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Volumn 291, Issue 4, 1999, Pages 801-813

Domain organization of Mac-2 binding protein and its oligomerization to linear and ring-like structures

Author keywords

Assembly; BTB POZ+IVR domain; Electron microscopy; Extracellular matrix; SRCR domain

Indexed keywords

BINDING PROTEIN; COLLAGEN; FIBRONECTIN; GLYCOPROTEIN; INTEGRIN; MAC 2 BINDING PROTEIN; OLIGOMER; PLASMA PROTEIN; PROLACTIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 0344563603     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2996     Document Type: Article
Times cited : (41)

References (34)
  • 3
    • 0033613909 scopus 로고    scopus 로고
    • Fold prediction and evolutionary analysis of the POZ domain: Structural and evolutionary relationship with the potassium channel tetramerization domain
    • Aravind L., Koonin E. V. Fold prediction and evolutionary analysis of the POZ domain: structural and evolutionary relationship with the potassium channel tetramerization domain. J. Mol. Biol. 285:1999;1353-1361.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1353-1361
    • Aravind, L.1    Koonin, E.V.2
  • 4
    • 0024559992 scopus 로고
    • Cell attachment properties of collagen type VI and Arg-Gly-Asp dependent binding to its α2(VI) and α3(VI) chains
    • Aumailley M., Mann K., von der Mark H., Timpl R. Cell attachment properties of collagen type VI and Arg-Gly-Asp dependent binding to its α2(VI) and α3(VI) chains. Exp. Cell Res. 181:1989;463-474.
    • (1989) Exp. Cell Res. , vol.181 , pp. 463-474
    • Aumailley, M.1    Mann, K.2    Von Der Mark, H.3    Timpl, R.4
  • 5
    • 0028022978 scopus 로고
    • Cloning and expression of a mouse macrophage cDNA coding for a membrane glycoprotein of the scavenger receptor cysteine-rich domain family
    • Chicheportiche A., Vasalli P. Cloning and expression of a mouse macrophage cDNA coding for a membrane glycoprotein of the scavenger receptor cysteine-rich domain family. J. Biol. Chem. 269:1994;5512-5517.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5512-5517
    • Chicheportiche, A.1    Vasalli, P.2
  • 6
    • 0028936928 scopus 로고
    • Electron microscopy of extracellular matrix components
    • Engel J. Electron microscopy of extracellular matrix components. Methods Enzymol. 245:1994;469-488.
    • (1994) Methods Enzymol. , vol.245 , pp. 469-488
    • Engel, J.1
  • 7
    • 0025253834 scopus 로고
    • An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors
    • Freeman M., Ashkenas J., Rees D. J. G., Kingsley D. M., Copeland N. G., Jenkins N. A., Krieger M. An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors. Proc. Natl Acad. Sci. USA. 87:1990;8810-8814.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8810-8814
    • Freeman, M.1    Ashkenas, J.2    Rees, D.J.G.3    Kingsley, D.M.4    Copeland, N.G.5    Jenkins, N.A.6    Krieger, M.7
  • 8
    • 0027210009 scopus 로고
    • Cloning and characterization of cyclophilin C-associated protein: A candidate natural cellular ligand for cyclophilin C
    • Friedman J., Trahey M., Weissman I. Cloning and characterization of cyclophilin C-associated protein: a candidate natural cellular ligand for cyclophilin C. Proc. Natl Acad. Sci. USA. 90:1993;6815-6819.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6815-6819
    • Friedman, J.1    Trahey, M.2    Weissman, I.3
  • 9
    • 0013823053 scopus 로고
    • A new method of preparation of a self-perforated micro plastic grid and its application (I)
    • Fukami A., Adachi K. A new method of preparation of a self-perforated micro plastic grid and its application (I). J. Electron Microsc. 14:1965;112-118.
    • (1965) J. Electron Microsc. , vol.14 , pp. 112-118
    • Fukami, A.1    Adachi, K.2
  • 10
    • 0033006297 scopus 로고    scopus 로고
    • Crystal structure of a scavanger receptor cysteine-rich domain sheds light on an ancient superfamily
    • Hohenester E., Sasaki T., Timpl R. Crystal structure of a scavanger receptor cysteine-rich domain sheds light on an ancient superfamily. Nature Struct. Biol. 3:1999;228-232.
    • (1999) Nature Struct. Biol. , vol.3 , pp. 228-232
