Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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 - 1 May 2016

Gerstmeier Jana, Newcomer Marcia E, Dennhardt Sophie, Romp Erik, Fischer Jana, Werz Oliver, Garscha Ulrike

Abstract excerpt

Leukotrienes (LTs) are proinflammatory lipid mediators formed from arachidonic acid in a 2-step reaction catalyzed by 5-lipoxygenase (5-LOX) requiring the formation of 5-HPETE [5(S)-hydroperoxy-6-trans-8,11,14-cis-eicosatetraenoic acid] and its subsequent transformation to LTA4 5-LOX is thought to receive arachidonic acid from the nuclear membrane-embedded 5-LOX-activating protein (FLAP). The crystal structure of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 5-Lipoxygenase-Activating Proteins
Share to Arachidonate 5-Lipoxygenase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Membrane

Share to Cell Movement

Share to Cell Nucleus

Share to Gene Expression Regulation, Enzymologic

Share to HEK293 Cells

Share to Indoles

Source

Open in PubMed Open full text

Identifiers

PMID: 26842853
DOI: 10.1096/fj.201500210R
PMCID: PMC4836370

Genes

LOX

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

5-Lipoxygenase-activating protein rescues activity of 5-lipoxygenase mutations that delay nuclear membrane association and disrupt product formation.PMID 26842853Read ↗

Characterization of the interaction of human 5-lipoxygenase with its activating protein FLAP.Semantic proximity Read ↗

The biology of 5-lipoxygenase: function, structure, and regulatory mechanisms.Semantic proximity Read ↗

The N-terminal "beta-barrel" domain of 5-lipoxygenase is essential for nuclear membrane translocation.Semantic proximity Read ↗

Coactosin-like protein functions as a stabilizing chaperone for 5-lipoxygenase: role of tryptophan 102.Semantic proximity Read ↗

The biochemical, molecular, and genomic aspects of leukotriene C4 synthase.Semantic proximity Read ↗

A Single Amino Acid Difference between Mouse and Human 5-Lipoxygenase Activating Protein (FLAP) Explains the Speciation and Differential Pharmacology of Novel FLAP Inhibitors.Semantic proximity Read ↗

Helical remodeling augments 5-lipoxygenase activitySemantic proximity Read ↗

Ceramide 1-phosphate is required for the translocation of group IVA cytosolic phospholipase A2 and prostaglandin synthesis.Semantic proximity Read ↗

Mutations of Triad Determinants Changes the Substrate Alignment at the Catalytic Center of Human ALOX5.Semantic proximity Read ↗

Human 15-LOX-1 active site mutations alter inhibitor binding and decrease potency.Semantic proximity Read ↗

Naturally occurring mutations in the human 5-lipoxygenase gene promoter that modify transcription factor binding and reporter gene transcription.Semantic proximity Read ↗

Functional Characterization of Knock-In Mice Expressing a 12/15-Lipoxygenating Alox5 Mutant Instead of the 5-Lipoxygenating Wild-Type Enzyme.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.