Tomomitsu Hatakeyama - Publications

Publications (48)

ECB-PERS-4214

Publications By Tomomitsu Hatakeyama

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Galactose-Specific, Hemolytic Lectin CEL-III from Cucumaria echinata., Hatakeyama T., Methods Mol Biol. January 1, 2020; 2132 159-164.
Carbohydrate recognition by the rhamnose-binding lectin SUL-I with a novel three-domain structure isolated from the venom of globiferous pedicellariae of the flower sea urchin Toxopneustes pileolus., Hatakeyama T, Ichise A, Unno H, Goda S, Oda T, Tateno H, Hirabayashi J, Sakai H, Nakagawa H., Protein Sci. August 1, 2017; 26 (8): 1574-1583.
Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III., Nagao T, Masaki R, Unno H, Goda S, Hatakeyama T., Biosci Biotechnol Biochem. October 1, 2016; 80 (10): 1966-9.
cDNA cloning and expression of Contractin A, a phospholipase A2-like protein from the globiferous pedicellariae of the venomous sea urchin Toxopneustes pileolus., Hatakeyama T, Higashi E, Nakagawa H., Toxicon. December 15, 2015; 108 46-52.
Mannose-recognition mutant of the galactose/N-acetylgalactosamine-specific C-type lectin CEL-I engineered by site-directed mutagenesis., Moriuchi H, Unno H, Goda S, Tateno H, Hirabayashi J, Hatakeyama T., Biochim Biophys Acta. July 1, 2015; 1850 (7): 1457-65.
cDNA cloning and characterization of a rhamnose-binding lectin SUL-I from the toxopneustid sea urchin Toxopneustes pileolus venom., Hatakeyama T, Ichise A, Yonekura T, Unno H, Goda S, Nakagawa H., Toxicon. February 1, 2015; 94 8-15.
Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process., Unno H, Goda S, Hatakeyama T., J Biol Chem. May 2, 2014; 289 (18): 12805-12.
Identification of the amino acid residues involved in the hemolytic activity of the Cucumaria echinata lectin CEL-III., Hisamatsu K, Nagao T, Unno H, Goda S, Hatakeyama T., Biochim Biophys Acta. August 1, 2013; 1830 (8): 4211-7.
Alteration of the carbohydrate-binding specificity of a C-type lectin CEL-I mutant with an EPN carbohydrate-binding motif., Hatakeyama T, Ishimine T, Baba T, Kimura M, Unno H, Goda S., Protein Pept Lett. July 1, 2013; 20 (7): 796-801.
Crystallization and preliminary crystallographic study of oligomers of the haemolytic lectin CEL-III from the sea cucumber Cucumaria echinata., Unno H, Hisamatsu K, Nagao T, Tateya Y, Matsumoto N, Goda S, Hatakeyama T., Acta Crystallogr Sect F Struct Biol Cryst Commun. April 1, 2013; 69 (Pt 4): 416-20.
Effects of detergents on the oligomeric structures of hemolytic lectin CEL-III as determined by small-angle X-ray scattering., Goda S, Sadakata H, Unno H, Hatakeyama T., Biosci Biotechnol Biochem. January 1, 2013; 77 (3): 679-81.
An assay for carbohydrate-binding activity of lectins using polyamidoamine dendrimer conjugated with carbohydrates., Hatakeyama T, Karino R, Terai Y, Kimura M, Unno H, Goda S., Biosci Biotechnol Biochem. January 1, 2012; 76 (10): 1999-2001.
Galactose recognition by a tetrameric C-type lectin, CEL-IV, containing the EPN carbohydrate recognition motif., Hatakeyama T, Kamiya T, Kusunoki M, Nakamura-Tsuruta S, Hirabayashi J, Goda S, Unno H., J Biol Chem. March 25, 2011; 286 (12): 10305-15.
Mitogenic activity of CEL-I, an N-acetylgalactosamine (GalNAc)-specific C-type lectin, isolated from the marine invertebrate Cucumaria echinata (Holothuroidea)., Jiang Z, Kim D, Yamasaki Y, Yamanishi T, Hatakeyama T, Yamaguchi K, Oda T., Biosci Biotechnol Biochem. January 1, 2010; 74 (8): 1613-6.
CEL-I, an N-acetylgalactosamine (GalNAc)-specific C-type lectin, induces nitric oxide production in RAW264.7 mouse macrophage cell line., Yamanishi T, Hatakeyama T, Yamaguchi K, Oda T., J Biochem. August 1, 2009; 146 (2): 209-17.
Effects of Ca2+ on refolding of the recombinant hemolytic lectin CEL-III., Hisamatsu K, Unno H, Goda S, Hatakeyama T., Biosci Biotechnol Biochem. May 1, 2009; 73 (5): 1203-5.
