Latrunculin alters the actin-monomer subunit interface to prevent polymerization.
Morton
W M
WM
The Wellcome Trust Centre for Cell Biology, Institute of Cell and Molecular Biology, University of Edinburgh, Swann Building, King's Buildings, Mayfield Road, Edinburgh EH9 3JR, UK.
Ayscough
K R
KR
McLaughlin
P J
PJ
D000199:Actins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D001704:Biopolymers / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D018360:Crystallography, X-Ray; D018260:Gelsolin / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D011161:Porifera / Q000737:chemistry*; D011485:Protein Binding / Q000187:drug effects; D011487:Protein Conformation / Q000187:drug effects; D013844:Thiazoles / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D053778:Thiazolidines; D015003:Yeasts / Q000235:genetics
D000199:Actins; D001704:Biopolymers; D019086:Bridged Bicyclo Compounds, Heterocyclic; D018260:Gelsolin; D013844:Thiazoles; D053778:Thiazolidines; C037067:latrunculin A