| Literature DB >> 20189813 |
Gianni Guizzunti1, Thomas P Brady2, Derek Fischer2, Vivek Malhotra1, Emmanuel A Theodorakis2.
Abstract
The cellular activity of norrisolide (7), a novel Golgi-vesiculating agent, was dissected as function of its chemical structure. This natural product induces irreversible vesiculation of the Golgi membranes and blocks protein transport at the level of the Golgi. The Golgi localization and fragmentation effects of 7 depend on the presence of the perhydroindane core, while the irreversibility of fragmentation depends on the acetyl group of 7. We show that fluorescent derivatives of norrisolide are able to localize to the Golgi apparatus and represent important tools for the study of the Golgi structure and function. Copyright 2010 Elsevier Ltd. All rights reserved.Entities:
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Year: 2010 PMID: 20189813 PMCID: PMC2838712 DOI: 10.1016/j.bmc.2010.02.007
Source DB: PubMed Journal: Bioorg Med Chem ISSN: 0968-0896 Impact factor: 3.641