当社グループは 3,000 以上の世界的なカンファレンスシリーズ 米国、ヨーロッパ、世界中で毎年イベントが開催されます。 1,000 のより科学的な学会からの支援を受けたアジア および 700 以上の オープン アクセスを発行ジャーナルには 50,000 人以上の著名人が掲載されており、科学者が編集委員として名高い
。オープンアクセスジャーナルはより多くの読者と引用を獲得
700 ジャーナル と 15,000,000 人の読者 各ジャーナルは 25,000 人以上の読者を獲得
Yoichiro Kuroda
Large numbers of senile plaques are thought to be characteristic of Alzheimer’s disease (AD), but these deposits are also a by-product of normal senescence. In AD and normal brains, senile plaques are primarily composed of amyloid-ß peptides (Aß P) with aluminum (Al). Evidence suggests the oligomerization of Aß P is part of the molecular mechanism of AD pathogenesis by forming neurotoxic amyloid channels. However, the relationship between Al and AD has been a subject of scientific debate for many years. The complex nature of Al bioavailability has made it difficult to evaluate its toxicity to the human brain. In 2004, Al concentration in CSF of AD patients analyzed to be 1.6 ± 0.4 times higher than normal people. Importantly, AD patients with more Al in CSF showed less MMSE score, indicating Al may decrease cognitive ability. Recently, Al accumulations in sporadic AD and familial AD brains were reported to be much higher than in normal control brains. Above its neurotoxicity, Al3+ has a crucial role as a cross-linker in ß-amyloid oligomerization. Therefore, I propose a hypothesis that ß-amyloid oligomerizes with Al, forming non-specific cation amyloid channels in cell membranes, which allows calcium to enter cells and finally causes neuronal death by together with Al’s own neurotoxicity.