Yuriko Yamagata

发表

SIRT7 has a critical role in bone formation by regulating lysine acylation of SP7/Osterix

Shihab U. Sobuz, S. Takeda, E. Bober, 2018, Nature Communications.

Entropic Stabilization of the Tryptophan Synthase α-Subunit from a Hyperthermophile, Pyrococcus furiosus

Haruki Nakamura, M. Ishida, A. Nakagawa, 2001, The Journal of Biological Chemistry.

Role of amino acid residues in left‐handed helical conformation for the conformational stability of a protein

Y. Yamagata, K. Takano, K. Yutani, 2001, Proteins.

Role of non‐glycine residues in left‐handed helical conformation for the conformational stability of human lysozyme

K. Takano, K. Yutani, Yuriko Yamagata, 2001, Proteins.

Protonation states of Asp residues in the human Nudix hydrolase MTH1 contribute to its broad substrate recognition

Teruya Nakamura, Y. Nakabeppu, S. Ikemizu, 2023, FEBS letters.

Visualization of mutagenic nucleotide processing by Escherichia coli MutT, a Nudix hydrolase

Teruya Nakamura, Yuriko Yamagata, 2022, Proceedings of the National Academy of Sciences of the United States of America.

Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants.

K. Yutani, Yuriko Yamagata, Kazufumi Takano, 1999, Biochemistry.

Contribution of salt bridges near the surface of a protein to the conformational stability.

Y. Yamagata, K. Takano, K. Yutani, 2000, Biochemistry.

Contribution of water molecules in the interior of a protein to the conformational stability.

Y. Yamagata, K. Takano, K. Yutani, 1998, Journal of molecular biology.

Effect of foreign N-terminal residues on the conformational stability of human lysozyme.

Y. Yamagata, K. Takano, K. Yutani, 1999, European journal of biochemistry.

Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,).

Y. Yamagata, S. Kuramitsu, K. Takano, 1999, Biochemistry.

Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7-A resolution.

S. Kim, Sung-Hou Kim, C. Kang, 1991, The Journal of biological chemistry.

Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants.

M. Oobatake, Y. Yamagata, E. Kanaya, 1996, Journal of molecular biology.

Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes.

K Nishikawa, K. Nishikawa, M. Ota, 1999, Protein engineering.

Crystallization and preliminary X-ray diffraction studies of 3-methyladenine-DNA glycosylase II from Escherichia coli.

Y. Yamagata, Y. Nakabeppu, M. Sekiguchi, 1988, Journal of molecular biology.

Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme.

Y. Yamagata, K. Takano, K. Yutani, 1999, Protein engineering.

Role of amino acid residues at turns in the conformational stability and folding of human lysozyme.

K. Takano, K. Yutani, K Yutani, 1999, Biochemistry.

Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants.

Y. Yamagata, K. Takano, K. Yutani, 1997, Biochemistry.