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Yumiko Ohhashi

Showing results (1-10 of 15) with videos related to

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The Journal of Biological Chemistry|December 31, 2003
Optimum amyloid fibril formation of a peptide fragment suggests the amyloidogenic preference of beta2-microglobulin under physiological conditionsYumiko Ohhashi, Kazuhiro Hasegawa, Hironobu Naiki, et al.
The Journal of Biological Chemistry|July 28, 2005
Ultrasonication-induced amyloid fibril formation of beta2-microglobulinYumiko Ohhashi, Miho Kihara, Hironobu Naiki, et al.
International Journal of Molecular Sciences|April 30, 2021
Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid FibrilsEri Chatani, Keisuke Yuzu, Yumiko Ohhashi, et al.
Nature Chemical Biology|January 19, 2010
Differences in prion strain conformations result from non-native interactions in a nucleusYumiko Ohhashi, Kazuki Ito, Brandon H Toyama, et al.
Journal of Biochemistry|July 19, 2003
Conformational dynamics of beta(2)-microglobulin analyzed by reduction and reoxidation of the disulfide bondMasayo Gozu, Young Ho Lee, Yumiko Ohhashi, et al.
Journal of Molecular Biology|February 22, 2011
Radically different amyloid conformations dictate the seeding specificity of a chimeric Sup35 prionCatherine K Foo, Yumiko Ohhashi, Mark J S Kelly, et al.
Biochemical and Biophysical Research Communications|April 23, 2003
Amyloidogenic synthetic peptides of beta2-microglobulin--a role of the disulfide bondKazuhiro Hasegawa, Yumiko Ohhashi, Itaru Yamaguchi, et al.
Journal of Biochemistry|January 5, 2002
The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pHYumiko Ohhashi, Yoshihisa Hagihara, Gennady Kozhukh, et al.
Biochemistry|January 27, 2007
The anti-amyloidogenic effect is exerted against Alzheimer's beta-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structureMie Hirohata, Kazuhiro Hasegawa, Shinobu Tsutsumi-Yasuhara, et al.
Nephrology, Dialysis, Transplantation : Official Publication of the European Dialysis and Transplant Association - European Renal Association|May 10, 2008
Lysophospholipids induce the nucleation and extension of beta2-microglobulin-related amyloid fibrils at a neutral pHTadakazu Ookoshi, Kazuhiro Hasegawa, Yumiko Ohhashi, et al.
Pageof 2

Showing results (1-10 of 15) with videos related to

Sort By:
Pageof 2
The Journal of Biological Chemistry|December 31, 2003
Optimum amyloid fibril formation of a peptide fragment suggests the amyloidogenic preference of beta2-microglobulin under physiological conditionsYumiko Ohhashi, Kazuhiro Hasegawa, Hironobu Naiki, et al.
The Journal of Biological Chemistry|July 28, 2005
Ultrasonication-induced amyloid fibril formation of beta2-microglobulinYumiko Ohhashi, Miho Kihara, Hironobu Naiki, et al.
International Journal of Molecular Sciences|April 30, 2021
Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid FibrilsEri Chatani, Keisuke Yuzu, Yumiko Ohhashi, et al.
Nature Chemical Biology|January 19, 2010
Differences in prion strain conformations result from non-native interactions in a nucleusYumiko Ohhashi, Kazuki Ito, Brandon H Toyama, et al.
Journal of Biochemistry|July 19, 2003
Conformational dynamics of beta(2)-microglobulin analyzed by reduction and reoxidation of the disulfide bondMasayo Gozu, Young Ho Lee, Yumiko Ohhashi, et al.
Journal of Molecular Biology|February 22, 2011
Radically different amyloid conformations dictate the seeding specificity of a chimeric Sup35 prionCatherine K Foo, Yumiko Ohhashi, Mark J S Kelly, et al.
Biochemical and Biophysical Research Communications|April 23, 2003
Amyloidogenic synthetic peptides of beta2-microglobulin--a role of the disulfide bondKazuhiro Hasegawa, Yumiko Ohhashi, Itaru Yamaguchi, et al.
Journal of Biochemistry|January 5, 2002
The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pHYumiko Ohhashi, Yoshihisa Hagihara, Gennady Kozhukh, et al.
Biochemistry|January 27, 2007
The anti-amyloidogenic effect is exerted against Alzheimer's beta-amyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structureMie Hirohata, Kazuhiro Hasegawa, Shinobu Tsutsumi-Yasuhara, et al.
Nephrology, Dialysis, Transplantation : Official Publication of the European Dialysis and Transplant Association - European Renal Association|May 10, 2008
Lysophospholipids induce the nucleation and extension of beta2-microglobulin-related amyloid fibrils at a neutral pHTadakazu Ookoshi, Kazuhiro Hasegawa, Yumiko Ohhashi, et al.
Pageof 2