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Volumn 32, Issue 1, 2003, Pages 68-74

Refolding and characterization of the functional ligand-binding domain of human lectin-like oxidized LDL receptor

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Indexed keywords

ESCHERICHIA COLI;

EID: 0344099414     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(03)00220-1     Document Type: Article
Times cited : (13)

References (30)
  • 2
    • 0032528913 scopus 로고    scopus 로고
    • Identification of the lectin-like receptor for oxidized low-density lipoprotein in human macrophages and its potential role as a scavenger receptor
    • H. Yoshida, N. Kondratenko, S. Green, D. Steinberg, O. Quehenberger, Identification of the lectin-like receptor for oxidized low-density lipoprotein in human macrophages and its potential role as a scavenger receptor, Biochem. J. 334 (Part 1) (1998) 9-13.
    • (1998) Biochem. J. , vol.334 , Issue.1 PART , pp. 9-13
    • Yoshida, H.1    Kondratenko, N.2    Green, S.3    Steinberg, D.4    Quehenberger, O.5
  • 4
    • 0034602694 scopus 로고    scopus 로고
    • A platelet-endothelium interaction mediated by lectin-like oxidized low-density lipoprotein receptor-1
    • M. Kakutani, T. Masaki, T. Sawamura, A platelet-endothelium interaction mediated by lectin-like oxidized low-density lipoprotein receptor-1, Proc. Natl. Acad. Sci. USA 97 (2000) 360-364.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 360-364
    • Kakutani, M.1    Masaki, T.2    Sawamura, T.3
  • 5
    • 0032482958 scopus 로고    scopus 로고
    • Lectin-like oxidized low-density lipoprotein receptor 1 mediates phagocytosis of aged/apoptotic cells in endothelial cells
    • K. Oka, T. Sawamura, K. Kikuta, S. Itokawa, N. Kume, T. Kita, T. Masaki, Lectin-like oxidized low-density lipoprotein receptor 1 mediates phagocytosis of aged/apoptotic cells in endothelial cells, Proc. Natl. Acad. Sci. USA 95 (1998) 9535-9540.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9535-9540
    • Oka, K.1    Sawamura, T.2    Kikuta, K.3    Itokawa, S.4    Kume, N.5    Kita, T.6    Masaki, T.7
  • 8
    • 0033553395 scopus 로고    scopus 로고
    • Upregulation of endothelial receptor for oxidized low-density lipoprotein (LOX-1) in cultured human coronary artery endothelial cells by angiotensin II type 1 receptor activation
    • D.Y. Li, Y.C. Zhang, M.I. Philips, T. Sawamura, J.L. Mehta, Upregulation of endothelial receptor for oxidized low-density lipoprotein (LOX-1) in cultured human coronary artery endothelial cells by angiotensin II type 1 receptor activation, Circ. Res. 84 (1999) 1043-1049.
    • (1999) Circ. Res. , vol.84 , pp. 1043-1049
    • Li, D.Y.1    Zhang, Y.C.2    Philips, M.I.3    Sawamura, T.4    Mehta, J.L.5
  • 9
    • 0033378304 scopus 로고    scopus 로고
    • Induction of lectin-like oxidized LDL receptor by oxidized LDL and lysophosphatidylcholine in cultured endothelial cells
    • T. Aoyama, H. Fujiwara, T. Masaki, T. Sawamura, Induction of lectin-like oxidized LDL receptor by oxidized LDL and lysophosphatidylcholine in cultured endothelial cells, J. Mol. Cell Cardiol. 31 (1999) 2101-2114.
    • (1999) J. Mol. Cell Cardiol. , vol.31 , pp. 2101-2114
    • Aoyama, T.1    Fujiwara, H.2    Masaki, T.3    Sawamura, T.4
  • 10
    • 0032581338 scopus 로고    scopus 로고
    • Identification and autoregulation of receptor for OX-LDL in cultured human coronary artery endothelial cells
    • J.L. Mehta, D.Y. Li, Identification and autoregulation of receptor for OX-LDL in cultured human coronary artery endothelial cells, Biochem. Biophys. Res. Commun. 248 (1998) 511-514.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 511-514
