Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Kaoru Nishiyama"'
Publikováno v:
The American Journal of the Medical Sciences. 365:e91-e92
Autor:
Masafumi Matsuo, Benjamas Sattayasevana, Taku Shirakawa, Kaoru Nishiyama, Waricha Janejindamai, Vichai Laosombat, Vip Viprakasit
Publikováno v:
Blood Cells, Molecules, and Diseases. 34:191-196
Two hundred and twenty-five G6PD-deficient subjects in Songklanagarind Hospital in the south of Thailand comprising 210 males and 15 females were studied. Neonatal jaundice was detected in 85% of these patients. Acute hemolysis related to infection w
Autor:
Shunichi Shiozawa, Masao Miwa, Norishige Yoshikawa, Yuji Inoue, Kazumoto Iijima, Hajime Nakamura, Hong Xu, Kaoru Nishiyama, Ryusuke Murakami, Ryojiro Tanaka, Taku Shirakawa
Publikováno v:
American Journal of Kidney Diseases. 34:289-295
Platelet-activating factor (PAF) is a potent mediator of inflammatory injury in renal diseases. PAF is degraded to inactive products by PAF acetylhydrolase. Recently, a point mutation (G to T transversion) of the PAF acetylhydrolase gene was observed
Autor:
Kaoru Nishiyama, Hong Xu, Kazumoto Iijima, Shunichi Shiozawa Ryojiro Tanaka, Yuji Inoue, Masao Miwa, Norishige Yoshikawa, Hajime Nakamura, Taku Shirakawa
Publikováno v:
Kidney International. 54(6):1867-1871
Platelet-activating factor acetylhydrolase gene mutation in Japanese nephrotic children. Background Platelet-activating factor (PAF) may be involved in the pathogenesis of steroid-responsive nephrotic syndrome (SRNS). PAF is degraded to inactive prod
Publikováno v:
Journal of Biological Chemistry. 250:1297-1300
Adenosine 3':5'-monophosphate-dependent protein kinase partially purified from silkworm pupae shows identical functional activities with those of mammalian protein kinases; the insect and mammalian kinases are completely exchangeable in the phosphory
Autor:
S Nakaya, Kaoru Nishiyama, M Inoue, Akira Kishimoto, Yasutomi Nishizuka, Hirohei Yamamura, Y Takai
Publikováno v:
Journal of Biological Chemistry. 251:1481-1487
Guanosine 3':5'-monophosphate (cyclic GMP)-dependent protein kinase (protein kinase G) partially purified from silkworm pupae was selectively activated by cyclic GMP at lower concentrations. Nevertheless, the enzyme seemed to differ from adenosine 3'
Publikováno v:
Biochemical and Biophysical Research Communications. 45:1560-1566
Two adenosine 3′,5′-monophosphate (cyclic AMP)-dependent protein kinases are partially purified from rat liver soluble fraction by ammonium sulfate fractionation, followed by DEAE-Sephadex and hydroxylapatite column chromatography. Both kinases a