National Institute of Child Health and Human Development · US

Funding

Regulation Of Intracellular Iron MetabolismZIAHD001602 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI ROUAULT, TRACEY A. · 2009 to 2025
$21.8M
Mammalian iron-sulfur cluster biogenesisZIAHD008814 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI ROUAULT, TRACEY A. · 2009 to 2025
$17.8M
Mammalian iron-sulfur cluster biogenesisZ01HD008814 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI ROUAULT, TRACEY A. · 2007 to 2008
$1.5M
Intramural NIH HHS Z01 HD008814
6 · The paper itself

Abstract

Iron-sulfur (Fe-S) clusters are inorganic cofactors that are fundamental to several biological processes in all three kingdoms of life. In most organisms, Fe-S clusters are initially assembled on a scaffold protein, ISCU, and subsequently transferred to target proteins or to intermediate carriers by a dedicated chaperone/co-chaperone system. The delivery of assembled Fe-S clusters to recipient proteins is a crucial step in the biogenesis of Fe-S proteins, and, in mammals, it relies on the activity of a multiprotein transfer complex that contains the chaperone HSPA9, the co-chaperone HSC20 and the scaffold ISCU. How the transfer complex efficiently engages recipient Fe-S target proteins involves specific protein interactions that are not fully understood. This mini review focuses on recent insights into the molecular mechanism of amino acid motif recognition and discrimination by the co-chaperone HSC20, which guides Fe-S cluster delivery.

Indexed as

Amino Acid MotifsAnimalsHumansIron-Sulfur ProteinsMolecular ChaperonesProtein BindingProtein Interaction MapsHSCB protein, humanIron-Sulfur ProteinsMolecular Chaperones

Identifiers

PMID27714045
PMCPMC5240853
OpenAlexW2511624662

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.