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.)

2025
1. Ludwig,K. and Heidorn-Czarna,M.
   Mitochondrial Proteases and Their Roles in Mitophagy in Plants, Animals, and Yeast
   Plant Cell Physiol (2025) PubMed  Europe PubMed DOI  V
2022
2. Wlodawer,A., Sekula,B., Gustchina,A. and Rotanova,T.V.
   Structure and the Mode of Activity of Lon Proteases from Diverse Organisms
   J Mol Biol (2022) 434, 167504-167504. PubMed  Europe PubMed DOI  PMC  EPMC
2019
3. Tsitsekian,D., Daras,G., Alatzas,A., Templalexis,D., Hatzopoulos,P. and Rigas,S.
   Comprehensive analysis of Lon proteases in plants highlights independent gene duplication events
   J Exp Bot (2019) 70, 2185-2197. PubMed  Europe PubMed DOI  V
2016
4. Xie,F., Li,G., Zhang,Y., Zhou,L., Liu,S., Liu,S. and Wang,C.
   The Lon protease homologue LonA, not LonC, contributes to the stress tolerance and biofilm formation of Actinobacillus pleuropneumoniae
   Microb Pathog (2016) 93, 38-43. PubMed  Europe PubMed DOI
2013
5. Rotanova,T.V., Dergousova,N.I. and Morozkin,A.D.
   Unique structural organization of ATP-dependent LonA proteases
   Russ J Bioorg Chem (2013) 39, 268-282. DOI
2012
6. 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.
   A Lon-like protease with no ATP-powered unfolding activity
   PLoS ONE (2012) 7, e40226-e40226. PubMed  Europe PubMed DOI  PMC  EPMC
2010
7. Rotanova,T.V. and Melnikov,E.E.
   A novel view on the architecture of the non-catalytic N-terminal region of ATP-dependent LonA proteases
   Biochem Suppl Ser B (Moscow) (2010) 4, 404-408. DOI  S
2007
8. Kolodziejczak,M., GibalaM., Urantowka,A. and Janska,H.
   The significance of Arabidopsis AAA proteases for activity and assembly/stability of mitochondrial OXPHOS complexes
   Physiologia Plantarum (2007) 129, 135-142.
2006
9. Rotanova,T.V., Botos,I., Melnikov,E.E., Rasulova,F., Gustchina,A., Maurizi,M.R. and Wlodawer,A.
   Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains
   Protein Sci (2006) 15, 1815-1828. PubMed  Europe PubMed DOI  PMC  EPMC
2005
10. [YEAR:1-3-2005]Bota,D.A., Ngo,J.K. and Davies,K.J.
    Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death
    Free Radic Biol Med (1-3-2005) 38, 665-677. PubMed  Europe PubMed DOI
2004
11. Besche,H. and Zwickl,P.
    The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active site
    Eur J Biochem (2004) 271, 4361-4365. PubMed  Europe PubMed DOI
12. 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.
    The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
    J Biol Chem (2004) 279, 8140-8148. PubMed  Europe PubMed DOI  S
13. Rotanova,T.V., Melnikov,E.E., Khalatova,A.G., Makhovskaya,O.V., Botos,I., Wlodawer,A. and Gustchina,A.
    Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains
    Eur J Biochem (2004) 271, 4865-4871. PubMed  Europe PubMed DOI
2003
14. Rotanova,T.V., Mel'nikov,E.E. and Tsirul'nikov,K.B.
    [Catalytic dyad Ser-Lys at the active site of Escherichia coli ATP-dependent Lon-proteinase]
    Bioorg Khim (2003) 29, 97-99. PubMed  Europe PubMed
2000
15. [YEAR:4-1-2000]Birghan,C., Mundt,E. and Gorbalenya,A.E.
    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
    EMBO J (4-1-2000) 19, 114-123. PubMed  Europe PubMed DOI  PMC  EPMC
1999
16. [YEAR:8-6-1999]Smith,C.K., Baker,T.A. and Sauer,R.T.
    Lon and Clp family proteases and chaperones share homologous substrate-recognition domains
    Proc Natl Acad Sci U S A (8-6-1999) 96, 6678-6682. PubMed  Europe PubMed  PMC  EPMC