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 The Mad2 partial unfolding model: regulating mitosis through Mad2 conformational  switching Skinner JJ; Wood S; Shorter J; Englander SW; Black BEJ Cell Biol  2008[Dec]; 183 (5): 761-8The metamorphic Mad2 protein acts as a molecular switch in the checkpoint  mechanism that monitors proper chromosome attachment to spindle microtubules  during cell division. The remarkably slow spontaneous rate of Mad2 switching  between its checkpoint inactive and active forms is catalyzed onto a  physiologically relevant time scale by a self-self interaction between its two  forms, culminating in a large pool of active Mad2. Recent structural,  biochemical, and cell biological advances suggest that the catalyzed conversion  of Mad2 requires a major structural rearrangement that transits through a  partially unfolded intermediate.|Animals[MESH]|Calcium-Binding Proteins/*chemistry/*metabolism[MESH]|Catalysis[MESH]|Cell Cycle Proteins/*chemistry/*metabolism[MESH]|Humans[MESH]|Kinetics[MESH]|Mad2 Proteins[MESH]|Mitosis/*physiology[MESH]|Models, Molecular[MESH]|Nuclear Proteins/metabolism[MESH]|Prions/chemistry/metabolism[MESH]|Protein Conformation[MESH]|Protein Folding[MESH]|Protein Multimerization[MESH]|Repressor Proteins/*chemistry/*metabolism[MESH]|Spindle Apparatus/metabolism[MESH]|Structure-Activity Relationship[MESH]
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