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Электронный каталог: Ryzhykau, Yu. L. - Chain-Like Supramolecular Assemblies of Inactivated Actin Oligomers Reveal a Multistage Assembly ...
Ryzhykau, Yu. L. - Chain-Like Supramolecular Assemblies of Inactivated Actin Oligomers Reveal a Multistage Assembly ...

Статья
Автор: Ryzhykau, Yu. L.
Biochemical and Biophysical Research Communications: Chain-Like Supramolecular Assemblies of Inactivated Actin Oligomers Reveal a Multistage Assembly ...
б.г.
ISBN отсутствует
Автор: Ryzhykau, Yu. L.
Biochemical and Biophysical Research Communications: Chain-Like Supramolecular Assemblies of Inactivated Actin Oligomers Reveal a Multistage Assembly ...
б.г.
ISBN отсутствует
Статья
Ryzhykau, Yu.L.
Chain-Like Supramolecular Assemblies of Inactivated Actin Oligomers Reveal a Multistage Assembly Pathway / Yu.L.Ryzhykau, A.V.Rogachev, A.I.Kuklin, [a.o.]. – Text : electronic // Biochemical and Biophysical Research Communications. – 2026. – Vol. 796. – P. 153122. – URL: https://doi.org/10.1016/j.bbrc.2025.153122. – Bibliogr.: 23.
Besides the conventional monomeric globular (G-actin) and polymeric fibrillar (F-actin) forms, actin can adopt a thermodynamically stable inactivated oligomeric state (I-actin) when it loses bound nucleotide and coordinating divalent cation under mild denaturing or stress conditions. However, the supramolecular organization of these assemblies remains poorly understood. Here, using size-exclusion chromatography coupled with small-angle X-ray scattering (SEC-SAXS) and negative-stain transmission electron microscopy (NS-TEM), we show that heat-inactivated actin (heat-I-actin) forms flat, disk-like oligomers (“beads”) that further assemble into linear, unbranched chains. SEC-SAXS reveals strongly elongated particles whose cross-sectional parameters closely match those previously established for I-actin oligomers by hydrodynamic measurements, while NS-TEM directly visualizes bead-like particles of ∼165 Å in diameter that occasionally align into unbranched chains, structures not seen for G- or F-actin. Together with previously published structural insights, these data support a multistage assembly pathway in which I-actin subunits first form dimers, then condense into flat oligomeric beads, which in turn connect into one-dimensional supramolecular chains. We discuss how such assemblies may relate to poorly characterized short oligomers of nuclear actin
Спец.(статьи,препринты) = С 332.8 - Синхротронное излучение. Лазеры на свободных электронах. Получение и использование рентгеновских лучей
Спец.(статьи,препринты) = 28.0 - Биология$
ОИЯИ = ОИЯИ (JINR)2026
Ryzhykau, Yu.L.
Chain-Like Supramolecular Assemblies of Inactivated Actin Oligomers Reveal a Multistage Assembly Pathway / Yu.L.Ryzhykau, A.V.Rogachev, A.I.Kuklin, [a.o.]. – Text : electronic // Biochemical and Biophysical Research Communications. – 2026. – Vol. 796. – P. 153122. – URL: https://doi.org/10.1016/j.bbrc.2025.153122. – Bibliogr.: 23.
Besides the conventional monomeric globular (G-actin) and polymeric fibrillar (F-actin) forms, actin can adopt a thermodynamically stable inactivated oligomeric state (I-actin) when it loses bound nucleotide and coordinating divalent cation under mild denaturing or stress conditions. However, the supramolecular organization of these assemblies remains poorly understood. Here, using size-exclusion chromatography coupled with small-angle X-ray scattering (SEC-SAXS) and negative-stain transmission electron microscopy (NS-TEM), we show that heat-inactivated actin (heat-I-actin) forms flat, disk-like oligomers (“beads”) that further assemble into linear, unbranched chains. SEC-SAXS reveals strongly elongated particles whose cross-sectional parameters closely match those previously established for I-actin oligomers by hydrodynamic measurements, while NS-TEM directly visualizes bead-like particles of ∼165 Å in diameter that occasionally align into unbranched chains, structures not seen for G- or F-actin. Together with previously published structural insights, these data support a multistage assembly pathway in which I-actin subunits first form dimers, then condense into flat oligomeric beads, which in turn connect into one-dimensional supramolecular chains. We discuss how such assemblies may relate to poorly characterized short oligomers of nuclear actin
Спец.(статьи,препринты) = С 332.8 - Синхротронное излучение. Лазеры на свободных электронах. Получение и использование рентгеновских лучей
Спец.(статьи,препринты) = 28.0 - Биология$
ОИЯИ = ОИЯИ (JINR)2026
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