Evidence map›Paper›PMID 11248039›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Human fatty acid synthase: role of interdomain in the formation of catalytically active synthase dimer.

S S Chirala, A Jayakumar, Z W Gu, S J Wakil

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed, 94 citations in OpenAlex.

  1. Review
  2. Article
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  4. Identification ofGenes · 2024
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  8. Observational
  9. Review
  10. Metabolism.Essays in biochemistry · 2020
    Review
  11. Flavonones fromInternational journal of molecular sciences · 2018
    Article
  12. Review
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  15. Review
  16. Article
  17. Effect of Gambisan on the Inhibition of Adipogenesis in 3T3-L1 Adipocytes.Evidence-based complementary and alternative medicine : eCAM · 2013
    Article
  18. Article
  19. Article
  20. The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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

4 authors at 1 institution in 1 country.

S S ChiralaVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
A Jayakumar
Z W Gu
S J Wakil
Baylor College of Medicine · US

Funding

ZEBRAFISH MUTANT NAGIE OKOF32GM019091 · NIGMS · PRINCETON UNIVERSITY · PI BRUCE, ASHLEY E · 1997 to 1999
–
NIGMS NIH HHS F32 GM019091NIGMS NIH HHS GM-19091
6 · The paper itself

Abstract

The human and animal fatty acid synthases are dimers of two identical multifunctional proteins (M(r) 272,000) arranged in an antiparallel configuration. This arrangement generates two active centers for fatty acid synthesis separated by interdomain (ID) regions and predicts that two appropriate halves of the monomer should be able to reconstitute an active fatty acid synthesizing center. This prediction was confirmed by the reconstitution of the synthase active center by using two heterologously expressed halves of the monomer protein. Each of these recombinant halves of synthase monomer contains half of the ID regions. We show here that the fatty acid synthase activity could not be reconstituted when the ID sequences present in the two recombinant halves are deleted, suggesting that these ID sequences are essential for fatty acid synthase dimer formation. Further, we confirm that the ID sequences are the only regions of fatty acid synthase monomers that showed significant dimer formation, by using the yeast two-hybrid system. These results are consistent with the proposal that the ID region, which has no known catalytic activity, associates readily and holds together the two dynamic active centers of the fatty acid synthase dimer, therefore playing an important role in the architecture of catalytically active fatty acid synthase.

Indexed as

AcyltransferasesCatalysisCatalytic DomainDimerizationFatty Acid Synthase, Type IHumansMultienzyme ComplexesRecombinant Fusion ProteinsTwo-Hybrid System TechniquesAcyltransferasesFatty Acid Synthase, Type IMultienzyme ComplexesRecombinant Fusion Proteins

Identifiers

PMID11248039
PMCPMC30614
OpenAlexW2013251768

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.