Zobrazeno 1 - 10
of 37
pro vyhledávání: '"T.B. Stanishneva-Konovalova"'
Autor:
Igor A. Yaroshevich, Evgeny Pichkur, I. S. Panina, Olga Sokolova, Vladimir I. Muronetz, Aleksandra A. Mamchur, Andrei V. Moiseenko, T.B. Stanishneva-Konovalova, S. S. Kudryavtseva
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
Scientific Reports
Scientific Reports
The GroEL–GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate protein binding, folding and release. Structural met
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44ab48046cce11a7522a9349b1243289
https://doaj.org/article/accfa7162fbd4527a18ab1b47e228906
https://doaj.org/article/accfa7162fbd4527a18ab1b47e228906
Autor:
I. S. Panina, T.B. Stanishneva-Konovalova, S. S. Kudryavtseva, Evgeny Pichkur, Igor A. Yaroshevich, Aleksandra A. Mamchur, D. V. Zlenko, Olga Sokolova, Vladimir I. Muronetz
Publikováno v:
Crystallography Reports. 66:846-853
Abstract Bacterial chaperonin GroEL is a complex ring-shaped protein oligomer that promotes the folding of other proteins by encapsulating them in the cavity. There is very little structural information about the disordered C-terminal fragment of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9bbb8517eec62b0a9b4d843676fc9701
https://doi.org/10.1134/s1063774521050163
https://doi.org/10.1134/s1063774521050163
Autor:
I. S. Panina, Igor A. Yaroshevich, S. S. Kudryavtseva, Aleksandra A. Mamchur, T.B. Stanishneva-Konovalova
Publikováno v:
Lobachevskii Journal of Mathematics. 41:1502-1508
Many serious medical conditions are caused by the accumulation of amyloid aggregates in tissues and organs. One of the most well-known amyloidogenic proteins is the prion protein (PrP), which may undergo conformational change between the normal cellu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eebf57e49c04a87a809b73afcb29149e
https://doi.org/10.1134/s1995080220080119
https://doi.org/10.1134/s1995080220080119
Publikováno v:
Microscopy and Microanalysis. 26:1292-1295
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f3fdd627bf1c336bd4a40c29ad696e92
https://doi.org/10.1017/s1431927620017602
https://doi.org/10.1017/s1431927620017602
Autor:
Aleksandra A. Mamchur, Evgeny Pichkur, S. S. Kudryavtseva, Olga Sokolova, Vladimir I. Muronetz, Igor A. Yaroshevich, T.B. Stanishneva-Konovalova, I. S. Panina, Andrei V. Moiseenko
Publikováno v:
Biomedicines
Biomedicines, Vol 9, Iss 1649, p 1649 (2021)
Volume 9
Issue 11
Biomedicines, Vol 9, Iss 1649, p 1649 (2021)
Volume 9
Issue 11
The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrPC, could lead to pathogenic transformation of the latter to the aggregation-prone PrPSc for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83baf6d15fd4599b41cec034d4980c27
http://europepmc.org/articles/PMC8615626
http://europepmc.org/articles/PMC8615626
Akademický článek
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Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 87:561-568
Bin/Amphyphysin/Rvs (BAR) domain proteins form a key link between membrane remodeling and cytoskeleton dynamics. They are dimers that bind to membranes via electrostatic interactions with different preferences toward negatively charged lipids. In the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9fc29b08ddb56f70e6dd8feae4f9cee8
https://doi.org/10.1002/prot.25678
https://doi.org/10.1002/prot.25678
Autor:
Olga Sokolova, Vladimir I. Muronetz, S. S. Kudryavtseva, Evgeny Pichkur, T.B. Stanishneva-Konovalova, Igor A. Yaroshevich
Publikováno v:
Microscopy and Microanalysis. 27:1120-1121
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c6867b2b480fdc63e1bf7c2e7c00f18
https://doi.org/10.1017/s1431927621004207
https://doi.org/10.1017/s1431927621004207
Autor:
Olga Sokolova, Bruce L. Goode, Chenyu Lou, Thomas J. Rands, Luther W. Pollard, Mikael V. Garabedian, T.B. Stanishneva-Konovalova
Publikováno v:
The Journal of Cell Biology
This study shows that in vivo actin nucleation by the yeast formin Bnr1 is controlled through the coordinated effects of two distinct regulators, a stationary inhibitor (the F-BAR protein Hof1) and a mobile activator (Bud6), establishing a positive f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5170a3cf4766aad885a9dcc9c2089111
http://europepmc.org/articles/PMC6168263
http://europepmc.org/articles/PMC6168263
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
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