Yoshihiro Nakamura

发表

Structural analysis of the complex of Keap1 with a prothymosin alpha peptide.

S. Yokoyama, B. Padmanabhan, Yoshihiro Nakamura, 2008, Acta crystallographica. Section F, Structural biology and crystallization communications.

Phylogenetic place of a mitochondria-lacking protozoan, Entamoeba histolytica, inferred from amino acid sequences of elongation factor 2

M. Hasegawa, J. Adachi, Ying Cao, 1994 .

Phytase of the yeast Arxula adeninivorans

H. Fukuhara, K. Sano, Yoshihiro Nakamura, 2004, Biotechnology Letters.

Studies on Hydrogen Production by Photosynthetic Bacteria after Anaerobic Fermentation of Starch by a Hyperthermophile, Pyrococcus furiosus

Y. Asada, J. Miyake, Yoshihiro Nakamura, 2011 .

Null mutants of Drosophila B-type lamin Dm(0) show aberrant tissue differentiation rather than obvious nuclear shape distortion or specific defects during cell proliferation.

K. Furukawa, T. Horigome, Yoshihiro Nakamura, 2005, Developmental biology.

Purification, crystallization and preliminary X-ray diffraction analysis of the Kelch-like motif region of mouse Keap1.

S. Yokoyama, Masayuki Yamamoto, K. I. Tong, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Crystal structures of the human adiponectin receptors

S. Yokoyama, S. Iwata, K. Hirata, 2015, Nature.

Crystal structure analysis of the PHD domain of the transcription co-activator Pygopus.

Y. Hayashizaki, T. Umehara, T. Kigawa, 2007, Journal of molecular biology.

Expression, purification, crystallization, and preliminary X-ray crystallographic studies of the human adiponectin receptors, AdipoR1 and AdipoR2

S. Yokoyama, S. Iwata, K. Hirata, 2015, Journal of Structural and Functional Genomics.

Human adiponectin receptor AdipoR1 assumes closed and open structures

S. Yokoyama, T. Terada, M. Shirouzu, 2020, Communications Biology.

Location of flavoprotein-aromatic compound oxygenases from Rhodococcus erythropolis

R. Kurane, Yoshihiro Nakamura, A. Suemori, 1994 .

Crystallization and preliminary X-ray diffraction studies of catalase-peroxidase from Synechococcus PCC 7942.

M. Tamoi, S. Shigeoka, T. Kinoshita, 2002, Acta crystallographica. Section D, Biological crystallography.

Purification and characterization of o-hydroxyphenylacetate 5-hydroxylase, m-hydroxyphenylacetate 6-hydroxylase and p-hydroxyphenylacetate 1-hydroxylase from Rhodococcus erythropolis

R. Kurane, Yoshihiro Nakamura, K. Nakajima, 1996 .

Protein phylogeny of translation elongation factor EF-1α suggests microsporidians are extremely ancient eukaryotes

M. Hasegawa, N. Okada, T. Hashimoto, 1996, Journal of Molecular Evolution.

Temperature- and detergent-dependent oligomeric structures of flavoprotein monohydroxybenzoate hydroxylases from Rhodococcus erythropolis

R. Kurane, Yoshihiro Nakamura, A. Suemori, 1996 .

Early evolution of eukaryotes inferred from protein phylogenies of translation elongation factors 1α and 2

M. Hasegawa, Yoshihiro Nakamura, T. Kamaishi, 1997 .

Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights into its instability.

S. Shigeoka, T. Ishikawa, Y. Yabuta, 2003, Journal of biochemistry.

Crystallization and preliminary X-ray diffraction analysis of chloroplastic ascorbate peroxidase of tobacco plants.

S. Shigeoka, T. Takeda, Y. Yabuta, 2002, Acta crystallographica. Section D, Biological crystallography.