M. Sawano

发表

Role of charged residues in stabilization of Pyrococcus horikoshii CutA1, which has a denaturation temperature of nearly 150 °C

N. Kunishima, Hitoshi Yamamoto, E. Katoh, 2012, The FEBS journal.

Thermodynamic analysis of unusually thermostable CutA1 protein from human brain and its protease susceptibility.

N. Kunishima, Hitoshi Yamamoto, E. Katoh, 2015, Journal of biochemistry.

Possible involvement of 65 kda MAP in elongation growth of azuki bean epicotyls.

M. Sawano, T. Shimmen, S. Sonobe, 2000, Plant & cell physiology.

Stabilization mechanism of the tryptophan synthase alpha-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry.

M. Ota, N. Kunishima, K. Yutani, 2005, Journal of biochemistry.

Crystal Structural and Functional Analysis of the Putative Dipeptidase from Pyrococcus horikoshii OT3

N. Kunishima, S. Yokoyama, K. Yutani, 2009, Journal of biophysics.

Thermodynamic basis for the stabilities of three CutA1s from Pyrococcus horikoshii,Thermus thermophilus, and Oryza sativa, with unusually high denaturation temperatures.

S. Yokoyama, Hitoshi Yamamoto, E. Katoh, 2008, Biochemistry.

Hyper‐thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C

S. Yokoyama, E. Katoh, B. Bagautdinov, 2006 .

Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 degrees C.

S. Yokoyama, E. Katoh, B. Bagautdinov, 2006, FEBS letters.