Proteasomes and their kin: proteases in the machine age
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/nrm1336.pdf
Reference100 articles.
1. Groll, M. et al. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386, 463–471 (1997). Despite being assembled from 14 unique polypeptides, the eukaryotic 20S proteasome is remarkably similar to its archaebacterial cousin. Furthermore, the closed state of the axial pore indicated that the 19S complex would regulate pore gating.
2. Unno, M. et al. The stucture of the mammalian 20S proteasome at 2.75 Å resolution. Structure 10, 609–618 (2002).
3. Lowe, J. et al. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268, 533–539 (1995).
4. Whitby, F. G. et al. Structural basis for the activation of 20S proteasomes by 11S regulators. Nature 408, 115–120 (2000). The structure of a non-ATPase regulatory complex bound to the yeast 20S complex led to a persuasive molecular model for protease pore opening by a regulatory complex.
5. Wang, J., Hartling, J. A. & Flanagan, J. M. The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell 91, 447–456 (1997).
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