Evidence map›Paper›PMID 22573333›Full record

ArticleThe Journal of biological chemistry2012

Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2+ regulation.

Priit Eek, Reet Järving, Ivar Järving, Nathaniel C Gilbert, Marcia E Newcomer, Nigulas Samel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

27 citing papers in PubMed, 67 citations in OpenAlex.

  1. Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Biochemical Characterization of 13-Lipoxygenases ofInternational journal of molecular sciences · 2021
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. 5-Lipoxygenase-activating protein rescues activity of 5-lipoxygenase mutations that delay nuclear membrane association and disrupt product formation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  13. Article
  14. The Polycystin-1, Lipoxygenase, and α-Toxin Domain Regulates Polycystin-1 Trafficking.Journal of the American Society of Nephrology : JASN · 2016
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. The structural basis for specificity in lipoxygenase catalysis.Protein science : a publication of the Protein Society · 2015
    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

6 authors at 2 institutions in 2 countries.

Priit EekDepartment of Chemistry, Tallinn University of Technology, Akadeemia tee 15, 12618 Tallinn, Estonia.
Reet Järving
Ivar Järving
Nathaniel C Gilbert
Marcia E Newcomer
Nigulas Samel
Tallinn University of Technology · EELouisiana State University · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
The Structural Basis for Control of 5-Lipoxgenease ActivityR01HL107887 · NHLBI · LOUISIANA STATE UNIV A&M COL BATON ROUGE · PI NEWCOMER, MARCIA E. · 2011 to 2014
$1.4M
NCRR NIH HHS P41 RR015301NCRR NIH HHS RR-15301NHLBI NIH HHS R01 HL107887
6 · The paper itself

Abstract

Lipoxygenases (LOXs) are a key part of several signaling pathways that lead to inflammation and cancer. Yet, the mechanisms of substrate binding and allosteric regulation by the various LOX isoforms remain speculative. Here we report the 2.47-Å resolution crystal structure of the arachidonate 11R-LOX from Gersemia fruticosa, which sheds new light on the mechanism of LOX catalysis. Our crystallographic and mutational studies suggest that the aliphatic tail of the fatty acid is bound in a hydrophobic pocket with two potential entrances. We speculate that LOXs share a common T-shaped substrate channel architecture that gives rise to the varying positional specificities. A general allosteric mechanism is proposed for transmitting the activity-inducing effect of calcium binding from the membrane-targeting PLAT (polycystin-1/lipoxygenase/α-toxin) domain to the active site via a conserved π-cation bridge.

Indexed as

Gene Expression RegulationAllosteric SiteAnimalsAnthozoaArachidonate LipoxygenasesCalciumCalcium-Binding ProteinsCatalytic DomainCell MembraneChromatography, High Pressure LiquidCrystallography, X-RayDimerizationEicosanoidsHumansKineticsLiposomes11-lipoxygenaseArachidonate LipoxygenasesCalciumCalcium-Binding ProteinsEicosanoidsLiposomes

Identifiers

PMID22573333
PMCPMC3381197
OpenAlexW2045221081

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.