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Volumn 45, Issue 21, 2006, Pages 6663-6673

Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ORGANS; CARBOHYDRATES; CELLS; IONIZATION; MASS SPECTROMETRY; MUTAGENESIS; SURFACE PLASMON RESONANCE; TISSUE CULTURE;

EID: 33744734683     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0600695     Document Type: Article
Times cited : (41)

References (55)
  • 2
    • 0021265943 scopus 로고
    • The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes
    • Young, S. P., Bomford, A., and Williams, R. (1984) The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes, Biochem. J. 219, 505-510.
    • (1984) Biochem. J. , vol.219 , pp. 505-510
    • Young, S.P.1    Bomford, A.2    Williams, R.3
  • 4
    • 4143051431 scopus 로고    scopus 로고
    • Transferrin receptor 1
    • Aisen, P. (2004) Transferrin receptor 1, Int. J. Biochem. Cell Biol. 36, 2137-2143.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2137-2143
    • Aisen, P.1
  • 5
    • 0031807617 scopus 로고    scopus 로고
    • Primary cell cultures from murine kidney and heart differ in endosomal pH
    • Rybak, S. L., and Murphy, R. F. (1998) Primary cell cultures from murine kidney and heart differ in endosomal pH, J. Cell. Physiol. 176, 216-222.
    • (1998) J. Cell. Physiol. , vol.176 , pp. 216-222
    • Rybak, S.L.1    Murphy, R.F.2
  • 7
    • 0041502601 scopus 로고    scopus 로고
    • The divalent metal-ion transporter (DCT1/DMT1/Nramp2)
    • (Templeton, D. M., Ed.) Marcel Dekker, New York
    • Gunshin, H., and Hediger, M. A. (2002) The divalent metal-ion transporter (DCT1/DMT1/Nramp2), in Molecular and Cellular Iron Transport (Templeton, D. M., Ed.) pp 155-173, Marcel Dekker, New York.
    • (2002) Molecular and Cellular Iron Transport , pp. 155-173
    • Gunshin, H.1    Hediger, M.A.2
  • 8
    • 0022448632 scopus 로고
    • Transferrin and apotransferrin: PH-dependent conformational changes associated with receptor-mediated uptake
    • Teeters, C. L., Lodish, H. F., Ciechanover, A., and Wallace, B. A. (1986) Transferrin and apotransferrin: pH-dependent conformational changes associated with receptor-mediated uptake, Ann. N.Y. Acad. Sci. 463, 403-407.
    • (1986) Ann. N.Y. Acad. Sci. , vol.463 , pp. 403-407
    • Teeters, C.L.1    Lodish, H.F.2    Ciechanover, A.3    Wallace, B.A.4
  • 9
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family
    • Kawabata, H., Yang, R., Hirama, T., Vuong, P. T., Kawano, S., Gombart, A. F., and Koeffler H. P. (1999) Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family, J. Biol. Chem. 274, 20826-20832.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3    Vuong, P.T.4    Kawano, S.5    Gombart, A.F.6    Koeffler, H.P.7
  • 10
    • 0027512245 scopus 로고
    • Role of oligosaccharides in the processing and function of human transferrin receptors. Effect of the loss of the three N-glycosyl oligosaccharides individually or together
    • Yang, B., Hoe, M. H., Black, P., and Hunt, R. C. (1993) Role of oligosaccharides in the processing and function of human transferrin receptors. Effect of the loss of the three N-glycosyl oligosaccharides individually or together, J. Biol. Chem. 268, 7435-7441.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7435-7441
    • Yang, B.1    Hoe, M.H.2    Black, P.3    Hunt, R.C.4
  • 12
    • 0025739245 scopus 로고
    • Acquisition of the functional properties of the transferrin receptor during its biosynthesis
    • Enns, C. A., Clinton, E. M., Reckhow, C. L., Root, B. J., Do, S.-I., and Cook, C. (1991) Acquisition of the functional properties of the transferrin receptor during its biosynthesis, J. Biol. Chem. 266, 13272-13277.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13272-13277
    • Enns, C.A.1    Clinton, E.M.2    Reckhow, C.L.3    Root, B.J.4    Do, S.-I.5    Cook, C.6
  • 13
    • 0021685289 scopus 로고
    • The human transferrin receptor gene: Genomic organization, and the complete primary structure of the receptor deduced from a cDNA sequence
    • McClelland, A., Kuhn, L. C., and Ruddle, F. H. (1984) The human transferrin receptor gene: genomic organization, and the complete primary structure of the receptor deduced from a cDNA sequence, Cell 39, 267-274.
