Search Results - "Khalatova, Anna G."

The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site by Botos, Istvan, Melnikov, Edward E., Cherry, Scott, Tropea, Joseph E., Khalatova, Anna G., Rasulova, Fatima, Dauter, Zbigniew, Maurizi, Michael R., Rotanova, Tatyana V., Wlodawer, Alexander, Gustchina, Alla

“…ATP-dependent Lon protease degrades specific short-lived regulatory proteins as well as defective and abnormal proteins in the cell. The crystal structure of…”
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Classification of ATP‐dependent proteases Lon and comparison of the active sites of their proteolytic domains by Rotanova, Tatyana V., Melnikov, Edward E., Khalatova, Anna G., Makhovskaya, Oksana V., Botos, Istvan, Wlodawer, Alexander, Gustchina, Alla

“…ATP‐dependent Lon proteases belong to the superfamily of AAA+ proteins. Until recently, the identity of the residues involved in their proteolytic active sites…”
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Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution by Botos, Istvan, Melnikov, Edward E, Cherry, Scott, Khalatova, Anna G, Rasulova, Fatima S, Tropea, Joseph E, Maurizi, Michael R, Rotanova, Tatyana V, Gustchina, Alla, Wlodawer, Alexander

“…The crystal structure of the small, mostly helical alpha domain of the AAA+ module of the Escherichia coli ATP-dependent protease Lon has been solved by single…”
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Crystal structure of the AAA + α domain of E. coli Lon protease at 1.9 Å resolution by Botos, Istvan, Melnikov, Edward E., Cherry, Scott, Khalatova, Anna G., Rasulova, Fatima S., Tropea, Joseph E., Maurizi, Michael R., Rotanova, Tatyana V., Gustchina, Alla, Wlodawer, Alexander

“…The crystal structure of the small, mostly helical α domain of the AAA + module of the Escherichia coli ATP-dependent protease Lon has been solved by single…”
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