    • Mehta, J.L.1    Li, D.Y.2
  • 11
    • 0032573388 scopus 로고    scopus 로고
    • Expression of lectin-like oxidized low density lipoprotein receptor-1 in human and murine macrophages: Upregulated expression by TNF-alpha
    • H. Moriwaki, N. Kume, H. Kataoka, T. Murase, E. Nishi, T. Sawamura, T. Masaki, T. Kita, Expression of lectin-like oxidized low density lipoprotein receptor-1 in human and murine macrophages: upregulated expression by TNF-alpha, FEBS Lett. 440 (1998) 29-32.
    • (1998) FEBS Lett. , vol.440 , pp. 29-32
    • Moriwaki, H.1    Kume, N.2    Kataoka, H.3    Murase, T.4    Nishi, E.5    Sawamura, T.6    Masaki, T.7    Kita, T.8
  • 14
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • W.I. Weis, M.E. Taylor, K. Drickamer, The C-type lectin superfamily in the immune system, Immunol. Rev. 163 (1998) 19-34.
    • (1998) Immunol. Rev. , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 15
    • 0035032519 scopus 로고    scopus 로고
    • Characterization of residues and sequences of the carbohydrate recognition domain required for cell surface localization and ligand binding of human lectin-like oxidized LDL receptor
    • X. Shi, S. Niimi, T. Ohtani, S. Machida, Characterization of residues and sequences of the carbohydrate recognition domain required for cell surface localization and ligand binding of human lectin-like oxidized LDL receptor, J. Cell Sci. 114 (2001) 1273-1282.
    • (2001) J. Cell Sci. , vol.114 , pp. 1273-1282
    • Shi, X.1    Niimi, S.2    Ohtani, T.3    Machida, S.4
  • 16
    • 0034827032 scopus 로고    scopus 로고
    • Involvement of conserved hydrophobic residues in the CTLD of human lectin-like oxidized LDL receptor in ligand binding
    • X. Shi, S. Ogawa, T. Otani, S. Machida, Involvement of conserved hydrophobic residues in the CTLD of human lectin-like oxidized LDL receptor in ligand binding, Mol. Cell Biol. Res. Commun. 4 (2001) 292-298.
    • (2001) Mol. Cell Biol. Res. Commun. , vol.4 , pp. 292-298
    • Shi, X.1    Ogawa, S.2    Otani, T.3    Machida, S.4
  • 17
    • 0035871224 scopus 로고    scopus 로고
    • Conserved C-terminal residues within the lectin-like domain of LOX-1 are essential for oxidized low-density-lipoprotein binding
    • M. Chen, S. Narumiya, T. Masaki, T. Sawamura, Conserved C-terminal residues within the lectin-like domain of LOX-1 are essential for oxidized low-density-lipoprotein binding, Biochem. J. 355 (2001) 289-296.
    • (2001) Biochem. J. , vol.355 , pp. 289-296
    • Chen, M.1    Narumiya, S.2    Masaki, T.3    Sawamura, T.4
  • 19
    • 0032504764 scopus 로고    scopus 로고
    • Inducible expression of lectin-like oxidized LDL receptor-1 in vascular endothelial cells
    • N. Kume, T. Murase, H. Moriwaki, T. Aoyama, T. Sawamura, T. Masaki, T. Kita, Inducible expression of lectin-like oxidized LDL receptor-1 in vascular endothelial cells, Circ. Res. 83 (1998) 322-327.
    • (1998) Circ. Res. , vol.83 , pp. 322-327
    • Kume, N.1    Murase, T.2    Moriwaki, H.3    Aoyama, T.4    Sawamura, T.5    Masaki, T.6    Kita, T.7
  • 20
    • 0034922951 scopus 로고    scopus 로고
    • Roles of lectin-like oxidized LDL receptor-1 and its soluble forms in atherogenesis
    • N. Kume, T. Kita, Roles of lectin-like oxidized LDL receptor-1 and its soluble forms in atherogenesis, Curr. Opin. Lipidol. 12 (2001) 419-423.
    • (2001) Curr. Opin. Lipidol. , vol.12 , pp. 419-423
    • Kume, N.1    Kita, T.2
  • 21
    • 0033053772 scopus 로고    scopus 로고
    • Structure of CD94 reveals a novel C-type lectin fold: Implications for the NK cell-associated CD94/NKG2 receptors
