Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Yoshiki Kamada"'
Publikováno v:
International Journal of Biological Sciences
Amyloidogenic human lysozyme variants deposit in cells and cause systemic amyloidosis. We recently observed that such lysozymes accumulate in the endoplasmic reticulum (ER) with the ER chaperone GRP78/BiP, accompanying the ER stress response. Here we
Publikováno v:
Biochimica et biophysica acta. 1850(6)
Background Naturally occurring single mutants, I56T, F57I, W64R and D67H of lysozyme in human, have been known to form abnormal protein aggregates (amyloid fibrils) and to accumulate in several organs, including the liver, spleen and kidney, resultin
Publikováno v:
International Journal of Biological Sciences
Some of the lysozyme mutants in humans cause systemic amyloidosis. Hen egg white lysozyme (HEWL) has been well studied as a model protein of amyloid fibrils formation. We previously identified an amyloid core region consisting of nine amino acids (de
Autor:
Yasushi Sugimoto, Tadashi Ueda, Yoshiki Kamada, Mitsuharu Matsumoto, Takahiro Kusakabe, Hiroshi Shinohara, Yuhei Tokunaga, Takatoshi Ohkuri
Publikováno v:
Biochemistry and cell biology = Biochimie et biologie cellulaire. 89(6)
The interaction of egg-white lysozyme with N-ovalbumin, the native form of egg-white ovalbumin with the denaturation temperature, Tm, of 78 °C, was investigated by the inhibition of lysozyme muramidase activity, differential scanning calorimetry, an