Cysteine-rich protein 2 accelerates actin filament cluster formation.

Autor: Takanori Kihara, Yasunobu Sugimoto, Satoko Shinohara, Shunpei Takaoka, Jun Miyake

Publikováno v: PLoS ONE, Vol 12, Iss 8, p e0183085 (2017)

Filamentous actin (F-actin) forms many types of structures and dynamically regulates cell morphology and movement, and plays a mechanosensory role for extracellular stimuli. In this study, we determined that the smooth muscle-related transcription fa

Externí odkaz: https://doaj.org/article/bf3ded7a8f8741d88a9ac6247594ce5b

Head-head interactions of resting myosin crossbridges in intact frog skeletal muscles, revealed by synchrotron x-ray fiber diffraction.

Autor: Kanji Oshima, Yasunobu Sugimoto, Thomas C Irving, Katsuzo Wakabayashi

Publikováno v: PLoS ONE, Vol 7, Iss 12, p e52421 (2012)

The intensities of the myosin-based layer lines in the x-ray diffraction patterns from live resting frog skeletal muscles with full thick-thin filament overlap from which partial lattice sampling effects had been removed were analyzed to elucidate th

Externí odkaz: https://doaj.org/article/0dd5a09797e744e09a31bc0652705d18

Multimerization of small G-protein H-Ras induced by chemical modification at hyper variable region with caged compound

Autor: Shinsaku Maruta, Daiki Morita, Makoto Miyata, Seigo Iwata, Yuhei O Tahara, Yasunobu Sugimoto, Rufiat Nahar

Publikováno v: The Journal of Biochemistry. 171:215-225

The lipid-anchored small G protein Ras is a central regulator of cellular signal transduction processes, thereby functioning as a molecular switch. Ras forms a nanocluster on the plasma membrane by modifying lipids in the hypervariable region (HVR) a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fce50d52db00de87ecd586b8aad84a00
https://doi.org/10.1093/jb/mvab120

Dynamic Properties of Human α-Synuclein Related to Propensity to Amyloid Fibril Formation

Autor: Tatsuhito Matsuo, Kaoru Shibata, Tomoharu Matsumoto, Fumiaki Kono, Satoru Fujiwara, Yasunobu Sugimoto, Akihiro Narita

Publikováno v: Journal of Molecular Biology. 431:3229-3245

α-Synuclein (αSyn) is an intrinsically disordered protein that can form amyloid fibrils. Fibrils of αSyn are implicated with the pathogenesis of Parkinson's disease and other synucleinopathies. Elucidating the mechanism of fibril formation of αSy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08f1298d497083967b472bf3d2297385
https://doi.org/10.1016/j.jmb.2019.05.047

Infrared Laser-Induced Amyloid Fibril Dissociation: A Joint Experimental/Theoretical Study on the GNNQQNY Peptide

Autor: Nobuyuki Sugiyama, Yasunobu Sugimoto, Takayasu Kawasaki, Koichi Tsukiyama, Viet Hoang Man, Phuong H. Nguyen, Junmei Wang, Philippe Derreumaux, Hiroko Yamamoto

Publikováno v: Journal of Physical Chemistry B
Journal of Physical Chemistry B, American Chemical Society, 2020, 124, pp.6266-6277. ⟨10.1021/acs.jpcb.0c05385⟩
Journal of Physical Chemistry B, American Chemical Society, 2020, 124 (29), pp.6266-6277. ⟨10.1021/acs.jpcb.0c05385⟩

Neurodegenerative diseases are usually characterized by plaques made of well-ordered aggregates of distinct amyloid proteins. Dissociating these very stable amyloid plaques is a critical clinical issue. In this study, we present a joint mid-infrared

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd835d5a1dd4841fa3318e0481aeab5f
https://hal.archives-ouvertes.fr/hal-03013476/file/manuscript_revised.pdf