    • (1984) Cell , vol.39 , pp. 267-274
    • McClelland, A.1    Kuhn, L.C.2    Ruddle, F.H.3
  • 14
    • 0021130929 scopus 로고
    • Primary structure of human transferrin receptor deduced from the mRNA sequence
    • Schneider, C., Owen, M. J., Banville, D., and Williams, J. G. (1984) Primary structure of human transferrin receptor deduced from the mRNA sequence, Nature 311, 675-678.
    • (1984) Nature , vol.311 , pp. 675-678
    • Schneider, C.1    Owen, M.J.2    Banville, D.3    Williams, J.G.4
  • 15
    • 0021174049 scopus 로고
    • Gene transfer, expression, and molecular cloning of the human transferrin receptor gene
    • Kuhn, L. C., McClelland, A., and Ruddle, F. H. (1984) Gene transfer, expression, and molecular cloning of the human transferrin receptor gene, Cell 37, 95-103.
    • (1984) Cell , vol.37 , pp. 95-103
    • Kuhn, L.C.1    McClelland, A.2    Ruddle, F.H.3
  • 16
    • 0033020518 scopus 로고    scopus 로고
    • The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis
    • Lebrön, J. A., and Bjorkman, P. J. (1999) The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis, J. Mol. Biol. 289, 1109-1118.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1109-1118
    • Lebrön, J.A.1    Bjorkman, P.J.2
  • 17
    • 2442657217 scopus 로고    scopus 로고
    • Mechanism for multiple ligand recognition by the human transferrin receptor
    • Giannetti, A. M., Snow, P. M., Zak, O., and Bjorkman, P. J. (2003) Mechanism for multiple ligand recognition by the human transferrin receptor, PLoS Biol. 1, 341-350.
    • (2003) PLoS Biol. , vol.1 , pp. 341-350
    • Giannetti, A.M.1    Snow, P.M.2    Zak, O.3    Bjorkman, P.J.4
  • 19
    • 0142095049 scopus 로고    scopus 로고
    • Iron release from transferrin, its C-lobe, and their complexes with transferrin receptor: Presence of N-lobe accelerates release from C-lobe at endosomal pH
    • Zak, O., and Aisen, P. (2003) Iron release from transferrin, its C-lobe, and their complexes with transferrin receptor: Presence of N-lobe accelerates release from C-lobe at endosomal pH, Biochemistry 42, 12330-12334.
    • (2003) Biochemistry , vol.42 , pp. 12330-12334
    • Zak, O.1    Aisen, P.2
  • 20
    • 0035009246 scopus 로고    scopus 로고
    • Pumping iron: The strange partnership of the hemochromatosis protein, a class I MHC homolog, with the transferrin receptor
    • Enns, C. A. (2001) Pumping iron: the strange partnership of the hemochromatosis protein, a class I MHC homolog, with the transferrin receptor, Traffic 2, 167-174.
