S. Kleymenov

发表

The mechanism of thermal aggregation of glutamate dehydrogenase. The effect of chemical chaperones.

N. Chebotareva, B. Kurganov, N. Sluchanko, 2022, Biochimie.

The dynamics of mass growth and oxygen consumption in ontogenesis of the newt Pleurodeles waltl: 3. The postlarval period

T. Alekseeva, S. Kleymenov, I. Vladimirova, 2017, Biology Bulletin.

Quantification of anti-aggregation activity of UV-irradiated α-crystallin.

B. Kurganov, K. Muranov, V. Borzova, 2015, International journal of biological macromolecules.

Mechanism of aggregation of UV-irradiated β(L)-crystallin.

M. A. Ostrovsky, B. Kurganov, K. Muranov, 2011, Experimental eye research.

Thermal denaturation and aggregation of apoform of glycogen phosphorylase b. Effect of crowding agents and chaperones

N. Chebotareva, B. Kurganov, V. F. Makeeva, 2014, Biopolymers.

Kinetics of aggregation of UV-irradiated glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle. Effect of agents possessing chaperone-like activity.

N. Chebotareva, B. Kurganov, R. Asryants, 2012, Biophysical chemistry.

Effect of GroEL on thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle.

I. Naletova, V. Muronetz, N. Chebotareva, 2010, Macromolecular bioscience.

A thermal after-effect of UV irradiation of muscle glycogen phosphorylase b

N. Chebotareva, B. Kurganov, T. B. Eronina, 2017, PloS one.

Heat-induced conformational changes of TET peptidase from crenarchaeon Desulfurococcus kamchatkensis

V. Popov, T. Petrova, E. Slutskaya, 2015, European Biophysics Journal.

Mechanisms of disturbance of the contractile function of slow skeletal muscles induced by myopathic mutations in the tropomyosin TPM3 gene

D. Levitsky, S. Kleymenov, V. Berg, 2020, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Nanocontainer derived from silkworm carotenoprotein for carotenoid extraction and presentation in biotechnology and biomedical applications

T. Friedrich, K. Boyko, A. Moysenovich, 2022, bioRxiv.

Effects of myopathy-causing mutations R91P and R245G in the TPM3 gene on structural and functional properties of slow skeletal muscle tropomyosin.

A. Tsaturyan, D. Levitsky, S. Kleymenov, 2020, Biochemical and biophysical research communications.

Effect of alpha-crystallin on thermostability of mitochondrial aspartate aminotransferase.

B. Kurganov, M. Sholukh, K. Muranov, 2009, International journal of biological macromolecules.

A change in the aggregation pathway of bovine serum albumin in the presence of arginine and its derivatives

B. Kurganov, V. Borzova, S. Kleymenov, 2017, Scientific Reports.

Structural basis for the ligand promiscuity of the neofunctionalized, carotenoid-binding fasciclin domain protein AstaP

K. Mineev, S. Goncharuk, E. Maksimov, 2022, bioRxiv.

Kinetics of Thermal Denaturation and Aggregation of Bovine Serum Albumin

N. Chebotareva, B. Kurganov, K. Muranov, 2016, PloS one.

A change in the pathway of dithiothreitol-induced aggregation of bovine serum albumin in the presence of polyamines and arginine.

B. Kurganov, V. Borzova, S. Kleymenov, 2017, International journal of biological macromolecules.

First Crystal Structure of Bacterial Oligopeptidase B in an Intermediate State: The Roles of the Hinge Region Modification and Spermine

A. G. Mikhailova, I. Kuranova, V. Timofeev, 2021, Biology.

Thermal unfolding of various human non-muscle isoforms of tropomyosin.

P. Datskevich, D. Levitsky, S. Kleymenov, 2019, Biochemical and biophysical research communications.

Thermal unfolding of homodimers and heterodimers of different skeletal-muscle isoforms of tropomyosin.

D. Levitsky, S. Kleymenov, Denis S Susorov, 2018, Biophysical chemistry.

Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3

K. Boyko, V. Popov, T. Rakitina, 2016, Scientific Reports.

Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold

E. Bocharov, V. Timofeev, T. Rakitina, 2018, Journal of biomolecular structure & dynamics.

Does the crowded cell-like environment reduce the chaperone-like activity of α-crystallin?

N. Chebotareva, B. Kurganov, V. F. Makeeva, 2011, Biochemistry.

Effect of 2-hydroxypropyl-β-cyclodextrin on thermal stability and aggregation of glycogen phosphorylase b from rabbit skeletal muscle.

N. Chebotareva, B. Kurganov, V. F. Makeeva, 2010, Biopolymers.

Structural and Functional Peculiarities of Cytoplasmic Tropomyosin Isoforms, the Products of TPM1 and TPM4 Genes

D. Levitsky, S. Kleymenov, V. Nefedova, 2021, International journal of molecular sciences.

Endogenous biorhythms of the mass specific rate of oxygen consumption in individual development of Lymnaea stagnalis (Lymnaeidae, Gastropoda)

A. Zotin, S. Kleymenov, 2013, Biology Bulletin.

Combined action of chemical chaperones on stability, aggregation and ologomeric state of muscle glycogen phosphorylase b.