Roles of the valine clusters in domain 3 of the hemolytic lectin CEL-III in its oligomerization and hemolytic abilities., Hisamatsu K, Unno H, Goda S, Hatakeyama T., Protein Pept Lett. January 1, 2009; 16 (4): 411-4.
Characterization of the {alpha}-helix region in domain 3 of the haemolytic lectin CEL-III: implications for self-oligomerization and haemolytic processes., Hisamatsu K, Tsuda N, Goda S, Hatakeyama T., J Biochem. January 1, 2008; 143 (1): 79-86.
C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil folds., Hatakeyama T, Unno H, Kouzuma Y, Uchida T, Eto S, Hidemura H, Kato N, Yonekura M, Kusunoki M., J Biol Chem. December 28, 2007; 282 (52): 37826-35.
CEL-I, an invertebrate N-acetylgalactosamine-specific C-type lectin, induces TNF-alpha and G-CSF production by mouse macrophage cell line RAW264.7 cells., Yamanishi T, Yamamoto Y, Hatakeyama T, Yamaguchi K, Oda T., J Biochem. November 1, 2007; 142 (5): 587-95.
Characterization of a recombinant C-type lectin, rCEL-IV, expressed in Escherichia coli cells using a synthetic gene., Hatakeyama T, Hozawa T, Hirotani I, Tsuda N, Kusunoki M, Shiba K., Biochim Biophys Acta. March 1, 2006; 1760 (3): 318-25.
Cytotoxicity of a GalNAc-specific C-type lectin CEL-I toward various cell lines., Kuramoto T, Uzuyama H, Hatakeyama T, Tamura T, Nakashima T, Yamaguchi K, Oda T., J Biochem. January 1, 2005; 137 (1): 41-50.
Characteristic recognition of N-acetylgalactosamine by an invertebrate C-type Lectin, CEL-I, revealed by X-ray crystallographic analysis., Sugawara H, Kusunoki M, Kurisu G, Fujimoto T, Aoyagi H, Hatakeyama T., J Biol Chem. October 22, 2004; 279 (43): 45219-25.
Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism., Uchida T, Yamasaki T, Eto S, Sugawara H, Kurisu G, Nakagawa A, Kusunoki M, Hatakeyama T., J Biol Chem. August 27, 2004; 279 (35): 37133-41.
Antibacterial activity of peptides derived from the C-terminal region of a hemolytic lectin, CEL-III, from the marine invertebrate Cucumaria echinata., Hatakeyama T, Suenaga T, Eto S, Niidome T, Aoyagi H., J Biochem. January 1, 2004; 135 (1): 65-70.
Characterization of recombinant CEL-I, a GalNAc-specific C-type lectin, expressed in Escherichia coli using an artificial synthetic gene., Hatakeyama T, Shiba K, Matsuo N, Fujimoto T, Oda T, Sugawara H, Aoyagi H., J Biochem. January 1, 2004; 135 (1): 101-7.
Characterization of functional domains of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata., Kouzuma Y, Suzuki Y, Nakano M, Matsuyama K, Tojo S, Kimura M, Yamasaki T, Aoyagi H, Hatakeyama T., J Biochem. September 1, 2003; 134 (3): 395-402.
Fishing for bioactive substances from scorpionfish and some sea urchins., Satoh F, Nakagawa H, Yamada H, Nagasaka K, Nagasaka T, Araki Y, Tomihara Y, Nozaki M, Sakuraba H, Ohshima T, Hatakeyama T, Aoyagi H., J Nat Toxins. December 1, 2002; 11 (4): 297-304.
Oligomerization process of the hemolytic lectin CEL-III purified from a sea cucumber, Cucumaria echinata., Kuwahara H, Yamasaki T, Hatakeyama T, Aoyagi H, Fujisawa T., J Biochem. May 1, 2002; 131 (5): 751-6.
Crystallization and preliminary crystallographic study of an invertebrate C-type lectin, CEL-I, from the marine invertebrate Cucumaria echinata., Hatakeyama T, Matsuo N, Aoyagi H, Sugawara H, Uchida T, Kurisu G, Kusunoki M., Acta Crystallogr D Biol Crystallogr. January 1, 2002; 58 (Pt 1): 143-4.
Amino acid sequence and carbohydrate-binding analysis of the N-acetyl-D-galactosamine-specific C-type lectin, CEL-I, from the Holothuroidea, Cucumaria echinata., Hatakeyama T, Matsuo N, Shiba K, Nishinohara S, Yamasaki N, Sugawara H, Aoyagi H., Biosci Biotechnol Biochem. January 1, 2002; 66 (1): 157-63.
Effects of chemical modification of carboxyl groups in the hemolytic lectin CEL-III on its hemolytic and carbohydrate-binding activities., Kuwahara H, Funada T, Hatakeyama T, Aoyagi H., Biosci Biotechnol Biochem. June 1, 2000; 64 (6): 1278-81.
