메뉴 건너뛰기




Volumn 288, Issue 39, 2013, Pages 27737-27751

The solution structure of heparan sulfate differs from that of heparin: Implications for function

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTICAL ULTRACENTRIFUGATION; HEPARAN SULFATES; PHYSIOLOGICAL ROLES; SOLUTION STRUCTURES;

EID: 84884749301     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.492223     Document Type: Article
Times cited : (34)

References (59)
  • 1
    • 0026693653 scopus 로고
    • Heparan sulphate proteoglycans. Molecular organisation of membrane-associated species and an approach to polysaccharide sequence analysis
    • Gallagher, J. T., Turnbull, J. E., and Lyon, M. (1992) Heparan sulphate proteoglycans. Molecular organisation of membrane-associated species and an approach to polysaccharide sequence analysis. Adv. Exp. Med. Biol. 313, 49-57
    • (1992) Adv. Exp. Med. Biol. , vol.313 , pp. 49-57
    • Gallagher, J.T.1    Turnbull, J.E.2    Lyon, M.3
  • 4
    • 0033635310 scopus 로고    scopus 로고
    • Heparin and heparan sulfate. Biosynthesis, structure and function
    • Sasisekharan R., and Venkataraman G. (2000) Heparin and heparan sulfate. Biosynthesis, structure and function. Curr. Opin. Chem. Biol. 4, 626-631
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 626-631
    • Sasisekharan, R.1    Venkataraman, G.2
  • 5
    • 0034643323 scopus 로고    scopus 로고
    • Specificities of heparan sulphate proteoglycans in developmental processes
    • Perrimon, N., and Bernfield, M. (2000) Specificities of heparan sulphate proteoglycans in developmental processes. Nature 404, 725-728
    • (2000) Nature , vol.404 , pp. 725-728
    • Perrimon, N.1    Bernfield, M.2
  • 6
    • 67650513329 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are receptors for the cell-surface trafficking and biological activity of transglutaminase-2
    • Scarpellini, A., Germack, R., Lortat-Jacob, H., Muramatsu T., Billett E., Johnson T., and Verderio, E. A. (2009) Heparan sulfate proteoglycans are receptors for the cell-surface trafficking and biological activity of transglutaminase-2. J. Biol. Chem. 284, 18411-18423
    • (2009) J. Biol. Chem. , vol.284 , pp. 18411-18423
    • Scarpellini, A.1    Germack, R.2    Lortat-Jacob, H.3    Muramatsu, T.4    Billett, E.5    Johnson, T.6    Verderio, E.A.7
  • 7
    • 0030796217 scopus 로고    scopus 로고
    • Specific binding of the chemokine platelet factor 4 to heparan sulfate
    • Stringer, S. E., and Gallagher, J. T. (1997) Specific binding of the chemokine platelet factor 4 to heparan sulfate. J. Biol. Chem. 272, 20508-20514
    • (1997) J. Biol. Chem. , vol.272 , pp. 20508-20514
    • Stringer, S.E.1    Gallagher, J.T.2
  • 8
    • 0002891925 scopus 로고    scopus 로고
    • Onthe regulation of fibroblast growth factor activity by heparin-like glycosaminoglycans
    • Sasisekharan, R., Ernst, S., and Venkataraman, G. (1997)Onthe regulation of fibroblast growth factor activity by heparin-like glycosaminoglycans. Angiogenesis. 1, 45-54
    • (1997) Angiogenesis. , vol.1 , pp. 45-54
    • Sasisekharan, R.1    Ernst, S.2    Venkataraman, G.3
  • 10
  • 11
    • 0030764559 scopus 로고    scopus 로고
    • Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate
    • Chen, Y., Maguire, T., Hileman, R. E., Fromm, J. R., Esko, J. D., Linhardt, R. J., and Marks, R. M. (1997) Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate. Nat. Med. 3, 866-871