N. Chebotareva, B. Kurganov, T. B. Eronina, 2022, International journal of biological macromolecules.

Effect of arginine on stability and aggregation of muscle glycogen phosphorylase b.

N. Chebotareva, B. Kurganov, T. B. Eronina, 2020, International journal of biological macromolecules.

Effect of proline on thermal inactivation, denaturation and aggregation of glycogen phosphorylase b from rabbit skeletal muscle.

N. Chebotareva, B. Kurganov, V. F. Makeeva, 2009, Biophysical chemistry.

De Novo Asp219Val Mutation in Cardiac Tropomyosin Associated with Hypertrophic Cardiomyopathy

E. Zaklyazminskaya, A. Tsaturyan, D. Levitsky, 2022, International journal of molecular sciences.

The dynamics of mass growth and oxygen consumption in ontogenesis of the newt Pleurodeles waltl: 3. The postlarval period

T. Alekseeva, S. Kleymenov, I. Vladimirova, 2017, Biology Bulletin.

Engineering catalytic properties and thermal stability of plant formate dehydrogenase by single-point mutations.

A. A. Alekseeva, V. Tishkov, S. Kleymenov, 2012, Protein engineering, design & selection : PEDS.

Counterbalance of Stability and Activity Observed for Thermostable Transaminase from Thermobaculum terrenum in the Presence of Organic Solvents

E. Y. Bezsudnova, V. Popov, T. Petrova, 2020, Catalysts.

Heat-induced conformational changes of TET peptidase from crenarchaeon Desulfurococcus kamchatkensis

V. Popov, T. Petrova, E. Slutskaya, 2015, European Biophysics Journal.

A Protein Aggregation Based Test for Screening of the Agents Affecting Thermostability of Proteins

B. Kurganov, R. Asryants, V. Borzova, 2011, PloS one.

Effect of Additional Amino Acid Replacements on the Properties of Multi-point Mutant Bacterial Formate Dehyderogenase PseFDH SM4S

D. L. Atroshenko, P. D. Parshin, V. Tishkov, 2022, Acta naturae.

Tropomyosin pseudo-phosphorylation can rescue the effects of cardiomyopathy-associated mutations.

A. Tsaturyan, N. Koubassova, D. Levitsky, 2020, International journal of biological macromolecules.

Structural and functional properties of αβ-heterodimers of tropomyosin with myopathic mutations Q147P and K49del in the β-chain.

D. Levitsky, S. Kleymenov, V. Berg, 2019, Biochemical and biophysical research communications.

Effect of Neurodegenerative Mutations in the NEFL Gene on Thermal Denaturation of the Neurofilament Light Chain Protein

N. Chebotareva, D. Levitsky, S. Kleymenov, 2023, Biochemistry (Moscow).

Effect of His6-tag Position on the Expression and Properties of Phenylacetone Monooxygenase from Thermobifida fusca

D. L. Atroshenko, P. D. Parshin, A. A. Pometun, 2020, Biochemistry (Moscow).

Role of a Structurally Equivalent Phenylalanine Residue in Catalysis and Thermal Stability of Formate Dehydrogenases from Different Sources

A. A. Alekseeva, V. Tishkov, S. Kleymenov, 2015, Biochemistry (Moscow).

Structural and Functional Properties of Tropomyosin Isoforms Tpm4.1 and Tpm2.1

D. Levitsky, S. Kleymenov, V. Nefedova, 2023, Biochemistry (Moscow).

Comparison of Thermal Stability of New Formate Dehydrogenases by Differential Scanning Calorimetry

S. A. Zarubina, P. D. Parshin, A. A. Pometun, 2018, Moscow University Chemistry Bulletin.

Structural basis for the carotenoid binding and transport function of a START domain.

T. Friedrich, K. Boyko, A. Moysenovich, 2022, Structure.

Dual effect of arginine on aggregation of phosphorylase kinase.

N. Chebotareva, B. Kurganov, N. Sluchanko, 2014, International journal of biological macromolecules.

Kinetic regime of Ca2+ and Mg2+-induced aggregation of phosphorylase kinase at 40°.

N. Chebotareva, B. Kurganov, T. B. Eronina, 2019, International journal of biological macromolecules.

Novel Mutation Glu98Lys in Cardiac Tropomyosin Alters Its Structure and Impairs Myocardial Relaxation

I. Katrukha, E. Zaklyazminskaya, A. Tsaturyan, 2023, International journal of molecular sciences.

Structural and Functional Properties of Kappa Tropomyosin

A. Tsaturyan, N. Koubassova, D. Levitsky, 2023, International journal of molecular sciences.

Chimeric versus isolated proteins: Biochemical characterization of the NADP+-dependent formate dehydrogenase from Pseudomonas sp. 101 fused with the Baeyer-Villiger monooxygenase from Thermobifida fusca.

F. Secundo, V. Tishkov, S. Kleymenov, 2023, International journal of biological macromolecules.