    • (2001) Traffic , vol.2 , pp. 167-174
    • Enns, C.A.1
  • 21
    • 2942554825 scopus 로고    scopus 로고
    • HFE and transferrin directly compete for transferrin receptor in solution and at the cell surface
    • Giannetti, A. M., and Bjorkman, P. J. (2004) HFE and transferrin directly compete for transferrin receptor in solution and at the cell surface, J. Biol. Chem. 279, 25866-25875.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25866-25875
    • Giannetti, A.M.1    Bjorkman, P.J.2
  • 22
    • 0034610781 scopus 로고    scopus 로고
    • Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor
    • Bennett, M. J., Lebrón, J. A., and Bjorkman, P. J. (2000) Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor, Nature 403, 46-53.
    • (2000) Nature , vol.403 , pp. 46-53
    • Bennett, M.J.1    Lebrón, J.A.2    Bjorkman, P.J.3
  • 23
    • 0033166453 scopus 로고    scopus 로고
    • A Conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is required for binding to transferrin
    • Dubljevic, V., Sali, A., and Goding, J. W. (1999) A Conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is required for binding to transferrin, Biochem. J. 341, 11-14.
    • (1999) Biochem. J. , vol.341 , pp. 11-14
    • Dubljevic, V.1    Sali, A.2    Goding, J.W.3
  • 24
    • 0025924788 scopus 로고
    • A new role for the transferrin receptor in the release of iron from transferrin
    • Bali, P. K., Zak, O., and Aisen, P. (1991) A new role for the transferrin receptor in the release of iron from transferrin, Biochemistry 30, 324-328.
    • (1991) Biochemistry , vol.30 , pp. 324-328
    • Bali, P.K.1    Zak, O.2    Aisen, P.3
  • 25
    • 0026069823 scopus 로고
    • Receptor-modulated iron release from transferrin: Differential effects on N- and C-terminal sites
    • Bali, P. K., and Aisen, P. (1991) Receptor-modulated iron release from transferrin: Differential effects on N- and C-terminal sites, Biochemistry 30, 9947-9952.
    • (1991) Biochemistry , vol.30 , pp. 9947-9952
    • Bali, P.K.1    Aisen, P.2
  • 26
    • 0026651788 scopus 로고
    • Receptor-induced switch in site-site cooperativity during iron release by transferrin
    • Bali, P. K., and Aisen, P. (1992) Receptor-induced switch in site-site cooperativity during iron release by transferrin, Biochemistry 31, 3963-3967.
    • (1992) Biochemistry , vol.31 , pp. 3963-3967
    • Bali, P.K.1    Aisen, P.2
  • 27
    • 0026635458 scopus 로고
    • Entry of iron into cells: A new role for the transferrin receptor in modulating iron release from transferrin
    • Aisen, P. (1992) Entry of iron into cells: a new role for the transferrin receptor in modulating iron release from transferrin, Ann. Neurol. 32 (Suppl.), S62-S68.
    • (1992) Ann. Neurol. , vol.32 , Issue.SUPPL.
    • Aisen, P.1
  • 28
    • 0242286688 scopus 로고    scopus 로고
    • Structural reorganization of the transferrin C-lobe and transferrin receptor upon complex formation: The C-lobe binds to the receptor helical domain
    • Liu, R. T., Guan, J. Q., Zak, O., Aisen, P., and Chance, M. R. (2003) Structural reorganization of the transferrin C-lobe and transferrin receptor upon complex formation: The C-lobe binds to the receptor helical domain, Biochemistry 42, 12447-12454.
    • (2003) Biochemistry , vol.42 , pp. 12447-12454
    • Liu, R.T.1    Guan, J.Q.2    Zak, O.3    Aisen, P.4    Chance, M.R.5
  • 29
    • 1342264310 scopus 로고    scopus 로고
    • Structure of the human transferrin receptor-transferrin complex
    • Cheng, Y., Zak, O., Aisen, P., Harrison, S. C., and Walz, T. (2004) Structure of the human transferrin receptor-transferrin complex, Cell 116, 565-576.
