Zobrazeno 1 - 10
of 55
pro vyhledávání: '"T. V. Rotanova"'
Autor:
A. E. Gustchina, A. G. Andrianova, Ivan V. Smirnov, T. V. Rotanova, A. M. Kudzhaev, V. A. Abrikosova
Publikováno v:
Acta Naturae
ATP-dependent Lon protease of Escherichia coli (EcLon), which belongs to the superfamily of AAA+ proteins, is a key component of the cellular proteome quality control system. It is responsible for the cleavage of mutant, damaged, and short-lived regu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c487c707de2c5cf9d507d64897f1adae
https://doi.org/10.32607/actanaturae.11197
https://doi.org/10.32607/actanaturae.11197
Autor:
A. M. Kudzhaev, Alexander Wlodawer, Weimin Wu, Rodolfo Ghirlando, Alla Gustchina, T. V. Rotanova, Joseph E. Tropea, George T. Lountos, Scott Cherry, Istvan Botos, Natalia de Val
Publikováno v:
Current Research in Structural Biology
Current Research in Structural Biology, Vol 1, Iss, Pp 13-20 (2019)
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://explore.openaire.eu/search/publication?articleId=doi_dedup___::92baa61ae063e7bc75980c974cde4afa
https://doi.org/10.1016/j.crstbi.2019.10.001
https://doi.org/10.1016/j.crstbi.2019.10.001
New insights into structural and functional relationships between LonA proteases and ClpB chaperones
Autor:
A. M. Kudzhaev, Alla Gustchina, Alexander Wlodawer, Mi Li, A. G. Andrianova, Istvan Botos, T. V. Rotanova
Publikováno v:
FEBS Open Bio
FEBS Open Bio, Vol 9, Iss 9, Pp 1536-1551 (2019)
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 unus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e89593d75dfaaa4aacb09af015c65de
http://europepmc.org/articles/PMC6722904
http://europepmc.org/articles/PMC6722904
Publikováno v:
Russian Journal of Bioorganic Chemistry. 44:518-527
The effect of the coiled-coil (CC) region of the α-helical inserted domain of Escherichia coli Lon protease (Ec-Lon) on the functional activity of the enzyme has been characterized. A recombinant form des-CC(G5)-Lon in which the deleted CC fragment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3f06f1212e1834247976325efe549bd8
https://doi.org/10.1134/s1068162018050084
https://doi.org/10.1134/s1068162018050084
Autor:
A. M. Kudzhaev, V. A. Sizov, E. O. Kuzmenko, V. A. Spiridonova, A. V. Melnichuk, T. V. Rotanova, O.V. Snigirev, E. A. Oleinichenko
Publikováno v:
Moscow University Physics Bulletin. 72:376-382
The binding to Lon protease through biotinylated aptamers whose structures contain G-quadruplex fragments with magnetic nanoparticles (MNPs) functionalized by streptavidin was investigated. The conditions of binding of target aptamers to MNPs are met
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::92852db924dd6470d94300869ec865a5
https://doi.org/10.3103/s0027134917040130
https://doi.org/10.3103/s0027134917040130
Publikováno v:
Russian Journal of Bioorganic Chemistry. 43:368-376
The truncated form of E. coli LonA protease (EcLon) lacking the N-terminal fragment 1–172 (Lon173) and the variant with deleted coiled-coil (CC) fragment 173–283 (dCC-Lon, a deletion form) are produced and characterized to study the role of the N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b4b415c8438ffe81fcf13b2ede6b7629
https://doi.org/10.1134/s1068162017040021
https://doi.org/10.1134/s1068162017040021
Publikováno v:
Russian Journal of Bioorganic Chemistry. 42:381-388
Bifunctional Escherichia coli LonA protease (Ec-Lon) belongs to the superfamily of AAA+ proteins. It is a key member of the quality control system of the cell proteome. The enzyme degrades abnormal and defective polypeptides, as well as a number of r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::56fae2a31155c87fe588740be4534038
https://doi.org/10.1134/s1068162016040142
https://doi.org/10.1134/s1068162016040142
Autor:
A. A. Gainutdinov, T. V. Rotanova, A. G. Andrianova, V. A. Spiridonova, A. M. Kudzhaev, A. V. Melnichuk
Publikováno v:
Russian Journal of Bioorganic Chemistry. 41:626-630
ATP-dependent Lon protease of E. coli (Ec-Lon) is a key enzyme of the quality control system of the cell proteome. Ec-Lon subunit comprises N-terminal non-catalytic region, ATPase module and proteolytic domain (serine-lysine endopeptidase). A distinc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbba9d5bfddcce214b3a5998907f7383
https://doi.org/10.1134/s1068162015060151
https://doi.org/10.1134/s1068162015060151
Publikováno v:
Acta Naturae
Multidomain ATP-dependent Lon protease of E. coli (Ec-Lon) is one of the key enzymes of the quality control system of the cellular proteome. A recombinant form of Ec-Lon with deletion of the inserted characteristic α-helical HI(CC) domain (Lon-dHI(C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c7155fb592676c62c415ba4720b00e99
https://pubmed.ncbi.nlm.nih.gov/28740729
https://pubmed.ncbi.nlm.nih.gov/28740729
Publikováno v:
Russian Journal of Bioorganic Chemistry. 39:268-282
Homooligomeric LonA proteases are the key components of the protein quality control system in bacteria and eukaryotes. Domain organization of the common pool of LonA proteases is determined by comparative analysis of primary and secondary structures
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::673a30fbed19b8208cb00f2be81cbc14
https://doi.org/10.1134/s1068162013030114
https://doi.org/10.1134/s1068162013030114