Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Tsuyoshi Mashima"'
Autor:
Takahiro Sakai, Tsuyoshi Mashima, Naoya Kobayashi, Hideaki Ogata, Lian Duan, Ryo Fujiki, Kowit Hengphasatporn, Taizo Uda, Yasuteru Shigeta, Emi Hifumi, Shun Hirota
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Abstract Overexpression of antibody light chains in small plasma cell clones can lead to misfolding and aggregation. On the other hand, the formation of amyloid fibrils from antibody light chains is related to amyloidosis. Although aggregation of ant
Externí odkaz:
https://doaj.org/article/62801ef19ea443e29807c5b10bd1a0ef
Autor:
Masaru Yamanaka, Tsuyoshi Mashima, Michio Ogihara, Mei Okamoto, Takayuki Uchihashi, Shun Hirota
Publikováno v:
PLoS ONE, Vol 16, Iss 11 (2021)
Various proteins form nanostructures exhibiting unique functions, making them attractive as next-generation materials. Ferritin is a hollow spherical protein that incorporates iron ions. Here, we found that hydrogels are simply formed from concentrat
Externí odkaz:
https://doaj.org/article/cb0fffb40c2a40249b44c9b51e9b3fd4
Autor:
Kodai Fujiwara, Michiko Ryuzaki, Masaru Yamanaka, Tsuyoshi Mashima, Tomonori Saotome, Shun-ichi Kidokoro, Shun Hirota
Publikováno v:
Chemistry Letters; Aug2024, Vol. 53 Issue 8, p1-4, 4p
Autor:
Shun Hirota, Chun-Liang Chiu, Chieh-Ju Chang, Pei-Hua Lo, Tien Chen, Hongxu Yang, Masaru Yamanaka, Tsuyoshi Mashima, Cheng Xie, Hiroshi Masuhara, Teruki Sugiyama
Publikováno v:
Chemical Communications. 58:12839-12842
Amyloid fibril formation of cytochrome c is spatially and temporally controlled by the optical trapping method, identifying that the structural change in the region containing Ala83 is essential for the amyloid fibril formation.
Autor:
Koji Oohora, Luc Brunsveld, Takashi Hayashi, Bas J.H.M. Rosier, Tsuyoshi Mashima, Tom F. A. de Greef
Publikováno v:
Angewandte Chemie. International Edition, 60, 20, pp. 11262-11266
Angewandte Chemie (International Ed. in English)
Angewandte Chemie-International Edition, 60(20), 11262-11266. Wiley
Angewandte Chemie. International Edition, 60, 11262-11266
Angewandte Chemie (International Ed. in English)
Angewandte Chemie-International Edition, 60(20), 11262-11266. Wiley
Angewandte Chemie. International Edition, 60, 11262-11266
Hexameric hemoprotein (HTHP) is employed as a scaffold protein for the supramolecular assembly and activation of the apoptotic signalling enzyme caspase‐9, using short DNA elements as modular recruitment domains. Caspase‐9 assembly and activation
Publikováno v:
Chemical Communications. 57:12074-12086
Supramolecules, which are formed by assembling multiple molecules by noncovalent intermolecular interactions instead of covalent bonds, often show additional properties that cannot be exhibited by a single molecule. Supramolecules have evolved into m
Publikováno v:
Journal of Porphyrins and Phthalocyanines. 24:259-267
Protein assemblies are being investigated as a new-class of biomaterials. A supramolecular assembly of a mutant hexameric tyrosine coordinated hemoprotein (HTHP) modified with a pyrene derivative is described. Cysteine was first introduced as a site-
Autor:
Tsuyoshi Mashima, Marleen H. M. E. van Stevendaal, Femke R. A. Cornelissens, Alexander F. Mason, Bas J. H. M. Rosier, Wiggert J. Altenburg, Koji Oohora, Shota Hirayama, Takashi Hayashi, Jan C. M. van Hest, Luc Brunsveld
Publikováno v:
Angewandte Chemie-International Edition, 61(17):e202115041. Wiley
The regulation of protein uptake and secretion is crucial for (inter)cellular signaling. Mimicking these molecular events is essential when engineering synthetic cellular systems. A first step towards achieving this goal is obtaining control over the
Publikováno v:
Journal of Porphyrins and Phthalocyanines. 21:824-831
To convert an originally tyrosine-coordinated heme to histidine-coordinated heme in hexameric tyrosine-coordinated hemoprotein, HTHP, Tyr45, a residue coordinating to the heme cofactor, and Arg25 located in the distal site are replaced with Phe45 and
Autor:
Michio Ogihara, Shun Hirota, Takayuki Uchihashi, Mei Okamoto, Tsuyoshi Mashima, Masaru Yamanaka
Publikováno v:
PLoS ONE, Vol 16, Iss 11, p e0259052 (2021)
PLoS ONE, Vol 16, Iss 11 (2021)
PLoS ONE
PLoS ONE, Vol 16, Iss 11 (2021)
PLoS ONE
Various proteins form nanostructures exhibiting unique functions, making them attractive as next-generation materials. Ferritin is a hollow spherical protein that incorporates iron ions. Here, we found that hydrogels are simply formed from concentrat