著者
西山 雅祥 樋口 秀男
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.44, no.2, pp.75-80, 2004 (Released:2004-03-23)

Kinesin is an ATP-driven molecular motor that moves processively along a microtubule in a stepwise manner. The steps occur not only in the forward direction, but also in the backward. Here, we have studied the bidirectional stepping mechanism of kinesin motors. The stepping mechanism of the forward and backward movements was well characterized by Feynman's thermal ratchet model. The driving force of the stepwise movement is essentially Brownian motion, but it is biased in the forward direction by utilizing the free energy released from the hydrolysis of ATP.
著者
上岡 龍一 市原 英明 古水 雄志
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.1, pp.005-010, 2014 (Released:2014-01-29)
参考文献数
26

We have produced hybrid liposomes (HL) which can be prepared by sonication of a mixture of vesicular and micellar molecules in a buffer solution. Some interesting results are as follows; HL remarkably inhibited the growth of cancer cells along with apoptosis in vitro and in vivo. Anticancer effects increased with a growth in membrane fluidity of HL and fluidity of plasma membranes of cancer cells. In clinical applications, prolonged survival and remarkable reduction of neoplasm were attained in patients with lymphoma after the treatment with HL without any side effects after the approval of the bioethics committee.
著者
金子 智行
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.41, no.6, pp.312-314, 2001-11-01
参考文献数
6
被引用文献数
1
著者
藤崎 久雄
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.40, no.3, pp.195-198, 0001-01-01 (Released:2001-04-26)
参考文献数
10
著者
矢吹 貞人
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.21, no.5, pp.237-246, 1981-09-25 (Released:2009-05-25)
参考文献数
7
著者
四釜 慶治 松岡 有樹 菅原 芳明
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.41, no.2, pp.74-79, 2001-03-25
被引用文献数
4

The reversible and stable binding of dioxygen to the heme iron (II) is the basis of myoglobin and hemoglobin functions. During reversible oxygen binding, however, the oxygenated form of myoglobin or hemoglobin is oxidized easily to the ferric (III) met-form with generation of the superoxide anion. Thus, stability property of each oxygenated form is of particular importance in vivo, since the iron (III) species cannot bind dioxygen and is therefore physiologically inactive. With special emphasis on the possible roles of the distal histidine, this overview represents a compendium for the molecular mechanism of autoxidation for myoglobin and hemoglobin molecules.

1 0 0 0 OA X線顕微鏡

著者
木原 裕 若林 克三
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.24, no.4, pp.178-182, 1984-07-25 (Released:2009-07-09)
参考文献数
13
著者
矢田 慶治 篠原 邦夫
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.33, no.4, pp.198-206, 1993-07-25 (Released:2009-07-09)
参考文献数
54
被引用文献数
1

Developments in soft x-ray microscopy which has unique advantages in observation of biological samples are reviwed. Some types of the x-ray microscopes have now resolution better than 0.1μm, exceeding that of light microscope, and are capable of quick imaging of rather thick (1-10μm) hydrated samples with x-rays in the region of water window (2.3-4.3nm). Future problems related to radiation damage and thermal diffusion in observation of hydrated sample are briefly introduced.
著者
太田 元規 福地 佐斗志 小池 亮太郎
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.57, no.2, pp.085-089, 2017 (Released:2017-03-30)
参考文献数
16

Protein-protein interactions are fundamental for all biological phenomena. The hub proteins interacting with a number of partner proteins play the vital role in the protein-protein interaction network. We investigated the subcellular localization of proteins in the network, and found that the proteins localized in the multiple subcellular compartments, especially the nucleus and cytoplasm, tend to be hub proteins. Examination on keywords associated with the proteins suggested that those related to post-translational modifications (PTMs) and transcriptions contributed to numerous interactions. Triggered by PTMs in the intrinsically disordered regions, they change interaction partners in the protein complex, and are translocated from cytoplasm to nucleus.