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小橋川 敬博


北海道大学大学院 構造生物学研究室研究員


kob@sci.hokudai.ac.jp


理学博士



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Yamaguchi M, Matoba K, Sawada R, Fujioka Y, Nakatogawa H, Yamamoto H, Kobashigawa Y, Hoshida H, Akada R, Ohsumi Y, Noda NN, Inagaki F.
Noncanonical recognition and UBL loading of distinct E2s by autophagy-essential Atg7.
Nat Struct Mol Biol. (2012)

Yokogawa M, Kobashigawa Y, Yoshida N, Ogura K, Harada K, Inagaki F.
NMR analyses of the interaction between the EEA1 FYVE domain and phosphoinositide embedded in lipid bilayer.
J Biol Chem., 287, 34936-34945 (2012)

Horiuchi M, Takahasi K, Kobashigawa Y, Ochiai M, Inagaki F.
A low-cost affinity purification system using β-1,3-glucan recognition protein and curdlan beads.
Protein Eng Des Sel., 25, 405-413 (2012)

Yamaguchi M, Noda NN, Yamamoto H, Shima T, Kumeta H, Kobashigawa Y, Akada R, Ohsumi Y, Inagaki F.
Structural Insights into Atg10-Mediated Formation of the Autophagy-Essential Atg12-Atg5 Conjugate.
Structure, 20, 1244-1254 (2012)

Kobashigawa Y, Inagaki F.
Structural biology: CrkL is not Crk-like.
Nat Chem Biol., 8, 504-505 (2012)

Kobashigawa Y, Saio T, Ushio M, Sekiguchi M, Yokochi M, Ogura K, Inagaki F.
Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein-protein complex structure determination.
J Biomol NMR., 53, 53-63 (2012)

Kobashigawa Y, Tomitaka A, Kumeta H, Noda NN, Yamaguchi M, Inagaki F.
Autoinhibition and phosphorylation-induced activation mechanisms of human cancer and autoimmune disease-related E3 protein Cbl-b.
Proc Natl Acad Sci U S A (2011)

Sekiguchi M, Kobashigawa Y, Kawasaki M, Yokochi M, Kiso T, Suzumura KI, Mori K, Teramura T, Inagaki F.
An evaluation tool for FKBP12-dependent and -independent mTOR inhibitors using a combination of FKBP-mTOR fusion protein, DSC and NMR.
Protein Eng Des Sel., 24, 811-817 (2011)

Kobashigawa Y, Harada K, Yoshida N, Ogura K, Inagaki F.
Phosphoinositide-incorporated lipid-protein nanodiscs: A tool for studying protein-lipid interactions.
Anal Biochem, 410, 77-83 (2011)

Saio T, Ogura K, Yokochi M, Kobashigawa Y, Inagaki F.
Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect.
J Biomol NMR, 44, 157-166 (2009)

Ogura K, Tandai T, Yoshinaga S, Kobashigawa Y, Kumeta H, Ito T, Sumimoto H, Inagaki F.
NMR structure of the heterodimer of Bem1 and Cdc24 PB1 domains from Saccharomyces cerevisiae.
J Biochem (Tokyo), 146, 317-325 (2009)

Kobashigawa Y, Kumeta H, Kanoh D, Inagaki F
The NMR structure of the TC10- and Cdc42-interacting domain of CIP4
J Biomol NMR, 44, 113-118 (2009)

Kobashigawa Y, Kumeta H, Ogura K, Inagaki F.
Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method.
J Biomol NMR, 43, 145-150 (2009)

Kobashigawa Y, Naito M, Inagaki F.
An efficient method for protein phosphorylation using the artificially introduction of cognate binding modules into kinases and substrates.
J Biotechnol., 131, 458-465 (2007)

Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F.
Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK.
Nat Struct Mol Biol., 14, 503-510 (2007)

Kobashigawa Y, Nishimiya Y, Miura K, Ohgiya S, Miura A, Tsuda S.
A part of ice nucleation protein exhibits the ice-binding ability.
FEBS Lett., 579, 1493-1497. (2005)

Watanabe M, Kobashigawa Y, Aizawa T, Demura M, Nitta K.
Volumetric behavior of the molten globule state of canine milk lysozyme.
Protein Pept Lett., 11, 325-330. (2004)

Watanabe M, Kobashigawa Y, Aizawa T, Demura M, Nitta K.
A non-native alpha-helix is formed in the beta-sheet region of the molten globule state of canine milk lysozyme.
Protein J., 23, 335-342. (2004)

Kumeta H, Miura A, Kobashigawa Y, Miura K, Oka C, Nemoto N, Nitta K, Tsuda S.
Low-temperature-induced structural changes in human lysozyme elucidated by three-dimensional NMR spectroscopy.
Biochemistry., 42, 1209-1216. (2003)

Kumeta H, Kobashigawa Y, Miura K, Nishimiya Y, Oka C, Nemoto N, Miura A, Nitta K, Tsuda S.
Assignments of 1H, 13C, and 15N resonances of human lysozyme at 4 degrees C.
J Biomol NMR., 22, 183-184. (2002)

Mizuguchi M, Kobashigawa Y, Kumaki Y, Demura M, Kawano K, Nitta K.
Effects of a helix substitution on the folding mechanism of bovine alpha-lactalbumin.
Proteins., 49, 95-103. (2002)

Tada M, Kobashigawa Y, Mizuguchi M, Miura K, Kouno T, Kumaki Y, Demura M, Nitta K, Kawano K.
Stabilization of protein by replacement of a fluctuating loop: structural analysis of a chimera of bovine alpha-lactalbumin and equine lysozyme.
Biochemistry., 41, 13807-13813. (2002)

Suetake T, Aizawa T, Koganesawa N, Osaki T, Kobashigawa Y, Demura M, Kawabata S, Kawano K, Tsuda S, Nitta K.
Free Full Text Production and characterization of recombinant tachycitin, the Cys-rich chitin-binding protein.
Protein Eng., 15, 763-769. (2002)

Kobashigawa Y, Miura K, Demura M, Nemoto N, Koshiba T, Nitta K, Tsuda S.
Assignment of 1H, 13C, and 15N resonances of canine milk lysozyme.
J Biomol NMR., 19, 387-388. (2001)

Niidome T, Murakami H, Kawazoe M, Hatakeyama T, Kobashigawa Y, Matsushita M, Kumaki Y, Demura M, Nitta K, Aoyagi H.
Carbohydrate recognition of gramicidin S analogues in aqueous medium.
Bioorg Med Chem Lett., 11, 1893-1896. (2001)

Kurokawa Y, Koganesawa N, Kobashigawa Y, Koshiba T, Demura M, Niita K.
Oxidative folding of human lysozyme: effects of the loss of two disulfide bonds and the introduction of a calcium-binding site.
J Protein Chem., 20, 293-303. (2001)

Koshiba T, Kobashigawa Y, Demura M, Nitta K.
Energetics of three-state unfolding of a protein: canine milk lysozyme.
Protein Eng., 14, 967-974. (2001)

Koshiba T, Yao M, Kobashigawa Y, Demura M, Nakagawa A, Tanaka I, Kuwajima K, Nitta K.
Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme.
Biochemistry., 39, 3248-3257. (2000)

Kobashigawa Y, Demura M, Koshiba T, Kumaki Y, Kuwajima K, Nitta K.
Hydrogen exchange study of canine milk lysozyme: stabilization mechanism of the molten globule.
Proteins., 40, 579-589. (2000)

Kobashigawa Y, Sakurai M, Nitta K.
Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state.
Protein Sci., 8, 2765-7272. (1999)










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