(+)-aristolochene

(+)-aristolochene is a lipid of Prenol Lipids (PR) class.

Cross Reference

There are no associated biomedical information in the current reference collection.

Current reference collection contains 147 references associated with (+)-aristolochene in LipidPedia. Due to lack of full text of references or no associated biomedical terms are recognized in our current text-mining method, we cannot extract any biomedical terms related to diseases, pathways, locations, functions, genes, lipids, and animal models from the associated reference collection.

Users can download the reference list at the bottom of this page and read the reference manually to find out biomedical information.

Here are additional resources we collected from PubChem and MeSH for (+)-aristolochene

PubChem Biomolecular Interactions and Pathways

NCBI Entrez Crosslinks

All references with (+)-aristolochene

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Authors Title Published Journal PubMed Link
pmid:16791319
pmid:12580479
pmid:18843388
pmid:
Noel JP et al. Structural elucidation of cisoid and transoid cyclization pathways of a sesquiterpene synthase using 2-fluorofarnesyl diphosphates. 2010 ACS Chem. Biol. pmid:20175559
Cane DE and Kang I Aristolochene synthase: purification, molecular cloning, high-level expression in Escherichia coli, and characterization of the Aspergillus terreus cyclase. 2000 Arch. Biochem. Biophys. pmid:10775423
Deligeorgopoulou A and Allemann RK Evidence for differential folding of farnesyl pyrophosphate in the active site of aristolochene synthase: a single-point mutation converts aristolochene synthase into an (E)-beta-farnesene synthase. 2003 Biochemistry pmid:12820883
Chen M et al. Mechanistic insights from the binding of substrate and carbocation intermediate analogues to aristolochene synthase. 2013 Biochemistry pmid:23905850
Shishova EY et al. X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate. 2007 Biochemistry pmid:17261032
Poliakov E et al. Biochemical evidence for the tyrosine involvement in cationic intermediate stabilization in mouse beta-carotene 15, 15'-monooxygenase. 2009 BMC Biochem. pmid:20003456