    • Hohenester, E.1    Sasaki, T.2    Timpl, R.3
  • 11
    • 0022548130 scopus 로고
    • Detection of antigens recognized by a novel monoclonal antibody in tissue and serum from patients with breast cancer
    • Iacobelli S., Arno E., D'Orazio A., Coletti G. Detection of antigens recognized by a novel monoclonal antibody in tissue and serum from patients with breast cancer. Cancer Res. 46:1986;3005-3010.
    • (1986) Cancer Res. , vol.46 , pp. 3005-3010
    • Iacobelli, S.1    Arno, E.2    D'Orazio, A.3    Coletti, G.4
  • 13
    • 0027936362 scopus 로고
    • Identification of human melanoma cellular and secreted ligands for galectin-3
    • Inohara H., Raz A. Identification of human melanoma cellular and secreted ligands for galectin-3. Biochem. Biophys. Res. Commun. 201:1994;1366-1375.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 1366-1375
    • Inohara, H.1    Raz, A.2
  • 14
    • 0029759376 scopus 로고    scopus 로고
    • Interactions between galectin-3 and Mac-2-binding protein mediate cell-cell adhesion
    • Inohara H., Akahani S., Koths K., Raz A. Interactions between galectin-3 and Mac-2-binding protein mediate cell-cell adhesion. Cancer Res. 56:1996;4530-4534.
    • (1996) Cancer Res. , vol.56 , pp. 4530-4534
    • Inohara, H.1    Akahani, S.2    Koths, K.3    Raz, A.4
  • 15
    • 0030804282 scopus 로고    scopus 로고
    • Properties of the extracellular calcium binding module of the proteoglycan testican
    • Kohfeldt E., Maurer P., Vannahme C., Timpl R. Properties of the extracellular calcium binding module of the proteoglycan testican. FEBS Letters. 414:1997;557-561.
    • (1997) FEBS Letters , vol.414 , pp. 557-561
    • Kohfeldt, E.1    Maurer, P.2    Vannahme, C.3    Timpl, R.4
  • 16
    • 0027229657 scopus 로고
    • Cloning and characterization of a human Mac-2 binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain
    • Koths K., Taylor E., Halenbeck R., Casipit C., Wang A. Cloning and characterization of a human Mac-2 binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain. J. Biol. Chem. 268:1993;14245-14249.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14245-14249
    • Koths, K.1    Taylor, E.2    Halenbeck, R.3    Casipit, C.4    Wang, A.5
  • 17
    • 0030828003 scopus 로고    scopus 로고
    • Overexpression, purification, characterization, and crystallization of the BTB/POZ domain from the PLZF oncoprotein
    • Li X., Lopez-Guisa J. M., Ninan N., Weiner E., Rauscher F. J. III, Marmorstein R. Overexpression, purification, characterization, and crystallization of the BTB/POZ domain from the PLZF oncoprotein. J. Biol. Chem. 272:1997;27324-27329.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27324-27329
    • Li, X.1    Lopez-Guisa, J.M.2    Ninan, N.3    Weiner, E.4    Rauscher F.J. III5    Marmorstein, R.6
  • 19
    • 0026499526 scopus 로고
    • Factors influencing the precision of quantitative scanning transmission electron microscopy
    • Müller S. A., Goldie K. N., Bürki R., Häring R., Engel A. Factors influencing the precision of quantitative scanning transmission electron microscopy. Ultramicroscopy. 46:1992;317-334.
    • (1992) Ultramicroscopy , vol.46 , pp. 317-334
    • Müller, S.A.1    Goldie, K.N.2    Bürki, R.3    Häring, R.4    Engel, A.5
  • 20
    • 0020054740 scopus 로고
    • Tissue distribution molecular profile, and shedding of a cytoplasmic antigen identified by the monoclonal antibody 465. 125 to human melanoma cells
    • Natali P. G., Wilson P. S., Imai K., Bigotti A., Ferrone S. Tissue distribution molecular profile, and shedding of a cytoplasmic antigen identified by the monoclonal antibody 465. 125 to human melanoma cells. Cancer Res. 42:1982;583-589.
    • (1982) Cancer Res. , vol.42 , pp. 583-589
    • Natali, P.G.1    Wilson, P.S.2    Imai, K.3    Bigotti, A.4    Ferrone, S.5
  • 21
    • 0032577178 scopus 로고    scopus 로고
    • Regulation of cellular adhesion to extracellular matrix proteins by galectin-3
    • Ochieg J., Leite-Browning M. L., Warfield P. Regulation of cellular adhesion to extracellular matrix proteins by galectin-3. Biochem. Biophys. Res. Commun. 246:1998;788-791.