Molecular mechanism for pore-formation in lipid membranes by the hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata., Kouriki-Nagatomo H, Hatakeyama T, Jelokhani-Niaraki M, Kondo M, Ehara T, Yamasaki N., Biosci Biotechnol Biochem. July 1, 1999; 63 (7): 1279-84.
Carbohydrate-dependent hemolytic activity of the conjugate composed of a C-type lectin, CEL-I, and an amphiphilic alpha-helical peptide, 4(3)-beta Ala2., Hatakeyama T, Kamine T, Konishi Y, Kuwahara H, Niidome T, Aoyagi H., Biosci Biotechnol Biochem. July 1, 1999; 63 (7): 1312-4.
Effect of the hemolytic lectin CEL-III from Holothuroidea Cucumaria echinata on the ANS fluorescence responses in sensitive MDCK and resistant CHO cells., Oda T, Shinmura N, Nishioka Y, Komatsu N, Hatakeyama T, Muramatsu T., J Biochem. April 1, 1999; 125 (4): 713-20.
Characterization of the interaction of hemolytic lectin CEL-III from the marine invertebrate, Cucumaria echinata, with artificial lipid membranes: involvement of neutral sphingoglycolipids in the pore-forming process., Hatakeyama T, Sato T, Taira E, Kuwahara H, Niidome T, Aoyagi H., J Biochem. February 1, 1999; 125 (2): 277-84.
Studies on the carbohydrate binding sites of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata., Sallay I, Hatakeyama T, Yamasaki N., Biosci Biotechnol Biochem. September 1, 1998; 62 (9): 1757-61.
Chemical modification of the hemolytic lectin CEL-III by succinic anhydride: involvement of amino groups in the oligomerization process., Hatakeyama T, Matsuyama Y, Funada T, Fukuyama S, Kuwahara H, Aoyagi H, Yamasaki N., Biosci Biotechnol Biochem. June 1, 1998; 62 (6): 1185-9.
Small-angle X-ray scattering study on CEL-III, a hemolytic lectin from Holothuroidea Cucumaria echinata, and its oligomer induced by the binding of specific carbohydrate., Fujisawa T, Kuwahara H, Hiromasa Y, Niidome T, Aoyagi H, Hatakeyama T., FEBS Lett. September 1, 1997; 414 (1): 79-83.
Temperature- and pH-dependent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata on various cell lines., Oda T, Tsuru M, Hatakeyama T, Nagatomo H, Muramatsu T, Yamasaki N., J Biochem. March 1, 1997; 121 (3): 560-7.
Carbohydrate-binding properties of the hemolytic lectin CEL-III from the holothuroidea Cucumaria echinata as analyzed using carbohydrate-coated microplate., Hatakeyama T, Miyamoto Y, Nagatomo H, Sallay I, Yamasaki N., J Biochem. January 1, 1997; 121 (1): 63-7.
Oligomerization of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata induced by the binding of carbohydrate ligands., Hatakeyama T, Furukawa M, Nagatomo H, Yamasaki N, Mori T., J Biol Chem. July 12, 1996; 271 (28): 16915-20.
An assay for lectin activity using microtiter plate with chemically immobilized carbohydrates., Hatakeyama T, Murakami K, Miyamoto Y, Yamasaki N., Anal Biochem. June 1, 1996; 237 (2): 188-92.
Amino acid sequence of a C-type lectin CEL-IV from the marine invertebrate Cucumaria echinata., Hatakeyama T, Ohuchi K, Kuroki M, Yamasaki N., Biosci Biotechnol Biochem. July 1, 1995; 59 (7): 1314-7.
Interaction of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane., Hatakeyama T, Nagatomo H, Yamasaki N., J Biol Chem. February 24, 1995; 270 (8): 3560-4.
Purification and characterization of four Ca(2+)-dependent lectins from the marine invertebrate, Cucumaria echinata., Hatakeyama T, Kohzaki H, Nagatomo H, Yamasaki N., J Biochem. July 1, 1994; 116 (1): 209-14.
Amino acid sequence of a lectin from the sea cucumber, Stichopus japonicus, and its structural relationship to the C-type animal lectin family., Himeshima T, Hatakeyama T, Yamasaki N., J Biochem. April 1, 1994; 115 (4): 689-92.
Purification and characterization of two lectins from the sea cucumber Stichopus japonicus., Hatakeyama T, Himeshima T, Komatsu A, Yamasaki N., Biosci Biotechnol Biochem. October 1, 1993; 57 (10): 1736-9.

