Evidence map›Paper›PMID 20952656›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Crystal structure of Spot 14, a modulator of fatty acid synthesis.

Christopher L Colbert, Chai-Wan Kim, Young-Ah Moon, Lisa Henry, Maya Palnitkar, William B McKean, Kevin Fitzgerald, Johann Deisenhofer, Jay D Horton, Hyock Joo Kwon

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 13% 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

48 citing papers in PubMed, 1 synthesis or guideline pooled it, 69 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Identification and Regulation of a Hepatic Lipogenic Metabolon.bioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Mechanism of action ofSaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2022
    Article
  15. Article
  16. Nutrients · 2022
    Article
  17. Review
  18. Article
  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

10 authors at 4 institutions in 1 country.

Christopher L ColbertDepartment of Biochemistry and Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, USA.
Chai-Wan Kim
Young-Ah Moon
Lisa Henry
Maya Palnitkar
William B McKean
Kevin Fitzgerald
Johann Deisenhofer
Jay D Horton
Hyock Joo Kwon
The University of Texas Southwestern Medical Center · USSouthwestern Medical CenterAlnylam Pharmaceuticals (United States) · USCenter for Systems Biology · US

Funding

TRANSCRIPTIONAL REGULATION OF LDL RECEPTOR PROMOTERP01HL020948 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI GOLDSTEIN, JOSEPH L · 1985 to 2021
$103.1M
Howard Hughes Medical InstituteNHLBI NIH HHS P01 HL020948
6 · The paper itself

Abstract

Spot 14 (S14) is a protein that is abundantly expressed in lipogenic tissues and is regulated in a manner similar to other enzymes involved in fatty acid synthesis. Deletion of S14 in mice decreased lipid synthesis in lactating mammary tissue, but the mechanism of S14's action is unknown. Here we present the crystal structure of S14 to 2.65 Å and biochemical data showing that S14 can form heterodimers with MIG12. MIG12 modulates fatty acid synthesis by inducing the polymerization and activity of acetyl-CoA carboxylase, the first committed enzymatic reaction in the fatty acid synthesis pathway. Coexpression of S14 and MIG12 leads to heterodimers and reduced acetyl-CoA carboxylase polymerization and activity. The structure of S14 suggests a mechanism whereby heterodimer formation with MIG12 attenuates the ability of MIG12 to activate ACC.

Indexed as

Models, MolecularAcetyl-CoA CarboxylaseAnimalsCHO CellsCricetinaeCricetulusCrystallography, X-RayFatty AcidsFemaleMiceMicrotubule-Associated ProteinsNuclear ProteinsProtein Structure, TertiaryStructure-Activity RelationshipTranscription FactorsAcetyl-CoA CarboxylaseFatty AcidsMicrotubule-Associated ProteinsMig12 protein, mouseNuclear ProteinsThrsp protein, mouseTranscription Factors

Identifiers

PMID20952656
PMCPMC2973905
OpenAlexW2055395834

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.