K. Aoki

发表

Efficiency of signalling through cytokine receptors depends critically on receptor orientation

Robert M. Stroud, John J. Wendoloski, Scott W. Reid, 1998, Nature.

Complete amino acid sequence of the large subunit of the low‐Ca2+‐requiring form of human Ca2+‐activated neutral protease (μCANP) deduced from its cDNA sequence

K. Suzuki, M. Koike, K. Aoki, 1986, FEBS letters.

Engineering a soluble extracellular erythropoietin receptor (EPObp) in Pichia pastoris to eliminate microheterogeneity, and its complex with erythropoietin.

R. Stroud, B. Liu, L. Giebel, 1999, Protein engineering.

Characterization and biological effects of recombinant human erythropoietin.

K. Aoki, J. Egrie, F. Lin, 1986, Immunobiology.

S7.7 The role of carbohydrate on the biological activity of erythropoietin

K. Aoki, J. Egrie, T. Strickland, 1993, Glycoconjugate Journal.

Investigation of the effects of altered receptor binding activity on the clearance of erythropoiesis-stimulating proteins: Nonerythropoietin receptor-mediated pathways may play a major role.

K. Aoki, S. Elliott, L. Narhi, 2009, Journal of pharmaceutical sciences.

Differentiation of the Local Structure Around Tryptophan 51 and 64 in Recombinant Human Erythropoietin by Tryptophan Phosphorescence

K. Aoki, B. Kerwin, G. Strambini, 2008, Photochemistry and photobiology.

Enhancement of therapeutic protein in vivo activities through glycoengineering

L. Buck, K. Aoki, T. Osslund, 2003, Nature Biotechnology.

Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease.

H. Kawasaki, K. Suzuki, K. Aoki, 1988, Biochemistry.

Efficiencyofsignallingthrough cytokine receptors dependscriticallyon receptororientation

J. Wendoloski, R. Stroud, J. Finer-Moore, 2006 .

NMR structure of human erythropoietin and a comparison with its receptor bound conformation

T. Harvey, R. Syed, J. Cheetham, 1998, Nature Structural Biology.

Changes in Conformation and Stability upon Formation of Complexes of Erythropoietin (EPO) and Soluble EPO Receptor

T. Arakawa, J. Philo, K. Aoki, 1997, Journal of protein chemistry.

Identification of the amino acid substitutions in two mutant forms of the recA protein from Escherichia coli: recA441 and recA629.

K. McEntee, K. Aoki, K. Knight, 1984, The Journal of biological chemistry.

Copper Staining Method for Extracting Biologically Active Proteins from Native Gels

T. Arakawa, J. Philo, T. Horan, 2001, Bioscience, biotechnology, and biochemistry.

Biophysical comparability of the same protein from different manufacturers: a case study using Epoetin alfa from Epogen and Eprex.

K. Aoki, B. Kerwin, S. Deechongkit, 2006, Journal of pharmaceutical sciences.

Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: one high-affinity and one low-affinity interaction.

T. Arakawa, J. Philo, K. Aoki, 1996, Biochemistry.

Effect of amino acid residues on conformational stability in eight mutant proteins variously substituted at a unique position of the tryptophan synthase alpha-subunit.

K. Aoki, K. Yutani, K. Ogasahara, 1984, The Journal of biological chemistry.

Asn to Lys mutations at three sites which are N-glycosylated in the mammalian protein decrease the aggregation of Escherichia coli-derived erythropoietin.

T. Arakawa, T. Boone, J. Cheetham, 2001, Protein engineering.

The effect of carbohydrate on the structure and stability of erythropoietin.

T. Arakawa, T. Boone, K. Aoki, 1991, The Journal of biological chemistry.