Evidence map›Paper›PMID 32091391›Full record

ArticleeLife2020

Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding.

Julia R Kardon, Jamie A Moroco, John R Engen, Tania A Baker

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. 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
2.2field-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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Regulation of cellular proteostasis via mitochondrial protein import.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Article
  3. Article
  4. Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. The yeast ALA synthase C-terminus positively controls enzyme structure and function.Protein science : a publication of the Protein Society · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Regulation of Heme Synthesis by Mitochondrial Homeostasis Proteins.Frontiers in cell and developmental biology · 2022
    Review
  17. Prime Real Estate: Metals, Cofactors and MICOS.Frontiers in cell and developmental biology · 2022
    Review
  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

4 authors at 2 institutions in 1 country.

Julia R KardonDepartment of Biochemistry, Brandeis University, Waltham, United States.ORCID 0000-0002-6621-4461
Jamie A MorocoDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, United States.ORCID 0000-0001-8250-5923
John R EngenDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, United States.ORCID 0000-0002-6918-9476
Tania A BakerDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.ORCID 0000-0002-0737-3411
Howard Hughes Medical Institute · USNortheastern University · US

Funding

Macromolecular interactions controlling the ALA synthases, keystone enzymes that initiate heme biosynthesisR01DK115558 · NIDDK · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BAKER, TANIA A · 2017 to 2021
$2.1M
Extending the applications of hydrogen exchange mass spectrometryR01GM101135 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2012 to 2015
$1.2M
Regulation of Heme Synthesis and Mitochondrial Physiology by the ClpX UnfoldaseF32DK095726 · NIDDK · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KARDON, JULIA R. · 2012 to 2014
$169k
Howard Hughes Medical InstituteNIDDK NIH HHS DK095726NIDDK NIH HHS R01 DK115558NIGMS NIH HHS GM101135
6 · The paper itself

Abstract

Mitochondria control the activity, quality, and lifetime of their proteins with an autonomous system of chaperones, but the signals that direct substrate-chaperone interactions and outcomes are poorly understood. We previously discovered that the mitochondrial AAA+ protein unfoldase ClpX (mtClpX) activates the initiating enzyme for heme biosynthesis, 5-aminolevulinic acid synthase (ALAS), by promoting cofactor incorporation. Here, we ask how mtClpX accomplishes this activation. Using

Indexed as

Protein Unfolding5-Aminolevulinate SynthetaseEnzyme ActivationMitochondriaProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins5-Aminolevulinate SynthetaseSaccharomyces cerevisiae ProteinsALASbiochemistrychaperonechemical biologyClpXheme biosynthesismitochondriapyridoxal phosphateS. cerevisiae

Identifiers

PMID32091391
PMCPMC7077987
OpenAlexW3008330404

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.