    • (1997) Nat. Med. , vol.3 , pp. 866-871
    • Chen, Y.1    Maguire, T.2    Hileman, R.E.3    Fromm, J.R.4    Esko, J.D.5    Linhardt, R.J.6    Marks, R.M.7
  • 16
    • 15244364003 scopus 로고    scopus 로고
    • Heparan sulfate-protein interactions. Therapeutic potential through structure-function insights
    • Coombe, D. R., and Kett, W. C. (2005) Heparan sulfate-protein interactions. Therapeutic potential through structure-function insights. Cell Mol. Life Sci. 62, 410-424
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 410-424
    • Coombe, D.R.1    Kett, W.C.2
  • 17
    • 0031650702 scopus 로고    scopus 로고
    • Bio-specific sequences and domains in heparan sulphate and the regulation of cell growth and adhesion
    • Lyon, M., and Gallagher, J. T. (1998) Bio-specific sequences and domains in heparan sulphate and the regulation of cell growth and adhesion. Matrix Biol. 17, 485-493
    • (1998) Matrix Biol. , vol.17 , pp. 485-493
    • Lyon, M.1    Gallagher, J.T.2
  • 18
    • 0027164634 scopus 로고
    • N.M.R., and molecular-modelling studies of the solution conformation of heparin
    • Mulloy, B., Forster, M. J., Jones, C., and Davies, D. B. (1993) N.M.R., and molecular-modelling studies of the solution conformation of heparin. Biochem. J. 293, 849-858
    • (1993) Biochem. J. , vol.293 , pp. 849-858
    • Mulloy, B.1    Forster, M.J.2    Jones, C.3    Davies, D.B.4
  • 19
    • 73249136226 scopus 로고    scopus 로고
    • Semi-rigid solution structures of heparin by constrained x-ray scattering modeling. New insight into heparin-protein complexes
    • Khan, S., Gor, J., Mulloy, B., and Perkins, S. J. (2010) Semi-rigid solution structures of heparin by constrained x-ray scattering modelling. New insight into heparin-protein complexes. J. Mol. Biol. 395, 504-521
    • (2010) J. Mol. Biol. , vol.395 , pp. 504-521
    • Khan, S.1    Gor, J.2    Mulloy, B.3    Perkins, S.J.4
  • 20
    • 77953734606 scopus 로고    scopus 로고
    • Catalytic mechanism of heparinase II investigated by site-directed mutagenesis and the crystal structure with its substrate
    • Shaya, D., Zhao, W., Garron, M. L., Xiao, Z., Cui, Q., Zhang, Z., Sulea, T., Linhardt, R. J., and Cygler, M. (2010) Catalytic mechanism of heparinase II investigated by site-directed mutagenesis and the crystal structure with its substrate. J. Biol. Chem. 285, 20051-20061
    • (2010) J. Biol. Chem. , vol.285 , pp. 20051-20061
    • Shaya, D.1    Zhao, W.2    Garron, M.L.3    Xiao, Z.4    Cui, Q.5    Zhang, Z.6    Sulea, T.7    Linhardt, R.J.8    Cygler, M.9
  • 22
    • 69949145065 scopus 로고    scopus 로고
    • Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights
    • Perkins, S. J., Okemefuna, A. I., Nan, R., Li, K., and Bonner, A. (2009) Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights. J. R. Soc. Interface 6, S679-S696
    • (2009) J. R. Soc. Interface , vol.6
    • Perkins, S.J.1    Okemefuna, A.I.2    Nan, R.3    Li, K.4    Bonner, A.5
  • 23
    • 58049165638 scopus 로고    scopus 로고
    • Location of secretory component on the Fc edge of dimeric IgA1 reveals insight into the role of secretory IgA1 in mucosal immunity
    • Bonner, A., Almogren, A., Furtado, P. B., Kerr, M. A., and Perkins, S. J. (2009) Location of secretory component on the Fc edge of dimeric IgA1 reveals insight into the role of secretory IgA1 in mucosal immunity. Mucosal Immunol. 2, 74-84
    • (2009) Mucosal Immunol. , vol.2 , pp. 74-84
