Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Tatyana V, Rotanova"'
Autor:
Istvan Botos, George T. Lountos, Weimin Wu, Scott Cherry, Rodolfo Ghirlando, Arsen M. Kudzhaev, Tatyana V. Rotanova, Natalia de Val, Joseph E. Tropea, Alla Gustchina, Alexander Wlodawer
Publikováno v:
Current Research in Structural Biology, Vol 1, Iss , Pp 13-20 (2019)
Energy-dependent Lon proteases play a key role in cellular regulation by degrading short-lived regulatory proteins and misfolded proteins in the cell. The structure of the catalytically inactive S679A mutant of Escherichia coli LonA protease (EcLon)
Externí odkaz:
https://doaj.org/article/3a4bafe2973a426e8039983c811a2c88
New insights into structural and functional relationships between LonA proteases and ClpB chaperones
Autor:
Tatyana V. Rotanova, Anna G. Andrianova, Arsen M. Kudzhaev, Mi Li, Istvan Botos, Alexander Wlodawer, Alla Gustchina
Publikováno v:
FEBS Open Bio, Vol 9, Iss 9, Pp 1536-1551 (2019)
LonA proteases and ClpB chaperones are key components of the protein quality control system in bacterial cells. LonA proteases form a unique family of ATPases associated with diverse cellular activities (AAA+) proteins due to the presence of an unusu
Externí odkaz:
https://doaj.org/article/e74245a635b04ea6a61984c9bda9d76a
Autor:
Alla, Gustchina, Mi, Li, Anna G, Andrianova, Arsen M, Kudzhaev, George T, Lountos, Bartosz, Sekula, Scott, Cherry, Joseph E, Tropea, Ivan V, Smirnov, Alexander, Wlodawer, Tatyana V, Rotanova
Publikováno v:
International journal of molecular sciences. 23(19)
ATP-dependent Lon proteases are key participants in the quality control system that supports the homeostasis of the cellular proteome. Based on their unique structural and biochemical properties, Lon proteases have been assigned in the MEROPS databas
Publikováno v:
J Mol Biol
Lon proteases, members of the AAA(+) superfamily of enzymes, are key components of the protein quality control system in bacterial cells, as well as in the mitochondria and other specialized organelles of higher organisms. These enzymes have been sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57a835ab24c8d4bbe5e4df7147c3d343
https://europepmc.org/articles/PMC9013511/
https://europepmc.org/articles/PMC9013511/
Autor:
Edward E, Melnikov, Anna G, Andrianova, Andrey D, Morozkin, Anton A, Stepnov, Oksana V, Makhovskaya, Istvan, Botos, Alla, Gustchina, Alexander, Wlodawer, Tatyana V, Rotanova
Publikováno v:
Acta Biochim Pol
We carried out chymotryptic digestion of multimeric ATP-dependent Lon protease from Escherichia coli. Four regions sensitive to proteolytic digestion were located in the enzyme and several fragments corresponding to the individual structural domains