Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Maria V. Sudnitsyna"'
Autor:
Maria V. Sudnitsyna, Nikolai B. Gusev
Publikováno v:
Cell Stress and Chaperones. 24:419-426
This study analyzed the interaction of commercial monoclonal anti-methylglyoxal antibodies that predominantly recognize argpyrimidine with unmodified and modified model proteins and small heat shock proteins. These antibodies specifically recognize m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71c3404c09a133f64669c956a4c26194
https://doi.org/10.1007/s12192-019-00975-3
https://doi.org/10.1007/s12192-019-00975-3
Publikováno v:
Cell Stress Chaperones
Charcot-Marie-Tooth (CMT) disease is major hereditary neuropathy. CMT has been linked to mutations in a range of proteins, including the small heat shock protein HspB1. Here we review the properties of several HspB1 mutants associated with CMT. In vi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e493400478c4b8b3392cb6de72b05e34
https://pubmed.ncbi.nlm.nih.gov/32301006
https://pubmed.ncbi.nlm.nih.gov/32301006
Autor:
Vladislav M Shatov, Lydia K. Muranova, Maria V. Sudnitsyna, Nikolai B. Gusev, A S Ryzhavskaya
Publikováno v:
Biochemistry. Biokhimiia. 84(11)
The review discusses the role of small heat shock proteins (sHsps) in human neurodegenerative disorders, such as Charcot-Marie-Tooth disease (CMT), Parkinson's and Alzheimer's diseases, and different forms of tauopathies. The effects of CMT-associate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d319e13ca80828ec1f0d99a67c56c6c1
https://pubmed.ncbi.nlm.nih.gov/31760916
https://pubmed.ncbi.nlm.nih.gov/31760916
Autor:
Victoria V. Nefedova, A S Ryzhavskaya, Nikolai B. Gusev, Lydia K. Muranova, Maria V. Sudnitsyna
Publikováno v:
Biochemistry (Moscow). 80:1734-1747
Classification of small heat shock proteins (sHsp) is presented and processes regulated by sHsp are described. Symptoms of hereditary distal neuropathy are described and the genes whose mutations are associated with development of this congenital dis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::225e6bc7740e060a199516f439416ccb
https://doi.org/10.1134/s000629791513009x
https://doi.org/10.1134/s000629791513009x
Publikováno v:
Biochemistry. Biokhimiia. 83(10)
The review is dedicated to phosphorylation of αB-crystallin (HspB5), one of ubiquitously expressed small heat shock proteins. We describe the structure and properties of αB-crystallin and protein kinases involved in its phosphorylation in different
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc37ff289a9d1b98d05e707b87180880
https://pubmed.ncbi.nlm.nih.gov/30472957
https://pubmed.ncbi.nlm.nih.gov/30472957
The interaction of human small heat shock protein HspB1, its point mutants associated with distal hereditary motor neuropathy, and three other small heat shock proteins (HspB5, HspB6, HspB8) with the light component of neurofilaments (NFL) was analyz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e50a4b274759d60a39f3077160c1ac3
https://europepmc.org/articles/PMC5465025/
https://europepmc.org/articles/PMC5465025/
Publikováno v:
Archives of Biochemistry and Biophysics. 538:16-24
Some properties of G84R and L99M mutants of HspB1 associated with peripheral distal neuropathies were investigated. Homooligomers formed by these mutants are larger than those of the wild type HspB1. Large oligomers of G84R and L99M mutants have comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a45eb75eb97f2a9093b06680458ccac4
https://doi.org/10.1016/j.abb.2013.07.028
https://doi.org/10.1016/j.abb.2013.07.028
Autor:
Alfred A. Antson, Maria V. Sudnitsyna, Natalya V. Artemova, Nikolai N. Sluchanko, Nikolai B. Gusev, Dmitrii I. Levitsky, Irina V. Safenkova
Publikováno v:
Biochemistry
Members of the 14-3-3 eukaryotic protein family predominantly function as dimers. The dimeric form can be converted into monomers upon phosphorylation of Ser(58) located at the subunit interface. Monomers are less stable than dimers and have been con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e8850c41651a957e643a84058926fdd
https://doi.org/10.1021/bi300674e
https://doi.org/10.1021/bi300674e
Publikováno v:
Current Protein & Peptide Science. 13:76-85
Small heat shock proteins (sHsp) form a large ubiquitous family of proteins expressed in all phyla of living organisms. The members of this family have low molecular masses (13-43 kDa) and contain a conservative α-crystallin domain. This domain (abo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b3882ef9addd4e860e24c995078a9a5
https://doi.org/10.2174/138920312799277875
https://doi.org/10.2174/138920312799277875
Autor:
Maria V. Sudnitsyna, Alfred A. Antson, Alim S. Seit-Nebi, Nikolai N. Sluchanko, Nikolai B. Gusev
Publikováno v:
Biochemistry. 50:9797-9808
Dimers formed by seven isoforms of the human 14-3-3 protein participate in multiple cellular processes. The dimeric form has been extensively characterized; however, little is known about the structure and properties of the monomeric form of 14-3-3.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b51ef24dc937ebeb6b4f204e224bf2ad
https://doi.org/10.1021/bi201374s
https://doi.org/10.1021/bi201374s