    • Bonner, A.1    Almogren, A.2    Furtado, P.B.3    Kerr, M.A.4    Perkins, S.J.5
  • 24
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini, L., Burke, D. F., von Delft, F., Mulloy, B., and Blundell, T. L. (2000) Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 407, 1029-1034
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 25
    • 0030891052 scopus 로고    scopus 로고
    • Molecular weight measurements of low molecular weight heparins by gel permeation chromatography
    • Mulloy, B., Gee, C., Wheeler, S. F., Wait, R., Gray, E., and Barrowcliffe, T. W. (1997) Molecular weight measurements of low molecular weight heparins by gel permeation chromatography. Thromb. Haemost. 77, 668-674
    • (1997) Thromb. Haemost. , vol.77 , pp. 668-674
    • Mulloy, B.1    Gee, C.2    Wheeler, S.F.3    Wait, R.4    Gray, E.5    Barrowcliffe, T.W.6
  • 26
    • 0022341862 scopus 로고
    • High-performance liquid chromatographic separation of heparinderived oligosaccharides
    • Rice, K. G., Kim, Y. S., Grant, A. C., Merchant, Z. M., and Linhardt, R. J. (1985) High-performance liquid chromatographic separation of heparinderived oligosaccharides. Anal. Biochem. 150, 325-331
    • (1985) Anal. Biochem. , vol.150 , pp. 325-331
    • Rice, K.G.1    Kim, Y.S.2    Grant, A.C.3    Merchant, Z.M.4    Linhardt, R.J.5
  • 28
    • 77950795510 scopus 로고    scopus 로고
    • Generating heparan sulfate saccharide libraries for glycomics applications
    • Powell, A. K., Ahmed, Y. A., Yates, E. A., and Turnbull, J. E. (2010) Generating heparan sulfate saccharide libraries for glycomics applications. Nat. Protoc. 5, 821-833
    • (2010) Nat. Protoc. , vol.5 , pp. 821-833
    • Powell, A.K.1    Ahmed, Y.A.2    Yates, E.A.3    Turnbull, J.E.4
  • 29
    • 0035865677 scopus 로고    scopus 로고
    • Combined strong anionexchange HPLC and PAGE approach for the purification of heparan sulphate oligosaccharides
    • Vivès, R. R., Goodger, S., and Pye, D. A. (2001) Combined strong anionexchange HPLC and PAGE approach for the purification of heparan sulphate oligosaccharides. Biochem. J. 354, 141-147
    • (2001) Biochem. J. , vol.354 , pp. 141-147
    • Vivès, R.R.1    Goodger, S.2    Pye, D.A.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0042860033 scopus 로고    scopus 로고
    • Conformation of heparin studied with macromolecular hydrodynamic methods and X-ray scattering, Eur
    • Pavlov, G., Finet, S., Tatarenko, K., Korneeva, E., and Ebel, C. (2003) Conformation of heparin studied with macromolecular hydrodynamic methods and X-ray scattering, Eur. Biophys. J. 32, 437-449
    • (2003) Biophys. J. , vol.32 , pp. 437-449
    • Pavlov, G.1    Finet, S.2    Tatarenko, K.3    Korneeva, E.4    Ebel, C.5
  • 32
    • 0021151003 scopus 로고
    • Structure and interactions of heparan sulfate proteoglycans from a mouse tumor basement membrane
    • Fujiwara, S., Wiedemann, H., Timpl, R., Lustig, A., and Engel, J. (1984) Structure and interactions of heparan sulfate proteoglycans from a mouse tumor basement membrane. Eur. J. Biochem. 143, 145-157
    • (1984) Eur. J. Biochem. , vol.143 , pp. 145-157
    • Fujiwara, S.1    Wiedemann, H.2    Timpl, R.3    Lustig, A.4    Engel, J.5
  • 33
    • 1842428822 scopus 로고    scopus 로고
    • Calculating sedimentation coefficient distribution by direct modeling of sedimentation velocity concentration profiles