Galactose-Specific, Hemolytic Lectin CEL-III from Cucumaria echinata., Hatakeyama T., Methods Mol Biol. January 1, 2020; 2132 159-164.

Carbohydrate recognition by the rhamnose-binding lectin SUL-I with a novel three-domain structure isolated from the venom of globiferous pedicellariae of the flower sea urchin Toxopneustes pileolus., Hatakeyama T, Ichise A, Unno H, Goda S, Oda T, Tateno H, Hirabayashi J, Sakai H, Nakagawa H., Protein Sci. August 1, 2017; 26 (8): 1574-1583.

Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III., Nagao T, Masaki R, Unno H, Goda S, Hatakeyama T., Biosci Biotechnol Biochem. October 1, 2016; 80 (10): 1966-9.

cDNA cloning and expression of Contractin A, a phospholipase A2-like protein from the globiferous pedicellariae of the venomous sea urchin Toxopneustes pileolus., Hatakeyama T, Higashi E, Nakagawa H., Toxicon. December 15, 2015; 108 46-52.

Mannose-recognition mutant of the galactose/N-acetylgalactosamine-specific C-type lectin CEL-I engineered by site-directed mutagenesis., Moriuchi H, Unno H, Goda S, Tateno H, Hirabayashi J, Hatakeyama T., Biochim Biophys Acta. July 1, 2015; 1850 (7): 1457-65.

cDNA cloning and characterization of a rhamnose-binding lectin SUL-I from the toxopneustid sea urchin Toxopneustes pileolus venom., Hatakeyama T, Ichise A, Yonekura T, Unno H, Goda S, Nakagawa H., Toxicon. February 1, 2015; 94 8-15.

Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process., Unno H, Goda S, Hatakeyama T., J Biol Chem. May 2, 2014; 289 (18): 12805-12.

Identification of the amino acid residues involved in the hemolytic activity of the Cucumaria echinata lectin CEL-III., Hisamatsu K, Nagao T, Unno H, Goda S, Hatakeyama T., Biochim Biophys Acta. August 1, 2013; 1830 (8): 4211-7.

