title: Finally, how histone deacetylase inhibitors disrupt mitosis!
abstract: The disruption of normal mitosis by histone deacetylase inhibitors is a significant contributor to the anticancer effects of these drugs. However, the mechanism by which these drugs affect mitosis is poorly understood. A number of recent papers have now thrown considerable light onto how these drugs elicit this very distinctive cell cycle disruption.
authors.affiliation: The University of Queensland Diamantina Institute, Princess Alexandra Hospital, Brisbane, Queensland, Australia. brianG@uq.edu.au
authors.forename: Brian
authors.initials: B
authors.lastname: Gabrielli
authors.forename: KeeMing
authors.initials: K
authors.lastname: Chia
authors.forename: Robyn
authors.initials: R
authors.lastname: Warrener
mesh_terms: D064127:Aurora Kinases; D018797:Cell Cycle Proteins / Q000378:metabolism; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism; D056572:Histone Deacetylase Inhibitors / Q000494:pharmacology*; D006655:Histone Deacetylases / Q000378:metabolism; D006657:Histones / Q000235:genetics / Q000378:metabolism; D006801:Humans; D051034:Inhibitor of Apoptosis Proteins / Q000378:metabolism; D059566:M Phase Cell Cycle Checkpoints / Q000187:drug effects; D008938:Mitosis / Q000187:drug effects*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D000077022:Survivin; D000097869:Polo-Like Kinase 1
chemical_list: D064127:Aurora Kinases; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D018841:HSP90 Heat-Shock Proteins; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases; D006657:Histones; D051034:Inhibitor of Apoptosis Proteins; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins; D000077022:Survivin; D000097869:Polo-Like Kinase 1; C107489:BIRC5 protein, human