著者
土方 敦司 塩生 くらら 中江 摂 塩生 真史 太田 元規 金谷 重彦 白井 剛
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.61, no.2, pp.102-106, 2021 (Released:2021-03-25)
参考文献数
11

The novel coronavirus disease (COVID-19) pandemic has emerged in late 2019 and rapidly spread all over the world. In order to assist structure-based discovery efforts for repurposing drugs against the infectious disease, we constructed homology models of SARS-CoV-2 proteins. We identified several potential drugs by comparing the ligand molecules in the template structures with approved or experimental drugs and compounds of natural drugs, including carfilzomib, sinefungin, tecadenoson, and trabodenoson, that would be further investigated for their potential for treating COVID-19.
著者
村田 武士
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.54, no.2, pp.079-084, 2014 (Released:2014-03-28)
参考文献数
28
被引用文献数
1 1

F- and V-ATPases are unique bio- and nano-molecular rotary motors among many types of bioenergy-transducing machineries. The rotational catalysis of F1-ATPase has been investigated in detail, and the molecular mechanisms have been proposed on the basis of crystal structures of the complex and extensive single-molecule observation of the rotation. Recently, we have obtained crystal structures of bacterial V1-ATPase (A3B3 and A3B3DF complexes) with and without nucleotide. On the basis of these new structures, we present a novel model of the rotational catalytic mechanism for V1-ATPase, which is apparently different from those of F1-ATPases.
著者
Takayoshi Tomono Hisao Kojima Satoshi Fukuchi Yukako Tohsato Masahiro Ito
出版者
一般社団法人 日本生物物理学会
雑誌
Biophysics and Physicobiology (ISSN:21894779)
巻号頁・発行日
vol.12, pp.57-68, 2015 (Released:2015-11-12)
参考文献数
59
被引用文献数
5

Glycans play important roles in such cell-cell interactions as signaling and adhesion, including processes involved in pathogenic infections, cancers, and neurological diseases. Glycans are biosynthesized by multiple glycosyltransferases (GTs), which function sequentially. Excluding mucin-type O-glycosylation, the non-reducing terminus of glycans is biosynthesized in the Golgi apparatus after the reducing terminus is biosynthesized in the ER. In the present study, we performed genome-wide analyses of human GTs by investigating the degree of conservation of homologues in other organisms, as well as by elucidating the phylogenetic relationship between cephalochordates and urochordates, which has long been controversial in deuterostome phylogeny. We analyzed 173 human GTs and functionally linked glycan synthesis enzymes by phylogenetic profiling and clustering, compiled orthologous genes from the genomes of other organisms, and converted them into a binary sequence based on the presence (1) or absence (0) of orthologous genes in the genomes. Our results suggest that the non-reducing terminus of glycans is biosynthesized by newly evolved GTs. According to our analysis, the phylogenetic profiles of GTs resemble the phylogenetic tree of life, where deuterostomes, metazoans, and eukaryotes are resolved into separate branches. Lineage-specific GTs appear to play essential roles in the divergence of these particular lineages. We suggest that urochordates lose several genes that are conserved among metazoans, such as those expressing sialyltransferases, and that the Golgi apparatus acquires the ability to synthesize glycans after the ER acquires this function.
著者
北沢 美帆 藤本 仰一
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.59, no.5, pp.266-270, 2019 (Released:2019-09-27)
参考文献数
11

Component number of flowers is an important aspect to capture floral morphology. Beside the diversity of floral shapes, basic numbers of the components are restricted to several numbers associated with the major clades of flowering plants. The developmental and evolutionary reason of such restriction has been a question for centuries. To answer this, we employed mathematical models developed for phyllotaxis, i.e., arrangement of leaves around the stem. The model showed that basic numbers of four and five, the major numbers in the largest clade of flowering plants, appeared spontaneously and stably, suggesting that preferences in developmental process underlie the restriction.
著者
遠藤 求
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.56, no.1, pp.033-035, 2016 (Released:2016-01-27)
参考文献数
10
著者
松本 篤幸 寺山 慧 奥野 恭史
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.62, no.3, pp.193-197, 2022 (Released:2022-07-25)
参考文献数
9
被引用文献数
1

タンパク質機能を理解する上で,その動的振る舞いを知ることは極めて重要である.我々は近年発展目覚ましいクライオ電子顕微鏡単粒子解析によって得られる3次元密度マップから,深層学習技術を利用して直接的に運動性の情報を抽出する手法DEFMapを開発した.本稿ではその概説と構造生物学への展開について紹介する.
著者
玉井 真悟 仲本 準 田中 元雅
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.60, no.4, pp.236-240, 2020 (Released:2020-07-29)
参考文献数
15

Propagation of amyloid is achieved by the combination of amyloid formation and disaggregation. Although both processes in the cell are regulated by molecular chaperones such as Hsp104 and Hsp70, the underlying molecular mechanism has remained elusive. Here we review a recent progress of metabolic regulation of amyloid fibrils, and discuss about the effects of dynamic conformational fluctuation of monomeric proteins on structural polymorphism of amyloid. The detailed analysis of the processes of amyloid formation and disaggregation by biophysical methods will provide important mechanistic insights into the cellular process responsible for amyloid propagation.
著者
古川 良明
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.60, no.6, pp.338-341, 2020 (Released:2020-11-28)
参考文献数
20

Mutations in the gene coding Cu/Zn-superoxide dismutase (SOD1) are known to cause amyotrophic lateral sclerosis (ALS), a neurodegenerative disease with no cures. SOD1 is a highly stable enzyme where copper and zinc ions bind and a disulfide bond forms, but is also known to accumulate as misfolded forms in spinal motoneurons of ALS. A key to understand such pathological changes in SOD1 is the contribution of metal binding as well as disulfide formation to the conformational stability of SOD1. In this review, I will summarize mechanisms of SOD1 misfolding in ALS where the metal binding and/or disulfide formation go awry.