    • Dam, J., and Schuck, P. (2004) Calculating sedimentation coefficient distribution by direct modeling of sedimentation velocity concentration profiles. Methods Enzymol. 384, 185-212
    • (2004) Methods Enzymol. , vol.384 , pp. 185-212
    • Dam, J.1    Schuck, P.2
  • 34
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 35
    • 0000670930 scopus 로고    scopus 로고
    • SAXS and USAXS on the high brilliance beamline at the ESRF
    • Narayanan, T., Diat, O., and Bosecke, P. (2001) SAXS and USAXS on the high brilliance beamline at the ESRF. Nucl. Instrum. Methods Phys. Res. A 467-468, 1005-1009
    • (2001) Nucl. Instrum. Methods Phys. Res. A , vol.467-468 , pp. 1005-1009
    • Narayanan, T.1    Diat, O.2    Bosecke, P.3
  • 37
    • 0026244044 scopus 로고
    • GNOM. A program package for small-angle scattering data-processing
    • 10.1107/S002188989100081X
    • Semenyuk, A. V., and Svergun, D. I. (1991) GNOM. A program package for small-angle scattering data-processing. J. Appl. Crystallogr. 24, 537-540, 10.1107/S002188989100081X
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 38
    • 9144240095 scopus 로고
    • DREIDING. A generic force field for molecular simulations
    • 10.1021/j100389a010
    • Mayo, S. L., Olafson, B. D., and Goddard, W. A., 3rd (1990) DREIDING. A generic force field for molecular simulations. J. Phys. Chem. 94, 8897-8909, 10.1021/j100389a010
    • (1990) J. Phys. Chem. , vol.94 , pp. 8897-8909
    • Mayo, S.L.1    Olafson, B.D.2    Goddard III, W.A.3
  • 39
    • 67651095769 scopus 로고    scopus 로고
    • Electrostatic interactions contribute to the folded-back conformation of wild-type human Factor H
    • Okemefuna, A. I., Nan, R., Gor, J., and Perkins, S. J. (2009) Electrostatic interactions contribute to the folded-back conformation of wild-type human Factor H. J. Mol. Biol. 391, 98-118
    • (2009) J. Mol. Biol. , vol.391 , pp. 98-118
    • Okemefuna, A.I.1    Nan, R.2    Gor, J.3    Perkins, S.J.4
  • 40
    • 36348990790 scopus 로고    scopus 로고
    • The partly-folded back solution structure arrangement of the 30 SCR domains in human complement receptor type 1 (CR1) permits access to its C3b and C4b ligands
    • Furtado, P. B., Huang, C. Y., Ihyembe, D., Hammond, R. A., Marsh, H. C., and Perkins, S. J. (2008) The partly-folded back solution structure arrangement of the 30 SCR domains in human complement receptor type 1 (CR1) permits access to its C3b and C4b ligands. J. Mol. Biol. 375, 102-118
    • (2008) J. Mol. Biol. , vol.375 , pp. 102-118
    • Furtado, P.B.1    Huang, C.Y.2    Ihyembe, D.3    Hammond, R.A.4    Marsh, H.C.5    Perkins, S.J.6
  • 41
    • 33748440940 scopus 로고    scopus 로고
    • The flexible 15 SCR extracellular domains of human complement receptor type 2 can mediate multiple ligand and antigen interactions
    • Gilbert, H. E., Asokan, R., Holers, V. M., and Perkins, S. J. (2006) The flexible 15 SCR extracellular domains of human complement receptor type 2 can mediate multiple ligand and antigen interactions. J. Mol. Biol. 362, 1132-1147
    • (2006) J. Mol. Biol. , vol.362 , pp. 1132-1147
    • Gilbert, H.E.1    Asokan, R.2    Holers, V.M.3    Perkins, S.J.4
  • 42
    • 0031587295 scopus 로고    scopus 로고
    • Pentameric and decameric structures in solution of the serum amyloid P component by x-ray and neutron scattering and molecular modelling analyses
    • Ashton, A. W., Boehm, M. K., Gallimore, J. R., Pepys, M. B., and Perkins, S. J. (1997) Pentameric and decameric structures in solution of the serum amyloid P component by x-ray and neutron scattering and molecular modelling analyses. J. Mol. Biol. 272, 408-422
