PMID:15550237
| Citation |
Horwich, AL (2004) Chaperoned protein disaggregation--the ClpB ring uses its central channel. Cell 119:579-81 |
|---|---|
| Abstract |
In this issue of Cell, exploit a clever manipulation of the Hsp100 ring chaperone, ClpB, to gain some mechanistic and physiologic understanding of the action of this chaperone in mediating ATP-dependent disaggregation of protein aggregates that accumulate in the bacterial cytoplasm under severe heat shock conditions. |
| Links |
PubMed Online version:10.1016/j.cell.2004.11.018 |
| Keywords |
Adenosine Triphosphate/metabolism; Escherichia coli Proteins/metabolism; Heat-Shock Proteins/metabolism; Heat-Shock Response/physiology; Models, Molecular; Molecular Chaperones/metabolism; Multiprotein Complexes/metabolism; Protein Subunits/physiology |
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