    • (2004) Cell , vol.116 , pp. 565-576
    • Cheng, Y.1    Zak, O.2    Aisen, P.3    Harrison, S.C.4    Walz, T.5
  • 30
    • 27644551255 scopus 로고    scopus 로고
    • The molecular mechanism for receptor-stimulated iron release from the plasma iron transport protein transferrin
    • Giannetti, A. M., Halbrooks, P. J., Mason, A. B., Vogt, T. M., Enns, C. A., and Bjorkman, P. J. (2005) The molecular mechanism for receptor-stimulated iron release from the plasma iron transport protein transferrin, Structure 13, 1613-1623.
    • (2005) Structure , vol.13 , pp. 1613-1623
    • Giannetti, A.M.1    Halbrooks, P.J.2    Mason, A.B.3    Vogt, T.M.4    Enns, C.A.5    Bjorkman, P.J.6
  • 31
    • 0023907964 scopus 로고
    • Characterization of the transferrin receptor in tunicamycin-treated A431 cells
    • Reckhow, C. L., and Enns, C. A. (1988) Characterization of the transferrin receptor in tunicamycin-treated A431 cells, J. Biol. Chem. 263, 7297-7301.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7297-7301
    • Reckhow, C.L.1    Enns, C.A.2
  • 32
    • 0030969501 scopus 로고    scopus 로고
    • Structure of human transferrin receptor oligosaccharides: Conservation of site-specific processing
    • Hayes, G. R., Williams, A. M., Lucas, J. J., and Enns, C. A. (1997) Structure of human transferrin receptor oligosaccharides: Conservation of site-specific processing, Biochemistry 36, 5276-5284.
    • (1997) Biochemistry , vol.36 , pp. 5276-5284
    • Hayes, G.R.1    Williams, A.M.2    Lucas, J.J.3    Enns, C.A.4
  • 33
    • 0026014164 scopus 로고
    • A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein
    • Williams, A. M., and Enns, C. A. (1991) A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein, J. Biol. Chem. 266, 17648-17654.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17648-17654
    • Williams, A.M.1    Enns, C.A.2
  • 34
    • 0026668826 scopus 로고
    • Loss of one asparagine-linked oligosaccharide from human transferrin receptors results in specific cleavage and association with the endoplasmic reticulum
    • Hoe, M. H., and Hunt, R. C. (1992) Loss of one asparagine-linked oligosaccharide from human transferrin receptors results in specific cleavage and association with the endoplasmic reticulum, J. Biol. Chem. 267, 4916-4923.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4916-4923
    • Hoe, M.H.1    Hunt, R.C.2
  • 35
    • 0024355289 scopus 로고
    • Changes in glycosylation alter the affinity of the human transferrin receptor for its ligand
    • Hunt, R. C., Riegler, R., and Davis, A. A. (1989) Changes in glycosylation alter the affinity of the human transferrin receptor for its ligand, J. Biol. Chem. 264, 9643-9648.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9643-9648
    • Hunt, R.C.1    Riegler, R.2    Davis, A.A.3
  • 36
    • 0027217557 scopus 로고
    • A region of the C-terminal portion of the human transferrin receptor contains an asparagine-linked glycosylation site critical for receptor structure and function
    • Williams, A. M., and Enns, C. A. (1993) A region of the C-terminal portion of the human transferrin receptor contains an asparagine-linked glycosylation site critical for receptor structure and function, J. Biol. Chem. 268, 12780-12786.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12780-12786
    • Williams, A.M.1    Enns, C.A.2
  • 37
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the carbohydrate moiety on the stability of glycoproteins
    • Wang, C., Eufemi, M., Turano, C., and Giartosio, A. (1996) Influence of the carbohydrate moiety on the stability of glycoproteins, Biochemistry 35, 7299-7307.
    • (1996) Biochemistry , vol.35 , pp. 7299-7307
    • Wang, C.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4
  • 39
    • 0034813966 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant nonglycosylated human serum transferrin containing a C-terminal hexahistidine tag
    • Mason, A. B., He, Q.-Y., Adams, T. E., Gumerov, D. R., Kaltashov, I. A., Nguyen, V., and MacGillivray, R. T. A. (2001) Expression, purification, and characterization of recombinant nonglycosylated human serum transferrin containing a C-terminal hexahistidine tag, Protein Expression Purif. 23, 142-150.