    • (1997) J. Mol. Biol. , vol.272 , pp. 408-422
    • Ashton, A.W.1    Boehm, M.K.2    Gallimore, J.R.3    Pepys, M.B.4    Perkins, S.J.5
  • 43
    • 0021112502 scopus 로고
    • Low resolution structural studies of mitochondrial ubiquinol-cytochrome c reductase in detergent solutions by neutron scattering
    • Perkins, S. J., and Weiss, H. (1983) Low resolution structural studies of mitochondrial ubiquinol-cytochrome c reductase in detergent solutions by neutron scattering. J. Mol. Biol. 168, 847-866
    • (1983) J. Mol. Biol. , vol.168 , pp. 847-866
    • Perkins, S.J.1    Weiss, H.2
  • 44
    • 0035965873 scopus 로고    scopus 로고
    • X-ray and neutron scattering analyses of hydration shells. A molecular interpretation based on sequence predictions and modelling fits
    • Perkins, S. J. (2001) X-ray and neutron scattering analyses of hydration shells. A molecular interpretation based on sequence predictions and modelling fits. Biophys. Chem. 93, 129-139
    • (2001) Biophys. Chem. , vol.93 , pp. 129-139
    • Perkins, S.J.1
  • 45
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • García De La Torre J., Huertas, M. L., and Carrasco, B. (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78, 719-730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • De La Torre, G.J.1    Huertas, M.L.2    Carrasco, B.3
  • 46
    • 35449002345 scopus 로고    scopus 로고
    • Analytical ultracentrifugation. Sedimentation velocity and sedimentation equilibrium
    • Cole, J. L., Lary, J. W., Moody, T. P., and Laue, T. M. (2008) Analytical ultracentrifugation. Sedimentation velocity and sedimentation equilibrium. Methods Cell Biol. 84, 143-179
    • (2008) Methods Cell Biol. , vol.84 , pp. 143-179
    • Cole, J.L.1    Lary, J.W.2    Moody, T.P.3    Laue, T.M.4
  • 48
    • 0001116625 scopus 로고
    • Potential energy surfaces of cellobiose and maltose in aqueous solution. A new treatment of disaccharide optical rotation
    • Stevens, E. S., and Sathyanarayana, B. K. (1989) Potential energy surfaces of cellobiose and maltose in aqueous solution. A new treatment of disaccharide optical rotation. J. Am. Chem. Soc. 111, 4149-4154
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 4149-4154
    • Stevens, E.S.1    Sathyanarayana, B.K.2
  • 49
    • 33746614761 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins. The concept of specificity
    • Kreuger, J., Spillmann, D., Li, J. P., and Lindahl, U. (2006) Interactions between heparan sulfate and proteins. The concept of specificity. J. Cell Biol. 174, 323-327
    • (2006) J. Cell Biol. , vol.174 , pp. 323-327
    • Kreuger, J.1    Spillmann, D.2    Li, J.P.3    Lindahl, U.4
  • 50
    • 0033650826 scopus 로고    scopus 로고
    • Conformation and dynamics of heparin and heparan sulfate
    • Mulloy, B., and Forster, M. J. (2000) Conformation and dynamics of heparin and heparan sulfate. Glycobiology 10, 1147-1156
    • (2000) Glycobiology , vol.10 , pp. 1147-1156
    • Mulloy, B.1    Forster, M.J.2
  • 51
    • 0342684436 scopus 로고    scopus 로고
    • Motional properties of E coli polysaccharide K5 in aqueous solution analyzed by NMR relaxation measurements
    • Hricovíni, M., Guerrini, M., Torri, G., and Casu, B. (1997) Motional properties of E. coli polysaccharide K5 in aqueous solution analyzed by NMR relaxation measurements. Carbohydr. Res. 300, 69-76
