Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Soichiro Kitazawa"'
Autor:
Yutaro Shiramasa, Ryu Yamamoto, Norika Kashiwagi, Fuka Sasaki, Sawaka Imai, Mikihito Ike, Soichiro Kitazawa, Tomoshi Kameda, Ryo Kitahara
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-15 (2024)
Abstract Intracellular aggregation of fused in sarcoma (FUS) is associated with the pathogenesis of familial amyotrophic lateral sclerosis (ALS). Under stress, FUS forms liquid droplets via liquid–liquid phase separation (LLPS). Two types of wild-t
Externí odkaz:
https://doaj.org/article/040f8a8d75f8403595f3310bee45706c
Publikováno v:
Molecules, Vol 22, Iss 9, p 1414 (2017)
Rational mutation of proteins based on their structural and dynamic characteristics is a useful strategy for amplifying specific fluctuations in proteins. Here, we show the effects of mutation on the conformational fluctuations and thermodynamic stab
Externí odkaz:
https://doaj.org/article/1252beeb4b044c54a0846a426c9ee44d
Autor:
Keiji Kitamura, Ayano Oshima, Fuka Sasaki, Yutaro Shiramasa, Ryu Yamamoto, Tomoshi Kameda, Soichiro Kitazawa, Ryo Kitahara
Publikováno v:
Journal of Physical Chemistry Letters; 8/1/2024, Vol. 15 Issue 30, p7620-7627, 8p
Autor:
Shujie Li, Takuya Yoshizawa, Yutaro Shiramasa, Mako Kanamaru, Fumika Ide, Keiji Kitamura, Norika Kashiwagi, Naoya Sasahara, Soichiro Kitazawa, Ryo Kitahara
Publikováno v:
Physical chemistry chemical physics : PCCP. 24(32)
The liquid-to-solid phase transition of FUS liquid condensates were accelerated in the aberrant LLPS (HP-LLPS). Arginine, dopamine, and pyrocatechol suppress the formation of the aberrant LLPS more strongly than the normal LLPS (LP-LLPS).
Autor:
Shujie Li, Yutaro Shiramasa, Keiji Kitamura, Norika Kashiwagi, Soichiro Kitazawa, Ryo Kitahara
Publikováno v:
Biophysical Journal. 122:487a
Publikováno v:
The journal of physical chemistry. B. 126(9)
Conformational fluctuation, namely, protein interconversion between different conformations, is crucial to protein function. Outer surface protein A (OspA), comprising N- and C-terminal globular domains linked by a central β-sheet, is expressed on t
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 88:1423-1433
Structural characterization of alternatively folded and partially disordered protein conformations remains challenging. Outer surface protein A (OspA) is a pivotal protein in Borrelia infection, which is the etiological agent of Lyme disease. OspA ex
Autor:
Tomoshi Kameda, Ryo Kitahara, Shun Sakuraba, Soichiro Kitazawa, Takuro Wakamoto, Takahiro Kawamura
Publikováno v:
Biophysical Journal. 112:1820-1828
Internal cavities in proteins produce conformational fluctuations and enable the binding of small ligands. Here, we report a NMR analysis of O2-binding sites by O2-induced paramagnetic relaxation enhancements (PREs) on amide groups of proteins in sol
Autor:
Masashi Fukutome, Chieko Koike, Ryo Kitahara, Tesshu Hori, Hiroki Matsushima, Katsunori Kitano, Satoru Moritoh, Kensuke Kobayashi, Chiseto Maejima, Soichiro Kitazawa, Kenta Kobayashi
Publikováno v:
Biochemical and biophysical research communications. 515(1)
Adeno-associated virus (AAV) has been studied as a safe delivery tool for gene therapy of retinal blinding diseases such as Leber's congenital amaurosis (LCA). The tropism of recombinant AAV (rAAV) including its specificity and efficiency in targetin