Zobrazeno 1 - 10
of 233
pro vyhledávání: '"Naotaka Hamasaki"'
Autor:
Xiuri Jin PhD, Sachiko Kinoshita PhD, Hiroyuki Kuma PhD, Tomohide Tsuda PhD, Tatsusada Yoshida PhD, Dongchon Kang MD, PhD, Naotaka Hamasaki MD, PhD
Publikováno v:
Clinical and Applied Thrombosis/Hemostasis, Vol 27 (2021)
The quantitative assay of protein S can help in rapidly identifying carriers of abnormal protein S molecules through a simple procedure (by determining the total protein S mass, total protein S activity, and protein S-specific activity in blood), wit
Externí odkaz:
https://doaj.org/article/5bb33030636a4ece9939c1797ac76e64
Publikováno v:
Internal Medicine
Thrombophilia is a serious unpredictable complication caused by gene mutations, resulting in anticoagulant deficiencies. We herein report a single-family case series of protein C (PC) deficiency. Case 1 involved a Japanese man whose PC deficiency res
Autor:
Dongchon Kang, Tatsusada Yoshida, Hiroyuki Kuma, Sachiko Kinoshita, Xiuri Jin, Tomohide Tsuda, Naotaka Hamasaki
Publikováno v:
Clinical and Applied Thrombosis/Hemostasis, Vol 27 (2021)
Clinical and Applied Thrombosis/Hemostasis
Clinical and Applied Thrombosis/Hemostasis
The quantitative assay of protein S can help in rapidly identifying carriers of abnormal protein S molecules through a simple procedure (by determining the total protein S mass, total protein S activity, and protein S-specific activity in blood), wit
Autor:
Takao Hamakubo, Dongchon Kang, Momi Iwata, Yilmaz Alguel, Naotaka Hamasaki, So Iwata, Hinako Hatae, Takuya Kobayashi, Alexander D. Cameron, Takatoshi Arakawa, Takeshi Murata, Chiyo Ikeda-Suno, Hiroko Iwanari, Yoshito Abe, Hiroyuki Kuma, Tomoya Hino, Takami Kobayashi-Yurugi
Publikováno v:
Science. 350:680-684
Getting rid of carbon dioxide In mammals, red blood cells deliver oxygen to tissues and remove carbon dioxide. Key to this essential process is a membrane protein called anion exchanger 1 (AE1) which transports bicarbonate (formed from carbon dioxide
Autor:
Koji Inaka, Hinako Hatae, So Iwata, Masayuki Kamo, Yoshito Abe, Naoki Furubayashi, Takuya Kobayashi, Ryo Okamura, Naotaka Hamasaki
Publikováno v:
Analytical biochemistry. 559
Band 3 mediates the Cl- and HCO3- exchange across the red blood cell membrane and plays a pivotal role for delivering oxygen appropriately to metabolically active tissues. For understanding molecular mechanisms, it is essential to know the structure
Autor:
Hiroko Tsuda, Xiuri Jin, Asuna Nakashima, Shinya Takazaki, Kazuna Motoyama, Tomohide Tsuda, Hiroyuki Kuma, Hinako Hatae, Naotaka Hamasaki, Ryo Matsuda
Publikováno v:
Thrombosis research. 168
Autor:
Yu Hu, Naotaka Hamasaki, Tao Guo, Liang Tang, Xuan Lu, Huafang Wang, Xiao-Rong Jian, Qing-Yun Wang
Publikováno v:
American Journal of Hematology. 88:899-905
Protein S (ProS) is a physiological inhibitor of coagulation with an important function in the down-regulation of thrombin generation. ProS deficiency is a major risk factor for venous thrombosis. This study enrolled 40 ProS-deficient probands to inv
Autor:
Yuko, Tanaka, Syunsuke, Fukino, Takashi, Oono, Wataru, Kodama, Kengo, Nishimura, Naotaka, Hamasaki
Publikováno v:
Gan to kagaku ryoho. Cancerchemotherapy. 43(5)
A 67-year-old woman who underwent left breast mastectomy and right breast partial mastectomy under the diagnosis of left breast cancer and suspected right breast cancer 10 years earlier was admitted because of dyspnea. Chest computed tomography revea
Autor:
Naotaka, Hamasaki
Publikováno v:
Rinsho byori. The Japanese journal of clinical pathology. 63(12)
Approximately 50% of Japanese individuals who develop venous thrombosis have reduced activities of protein S, the major component of the Activated Protein C (APC) anticoagulant system. The significance of the measurement of protein S-specific activit
Arg 901 in the AE1 C-terminal tail is involved in conformational change but not in substrate binding
Autor:
Mikako Yagi, Dongchon Kang, Tadashi Ueda, Tomohiro Yamaguchi, Yoshito Abe, Shinya Takazaki, Naotaka Hamasaki
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1818(3):658-665
In our previous paper, we demonstrated that Arg 901 in the C-terminal tail of human AE1 (band 3, anion exchanger 1) had a functional role in conformational change during anion exchange. To further examine how Arg 901 is involved in conformational cha