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Results: 1-10 |
Results: 10
Matrix metalloproteinase (MMP) system in brain: identification and characterization of brain-specific MMP highly expressed in cerebellum
Authors: Sekine-Aizawa, Y Hama, E Watanabe, K Tsubuki, S Kanai-Azuma, M Kanai, Y Arai, H Aizawa, H Iwata, N Saido, TC
Citation: Y. Sekine-aizawa et al., Matrix metalloproteinase (MMP) system in brain: identification and characterization of brain-specific MMP highly expressed in cerebellum, EUR J NEURO, 13(5), 2001, pp. 935-948
Metabolic regulation of brain A beta by neprilysin
Authors: Iwata, N Tsubuki, S Takaki, Y Shirotani, K Lu, B Gerard, NP Gerard, C Hama, E Lee, HJ Saido, TC
Citation: N. Iwata et al., Metabolic regulation of brain A beta by neprilysin, SCIENCE, 292(5521), 2001, pp. 1550-1552
Neprilysin degrades both amyloid beta peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases
Authors: Shirotani, K Tsubuki, S Iwata, N Takaki, Y Harigaya, W Maruyama, K Kiryu-Seo, S Kiyama, H Iwata, H Tomita, T Iwatsubo, T Saido, TC
Citation: K. Shirotani et al., Neprilysin degrades both amyloid beta peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases, J BIOL CHEM, 276(24), 2001, pp. 21895-21901
MST, a physiological caspase substrate, highly sensitizes apoptosis both upstream and downstream of caspase activation
Authors: Lee, KK Ohyama, T Yajima, N Tsubuki, S Yonehara, S
Citation: Kk. Lee et al., MST, a physiological caspase substrate, highly sensitizes apoptosis both upstream and downstream of caspase activation, J BIOL CHEM, 276(22), 2001, pp. 19276-19285
Clearance of amyloid beta-peptide from brain: transport or metabolism? Reply
Authors: Iwata, N Tsubuki, S Hama, E Takaki, Y Shirotani, K Saido, TC
Citation: N. Iwata et al., Clearance of amyloid beta-peptide from brain: transport or metabolism? Reply, NAT MED, 6(7), 2000, pp. 718-719
Identification of the major A beta(1-42)-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition
Authors: Iwata, N Tsubuki, S Takaki, Y Watanabe, K Sekiguchi, M Hosoki, E Kawashima-Morishima, M Lee, HJ Hama, E Sekine-Aizawa, Y Saido, TC
Citation: N. Iwata et al., Identification of the major A beta(1-42)-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition, NAT MED, 6(2), 2000, pp. 143-150
Biochemical identification of the neutral endopeptidase family member responsible for the catabolism of amyloid beta peptide in the brain
Authors: Takaki, Y Iwata, N Tsubuki, S Taniguchi, S Toyoshima, S Lu, B Gerard, NP Gerard, C Lee, HJ Shirotani, K Saido, TC
Citation: Y. Takaki et al., Biochemical identification of the neutral endopeptidase family member responsible for the catabolism of amyloid beta peptide in the brain, J BIOCHEM, 128(6), 2000, pp. 897-902
Egg envelope glycoprotein gp37 as a Xenopus homolog of mammalian ZP1, based on cDNA cloning
Authors: Kubo, H Kawano, T Tsubuki, S Kotani, M Kawasaki, H Kawashima, S
Citation: H. Kubo et al., Egg envelope glycoprotein gp37 as a Xenopus homolog of mammalian ZP1, based on cDNA cloning, DEVELOP GR, 42(4), 2000, pp. 419-427
Dual roles of proteasome in the metabolism of presenilin 1
Authors: Honda, T Yasutake, K Nihonmatsu, N Mercken, M Takahashi, H Murayama, O Murayama, M Sato, K Omori, A Tsubuki, S Saido, TC Takashima, A
Citation: T. Honda et al., Dual roles of proteasome in the metabolism of presenilin 1, J NEUROCHEM, 72(1), 1999, pp. 255-261
Calpain inhibitor entrapped in liposome rescues ischemic neuronal damage
Authors: Yokota, M Tani, E Tsubuki, S Yamaura, I Nakagaki, I Hori, S Saido, TC
Citation: M. Yokota et al., Calpain inhibitor entrapped in liposome rescues ischemic neuronal damage, BRAIN RES, 819(1-2), 1999, pp. 8-14
Risultati: 1-10 |