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Biochemical and Biophysical Research Communications|November 26, 2009
Effects of His mutations on the fibrillation of amyloidogenic Vlambda6 protein Wil under acidic and physiological conditionsTomonori Mishima, Takatoshi Ohkuri, Akira Monji, et al.Biochimica Et Biophysica Acta|February 6, 2010
Mutation of His 834 in human anion exchanger 1 affects substrate bindingShinya Takazaki, Yoshito Abe, Tomohiro Yamaguchi, et al.Journal of Biochemistry|June 6, 2006
The functional role of arginine 901 at the C-terminus of the human anion transporter band 3 proteinShinya Takazaki, Yoshito Abe, Donchon Kang, et al.Biochimica Et Biophysica Acta. General Subjects|September 26, 2018
Inhibition of amyloid fibril formation in the variable domain of λ6 light chain mutant Wil caused by the interaction between its unfolded state and epigallocatechin-3-O-gallateYoshito Abe, Naoki Odawara, Nantanat Aeimhirunkailas, et al.Protein Science : a Publication of the Protein Society|February 8, 2013
Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 proteinMasahiro Abe, Yoshito Abe, Takatoshi Ohkuri, et al.Biochimica Et Biophysica Acta|November 9, 2013
Involvement of histidine in complex formation of PriB and single-stranded DNASaki Fujiyama, Yoshito Abe, Taichi Takenawa, et al.Genes to Cells : Devoted to Molecular & Cellular Mechanisms|July 4, 2013
Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coliTakahiko Aramaki, Yoshito Abe, Takatoshi Ohkuri, et al.Biochimica Et Biophysica Acta|December 14, 2011
Arg 901 in the AE1 C-terminal tail is involved in conformational change but not in substrate bindingShinya Takazaki, Yoshito Abe, Tomohiro Yamaguchi, et al.Biochemical and Biophysical Research Communications|February 2, 2022
Compound screening identified gossypetin and isoquercitrin as novel inhibitors for amyloid fibril formations of Vλ6 proteins associated with AL amyloidosisDaisuke Takahashi, Eri Matsunaga, Tomohiro Yamashita, et al.Biochemical and Biophysical Research Communications|December 21, 2004
Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding siteSeijiro Shioi, Toyoyuki Ose, Katsumi Maenaka, et al.Pageof 14