Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Yasuo SUMIDA"'
Autor:
Takashi UMEHARA, Marino OGASAHARA, D.M.V. Supun PREMARATHNE, Yuka SASAKAWA, Yasuo SUMIDA, Masayuki SHIMADA
Publikováno v:
The Journal of Reproduction and Development, Vol 70, Iss 3, Pp 202-206 (2024)
Ovarian fibrosis contributes to age-related ovarian dysfunction. In our previous study, we observed ovarian fibrosis in both obese and aging mice with intracellular lipid droplets in the fibrotic ovaries. Although the importance of mitochondria in ov
Externí odkaz:
https://doaj.org/article/c0aa709f0e764b44aa30ac28870be3a3
Publikováno v:
Biochemical and Biophysical Research Communications. 271:620-625
The effect of administration of aluminum to rats on the level of three phospholipase C (PLC) isozymes (beta1, gamma1, and delta1) was assessed in a variety of brain tissues. After exposure to aluminum, a statistically significant increase in malondia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8cd36b18070a9e3d71624fbfeb3e78a
https://doi.org/10.1006/bbrc.2000.2679
https://doi.org/10.1006/bbrc.2000.2679
Publikováno v:
Biochemical and Biophysical Research Communications. 252:92-96
We have previously examined the involvement of the B cell leukemia-2 gene product (Bcl-2) family proteins (Bcl-2, Bcl-x, Bax, Bak, and Bad) in Alzheimer's disease (AD) and found that Bcl-2, Bcl-x, Bak, and Bad were upregulated. As AD is an aging-asso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a47c52d598e6e0f18cc265b68d6f7f11
https://doi.org/10.1006/bbrc.1998.9577
https://doi.org/10.1006/bbrc.1998.9577
Autor:
Takashi Taniguchi, Kimio Akagawa, Tomoaki Shirao, Sadaki Fujimoto, Yasuo Sumida, Yasuji Matsuoka, Shun Shimohama
Publikováno v:
Biochemical and Biophysical Research Communications. 251:394-398
We have previously reported the differential involvement of synaptic proteins in Alzheimer's disease (AD). As AD is an aging-associated disease, in the present study we examined the developmental and aging-related changes in synaptic proteins such as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8dc1804f10c166229ea7061305070ec
https://doi.org/10.1006/bbrc.1998.9480
https://doi.org/10.1006/bbrc.1998.9480
Publikováno v:
Neuroscience Letters. 245:159-162
myo -Inositol monophosphatase (E.C.3.1.3.25) catalyzes the hydrolysis of myo -inositol 1- phosphate in the presence of Mg 2+ at a physiologic pH to form free myo -inositol, maintaining a supply that represents the precursor for inositol phospholipid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e326e330c63c4b169755c84ca2fcf46
https://doi.org/10.1016/s0304-3940(98)00209-2
https://doi.org/10.1016/s0304-3940(98)00209-2
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1314:167-174
We examined in detail the tyrosine phosphorylation of proteins, especially inositol phospholipid-specific phospholipase C (PLC) γ 2, during activation of respiratory burst of guinea pig polymorphonuclear leukocytes (PMNs) by pervanadate. The pervana
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::081e46cecae9eef91d3c358e6005ff3e
https://doi.org/10.1016/s0167-4889(96)00077-8
https://doi.org/10.1016/s0167-4889(96)00077-8
Autor:
Tadafumi Takenawa, Sadaki Fujimoto, Yasuo Sumida, Jun Kimura, Yasuji Matsuoka, Takashi Taniguchi, Shun Shimohama
Publikováno v:
Biochemical and biophysical research communications. 243(1)
Phosphoinositide-specific phospholipase C (PLC) is a key enzyme in signal transduction. In the present study we examined developmental and aging changes in three PLC isozymes (beta 1, gamma 1, and delta 1) in the rat brain. Enzyme assays and immunobl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ba733bb6122e83a77e3e1cb99e4b68e
https://pubmed.ncbi.nlm.nih.gov/9473506
https://pubmed.ncbi.nlm.nih.gov/9473506
Autor:
Sadaki Fujimoto, Shun Shimohama, Yasuo Sumida, Isako Okano, Jyunji Tsuda, Yutaka Tanaka, Naoko Kawakami
Publikováno v:
Biologicalpharmaceutical bulletin. 19(6)
We have purified bovine brain Zn(2+)-dependent acid phosphatase (Zn(2+)-APase), which requires Zn2+ ions to hydrolyze the substrate p-nitrophenyl phosphate (pNPP) in an acidic environment. The substrate specificity and metal requirement of Zn(2+)-APa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b05e7849e903582eb4676a40a98eb038
https://pubmed.ncbi.nlm.nih.gov/8799493
https://pubmed.ncbi.nlm.nih.gov/8799493