메뉴 건너뛰기




Volumn 28, Issue 4, 2003, Pages 210-214

Disulfide bonds as switches for protein function

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; DISULFIDE; DITHIOL DERIVATIVE; PROTEIN;

EID: 0037397499     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(03)00057-4     Document Type: Review
Times cited : (514)

References (60)
  • 1
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton J.M. Disulphide bridges in globular proteins. J. Mol. Biol. 151:1981;261-287.
    • (1981) J. Mol. Biol. , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 2
    • 0001227472 scopus 로고
    • Harnessing disulfide-bonds using protein engineering
    • Wetzel R. Harnessing disulfide-bonds using protein engineering. Trends Biochem. Sci. 12:1987;478-482.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 478-482
    • Wetzel, R.1
  • 3
    • 0035178990 scopus 로고    scopus 로고
    • Thrombospondins: Multifunctional regulators of cell interactions
    • Adams J.C. Thrombospondins: multifunctional regulators of cell interactions. Annu. Rev. Cell Dev. Biol. 17:2001;25-51.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 25-51
    • Adams, J.C.1
  • 4
    • 0023035074 scopus 로고
    • The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins
    • Lawler J., Hynes R.O. The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins. J. Cell Biol. 103:1986;1635-1648.
    • (1986) J. Cell Biol. , vol.103 , pp. 1635-1648
    • Lawler, J.1    Hynes, R.O.2
  • 5
    • 0025109879 scopus 로고
    • Free thiols of platelet thrombospondin
    • Speziale M.V., Detwiler T.C. Free thiols of platelet thrombospondin. J. Biol. Chem. 265:1990;17859-17867.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17859-17867
    • Speziale, M.V.1    Detwiler, T.C.2
  • 6
    • 0026667093 scopus 로고
    • Disulfides modulate RGD-inhibitable cell adhesive activity of thrombospondin
    • Sun X., et al. Disulfides modulate RGD-inhibitable cell adhesive activity of thrombospondin. J. Cell Biol. 118:1992;693-701.
    • (1992) J. Cell Biol. , vol.118 , pp. 693-701
    • Sun, X.1
  • 7
    • 0028625495 scopus 로고
    • Thrombospondin 1 as an enzyme inhibitor
    • Hogg P.J. Thrombospondin 1 as an enzyme inhibitor. Thromb. Haemost. 72:1994;787-792.
    • (1994) Thromb. Haemost. , vol.72 , pp. 787-792
    • Hogg, P.J.1
  • 8
    • 0028966229 scopus 로고
    • Calcium ion binding to thrombospondin 1
    • Misenheimer T.M., Mosher D.F. Calcium ion binding to thrombospondin 1. J. Biol. Chem. 270:1995;1729-1733.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1729-1733
    • Misenheimer, T.M.1    Mosher, D.F.2
  • 9
    • 0030771752 scopus 로고    scopus 로고
    • Interaction of platelet-derived growth factor with thrombospondin 1: Dependence on the disulfide-bond arrangement in thrombospondin 1
    • Hogg P.J., et al. Interaction of platelet-derived growth factor with thrombospondin 1: dependence on the disulfide-bond arrangement in thrombospondin 1. Biochem. J. 326:1997;709-716.
    • (1997) Biochem. J. , vol.326 , pp. 709-716
    • Hogg, P.J.1
  • 10
    • 0000550873 scopus 로고    scopus 로고
    • Identification of monoclonal antibodies that recognize different disulfide-bonded forms of thrombospondin 1
    • Matthias L.J., et al. Identification of monoclonal antibodies that recognize different disulfide-bonded forms of thrombospondin 1. Biochim. Biophys. Acta. 1296:1996;138-144.
    • (1996) Biochim. Biophys. Acta , vol.1296 , pp. 138-144
    • Matthias, L.J.1
  • 11
    • 0029780967 scopus 로고    scopus 로고
    • Catalysis of disulfide isomerization in thrombospondin 1 by protein disulfide isomerase
    • Hotchkiss K.A., et al. Catalysis of disulfide isomerization in thrombospondin 1 by protein disulfide isomerase. Biochemistry. 35:1996;9761-9767.
    • (1996) Biochemistry , vol.35 , pp. 9761-9767
    • Hotchkiss, K.A.1
  • 12
    • 0032874303 scopus 로고    scopus 로고
    • Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III
    • Milev Y., Essex D.W. Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III. Arch. Biochem. Biophys. 361:1999;120-126.
    • (1999) Arch. Biochem. Biophys. , vol.361 , pp. 120-126
    • Milev, Y.1    Essex, D.W.2
  • 13
    • 0029025521 scopus 로고
    • Characterization of protein disulfide isomerase released from activated platelets