    • J.C. Boyington, A.N. Riaz, A. Patamawenu, J.E. Coligan, A.G. Brooks, P.D. Sun, Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors, Immunity 10 (1999) 75-82.
    • (1999) Immunity , vol.10 , pp. 75-82
    • Boyington, J.C.1    Riaz, A.N.2    Patamawenu, A.3    Coligan, J.E.4    Brooks, A.G.5    Sun, P.D.6
  • 22
    • 0034610309 scopus 로고    scopus 로고
    • Crystal structure of human CD69: A C-type lectin-like activation marker of hematopoietic cells
    • K. Natarajan, M.W. Sawicki, D.H. Margulies, R.A. Mariuzza, Crystal structure of human CD69: a C-type lectin-like activation marker of hematopoietic cells, Biochemistry 39 (2000) 14779-14786.
    • (2000) Biochemistry , vol.39 , pp. 14779-14786
    • Natarajan, K.1    Sawicki, M.W.2    Margulies, D.H.3    Mariuzza, R.A.4
  • 23
    • 0035862324 scopus 로고    scopus 로고
    • The functional binding site for the C-type lectin-like natural killer cell receptor Ly49A spans three domains of its major histocompatibility complex Class I ligand
    • N. Matsumoto, M. Mitsuki, K. Tajima, W.M. Yokoyama, K. Yomamoto, The functional binding site for the C-type lectin-like natural killer cell receptor Ly49A spans three domains of its major histocompatibility complex Class I ligand, J. Exp. Med. 193 (2001) 147-157.
    • (2001) J. Exp. Med. , vol.193 , pp. 147-157
    • Matsumoto, N.1    Mitsuki, M.2    Tajima, K.3    Yokoyama, W.M.4    Yomamoto, K.5
  • 24
    • 0035831550 scopus 로고    scopus 로고
    • Crystal structure of the C-type lectin-like domain from the human hematopoietic cell receptor CD69
    • A.S. Llera, F. Viedma, F. Sanchez-Madrid, J. Tormo, Crystal structure of the C-type lectin-like domain from the human hematopoietic cell receptor CD69, J. Biol. Chem. 276 (2001) 7312-7319.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7312-7319
    • Llera, A.S.1    Viedma, F.2    Sanchez-Madrid, F.3    Tormo, J.4
  • 25
    • 0034697357 scopus 로고    scopus 로고
    • A distinct seven-residue trigger sequence is indispensable for proper coiled-coil formation of the human macrophage scavenger receptor oligomerization domain
    • S. Frank, A. Lustig, T. Schulthess, J. Engel, R.A. Kammerer, A distinct seven-residue trigger sequence is indispensable for proper coiled-coil formation of the human macrophage scavenger receptor oligomerization domain, J. Biol. Chem. 275 (2000) 11672-11677.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11672-11677
    • Frank, S.1    Lustig, A.2    Schulthess, T.3    Engel, J.4    Kammerer, R.A.5
  • 28
    • 0033006297 scopus 로고    scopus 로고
    • Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily
    • E. Hohenester, T. Sasaki, R. Timpl, Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily, Nat. Struct. Biol. 6 (1999) 228-232.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 228-232
    • Hohenester, E.1    Sasaki, T.2    Timpl, R.3
  • 29
    • 0034624223 scopus 로고    scopus 로고
    • Cycloamylose as an efficient artificial chaperone for protein refolding
    • S. Machida, S. Ogawa, S. Xiaohua, T. Takaha, K. Fujii, K. Hayashi, Cycloamylose as an efficient artificial chaperone for protein refolding, FEBS Lett. 486 (2000) 131-135.
    • (2000) FEBS Lett. , vol.486 , pp. 131-135
    • Machida, S.1    Ogawa, S.2    Xiaohua, S.3    Takaha, T.4    Fujii, K.5    Hayashi, K.6
  • 30
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which more generally applicable
    • G.L. Peterson, A simplification of the protein assay method of Lowry et al. which more generally applicable, Anal. Biochem. 83 (1977) 346-356.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.