Alteration of the carbohydrate-binding specificity of a C-type lectin CEL-I mutant with an EPN carbohydrate-binding motif., Hatakeyama T, Ishimine T, Baba T, Kimura M, Unno H, Goda S., Protein Pept Lett. July 1, 2013; 20 (7): 796-801.

Crystallization and preliminary crystallographic study of oligomers of the haemolytic lectin CEL-III from the sea cucumber Cucumaria echinata., Unno H, Hisamatsu K, Nagao T, Tateya Y, Matsumoto N, Goda S, Hatakeyama T., Acta Crystallogr Sect F Struct Biol Cryst Commun. April 1, 2013; 69 (Pt 4): 416-20.

Effects of detergents on the oligomeric structures of hemolytic lectin CEL-III as determined by small-angle X-ray scattering., Goda S, Sadakata H, Unno H, Hatakeyama T., Biosci Biotechnol Biochem. January 1, 2013; 77 (3): 679-81.

An assay for carbohydrate-binding activity of lectins using polyamidoamine dendrimer conjugated with carbohydrates., Hatakeyama T, Karino R, Terai Y, Kimura M, Unno H, Goda S., Biosci Biotechnol Biochem. January 1, 2012; 76 (10): 1999-2001.

Galactose recognition by a tetrameric C-type lectin, CEL-IV, containing the EPN carbohydrate recognition motif., Hatakeyama T, Kamiya T, Kusunoki M, Nakamura-Tsuruta S, Hirabayashi J, Goda S, Unno H., J Biol Chem. March 25, 2011; 286 (12): 10305-15.

Mitogenic activity of CEL-I, an N-acetylgalactosamine (GalNAc)-specific C-type lectin, isolated from the marine invertebrate Cucumaria echinata (Holothuroidea)., Jiang Z, Kim D, Yamasaki Y, Yamanishi T, Hatakeyama T, Yamaguchi K, Oda T., Biosci Biotechnol Biochem. January 1, 2010; 74 (8): 1613-6.

CEL-I, an N-acetylgalactosamine (GalNAc)-specific C-type lectin, induces nitric oxide production in RAW264.7 mouse macrophage cell line., Yamanishi T, Hatakeyama T, Yamaguchi K, Oda T., J Biochem. August 1, 2009; 146 (2): 209-17.

Effects of Ca2+ on refolding of the recombinant hemolytic lectin CEL-III., Hisamatsu K, Unno H, Goda S, Hatakeyama T., Biosci Biotechnol Biochem. May 1, 2009; 73 (5): 1203-5.

Roles of the valine clusters in domain 3 of the hemolytic lectin CEL-III in its oligomerization and hemolytic abilities., Hisamatsu K, Unno H, Goda S, Hatakeyama T., Protein Pept Lett. January 1, 2009; 16 (4): 411-4.

Characterization of the {alpha}-helix region in domain 3 of the haemolytic lectin CEL-III: implications for self-oligomerization and haemolytic processes., Hisamatsu K, Tsuda N, Goda S, Hatakeyama T., J Biochem. January 1, 2008; 143 (1): 79-86.

C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil folds., Hatakeyama T, Unno H, Kouzuma Y, Uchida T, Eto S, Hidemura H, Kato N, Yonekura M, Kusunoki M., J Biol Chem. December 28, 2007; 282 (52): 37826-35.

CEL-I, an invertebrate N-acetylgalactosamine-specific C-type lectin, induces TNF-alpha and G-CSF production by mouse macrophage cell line RAW264.7 cells., Yamanishi T, Yamamoto Y, Hatakeyama T, Yamaguchi K, Oda T., J Biochem. November 1, 2007; 142 (5): 587-95.

Characterization of a recombinant C-type lectin, rCEL-IV, expressed in Escherichia coli cells using a synthetic gene., Hatakeyama T, Hozawa T, Hirotani I, Tsuda N, Kusunoki M, Shiba K., Biochim Biophys Acta. March 1, 2006; 1760 (3): 318-25.

