Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Anastasia V. Pivovarova"'
Autor:
Tatiana B. Eronina, Valeriya V. Mikhaylova, Natalia A. Chebotareva, Sergey Y. Kleymenov, Anastasia V. Pivovarova, Boris I. Kurganov
Publikováno v:
International Journal of Biological Macromolecules. 203:406-416
Chemical chaperones are a class of small molecules, which enhance protein stability, folding, inhibit protein aggregation, and are used for long-term storage of therapeutic proteins. The combined action of chemical chaperones trehalose, betaine and l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7e6735bd99fc06cd47cb6007986d3fc
https://doi.org/10.1016/j.ijbiomac.2022.01.106
https://doi.org/10.1016/j.ijbiomac.2022.01.106
Autor:
Sergey Yu. Kleymenov, Alexander M. Matyushenko, D. V. Shchepkin, Galina V. Kopylova, Anastasia V. Pivovarova, Victoria V. Nefedova, Valentina Y. Berg, Sergey Y. Bershitsky, Dmitrii I. Levitsky
Publikováno v:
FASEB journal : official publication of the Federation of American Societies for Experimental BiologyREFERENCES. 34(10)
Several congenital myopathies of slow skeletal muscles are associated with mutations in the tropomyosin (Tpm) TPM3 gene. Tropomyosin is an actin-binding protein that plays a crucial role in the regulation of muscle contraction. Two Tpm isoforms, γ (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80db2efaa9b046589c61b2a216e15e11
https://pubmed.ncbi.nlm.nih.gov/32797717
https://pubmed.ncbi.nlm.nih.gov/32797717
Autor:
Galina V. Kopylova, Alexander M. Matyushenko, Anastasia V. Pivovarova, Katerina E. Popruga, Sergey Y. Bershitsky, Dmitrii I. Levitsky, Natalya V. Artemova, D. V. Shchepkin
Publikováno v:
Biochemistry. 56(1)
Hypertrophic cardiomyopathy (HCM) is a severe heart disease caused by missense mutations in genes encoding sarcomeric proteins of cardiac muscle. Many of these mutations are identified in the gene encoding the cardiac isoform of tropomyosin (Tpm), an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1cf507ab8a124463544896919915f91
https://pubmed.ncbi.nlm.nih.gov/27983818
https://pubmed.ncbi.nlm.nih.gov/27983818
Autor:
Natalia A. Chebotareva, Anastasia V. Pivovarova, Dmitrii I. Levitsky, Pekka Lappalainen, Elena Kremneva
Publikováno v:
Biochemistry. 52:152-160
Differential scanning calorimetry (DSC) was applied to investigate the thermal unfolding of rabbit skeletal muscle G-actin in its complexes with actin-binding proteins, cofilin, twinfilin, and profilin. The results show that the effects of these prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d98067927a7c9f52f69328722fefd72
https://doi.org/10.1021/bi3012884
https://doi.org/10.1021/bi3012884
Publikováno v:
FEBS Journal. 277:3812-3822
Differential scanning calorimetry was used to investigate the thermal unfolding of actin specifically cleaved within the DNaseI-binding loop between residues Met47-Gly48 or Gly42-Val43 by two bacterial proteases, subtilisin or ECP32/grimelysin (ECP),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::23b686b0eabe8f7789d7e08c62f5d728
https://doi.org/10.1111/j.1742-4658.2010.07782.x
https://doi.org/10.1111/j.1742-4658.2010.07782.x
Autor:
Nikolai N. Sluchanko, Anastasia V. Pivovarova, Dmitrii I. Levitsky, Nikolai B. Gusev, Alim S. Seit-Nebi, Ivan S. Chernik
Publikováno v:
Archives of Biochemistry and Biophysics. 477:305-312
Effect of mutations mimicking phosphorylation on the structure of human 14-3-3zeta protein was analyzed by different methods. Mutation S58E increased intrinsic Trp fluorescence and binding of bis-ANS to 14-3-3. At low protein concentration mutation S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f318fab612385e759527ed5196a259d4
https://doi.org/10.1016/j.abb.2008.05.020
https://doi.org/10.1016/j.abb.2008.05.020
Autor:
Natalia A. Chebotareva, Nikolai B. Gusev, Dmitrii I. Levitsky, Anastasia V. Pivovarova, Ivan S. Chernik
Publikováno v:
FEBS Journal. 274:5937-5948
Previously, we have shown that the small heat shock protein with apparent molecular mass 27 kDa (Hsp27) does not affect the thermal unfolding of F-actin, but effectively prevents aggregation of thermally denatured F-actin [Pivovarova AV, Mikhailova V
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b3af6b8d055a1aa6547f2db67ccdbb19
https://doi.org/10.1111/j.1742-4658.2007.06117.x
https://doi.org/10.1111/j.1742-4658.2007.06117.x
Publikováno v:
The FEBS journal. 277(18)
Differential scanning calorimetry was used to investigate the thermal unfolding of actin specifically cleaved within the DNaseI-binding loop between residues Met47-Gly48 or Gly42-Val43 by two bacterial proteases, subtilisin or ECP32/grimelysin (ECP),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::11cdf251dc38edc88bd3f2e0371f1730
https://pubmed.ncbi.nlm.nih.gov/20718862
https://pubmed.ncbi.nlm.nih.gov/20718862
Autor:
Anastasia V. Pivovarova, Ivan S. Chernik, Denis I. Markov, Nikolai B. Gusev, Dmitrii I. Levitsky
Publikováno v:
FEBS letters. 582(10)
We applied different methods, such as turbidity measurements, dynamic light scattering, differential scanning calorimetry and co-sedimentation assay, to analyze the interaction of small heat shock protein Hsp27 with isolated myosin head (myosin subfr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36c4e4ac9d33b0363b11870660479bb8
https://pubmed.ncbi.nlm.nih.gov/18387368
https://pubmed.ncbi.nlm.nih.gov/18387368
Autor:
Anastasia V, Pivovarova, Natalia A, Chebotareva, Ivan S, Chernik, Nikolai B, Gusev, Dmitrii I, Levitsky
Publikováno v:
The FEBS journal. 274(22)
Previously, we have shown that the small heat shock protein with apparent molecular mass 27 kDa (Hsp27) does not affect the thermal unfolding of F-actin, but effectively prevents aggregation of thermally denatured F-actin [Pivovarova AV, Mikhailova V
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2a717041c4767a24fd49c20d4628c33b
https://pubmed.ncbi.nlm.nih.gov/17944945
https://pubmed.ncbi.nlm.nih.gov/17944945