    • (2001) Protein Expression Purif. , vol.23 , pp. 142-150
    • Mason, A.B.1    He, Q.-Y.2    Adams, T.E.3    Gumerov, D.R.4    Kaltashov, I.A.5    Nguyen, V.6    MacGillivray, R.T.A.7
  • 41
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
    • Lebrón, J. A., Bennett, M. J., Vaughn, D. E., Chirino, A. J., Snow, P. M., Mintier, G. A., Feder, J. N., and Bjorkman, P. J. (1998) Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor, Cell 93, 111-123.
    • (1998) Cell , vol.93 , pp. 111-123
    • Lebrón, J.A.1    Bennett, M.J.2    Vaughn, D.E.3    Chirino, A.J.4    Snow, P.M.5    Mintier, G.A.6    Feder, J.N.7    Bjorkman, P.J.8
  • 42
    • 0026134726 scopus 로고
    • Efficient production and isolation of recombinant amino-terminal half-molecule of human serum transferrin from baby hamster kidney cells
    • Mason, A. B., Funk, W. D., MacGillivray, R. T. A., and Woodworth, R. C. (1991) Efficient production and isolation of recombinant amino-terminal half-molecule of human serum transferrin from baby hamster kidney cells, Protein Expression Purif. 2, 214-220.
    • (1991) Protein Expression Purif. , vol.2 , pp. 214-220
    • Mason, A.B.1    Funk, W.D.2    MacGillivray, R.T.A.3    Woodworth, R.C.4
  • 43
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 44
    • 28244493040 scopus 로고    scopus 로고
    • Composition of pH sensitive triad in C-lobe of human serum transferrin. Comparison to sequences of ovotransferrin and lactoferrin provides insight into functional differences in iron release
    • Halbrooks, P. J., Giannetti, A. M., Klein, J. S., Bjorkman, P. J., Larouche, J. R., Smith, V. C., MacGillivray, R. T. A., Everse, S. J., and Mason, A. B. (2005) Composition of pH sensitive triad in C-lobe of human serum transferrin. Comparison to sequences of ovotransferrin and lactoferrin provides insight into functional differences in iron release, Biochemistry 44, 15451-15460.
    • (2005) Biochemistry , vol.44 , pp. 15451-15460
    • Halbrooks, P.J.1    Giannetti, A.M.2    Klein, J.S.3    Bjorkman, P.J.4    Larouche, J.R.5    Smith, V.C.6    MacGillivray, R.T.A.7    Everse, S.J.8    Mason, A.B.9
  • 45
    • 0026551323 scopus 로고
    • Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis
    • Fagerstam, L. G., Frostell-Karlsson, A., Karlsson, R., Persson, B., and Ronnberg, I. (1992) Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis, J. Chromatogr. 597, 397-410.
    • (1992) J. Chromatogr. , vol.597 , pp. 397-410
    • Fagerstam, L.G.1    Frostell-Karlsson, A.2    Karlsson, R.3    Persson, B.4    Ronnberg, I.5
  • 46
    • 0027916175 scopus 로고
    • Biospecific interaction analysis using biosensor technology
    • Malmqvist, M. (1993) Biospecific interaction analysis using biosensor technology, Nature 361, 186-187.
    • (1993) Nature , vol.361 , pp. 186-187
    • Malmqvist, M.1
  • 47
    • 0031958764 scopus 로고    scopus 로고
    • CLAMP: A biosensor kinetic data analysis program
    • Myszka, D. G., and Morton, T. A. (1998) CLAMP: a biosensor kinetic data analysis program, Trends Biochem. Sci. 23, 149-150.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 149-150
    • Myszka, D.G.1    Morton, T.A.2
  • 48
    • 4744344760 scopus 로고    scopus 로고
    • Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method
    • Peschke, M., Verkerk, U. H., and Kebarle, P. (2004) Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method, J. Am. Soc. Mass Spectrom. 15, 1424-1434.
