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  1. 1.   Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
  2. Gustchina,Alla; Li,Mi; Andrianova, Anna G; Kudzhaev, Arsen M; Lountos,George; Sekula, Bartosz; Cherry,Scott; Tropea, Joseph E; Smirnov, Ivan V; Wlodawer,Alexander; Rotanova, Tatyana V
  3. International Journal of Molecular Sciences. 2022, Sep 28; 23(19):
  1. 2.   Involvement of the N Domain Residues E34, K35, and R38 in the Functionally Active Structure of Escherichia coli Lon Protease
  2. Andrianova, A. G.; Kudzhaev, A. M.; Abrikosova, V. A.; Gustchina,Alla; Smirnov, I. V.; Rotanova, T. V.
  3. Acta Naturae. 2020, Oct-Dec; 12(4): 86-97.
  1. 3.   Cryo-EM structure of substrate-free E. coli Lon protease provides insights into the dynamics of Lon machinery
  2. Botos, Istvan; Lountos,George; Wu,Weimin; Cherry,Scott; Ghirlando, Rodolfo; Kudzhaev, Arsen M; Rotanova, Tatyana V; de Val, Natalia; Tropea,Joseph; Gustchina,Alla; Wlodawer,Alexander
  3. Current research in structural biology. 2019, Nov; 1: 13-20.
  1. 4.   New insights into structural and functional relationships between LonA proteases and ClpB chaperones
  2. Rotanova, Tatyana V; Andrianova, Anna G; Kudzhaev, Arsen M; Li,Mi; Botos, Istvan; Wlodawer,Alexander; Gustchina,Alla
  3. FEBS open bio. 2019, JUL 21;
  1. 5.   Structure of the N-terminal fragment of Escherichia coli Lon protease
  2. Li, M.; Gustchina, A.; Rasulova, F. S.; Melnikov, E. E.; Maurizi, M. R.; Rotanova, T. V.; Dauter, Z.; Wlodawer, A.
  3. Acta Crystallographica Section D-Biological Crystallography. 2010, Aug; 66: 865-873.
  1. 6.   A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants
  2. Tang, W. K.; Li, D. Y.; Li, C. C.; Esser, L.; Dai, R. M.; Guo, L. A.; Xia, D.
  3. Embo Journal. 2010, Jul; 29(13): 2217-2229.
  1. 7.   Slicing a protease: Structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains
  2. Rotanova, T. V.; Botos, I.; Melnikov, E. E.; Rasulova, F.; Gustchina, A.; Maurizi, M. R.; Wlodawer, A.
  3. Protein Science. 2006, Aug; 15(8): 1815-1828.
  1. 8.   Multifunctional roles of the conserved arg residues in the second region of homology of p97/valosin-containing protein
  2. Wang, Q.; Song, C. C.; Irizarry, L.; Dai, R. M.; Zhang, X. D.; Li, C. C. H.
  3. Journal of Biological Chemistry. 2005, DEC 9; 280(49): 40515-40523.
  1. 9.   Crystal structure of the N-terminal domain of E-coli Lon protease
  2. Li, M.; Rasulova, F.; Melnikov, E. E.; Rotanova, T. V.; Gustchina, A.; Maurizi, M. R.; Wlodawer, A.
  3. Protein Science. 2005, NOV; 14(11): 2895-2900.
  1. 10.   Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains
  2. Rotanova, T. V.; Melnikov, E. E.; Khalatova, A. G.; Makhovskaya, O. V.; Botos, I.; Wlodawer, A.; Gustchina, A.
  3. European Journal of Biochemistry. 2004, DEC; 271(23-24): 4865-4871.
  1. 11.   Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions
  2. Wang, Q.; Song, C. C.; Li, C. C. H.
  3. Journal of Structural Biology. 2004, APR-MAY; 146(1-2): 44-57.
  1. 12.   Late domain-dependent inhibition of equine infectious anemia virus budding
  2. Miranda, S. X.; Ablan, S.; Demirov, D. G.; Chen, C. P.; Montelaro, R. C.; Freed, E. O.
  3. Journal of Virology. 2004 78(2): 724-732.
  1. 13.   Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities
  2. Wang, Q.; Song, C. C.; Li, C. C. H.
  3. Biochemical and Biophysical Research Communications. 2003 300(2): 253-260.
  1. 14.   D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP
  2. Wang, Q.; Song, C. C.; Yang, X. Y.; Li, C. C. H.
  3. Journal of Biological Chemistry. 2003 278(35): 32784-32793.
  1. 15.   ATPase activity of p97-valosin-containing protein (VCP) - D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity
  2. Song, C. C.; Wang, Q.; Li, C. C. H.
  3. Journal of Biological Chemistry. 2003 278(6): 3648-3655.
  1. 16.   Valosin-containing protein is a multiubiquitin chain targeting factor required in ubiquitin-proteasome degradation
  2. Dai, R. M.; Li, C. C. H.
  3. Nature Cell Biology. 2001 3(8): 740-744.
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