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Kentaro Hanada

Department of Biochemistry

National Institute of Infectious Diseases

1-23-1 Toyama

Shinjuku-ku

Japan

[email]@nih.go.jp

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Affiliation

Department of Biochemistry, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Japan. 1997 - 2009

References

CERT-mediated trafficking of ceramide. Hanada, K., Kumagai, K., Tomishige, N., Yamaji, T. Biochim. Biophys. Acta (2009) [Pubmed]
CERT and intracellular trafficking of ceramide. Hanada, K., Kumagai, K., Tomishige, N., Kawano, M. Biochim. Biophys. Acta (2007) [Pubmed]
Sphingolipids in infectious diseases. Hanada, K. Jpn. J. Infect. Dis. (2005) [Pubmed]
Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Hanada, K. Biochim. Biophys. Acta (2003) [Pubmed]
Molecular machinery for non-vesicular trafficking of ceramide. Hanada, K., Kumagai, K., Yasuda, S., Miura, Y., Kawano, M., Fukasawa, M., Nishijima, M. Nature (2003) [Pubmed]
Plasmodium falciparum phospholipase C hydrolyzing sphingomyelin and lysocholinephospholipids is a possible target for malaria chemotherapy. Hanada, K., Palacpac, N.M., Magistrado, P.A., Kurokawa, K., Rai, G., Sakata, D., Hara, T., Horii, T., Nishijima, M., Mitamura, T. J. Exp. Med. (2002) [Pubmed]
Neutral sphingomyelinase activity dependent on Mg2+ and anionic phospholipids in the intraerythrocytic malaria parasite Plasmodium falciparum. Hanada, K., Mitamura, T., Fukasawa, M., Magistrado, P.A., Horii, T., Nishijima, M. Biochem. J. (2000) [Pubmed]
Specificity of inhibitors of serine palmitoyltransferase (SPT), a key enzyme in sphingolipid biosynthesis, in intact cells. A novel evaluation system using an SPT-defective mammalian cell mutant. Hanada, K., Nishijima, M., Fujita, T., Kobayashi, S. Biochem. Pharmacol. (2000) [Pubmed]
D-Serine inhibits serine palmitoyltransferase, the enzyme catalyzing the initial step of sphingolipid biosynthesis. Hanada, K., Hara, T., Nishijima, M. FEBS Lett. (2000) [Pubmed]
Mammalian cell mutants resistant to a sphingomyelin-directed cytolysin. Genetic and biochemical evidence for complex formation of the LCB1 protein with the LCB2 protein for serine palmitoyltransferase. Hanada, K., Hara, T., Fukasawa, M., Yamaji, A., Umeda, M., Nishijima, M. J. Biol. Chem. (1998) [Pubmed]
A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis. Hanada, K., Hara, T., Nishijima, M., Kuge, O., Dickson, R.C., Nagiec, M.M. J. Biol. Chem. (1997) [Pubmed]