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Nikolai N. Sluchanko
Nikolai N. Sluchanko
A.N.Bach Institute of biochemistry, Federal Research Center of Biotechnology of RAS
在 york.ac.uk 的电子邮件经过验证
标题
引用次数
引用次数
年份
Structural basis for the interaction of a human small heat shock protein with the 14-3-3 universal signaling regulator
NN Sluchanko, S Beelen, AA Kulikova, SD Weeks, AA Antson, NB Gusev, ...
Structure 25 (2), 305-316, 2017
1252017
Moonlighting chaperone‐like activity of the universal regulatory 14‐3‐3 proteins
NN Sluchanko, NB Gusev
The FEBS journal 284 (9), 1279-1295, 2017
1012017
Oligomeric structure of 14-3-3 protein: what do we know about monomers?
NN Sluchanko, NB Gusev
FEBS letters 586 (24), 4249-4256, 2012
1012012
The signaling state of orange carotenoid protein
EG Maksimov, EA Shirshin, NN Sluchanko, DV Zlenko, EY Parshina, ...
Biophysical journal 109 (3), 595-607, 2015
912015
14-3-3 proteins and regulation of cytoskeleton
NN Sluchanko, NB Gusev
Biochemistry (Moscow) 75, 1528-1546, 2010
892010
The mechanism of SARS-CoV-2 nucleocapsid protein recognition by the human 14-3-3 proteins
KV Tugaeva, DEDP Hawkins, JLR Smith, OW Bayfield, DS Ker, ...
Journal of Molecular Biology 433 (8), 166875, 2021
732021
A comparative study of three signaling forms of the orange carotenoid protein
EG Maksimov, M Moldenhauer, EA Shirshin, EA Parshina, NN Sluchanko, ...
Photosynthesis Research 130, 389-401, 2016
732016
Structural and functional effects of two stabilizing substitutions, D137L and G126R, in the middle part of α‐tropomyosin molecule
AM Matyushenko, NV Artemova, DV Shchepkin, GV Kopylova, ...
The FEBS journal 281 (8), 2004-2016, 2014
702014
The photocycle of orange carotenoid protein conceals distinct intermediates and asynchronous changes in the carotenoid and protein components
EG Maksimov, NN Sluchanko, YB Slonimskiy, EA Slutskaya, AV Stepanov, ...
Scientific reports 7 (1), 15548, 2017
692017
Assembly of photoactive orange carotenoid protein from its domains unravels a carotenoid shuttle mechanism
M Moldenhauer, NN Sluchanko, D Buhrke, DV Zlenko, NN Tavraz, ...
Photosynthesis Research 133, 327-341, 2017
682017
The purple Trp288Ala mutant of Synechocystis OCP persistently quenches phycobilisome fluorescence and tightly interacts with FRP
NN Sluchanko, KE Klementiev, EA Shirshin, GV Tsoraev, T Friedrich, ...
Biochimica et Biophysica Acta (BBA)-Bioenergetics 1858 (1), 1-11, 2017
672017
Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms
G Gogl, KV Tugaeva, P Eberling, C Kostmann, G Trave, NN Sluchanko
Nature communications 12 (1), 1677, 2021
652021
Intrinsic disorder associated with 14-3-3 proteins and their partners
NN Sluchanko, DM Bustos
Progress in molecular biology and translational science 166, 19-61, 2019
552019
Dissection of the deep-blue autofluorescence changes accompanying amyloid fibrillation
TN Tikhonova, NR Rovnyagina, AY Zherebker, NN Sluchanko, ...
Archives of biochemistry and biophysics 651, 13-20, 2018
542018
Association of multiple phosphorylated proteins with the 14-3-3 regulatory hubs: problems and perspectives
NN Sluchanko
Journal of molecular biology 430 (1), 20-26, 2018
542018
Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3ζ
NN Sluchanko, AS Seit-Nebi, NB Gusev
FEBS letters 583 (17), 2739-2742, 2009
512009
Effect of mutations mimicking phosphorylation on the structure and properties of human 14-3-3ζ
NN Sluchanko, IS Chernik, AS Seit-Nebi, AV Pivovarova, DI Levitsky, ...
Archives of biochemistry and biophysics 477 (2), 305-312, 2008
512008
Monomeric 14-3-3ζ has a chaperone-like activity and is stabilized by phosphorylated HspB6
NN Sluchanko, NV Artemova, MV Sudnitsyna, IV Safenkova, AA Antson, ...
Biochemistry 51 (31), 6127-6138, 2012
492012
Properties of the monomeric form of human 14-3-3ζ protein and its interaction with tau and HspB6
NN Sluchanko, MV Sudnitsyna, AS Seit-Nebi, AA Antson, NB Gusev
Biochemistry 50 (45), 9797-9808, 2011
492011
Probable participation of 14-3-3 in tau protein oligomerization and aggregation
NN Sluchanko, NB Gusev
Journal of Alzheimer's disease 27 (3), 467-476, 2011
492011
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