This research was originally published in the Journal of Biological Chemistry. Eri Chatani, Hisashi Yagi, Hironobu Naiki and Yuji Goto. Polymorphism of β2-Microglobulin Amyloid Fibrils Manifested by Ultrasonication-enhanced Fibril Formation in Trifluoroethanol. J. Biol. Chem. 2012; 287, 22827-22837. © the American Society for Biochemistry and Molecular Biolog
The amyloidogenic variant of β2-microglobulin, D76N, can readily convert into genuine fibrils under ...
I began my research in the Eisenberg laboratory by studying the polymorphic nature of amyloid protei...
Amyloid fibril formation is implicated in different human diseases. The transition between native α-...
The polymorphic property of amyloid structures has been focused on as a molecular basis of the prese...
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. Kotaro Yanagi, Mizue ...
This research was originally published in the Journal of Biological Chemistry. Gennady V. Kozhukh, Y...
One and the same protein can self-assemble into amyloid fibrils with different morphologies. The phe...
This research was originally published in the Journal of Biological Chemistry. Daisaku Ozawa, Kazuhi...
All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from protei...
This research was originally published in the Journal of Biological Chemistry. Yumiko Ohhashi, Kazuh...
All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from protei...
This research was originally published in the Journal of Biological Chemistry. Young-Ho Lee, Eri Cha...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins, which then...
The amyloidogenic variant of β2-microglobulin, D76N, can readily convert into genuine fibrils under ...
The amyloidogenic variant of β2-microglobulin, D76N, can readily convert into genuine fibrils under ...
I began my research in the Eisenberg laboratory by studying the polymorphic nature of amyloid protei...
Amyloid fibril formation is implicated in different human diseases. The transition between native α-...
The polymorphic property of amyloid structures has been focused on as a molecular basis of the prese...
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. Kotaro Yanagi, Mizue ...
This research was originally published in the Journal of Biological Chemistry. Gennady V. Kozhukh, Y...
One and the same protein can self-assemble into amyloid fibrils with different morphologies. The phe...
This research was originally published in the Journal of Biological Chemistry. Daisaku Ozawa, Kazuhi...
All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from protei...
This research was originally published in the Journal of Biological Chemistry. Yumiko Ohhashi, Kazuh...
All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from protei...
This research was originally published in the Journal of Biological Chemistry. Young-Ho Lee, Eri Cha...
Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins, which then...
The amyloidogenic variant of β2-microglobulin, D76N, can readily convert into genuine fibrils under ...
The amyloidogenic variant of β2-microglobulin, D76N, can readily convert into genuine fibrils under ...
I began my research in the Eisenberg laboratory by studying the polymorphic nature of amyloid protei...
Amyloid fibril formation is implicated in different human diseases. The transition between native α-...