Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Munehiro Kumashiro"'
Autor:
Shinichi Sato, Shogo Miyano, Keita Nakane, Zhengyi Liu, Munehiro Kumashiro, Tomohide Saio, Yuya Tanaka, Akira Shigenaga, Chizu Fujimura, Eri Koyanagi, Hafumi Nishi, Shusuke Tomoshige, Minoru Ishikawa
Publikováno v:
Tetrahedron Chem, Vol 12, Iss , Pp 100111- (2024)
Our ex situ tyrosine bioconjugation method utilizes the oxidation of N-methylurazole by Bobbitt's salt or electrochemical activation to generate stable radicals for selective tyrosine labeling, thereby addressing the longstanding challenges in protei
Externí odkaz:
https://doaj.org/article/a0400cbecd224dc386991e75fa935f8a
Publikováno v:
Membranes, Vol 12, Iss 2, p 131 (2022)
The antimicrobial peptide magainin 2 (M2) interacts with and induces structural damage in bacterial cell membranes. Although extensive biophysical studies have revealed the interaction mechanism between M2 and membranes, the mechanism of membrane-med
Externí odkaz:
https://doaj.org/article/dc85415354bd49fcac49271c75ba873f
Autor:
Soichiro Kawagoe, Munehiro Kumashiro, Takuya Mabuchi, Hiroyuki Kumeta, Koichiro Ishimori, Tomohide Saio
Publikováno v:
Biochemistry. 61:2897-2908
A transcriptional regulatory system called heat shock response (HSR) has been developed in eukaryotic cells to maintain proteome homeostasis under various stresses. Heat shock factor-1 (Hsf1) plays a central role in HSR, mainly by upregulating molecu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0e78bce81de03b673efd90092cbbc93
https://doi.org/10.1021/acs.biochem.2c00492
https://doi.org/10.1021/acs.biochem.2c00492
Publikováno v:
Chirality. 32:594-604
α1-Acid glycoprotein (AGP) interacts with lipid membranes as a peripheral membrane protein so as to decrease the drug-binding capacity accompanying the β→α conformational change that is considered a protein-mediated uptake mechanism for releasin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbc3d04cce8de6b015798aeae5d8ebb1
https://doi.org/10.1002/chir.23208
https://doi.org/10.1002/chir.23208
Publikováno v:
ProteinsREFERENCES. 89(10)
The 18.5-kDa isoform of myelin basic protein (MBP) interacts with the membrane surface of the myelin sheath to construct its compact multilamellar structure. This study characterized the conformation of MBP in the membrane by measuring the vacuum-ult
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::471ab0cfe302b0fcfaa78fbdd19a5c87
https://pubmed.ncbi.nlm.nih.gov/33998060
https://pubmed.ncbi.nlm.nih.gov/33998060
Publikováno v:
ChiralityREFERENCES. 32(5)
α
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::315f10ca6cf2c2acacddfc6ff80ffe95
https://pubmed.ncbi.nlm.nih.gov/32125028
https://pubmed.ncbi.nlm.nih.gov/32125028