Dissecting cell biology with chemical scalpels.
Understanding complex cellular processes requires methods for specifically perturbing protein function in a temporally defined fashion. In recent years a variety of chemical tools have been used to study the cytoskeleton and cell division, protein trafficking, and the destruction of proteins by the ubiquitin-proteasome system. The ability to use combinations of reversible inhibitors is proving to be especially helpful in dissecting complex cellular events. Furthermore, the identification of novel inhibitors through unbiased screening approaches is revealing novel drugable steps in important cellular pathways.
Hathaway
Nathaniel A
NA
Department of Cell Biology, Harvard Medical School, 240 Longwood Ave, Boston, Massachussetts 02115, USA.
King
Randall W
RW
D000818:Animals; D064127:Aurora Kinases; D001671:Biochemistry / Q000379:methods; D001695:Biology / Q000379:methods*; D002455:Cell Division; D003599:Cytoskeleton / Q000378:metabolism; D015723:Gene Library; D006801:Humans; D008954:Models, Biological; D010641:Phenotype; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D021381:Protein Transport; D034622:RNA Interference; D025801:Ubiquitin / Q000378:metabolism
D025801:Ubiquitin; D064127:Aurora Kinases; D017346:Protein Serine-Threonine Kinases; D046988:Proteasome Endopeptidase Complex