Dmitrii I. Levitsky - Concepedia

Author

Dmitrii I. Levitsky

A N Bach Institute of Biochemistry ORCID

Also Known As

D I Levitsky, D LEVITSKY, D Levitsky, D. I Levitsky, D. I. Levitsky, D. Levitsky, D.I. Levitsky, Dmitrii I. Levitsky, Dmitrii I Levitsky, Dmitrii I. LEVITSKY

126

Publications

2.4K

Citations

H-Index

Concepts

All Affiliations

A N Bach Institute of Biochemistry Lomonosov Moscow State University Russian Academy of Sciences Institute of Immunology and Physiology Koltzov Institute of Developmental Biology

About

Dmitrii I. Levitsky is an author at A N Bach Institute of Biochemistry specializing in medicine, molecular biology, and cytoskeleton.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	18	21	1.1K
2	Natural Sciences	13	15	546
3	Biochemistry	11	13	764
4	Engineering	1	1	22
5	Health Sciences	1	1	52

Dmitrii I. Levitsky

Publications

1.9K

Citations

H-Index

Page 1

	Year	Citations
Function of the sarcoplasmic reticulum and expression of its Ca2(+)-ATPase gene in pressure overload-induced cardiac hypertrophy in the rat. D. de la Bastie, Dmitrii I. Levitsky, L. Rappaport, Circulation Research Cardiac MuscleHeart FailureSarcoplasmic ReticulumCellular PhysiologyCardiology	1990	341
Effects of Two Familial Hypertrophic Cardiomyopathy Mutations in α-Tropomyosin, Asp175Asn and Glu180Gly, on the Thermal Unfolding of Actin-Bound Tropomyosin Elena Kremneva, Sabrina E. Boussouf, Olga Nikolaeva, Biophysical Journal Thermal UnfoldingCardiomyopathyMolecular PhysiologyProtein FoldingNatural Sciences	2004	87
Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin Anastasiya V. Pivovarova, V. V. Mikhailova, Ivan S. Chernik, Biochemical and Biophysical Research Communications Protein ChemistryProtein FunctionProtein AssemblyBiochemistryProtein Folding	2005	85
Small heat shock protein Hsp27 prevents heat‐induced aggregation of F‐actin by forming soluble complexes with denatured actin Anastasia V. Pivovarova, Natalia A. Chebotareva, Ivan S. Chernik, FEBS Journal	2007	76
Mechanism of Chaperone-like Activity. Suppression of Thermal Aggregation of β<sub>L</sub>-Crystallin by α-Crystallin Helen A. Khanova, Kira A. Markossian, Boris I. Kurganov, Biochemistry	2005	70
Mechanism of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-phosphate Dehydrogenase Kira A. Markossian, Helen A. Khanova, S. Yu. Kleimenov, Biochemistry	2006	62
Structural and functional effects of two stabilizing substitutions, D137L and G126R, in the middle part of α‐tropomyosin molecule Alexander M. Matyushenko, Natalia V. Artemova, Daniil V. Shchepkin, FEBS Journal Muscle FunctionAldo-keto ReductaseMolecular BiologyCytoskeletonMechanotransduction	2014	59
Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase Helen A. Khanova, Kira A. Markossian, S. Yu. Kleimenov, Biophysical Chemistry Protein ChemistryEnergy MetabolismMolecular PhysiologyCellular EnzymologyBiochemistry	2006	52
Effects of nucleotide binding on thermal transitions and domain structure of myosin subfragment 1 Dmitrii I. Levitsky, Valery L. Shnyrov, Nikolai V. Khvorov, European Journal of Biochemistry	1992	51
Mutations in the relay loop region result in dominant‐negative inhibition of myosin II function in <i>Dictyostelium</i> Georgios Tsiavaliaris, Setsuko Fujita‐Becker, Renu Batra, EMBO Reports Signal TransductionMolecular PhysiologyMolecular BiologyCell MotilityCytoskeleton	2002	51

Page 1