This research was originally published in the Journal of Biological Chemistry. Daisaku Ozawa, Kazuhiro Hasegawa, Young-Ho Lee, Kazumasa Sakurai, Kotaro Yanagi, Tadakazu Ookoshi, Yuji Goto and Hironobu Naiki. Inhibition of β2-Microglobulin Amyloid Fibril Formation by α2-Macroglobulin. J. Biol. Chem. 2011; 286, 9668-9676. © the American Society for Biochemistry and Molecular Biolog
This research was originally published in the Journal of Biological Chemistry. Mayu S. Terakawa, His...
We demonstrate herein that human macrophage migration inhibitory factor (MIF), a pro-inflammatory cy...
AbstractAmyloid fibril accumulation is a pathological hallmark of several devastating disorders, inc...
The relationship between various amyloidoses and chaperones is gathering attention. In patients with...
This research was originally published in the Journal of Biological Chemistry. Gennady V. Kozhukh, Y...
This research was originally published in the Journal of Biological Chemistry. Miho Kihara, Eri Chat...
This research was originally published in the Journal of Biological Chemistry. Eri Chatani, Hisashi ...
This research was originally published in the Journal of Biological Chemistry. Yumiko Ohhashi, Kazuh...
This research was originally published in the Journal of Biological Chemistry. Yumiko Ohhashi, Miho ...
This research was originally published in the Journal of Biological Chemistry. P. Patrizia Mangione,...
Systemic amyloidosis is caused by misfolding and aggregation of globular proteins in vivo for which ...
Alpha-macroglobulins are ancient proteins that include monomeric, dimeric, and tetrameric family mem...
This research was originally published in the Journal of Biological Chemistry. Young-Ho Lee, Eri Cha...
Abstractβ2-microglobulin (β2m) is a 99-residue protein that aggregates to form amyloid fibrils in di...
Glycosaminoglycan and proteoglycan inhibit the depolymerization of β2-microglobulin amyloid fibrils ...
This research was originally published in the Journal of Biological Chemistry. Mayu S. Terakawa, His...
We demonstrate herein that human macrophage migration inhibitory factor (MIF), a pro-inflammatory cy...
AbstractAmyloid fibril accumulation is a pathological hallmark of several devastating disorders, inc...
The relationship between various amyloidoses and chaperones is gathering attention. In patients with...
This research was originally published in the Journal of Biological Chemistry. Gennady V. Kozhukh, Y...
This research was originally published in the Journal of Biological Chemistry. Miho Kihara, Eri Chat...
This research was originally published in the Journal of Biological Chemistry. Eri Chatani, Hisashi ...
This research was originally published in the Journal of Biological Chemistry. Yumiko Ohhashi, Kazuh...
This research was originally published in the Journal of Biological Chemistry. Yumiko Ohhashi, Miho ...
This research was originally published in the Journal of Biological Chemistry. P. Patrizia Mangione,...
Systemic amyloidosis is caused by misfolding and aggregation of globular proteins in vivo for which ...
Alpha-macroglobulins are ancient proteins that include monomeric, dimeric, and tetrameric family mem...
This research was originally published in the Journal of Biological Chemistry. Young-Ho Lee, Eri Cha...
Abstractβ2-microglobulin (β2m) is a 99-residue protein that aggregates to form amyloid fibrils in di...
Glycosaminoglycan and proteoglycan inhibit the depolymerization of β2-microglobulin amyloid fibrils ...
This research was originally published in the Journal of Biological Chemistry. Mayu S. Terakawa, His...
We demonstrate herein that human macrophage migration inhibitory factor (MIF), a pro-inflammatory cy...
AbstractAmyloid fibril accumulation is a pathological hallmark of several devastating disorders, inc...