「寄付講座 臨床遺伝学研究室」の研究業績のデータです。 [ 論　文 ] 1. Tsukimura T., Kawashima I., Togawa T., Kodama T., Suzuki T., Watanabe T., Chiba Y., Jigami Y., Fukushige T., Kanekura T., Sakuraba H.: Efficient uptake of recombinant α-galactosidase A produced with a gene-manipulated yeast by Fabry mice kidneys. Mol. Med., 18: 76-82, 2012. 2. Saito S., Ohno K., Suzuki T., Sakuraba H.: Structural bases of Wolman disease and cholesteryl ester storage disease. Mol. Genet. Metab., 105: 244-248, 2012. 3. Saito S., Ohono K., Sekijima M., Suzuki T., Sakuraba H.: Database of the clinical phenotypes, genotypes, and mutant arylsulfatase B structures in mucopolysaccharidosis type �Y. J. Hum. Genet., 57: 280-282, 2012. 4. Togawa T., Tsukimura T., Kodama T., Tanaka T., Kawashima I., Saito S., Ohno K., Fukushige T., Kanekura T., Satomura A., D.-H. Kang, B. H. Lee, H.-W. Yoo, Doi K., Noiri E., Sakuraba H.: Fabry disease: Biochemical, pathological and structural studies of the α-galactosidase A with E66Q amino acid substitution. Mol. Genet. Metab., 105: 615-620, 2012. 5. Doi K., Noiri E., Ishizu T., Negishi K., Suzuki Y., Hamasaki Y., Honda K., Fujita T., Tsukimura T., Togawa T., Saito S., Sakuraba H.: High-throughput screening identified disease-causing mutants and functional variants of α-galactosidase A gene in Japanese male hemodialysis patients. J. Hum. Genet., 57: 575-579, 2012. 6. Mitobe S., Togawa T., Tsukimura T., Kodama T., Tanaka T., Doi k., Noiri E., Akai Y., SaitoY., Yoshino M., Takenaka T., Saito S., Ohno K., and Sakuraba H.: Mutant α-galactosidase A with M296I does not cause elevation of the plasma globotriaosylsphingosine level. Mol. Genet. Metab., 107: 623-626, 2012. 7. Maita N., Taniguchi H., Sakuraba H.: Crystallization, X-ray diffraction analysis and SIRAS phasing of human α-L-iduronidase. Acta Cryst., F68: 1363-1366, 2012.