Literature for family S16

(Topics flags: S Structure, V Review. To select only the references relevant to a single topic, click the link above. See explanation.)

2022
1. Wlodawer,A., Sekula,B., Gustchina,A. and Rotanova,T.V. \<br\>Structure and the Mode of Activity of Lon Proteases from Diverse Organisms\<br\>J Mol Biol (2022) 434, 167504. PubMed  Europe PubMed DOI  PMC  EPMC
2019
2. Tsitsekian,D., Daras,G., Alatzas,A., Templalexis,D., Hatzopoulos,P. and Rigas,S. \<br\>Comprehensive analysis of Lon proteases in plants highlights independent gene duplication events\<br\>J Exp Bot (2019) 70, 2185-2197. PubMed  Europe PubMed DOI  V
2016
3. Xie,F., Li,G., Zhang,Y., Zhou,L., Liu,S., Liu,S. and Wang,C. \<br\>The Lon protease homologue LonA, not LonC, contributes to the stress tolerance and biofilm formation of Actinobacillus pleuropneumoniae\<br\>Microb Pathog (2016) 93, 38-43. PubMed  Europe PubMed DOI
2013
4. Rotanova,T.V., Dergousova,N.I. and Morozkin,A.D. \<br\>Unique structural organization of ATP-dependent LonA proteases\<br\>Russ J Bioorganic Chem (2013) 39, 268-282. DOI
2012
5. Liao,J.H., Kuo,C.I., Huang,Y.Y., Lin,Y.C., Lin,Y.C., Yang,C.Y., Wu,W.L., Chang,W.H., Liaw,Y.C., Lin,L.H., Chang,C.I. and Wu,S.H. \<br\>A Lon-like protease with no ATP-powered unfolding activity\<br\>PLoS ONE (2012) 7, e40226. PubMed  Europe PubMed DOI  PMC  EPMC
2010
6. Rotanova,T.V. and Melnikov,E.E. \<br\>A novel view on the architecture of the non-catalytic N-terminal region of ATP-dependent LonA proteases\<br\>Biochem Suppl Ser B (Moscow) (2010) 4, 404-408. DOI  S
2007
7. Kolodziejczak,M., GibalaM., Urantowka,A. and Janska,H. \<br\>The significance of Arabidopsis AAA proteases for activity and assembly/stability of mitochondrial OXPHOS complexes\<br\>Physiologia Plantarum (2007) 129, 135-142.
2006
8. Rotanova,T.V., Botos,I., Melnikov,E.E., Rasulova,F., Gustchina,A., Maurizi,M.R. and Wlodawer,A. \<br\>Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains\<br\>Protein Sci (2006) 15, 1815-1828. PubMed  Europe PubMed DOI  PMC  EPMC
2005
9. [YEAR:1-3-2005]Bota,D.A., Ngo,J.K. and Davies,K.J. \<br\>Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death\<br\>Free Radic Biol Med (1-3-2005) 38, 665-677. PubMed  Europe PubMed DOI
2004
10. Besche,H. and Zwickl,P. \<br\>The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active site\<br\>Eur J Biochem (2004) 271, 4361-4365. PubMed  Europe PubMed DOI
11. Botos,I., Melnikov,E.E., Cherry,S., Tropea,J.E., Khalatova,A.G., Rasulova,F., Dauter,Z., Maurizi,M.R., Rotanova,T.V., Wlodawer,A. and Gustchina,A. \<br\>The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site\<br\>J Biol Chem (2004) 279, 8140-8148. PubMed  Europe PubMed DOI  S
12. Rotanova,T.V., Melnikov,E.E., Khalatova,A.G., Makhovskaya,O.V., Botos,I., Wlodawer,A. and Gustchina,A. \<br\>Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains\<br\>Eur J Biochem (2004) 271, 4865-4871. PubMed  Europe PubMed DOI
2003
13. Rotanova,T.V., Mel'nikov,E.E. and Tsirul'nikov,K.B. \<br\>[Catalytic dyad Ser-Lys at the active site of Escherichia coli ATP-dependent Lon-proteinase]\<br\>Bioorg Khim (2003) 29, 97-99. PubMed  Europe PubMed
2000
14. [YEAR:4-1-2000]Birghan,C., Mundt,E. and Gorbalenya,A.E. \<br\>A non-canonical Lon proteinase lacking the ATPase domain employs the Ser-Lys catalytic dyad to exercise broad control over the life cycle of a double-stranded RNA virus\<br\>EMBO J (4-1-2000) 19, 114-123. PubMed  Europe PubMed DOI  PMC  EPMC
1999
15. [YEAR:8-6-1999]Smith,C.K., Baker,T.A. and Sauer,R.T. \<br\>Lon and Clp family proteases and chaperones share homologous substrate-recognition domains\<br\>Proc Natl Acad Sci U S A (8-6-1999) 96, 6678-6682. PubMed  Europe PubMed  PMC  EPMC