Cytotoxicity of a GalNAc-specific C-type lectin CEL-I toward various cell lines., Kuramoto T, Uzuyama H, Hatakeyama T, Tamura T, Nakashima T, Yamaguchi K, Oda T., J Biochem. January 1, 2005; 137 (1): 41-50.

Characteristic recognition of N-acetylgalactosamine by an invertebrate C-type Lectin, CEL-I, revealed by X-ray crystallographic analysis., Sugawara H, Kusunoki M, Kurisu G, Fujimoto T, Aoyagi H, Hatakeyama T., J Biol Chem. October 22, 2004; 279 (43): 45219-25.

Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism., Uchida T, Yamasaki T, Eto S, Sugawara H, Kurisu G, Nakagawa A, Kusunoki M, Hatakeyama T., J Biol Chem. August 27, 2004; 279 (35): 37133-41.

Antibacterial activity of peptides derived from the C-terminal region of a hemolytic lectin, CEL-III, from the marine invertebrate Cucumaria echinata., Hatakeyama T, Suenaga T, Eto S, Niidome T, Aoyagi H., J Biochem. January 1, 2004; 135 (1): 65-70.

Characterization of recombinant CEL-I, a GalNAc-specific C-type lectin, expressed in Escherichia coli using an artificial synthetic gene., Hatakeyama T, Shiba K, Matsuo N, Fujimoto T, Oda T, Sugawara H, Aoyagi H., J Biochem. January 1, 2004; 135 (1): 101-7.

Characterization of functional domains of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata., Kouzuma Y, Suzuki Y, Nakano M, Matsuyama K, Tojo S, Kimura M, Yamasaki T, Aoyagi H, Hatakeyama T., J Biochem. September 1, 2003; 134 (3): 395-402.

Fishing for bioactive substances from scorpionfish and some sea urchins., Satoh F, Nakagawa H, Yamada H, Nagasaka K, Nagasaka T, Araki Y, Tomihara Y, Nozaki M, Sakuraba H, Ohshima T, Hatakeyama T, Aoyagi H., J Nat Toxins. December 1, 2002; 11 (4): 297-304.

Oligomerization process of the hemolytic lectin CEL-III purified from a sea cucumber, Cucumaria echinata., Kuwahara H, Yamasaki T, Hatakeyama T, Aoyagi H, Fujisawa T., J Biochem. May 1, 2002; 131 (5): 751-6.

Crystallization and preliminary crystallographic study of an invertebrate C-type lectin, CEL-I, from the marine invertebrate Cucumaria echinata., Hatakeyama T, Matsuo N, Aoyagi H, Sugawara H, Uchida T, Kurisu G, Kusunoki M., Acta Crystallogr D Biol Crystallogr. January 1, 2002; 58 (Pt 1): 143-4.

Amino acid sequence and carbohydrate-binding analysis of the N-acetyl-D-galactosamine-specific C-type lectin, CEL-I, from the Holothuroidea, Cucumaria echinata., Hatakeyama T, Matsuo N, Shiba K, Nishinohara S, Yamasaki N, Sugawara H, Aoyagi H., Biosci Biotechnol Biochem. January 1, 2002; 66 (1): 157-63.

Effects of chemical modification of carboxyl groups in the hemolytic lectin CEL-III on its hemolytic and carbohydrate-binding activities., Kuwahara H, Funada T, Hatakeyama T, Aoyagi H., Biosci Biotechnol Biochem. June 1, 2000; 64 (6): 1278-81.

Molecular mechanism for pore-formation in lipid membranes by the hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata., Kouriki-Nagatomo H, Hatakeyama T, Jelokhani-Niaraki M, Kondo M, Ehara T, Yamasaki N., Biosci Biotechnol Biochem. July 1, 1999; 63 (7): 1279-84.

