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Experimental Eye Research|March 9, 2019
Negative charge at aspartate 151 is important for human lens αA-crystallin stability and chaperone functionTakumi Takata, Toshiya Matsubara, Tooru Nakamura-Hirota, et al.
Biochimica Et Biophysica Acta. Proteins and Proteomics|March 14, 2018
D-Amino acids in protein: The mirror of life as a molecular index of agingNoriko Fujii, Takumi Takata, Norihiko Fujii, et al.
Protein Science : a Publication of the Protein Society|June 24, 2008
Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallinTakumi Takata, Julie T Oxford, Borries Demeler, et al.
Protein Science : a Publication of the Protein Society|June 26, 2024
Characterization of βB2-crystallin tryptophan mutants reveals two different folding states in solutionJiayue Sun, Ken Morishima, Rintaro Inoue, et al.
ACS Omega|August 29, 2019
Isomeric Replacement of a Single Aspartic Acid Induces a Marked Change in Protein Function: The Example of Ribonuclease AHiroaki Sakaue, Tadatoshi Kinouchi, Norihiko Fujii, et al.
Plos One|April 15, 2021
Isomerization of Asp is essential for assembly of amyloid-like fibrils of αA-crystallin-derived peptideKosuke Magami, Naomi Hachiya, Kazuo Morikawa, et al.
Biochimica Et Biophysica Acta|December 3, 2014
Alpha B- and βA3-crystallins containing d-aspartic acids exist in a monomeric stateHiroaki Sakaue, Takumi Takata, Norihiko Fujii, et al.
Biochemical and Biophysical Research Communications|April 25, 2006
Differential analysis of D-beta-Asp-containing proteins found in normal and infrared irradiated rabbit lensTakumi Takata, Tadashi Shimo-Oka, Masami Kojima, et al.
Biochemistry|July 10, 2007
Deamidation alters the structure and decreases the stability of human lens betaA3-crystallinTakumi Takata, Julie T Oxford, Theodore R Brandon, et al.
Investigative Ophthalmology & Visual Science|August 29, 2007
Localization of D-beta-aspartic acid-containing proteins in human eyesYuichi Kaji, Tetsuro Oshika, Yutaka Takazawa, et al.
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