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Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity
- 1.0352899 - MBÚ 2011 RIV US eng J - Journal Article
García-Nafría, J. - Ondrovičová, G. - Blagova, E. - Levdikov, V. M. - Bauer, J. A. - Suzuki, C. K. - Kutejová, Eva - Wilkinson, A. J. - Wilson, K. S.
Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity.
Protein Science. Roč. 19, č. 5 (2010), s. 987-999. ISSN 0961-8368. E-ISSN 1469-896X
Institutional research plan: CEZ:AV0Z50200510
Keywords : ATP-dependent protease * Lon protease * catalytic dyad
Subject RIV: CE - Biochemistry
Impact factor: 2.741, year: 2010
ATP-dependent proteases are crucial for cellular homeostasis. By degrading short-lived regulatory proteins, they play an important role in the control of many cellular pathways and, through the degradation of abnormally misfolded proteins, protect the cell from a buildup of aggregates. Disruption or disregulation of mammalian mitochondrial Lon protease leads to severe changes in the cell, linked with carcinogenesis, apoptosis, and necrosis
Permanent Link: http://hdl.handle.net/11104/0192290
Number of the records: 1