Zobrazeno 1 - 10
of 151
pro vyhledávání: '"Mitsuhiro Hirai"'
Publikováno v:
Molecules, Vol 28, Iss 18, p 6555 (2023)
Molecular crowding environments play a crucial role in understanding the mechanisms of biological reactions. Inside living cells, a diverse array of molecules coexists within a volume fraction ranging from 10% to 30% v/v. However, conventional spectr
Externí odkaz:
https://doaj.org/article/0fec2b90d20a46d88377b78810e87a0f
Autor:
Mitsuhiro Hirai, Satoshi Ajito, Tatsuo Iwasa, Durige Wen, Noriyuki Igarashi, Nobutaka Shimizu
Publikováno v:
ACS Omega, Vol 5, Iss 19, Pp 10815-10825 (2020)
Externí odkaz:
https://doaj.org/article/53045910bbbc4a2088247d5a69c0278c
Publikováno v:
Protein Sci
Pigeon iron-sulfur (Fe-S) cluster assembly 1 homolog (clISCA1) is a target protein for research into the biomagnetoreception mechanism, as the clCRY4/clISCA1 oligomer, a complex composed of the columnar clISCA1 oligomer and the magnetosensor candidat
Autor:
Satoshi Ajito, Mitsuhiro Hirai, Noriyuki Igarashi, Tatsuo Iwasa, Durige Wen, Nobutaka Shimizu
Publikováno v:
ACS Omega
ACS Omega, Vol 5, Iss 19, Pp 10815-10825 (2020)
ACS Omega, Vol 5, Iss 19, Pp 10815-10825 (2020)
Organisms with tolerance to extreme environmental conditions (cryptobiosis) such as desiccation and freezing are known to accumulate stress proteins and/or sugars. Trehalose, a disaccharide, has received considerable attention in the context of crypt
Autor:
Noboru Ohta, Noriyuki Igarashi, Rika Kawai-Hirai, Nobutaka Shimizu, Satoshi Ajito, Kosuke Takahashi, Mitsuhiro Hirai, Durige Wen, Tatsuo Iwasa, Xing Li
Publikováno v:
The Journal of Physical Chemistry B. 123:3421-3429
Ultrafine bubbles (UFBs) are defined as small gas-filled bubbles with a diameter smaller than 1 μm. UFBs are stable for several weeks in aqueous solutions due to their small size. Although the mechanism of the stability of UFBs remains under intensi
Autor:
Satoshi Ajito, Kaori Wakamatsu, Shin-ichi Takata, Mitsuhiro Hirai, Motoyasu Adachi, Hiroki Iwase, Rumi Shimizu, Shigeki Arai
Publikováno v:
The Journal of Physical Chemistry B. 123:3189-3198
The interior of living cells is a molecular-crowding environment, where large quantities of various molecules coexist. Investigations into the nature of this environment are essential for an understanding of both the elaborate biological reactions an
Autor:
Agata Rekas, Keyun Shou, Dirk K. Hincha, Anja Thalhammer, Christopher J. Garvey, Anne Bremer, Andreas M. Stadler, Tobias Rindfleisch, Mitsuhiro Hirai, Patrick Knox-Brown
Publikováno v:
Physical Chemistry Chemical Physics
The plant stress protein COR15A stabilizes chloroplast membranes during freezing. COR15A is an intrinsically disordered protein (IDP) in aqueous solution, but acquires an alpha-helical structure during dehydration or the increase of solution osmolari
Autor:
Noboru Ohta, Mitsuhiro Hirai, Hiroki Iwase, Satoshi Ajito, Noriyuki Igarashi, Nobutaka Shimizu
Publikováno v:
Physica B: Condensed Matter. 551:249-255
Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synch
Autor:
Satoshi Ajito, Noriyuki Igarashi, Anne L. Martel, Nobutaka Shimizu, Hiroki Iwase, Shin-ichi Takata, Mitsuhiro Hirai, Masaaki Sugiyama, Lionel Porcar
Publikováno v:
Physica B: Condensed Matter. 551:212-217
The interior of cell is crowded with various kinds of macromolecules, and proteins are designed to function under crowding environment. However, experimental studies showing the direct evidence of the effect of macromolecular crowding environment on
Autor:
Nobutaka Shimizu, Noriyuki Igarashi, Satoshi Ajito, Noboru Ohta, Mitsuhiro Hirai, Shouki Sato
Publikováno v:
The Journal of Physical Chemistry B. 122:9482-9489
This study focuses on the interaction of human amyloid β-peptide (Aβ) with a lipid-raft model membrane under macromolecular crowding conditions that mimic the intracellular environment. Aβ is central to the development of Alzheimer's disease (AD)