    • (1997) Carbohydr. Res. , vol.300 , pp. 69-76
    • Hricovíni, M.1    Guerrini, M.2    Torri, G.3    Casu, B.4
  • 52
    • 44449125309 scopus 로고    scopus 로고
    • The structural plasticity of heparan sulfate NA-domains and hence their role in mediating multivalent interactions is confirmed by high-accuracy 15N-NMR relaxation studies
    • Mobli, M., Nilsson, M., and Almond, A. (2008) The structural plasticity of heparan sulfate NA-domains and hence their role in mediating multivalent interactions is confirmed by high-accuracy 15N-NMR relaxation studies. Glycoconj. J. 25, 401-414
    • (2008) Glycoconj. J. , vol.25 , pp. 401-414
    • Mobli, M.1    Nilsson, M.2    Almond, A.3
  • 53
    • 0028763769 scopus 로고
    • The effect of variation of substitution on the solution conformation of heparin. A spectroscopic and molecular modelling study
    • Mulloy, B., Forster, M. J., Jones, C., Drake, A. F., Johnson, E. A., and Davies, D. B. (1994) The effect of variation of substitution on the solution conformation of heparin. A spectroscopic and molecular modelling study. Carbohydr. Res. 255, 1-26
    • (1994) Carbohydr. Res. , vol.255 , pp. 1-26
    • Mulloy, B.1    Forster, M.J.2    Jones, C.3    Drake, A.F.4    Johnson, E.A.5    Davies, D.B.6
  • 54
    • 58849162321 scopus 로고    scopus 로고
    • Analysis and validation of carbohydrate three-dimensional structures
    • Lütteke, T. (2009) Analysis and validation of carbohydrate three-dimensional structures. Acta Crystallogr. D Biol Crystallogr. 65, 156-168
    • (2009) Acta Crystallogr. D Biol Crystallogr. , vol.65 , pp. 156-168
    • Lütteke, T.1
  • 55
    • 84861899181 scopus 로고    scopus 로고
    • Heparan sulfate. A heparin in miniature
    • Gallagher, J. T. (2012) Heparan sulfate. A heparin in miniature. Handb. Exp. Pharmacol. 207, 347-360
    • (2012) Handb. Exp. Pharmacol. , vol.207 , pp. 347-360
    • Gallagher, J.T.1
  • 56
    • 84862183665 scopus 로고    scopus 로고
    • Bivalent and co-operative binding of complement factor H to heparan sulfate and heparin
    • Khan, S., Nan, R., Gor, J., Mulloy, B., and Perkins, S. J. (2012) Bivalent and co-operative binding of complement factor H to heparan sulfate and heparin. Biochem. J. 444, 417-428
    • (2012) Biochem. J. , vol.444 , pp. 417-428
    • Khan, S.1    Nan, R.2    Gor, J.3    Mulloy, B.4    Perkins, S.J.5
  • 57
    • 0036721004 scopus 로고    scopus 로고
    • Characterization of the binding site on heparan sulfate for macrophage inflammatory protein 1
    • Stringer, S. E., Forster, M. J., Mulloy, B., Bishop, C. R., Graham, G. J., and Gallagher, J. T. (2002) Characterization of the binding site on heparan sulfate for macrophage inflammatory protein 1. Blood 100, 1543-1550
    • (2002) Blood , vol.100 , pp. 1543-1550
    • Stringer, S.E.1    Forster, M.J.2    Mulloy, B.3    Bishop, C.R.4    Graham, G.J.5    Gallagher, J.T.6
  • 59
    • 13244253766 scopus 로고    scopus 로고
    • Pdb-care (PDB carbohydrate residue check). A program to support annotation of complex carbohydrate structures in PDB files
    • Lütteke, T., and von der Lieth, C. W. (2004) pdb-care (PDB carbohydrate residue check). A program to support annotation of complex carbohydrate structures in PDB files. BMC Bioinformatics 5, 69
    • (2004) BMC Bioinformatics , vol.5 , pp. 69
    • Lütteke, T.1    Von Der Lieth, C.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.