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 1424-1434
    • Peschke, M.1    Verkerk, U.H.2    Kebarle, P.3
  • 49
    • 0035984339 scopus 로고    scopus 로고
    • Studies of biomolecular conformations and conformational dynamic by mass spectrometry
    • Kaltashov, I. A., and Eyles, S. J. (2002) Studies of biomolecular conformations and conformational dynamic by mass spectrometry, Mass Spectrom. Rev. 21, 37-71.
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 37-71
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 50
    • 0014670260 scopus 로고
    • Fluorescence and absorption studies of the binding of copper and iron to transferrin
    • Lehrer, S. S. (1969) Fluorescence and absorption studies of the binding of copper and iron to transferrin, J. Biol. Chem. 244, 3613-3617.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3613-3617
    • Lehrer, S.S.1
  • 51
    • 0027173204 scopus 로고
    • Expression of glycosylated and nonglycosylated human transferrin in mammalian cells. Characterization of the recombinant proteins with comparison to three commercially available transferrins
    • Mason, A. B., Miller, M. K., Funk, W. D., Banfield, D. K., Savage, K. J., Oliver, R. W. A., Green, B. N., MacGillivray, R. T. A., and Woodworth, R. C. (1993) Expression of glycosylated and nonglycosylated human transferrin in mammalian cells. Characterization of the recombinant proteins with comparison to three commercially available transferrins, Biochemistry 32, 5472-5479.
    • (1993) Biochemistry , vol.32 , pp. 5472-5479
    • Mason, A.B.1    Miller, M.K.2    Funk, W.D.3    Banfield, D.K.4    Savage, K.J.5    Oliver, R.W.A.6    Green, B.N.7    MacGillivray, R.T.A.8    Woodworth, R.C.9
  • 52
    • 0023899377 scopus 로고
    • A high yield purification of the human transferrin receptor and properties of its major extracellular fragment
    • Turkewitz, A. P., Amatruda, J. F., Borhani, D., Harrison, S. C., and Schwartz, A. L. (1988) A high yield purification of the human transferrin receptor and properties of its major extracellular fragment, J. Biol. Chem. 263, 8318-8325.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8318-8325
    • Turkewitz, A.P.1    Amatruda, J.F.2    Borhani, D.3    Harrison, S.C.4    Schwartz, A.L.5
  • 53
    • 1042276706 scopus 로고    scopus 로고
    • Transferring mechanism of interaction with receptor 1
    • Hemadi, M., Kahn, P. H., Miquel, G., and Hage Chahine, J. M. (2004) Transferring mechanism of interaction with receptor 1, Biochemistry 43, 1736-1745.
    • (2004) Biochemistry , vol.43 , pp. 1736-1745
    • Hemadi, M.1    Kahn, P.H.2    Miquel, G.3    Hage Chahine, J.M.4
  • 54
    • 0025878342 scopus 로고
    • Crystallization and X-ray diffraction studies of a soluble form of the human transferrin receptor
    • Borhani, D. W., and Harrison, S. C. (1991) Crystallization and X-ray diffraction studies of a soluble form of the human transferrin receptor, J. Mol. Biol. 218, 685-689.
    • (1991) J. Mol. Biol. , vol.218 , pp. 685-689
    • Borhani, D.W.1    Harrison, S.C.2
  • 55
    • 0032532742 scopus 로고    scopus 로고
    • Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy
    • Fuchs, H., Lücken, U., Tauber, R., Engel, A., and Gessner, R. (1998) Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy, Structure 6, 1235-1243.
    • (1998) Structure , vol.6 , pp. 1235-1243
    • Fuchs, H.1    Lücken, U.2    Tauber, R.3    Engel, A.4    Gessner, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.