    • (1998) Biochem. Biophys. Res. Commun. , vol.246 , pp. 788-791
    • Ochieg, J.1    Leite-Browning, M.L.2    Warfield, P.3
  • 22
    • 0029916999 scopus 로고    scopus 로고
    • Scavenger receptors in innate immunity
    • Pearson A. M. Scavenger receptors in innate immunity. Curr. Opin. Immunol. 8:1996;20-28.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 20-28
    • Pearson, A.M.1
  • 24
    • 0028158348 scopus 로고
    • The SRCR superfamily: A family reminiscent of the Ig superfamily
    • Resnik D., Pearson A., Krieger M. The SRCR superfamily: a family reminiscent of the Ig superfamily. Trends. Biochem. Sci. 19:1994;5-8.
    • (1994) Trends. Biochem. Sci. , vol.19 , pp. 5-8
    • Resnik, D.1    Pearson, A.2    Krieger, M.3
  • 25
    • 0030757226 scopus 로고    scopus 로고
    • Drosophila kelch is an oligomeric ring canal actin organizer
    • Robinson D. N., Cooley L. Drosophila kelch is an oligomeric ring canal actin organizer. J. Cell Biol. 138:1997;799-810.
    • (1997) J. Cell Biol. , vol.138 , pp. 799-810
    • Robinson, D.N.1    Cooley, L.2
  • 26
    • 0026047293 scopus 로고
    • Mac-2-binding glycoproteins. Putative ligands for cytosolic α-galactoside lectin
    • Rosenberg I., Cherayil B. J., Isselbacher K. J., Pillai S. Mac-2-binding glycoproteins. Putative ligands for cytosolic α-galactoside lectin. J. Biol. Chem. 266:1991;18731-18736.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18731-18736
    • Rosenberg, I.1    Cherayil, B.J.2    Isselbacher, K.J.3    Pillai, S.4
  • 27
    • 0032536822 scopus 로고    scopus 로고
    • Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds β1 integrins, collagens and fibronectin
    • Sasaki T., Brakebusch C., Engel J., Timpl R. Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds β1 integrins, collagens and fibronectin. EMBO J. 17:1998;1606-1613.
    • (1998) EMBO J. , vol.17 , pp. 1606-1613
    • Sasaki, T.1    Brakebusch, C.2    Engel, J.3    Timpl, R.4
  • 28
    • 0026673762 scopus 로고
    • Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin
    • Sato S., Hughes R. C. Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin. J. Biol. Chem. 267:1992;6983-6990.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6983-6990
    • Sato, S.1    Hughes, R.C.2
  • 29
    • 0032557645 scopus 로고    scopus 로고
    • X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution
    • Seetharaman J., Kanigsberg A., Slaaby R., Leffler H., Barondes S. H., Rini J. M. X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution. J. Biol. Chem. 273:1998;13047-13052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13047-13052
    • Seetharaman, J.1    Kanigsberg, A.2    Slaaby, R.3    Leffler, H.4    Barondes, S.H.5    Rini, J.M.6
  • 31
    • 0032981556 scopus 로고    scopus 로고
    • Cyclophilin C-associated protein: A normal secreted glycoprotein that down-modulates endotoxin and proinflammatory responces in vivo
    • Trahey M., Weissman I. L. Cyclophilin C-associated protein: a normal secreted glycoprotein that down-modulates endotoxin and proinflammatory responces in vivo. Proc. Natl Acad. Sci. USA. 96:1999;3006-3011.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3006-3011
    • Trahey, M.1    Weissman, I.L.2
  • 33
    • 0026095012 scopus 로고
    • Carbohydrate-binding protein 35 (Mac-2), a laminin binding lectin, forms functional dimers using cysteine 186
    • Woo H. J., Lotz M. M., Jung J. U., Mercurio A. M. Carbohydrate-binding protein 35 (Mac-2), a laminin binding lectin, forms functional dimers using cysteine 186. J. Biol. Chem. 266:1991;18419-18422.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18419-18422
    • Woo, H.J.1    Lotz, M.M.2    Jung, J.U.3    Mercurio, A.M.4
  • 34
    • 0000594001 scopus 로고    scopus 로고
    • Role of the carboxyl-terminal lectin domain in self-association of galectin-3
    • Yang R. Y., Hill P. N., Hsu D. K., Liu F. T. Role of the carboxyl-terminal lectin domain in self-association of galectin-3. Biochemistry. 37:1998;4086-4092.
    • (1998) Biochemistry , vol.37 , pp. 4086-4092
    • Yang, R.Y.1    Hill, P.N.2    Hsu, D.K.3    Liu, F.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.