Carbohydrate-dependent hemolytic activity of the conjugate composed of a C-type lectin, CEL-I, and an amphiphilic alpha-helical peptide, 4(3)-beta Ala2., Hatakeyama T, Kamine T, Konishi Y, Kuwahara H, Niidome T, Aoyagi H., Biosci Biotechnol Biochem. July 1, 1999; 63 (7): 1312-4.

Effect of the hemolytic lectin CEL-III from Holothuroidea Cucumaria echinata on the ANS fluorescence responses in sensitive MDCK and resistant CHO cells., Oda T, Shinmura N, Nishioka Y, Komatsu N, Hatakeyama T, Muramatsu T., J Biochem. April 1, 1999; 125 (4): 713-20.

Characterization of the interaction of hemolytic lectin CEL-III from the marine invertebrate, Cucumaria echinata, with artificial lipid membranes: involvement of neutral sphingoglycolipids in the pore-forming process., Hatakeyama T, Sato T, Taira E, Kuwahara H, Niidome T, Aoyagi H., J Biochem. February 1, 1999; 125 (2): 277-84.

Studies on the carbohydrate binding sites of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata., Sallay I, Hatakeyama T, Yamasaki N., Biosci Biotechnol Biochem. September 1, 1998; 62 (9): 1757-61.

Chemical modification of the hemolytic lectin CEL-III by succinic anhydride: involvement of amino groups in the oligomerization process., Hatakeyama T, Matsuyama Y, Funada T, Fukuyama S, Kuwahara H, Aoyagi H, Yamasaki N., Biosci Biotechnol Biochem. June 1, 1998; 62 (6): 1185-9.

Small-angle X-ray scattering study on CEL-III, a hemolytic lectin from Holothuroidea Cucumaria echinata, and its oligomer induced by the binding of specific carbohydrate., Fujisawa T, Kuwahara H, Hiromasa Y, Niidome T, Aoyagi H, Hatakeyama T., FEBS Lett. September 1, 1997; 414 (1): 79-83.

Temperature- and pH-dependent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata on various cell lines., Oda T, Tsuru M, Hatakeyama T, Nagatomo H, Muramatsu T, Yamasaki N., J Biochem. March 1, 1997; 121 (3): 560-7.

Carbohydrate-binding properties of the hemolytic lectin CEL-III from the holothuroidea Cucumaria echinata as analyzed using carbohydrate-coated microplate., Hatakeyama T, Miyamoto Y, Nagatomo H, Sallay I, Yamasaki N., J Biochem. January 1, 1997; 121 (1): 63-7.

Oligomerization of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata induced by the binding of carbohydrate ligands., Hatakeyama T, Furukawa M, Nagatomo H, Yamasaki N, Mori T., J Biol Chem. July 12, 1996; 271 (28): 16915-20.

An assay for lectin activity using microtiter plate with chemically immobilized carbohydrates., Hatakeyama T, Murakami K, Miyamoto Y, Yamasaki N., Anal Biochem. June 1, 1996; 237 (2): 188-92.

Amino acid sequence of a C-type lectin CEL-IV from the marine invertebrate Cucumaria echinata., Hatakeyama T, Ohuchi K, Kuroki M, Yamasaki N., Biosci Biotechnol Biochem. July 1, 1995; 59 (7): 1314-7.

Interaction of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane., Hatakeyama T, Nagatomo H, Yamasaki N., J Biol Chem. February 24, 1995; 270 (8): 3560-4.

Purification and characterization of four Ca(2+)-dependent lectins from the marine invertebrate, Cucumaria echinata., Hatakeyama T, Kohzaki H, Nagatomo H, Yamasaki N., J Biochem. July 1, 1994; 116 (1): 209-14.

Amino acid sequence of a lectin from the sea cucumber, Stichopus japonicus, and its structural relationship to the C-type animal lectin family., Himeshima T, Hatakeyama T, Yamasaki N., J Biochem. April 1, 1994; 115 (4): 689-92.

Purification and characterization of two lectins from the sea cucumber Stichopus japonicus., Hatakeyama T, Himeshima T, Komatsu A, Yamasaki N., Biosci Biotechnol Biochem. October 1, 1993; 57 (10): 1736-9.

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