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Article

Human 15-LOX-1 active site mutations alter inhibitor binding and decrease potency.

Bioorganic & medicinal chemistry - 1 Nov 2016

Armstrong Michelle, van Hoorebeke Christopher, Horn Thomas, Deschamps Joshua, Freedman J Cody, Kalyanaraman Chakrapani, Jacobson Matthew P, Holman Theodore

Abstract excerpt

Human 15-lipoxygenase-1 (h15-LOX-1 or h12/15-LOX) reacts with polyunsaturated fatty acids and produces bioactive lipid derivatives that are implicated in many important human diseases. One such disease is stroke, which is the fifth leading cause of death and the first leading cause of disability in America. The discovery of h15-LOX-1 inhibitors could potentially lead to novel therapeutics in the treatment of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 27647374
DOI: 10.1016/j.bmc.2016.08.063
PMCID: PMC5065787

Genes

LOX

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.

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