Evidence map›Paper›PMID 23985801›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2013

Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa.

Albert Garreta, Silvana P Val-Moraes, Queralt García-Fernández, Montserrat Busquets, Carlos Juan, Antonio Oliver, Antonio Ortiz, Betty J Gaffney, Ignacio Fita, Àngels Manresa and 1 more

Abstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
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

37 citing papers in PubMed.

  1. Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Lipoxygenases at the Intersection of Infection and Carcinogenesis.International journal of molecular sciences · 2024
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Role of Host and Bacterial Lipids inFrontiers in immunology · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. EPR Spectroscopic Studies of Lipoxygenases.Chemistry, an Asian journal · 2020
    Review
  16. Article
  17. Article
  18. A 5‑lipoxygenase-specific sequence motif impedes enzyme activity and confers dependence on a partner protein.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2019
    Article
  19. Frontiers in microbiology · 2019
    Article
  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

11 authors.

Albert Garreta1Institut de Biologia Molecular, Parc Científic de Barcelona, Baldiri Reixac 10, 08028 Barcelona, Spain. xcvcri@ibmb.csic.es.
Silvana P Val-Moraes
Queralt García-Fernández
Montserrat Busquets
Carlos Juan
Antonio Oliver
Antonio Ortiz
Betty J Gaffney
Ignacio Fita
Àngels Manresa
Xavi Carpena

Funding

Reactive Intermediates in Lipoxygenase PathwaysR01GM065268 · NIGMS · FLORIDA STATE UNIVERSITY · PI GAFFNEY, BETTY J · 2003 to 2012
$1.7M
NIGMS NIH HHS R01 GM065268
6 · The paper itself

Abstract

Lipoxygenases (LOXs), which are essential in eukaryotes, have no confirmed function in prokaryotes that are devoid of polyunsaturated fatty acids. The structure of a secretable LOX from Pseudomonas aeruginosa (Pa_LOX), the first available from a prokaryote, presents significant differences with respect to eukaryotic LOXs, including a cluster of helices acting as a lid to the active center. The mobility of the lid and the structural variability of the N-terminal region of Pa_LOX was confirmed by comparing 2 crystal forms. The binding pocket contains a phosphatidylethanolamine phospholipid with branches of 18 (sn-1) and 14/16 (sn-2) carbon atoms in length. Carbon atoms from the sn-1 chain approach the catalytic iron in a manner that sheds light on how the enzymatic reaction might proceed. The findings in these studies suggest that Pa_LOX has the capacity to extract and modify unsaturated phospholipids from eukaryotic membranes, allowing this LOX to play a role in the interaction of P. aeruginosa with host cells.

Indexed as

Amino Acid MotifsAmino Acid SequenceCatalytic DomainLipoxygenaseMolecular Docking SimulationMolecular Sequence DataPhosphatidylethanolaminesProtein BindingPseudomonas aeruginosaLipoxygenasephosphatidylethanolaminePhosphatidylethanolaminesenzyme mechanismshost–pathogen interactionslipid peroxidationmembrane interactionprotein–phospholipid complexes

Identifiers

PMID23985801
PMCPMC3834787

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.