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Ekaterina Kots
Ekaterina Kots
Weill Cornell Medicine, Department of Physiology & Biophysics
Подтвержден адрес электронной почты в домене med.cornell.edu
Название
Процитировано
Процитировано
Год
Localization atomic force microscopy
GR Heath, E Kots, JL Robertson, S Lansky, G Khelashvili, H Weinstein, ...
Nature 594 (7863), 385-390, 2021
1302021
Slow-binding inhibition of acetylcholinesterase by an alkylammonium derivative of 6-methyluracil: mechanism and possible advantages for myasthenia gravis treatment
AD Kharlamova, SV Lushchekina, KA Petrov, ED Kots, F Nachon, ...
Biochemical Journal 473 (9), 1225-1236, 2016
492016
Modeling the complete catalytic cycle of aspartoacylase
ED Kots, MG Khrenova, SV Lushchekina, SD Varfolomeev, BL Grigorenko, ...
The Journal of Physical Chemistry B 120 (18), 4221-4231, 2016
342016
Role of acetylcholinesterase in β-amyloid aggregation studied by accelerated molecular dynamics
SV Lushchekina, ED Kots, DA Novichkova, KA Petrov, P Masson
BioNanoScience 7, 396-402, 2017
332017
Role of protein dimeric interface in allosteric inhibition of N-acetyl-aspartate hydrolysis by human aspartoacylase
ED Kots, SV Lushchekina, SD Varfolomeev, AV Nemukhin
Journal of Chemical Information and Modeling 57 (8), 1999-2008, 2017
282017
Diversity of mechanisms in Ras–GAP catalysis of guanosine triphosphate hydrolysis revealed by molecular modeling
BL Grigorenko, ED Kots, AV Nemukhin
Organic & biomolecular chemistry 17 (19), 4879-4891, 2019
232019
Three faces of N-acetylaspartate: activator, substrate, and inhibitor of human aspartoacylase
MG Khrenova, ED Kots, SD Varfolomeev, SV Lushchekina, AV Nemukhin
The Journal of Physical Chemistry B 121 (40), 9389-9397, 2017
222017
Macrocyclic derivatives of 6-methyluracil as ligands of the peripheral anionic site of acetylcholinesterase
VE Semenov, RK Giniyatullin, SV Lushchekina, ED Kots, KA Petrov, ...
MedChemComm 5 (11), 1729-1735, 2014
162014
Molecular determinants of pH sensing in the proton-activated chloride channel
J Osei-Owusu, E Kots, Z Ruan, L Mihaljević, KH Chen, A Tamhaney, X Ye, ...
Proceedings of the National Academy of Sciences 119 (31), e2200727119, 2022
152022
BTG1 mutation yields supercompetitive B cells primed for malignant transformation
C Mlynarczyk, M Teater, J Pae, CR Chin, L Wang, T Arulraj, D Barisic, ...
Science 379 (6629), eabj7412, 2023
122023
Aspartoacylase: a central nervous system enzyme. Structure, catalytic activity and regulation mechanisms
ED Kots, MG Khrenova, AV Nemukhin, SD Varfolomeev
Russian Chemical Reviews 88 (1), 1, 2019
112019
Molecular polymorphism of human enzymes as the basis of individual sensitivity to drugs. supercomputer-assisted modeling as a tool for analysis of structural changes and …
SD Varfolomeev, SV Lushchekina, AV Nemukhin, AM Kulakova, ED Kots, ...
Russian Chemical Bulletin 65, 1592-1607, 2016
112016
Allosteric Control of N-Acetyl-Aspartate Hydrolysis by the Y231C and F295S Mutants of Human Aspartoacylase
ED Kots, MG Khrenova, AV Nemukhin
Journal of Chemical Information and Modeling 59 (5), 2299-2308, 2018
92018
The allosteric mechanism leading to an open-groove lipid conductive state of the TMEM16F scramblase
G Khelashvili, E Kots, X Cheng, MV Levine, H Weinstein
Communications Biology 5 (1), 990, 2022
82022
Modeling of the glycine tripeptide cyclization in the Ser65Gly/Tyr66Gly mutant of green fluorescent protein
BL Grigorenko, ED Kots, AI Krylov, AV Nemukhin
Mendeleev Communications 29 (2), 187-189, 2019
82019
Supercomputer technologies for structural-kinetic study of mechanisms of enzyme catalysis: A quantum-chemical description of aspartoacylase catalysis
SD Varfolomeev, ED Kots, MG Khrenova, SV Lushchekina, AV Nemukhin
Doklady Physical Chemistry 474, 89-92, 2017
82017
Reaction Mechanism of Guanosine Triphosphate Hydrolysis by the Vision-Related Protein Complex Arl3–RP2
MG Khrenova, ED Kots, AV Nemukhin
The Journal of Physical Chemistry B 120 (16), 3873-3879, 2016
72016
Conformational transitions in BTG1 antiproliferative protein and their modulation by disease mutants
E Kots, C Mlynarczyk, A Melnick, G Khelashvili
Biophysical Journal 121 (19), 3753-3764, 2022
52022
Simulation of pH-Dependent Conformational Transitions in Membrane Proteins: The CLC-ec1 Cl/H+ Antiporter
E Kots, DM Shore, H Weinstein
Molecules 26 (22), 6956, 2021
42021
An equilibrium constant pH molecular dynamics method for accurate prediction of pH-dependence in protein systems: Theory and application
E Kots, DM Shore, H Weinstein
bioRxiv, 2020.11. 23.394015, 2020
42020
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