    • Chen K., et al. Characterization of protein disulfide isomerase released from activated platelets. Br. J. Haematol. 90:1995;425-431.
    • (1995) Br. J. Haematol. , vol.90 , pp. 425-431
    • Chen, K.1
  • 14
    • 0029144477 scopus 로고
    • Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane
    • Essex D.W., et al. Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood. 86:1995;2168-2173.
    • (1995) Blood , vol.86 , pp. 2168-2173
    • Essex, D.W.1
  • 15
    • 0025045118 scopus 로고
    • Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal
    • Yoshimori T., et al. Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal. J. Biol. Chem. 265:1990;15984-15990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15984-15990
    • Yoshimori, T.1
  • 16
    • 0029163450 scopus 로고
    • Secretion, surface localization, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes
    • Terada K., et al. Secretion, surface localization, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes. J. Biol. Chem. 270:1995;20410-20416.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20410-20416
    • Terada, K.1
  • 17
    • 0029826005 scopus 로고    scopus 로고
    • Surface thiols of human lymphocytes and their changes after in vitro and in vivo activation
    • Lawrence D.A., et al. Surface thiols of human lymphocytes and their changes after in vitro and in vivo activation. J. Leukoc. Biol. 60:1996;611-618.
    • (1996) J. Leukoc. Biol. , vol.60 , pp. 611-618
    • Lawrence, D.A.1
  • 18
    • 0030853923 scopus 로고    scopus 로고
    • Membrane-bound proteindisulfide isomerase (PDI) is involved in regulation of surface expression of thiols and drug sensitivity of B-CLL cells
    • Tager M., et al. Membrane-bound proteindisulfide isomerase (PDI) is involved in regulation of surface expression of thiols and drug sensitivity of B-CLL cells. Exp. Hematol. 25:1997;601-607.
    • (1997) Exp. Hematol. , vol.25 , pp. 601-607
    • Tager, M.1
  • 19
    • 0033593450 scopus 로고    scopus 로고
    • Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase
    • Jiang X.-M., et al. Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase. J. Biol. Chem. 274:1999;2416-2423.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2416-2423
    • Jiang, X.-M.1
  • 20
    • 0035908117 scopus 로고    scopus 로고
    • Control of von Willebrand factor multimer size by thrombospondin-1
    • Xie L., et al. Control of von Willebrand factor multimer size by thrombospondin-1. J. Exp. Med. 193:2001;1341-1349.
    • (2001) J. Exp. Med. , vol.193 , pp. 1341-1349
    • Xie, L.1
  • 21
    • 0037108554 scopus 로고    scopus 로고
    • The von Willebrand Factor reducing activity of thrombospondin-1 is located in the calcium-binding/C-terminal sequence and requires a free thiol at position 974
    • Pimanda J.E., et al. The von Willebrand Factor reducing activity of thrombospondin-1 is located in the calcium-binding/C-terminal sequence and requires a free thiol at position 974. Blood. 100:2002;2832-2838.
    • (2002) Blood , vol.100 , pp. 2832-2838
    • Pimanda, J.E.1
  • 22
    • 0030861045 scopus 로고    scopus 로고
    • Generation of angiostatin by reduction and proteolysis of plasmin. Catalysis by a plasmin reductase secreted by cultured cells
    • Stathakis P., et al. Generation of angiostatin by reduction and proteolysis of plasmin. Catalysis by a plasmin reductase secreted by cultured cells. J. Biol. Chem. 272:1997;20641-20645.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20641-20645
    • Stathakis, P.1
  • 23
    • 0033605663 scopus 로고    scopus 로고
    • Angiostatin formation involves disulfide-bond reduction and proteolysis in kringle 5 of plasmin
    • Stathakis P., et al. Angiostatin formation involves disulfide-bond reduction and proteolysis in kringle 5 of plasmin. J. Biol. Chem. 274:1999;8910-8916.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8910-8916
    • Stathakis, P.1
  • 24
    • 0027970092 scopus 로고
    • Angiostatin: A novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma
    • O'Reilly M.S., et al. Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma. Cell. 79:1994;315-328.
    • (1994) Cell , vol.79 , pp. 315-328
    • O'Reilly, M.S.1
  • 25
    • 0034649626 scopus 로고    scopus 로고
    • Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase
    • Lay A.J., et al. Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase. Nature. 408:2000;869-873.
    • (2000) Nature , vol.408 , pp. 869-873
    • Lay, A.J.1
  • 26
    • 0037088650 scopus 로고    scopus 로고
    • Plasmin reduction by phosphoglycerate kinase is a thiol-independent process
    • Lay A.J., et al. Plasmin reduction by phosphoglycerate kinase is a thiol-independent process. J. Biol. Chem. 277:2002;9062-9068.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9062-9068
    • Lay, A.J.1
  • 27
    • 0037192807 scopus 로고    scopus 로고
    • Identification of annexin II heterotetramer as a plasmin reductase
    • Kwon M., et al. Identification of annexin II heterotetramer as a plasmin reductase. J. Biol. Chem. 277:2002;10903-10911.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10903-10911
    • Kwon, M.1
  • 28
    • 12644251975 scopus 로고    scopus 로고
    • The mechanism of cancer-mediated conversion of plasminogen to the angiogenesis inhibitor angiostatin
    • Gately S., et al. The mechanism of cancer-mediated conversion of plasminogen to the angiogenesis inhibitor angiostatin. Proc. Natl. Acad. Sci. U. S. A. 94:1997;10868-10872.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 10868-10872
    • Gately, S.1
  • 29
    • 0035937779 scopus 로고    scopus 로고
    • Purification and characterization of A61. An angiostatin-like plasminogen fragment produced by plasmin autodigestion in the absence of sulfhydryl donors
    • Kassam G., et al. Purification and characterization of A61. An angiostatin-like plasminogen fragment produced by plasmin autodigestion in the absence of sulfhydryl donors. J. Biol. Chem. 276:2001;8924-8933.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8924-8933
    • Kassam, G.1
  • 30
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert D.M., Kim P.S. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:2001;777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 31
    • 0025198478 scopus 로고
    • Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains
    • Wang J.H., et al. Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Nature. 348:1990;411-418.
    • (1990) Nature , vol.348 , pp. 411-418
    • Wang, J.H.1
  • 32
    • 0025224767 scopus 로고
    • Crystal structure of an HIV-binding recombinant fragment of human CD4
    • Ryu S.E., et al. Crystal structure of an HIV-binding recombinant fragment of human CD4. Nature. 348:1990;419-426.
    • (1990) Nature , vol.348 , pp. 419-426
    • Ryu, S.E.1
  • 33
    • 0027219115 scopus 로고
    • 2-terminal domains
    • 2-terminal domains. Science. 260:1993;979-983.
    • (1993) Science , vol.260 , pp. 979-983
    • Brady, R.L.1
  • 34
    • 0036341983 scopus 로고    scopus 로고
    • Disulfide exchange in domain 2 of CD4 is required for entry of the human immunodeficiency virus type 1
    • Matthias L.J., et al. Disulfide exchange in domain 2 of CD4 is required for entry of the human immunodeficiency virus type 1. Nat. Immun. 3:2002;727-732.
    • (2002) Nat. Immun. , vol.3 , pp. 727-732
    • Matthias, L.J.1
  • 35
    • 0026084915 scopus 로고
    • Identification of a thioredoxin-related protein associated with plasma membranes
    • Martin H., Dean M. Identification of a thioredoxin-related protein associated with plasma membranes. Biochem. Biophys. Res. Commun. 175:1991;123-128.
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 123-128
    • Martin, H.1    Dean, M.2
  • 36
    • 0026443077 scopus 로고
    • Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway
    • Rubartelli A., et al. Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway. J. Biol. Chem. 267:1992;24161-24164.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24161-24164
    • Rubartelli, A.1
  • 37
    • 0037296312 scopus 로고    scopus 로고
    • Redox control on the cell surface: Implications for HIV-1 entry
    • Matthias L.J., Hogg P.J. Redox control on the cell surface: implications for HIV-1 entry. Antioxid. Redox Signal. 5:2003;133-138.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 133-138
    • Matthias, L.J.1    Hogg, P.J.2
  • 38
    • 0345772126 scopus 로고    scopus 로고
    • Inhibitors of protein disulfide isomerase (PDI) prevent cleavage of disulfide-bonds in receptor-bound gp120 and prevent HIV-1 entry
    • Gallina A., et al. Inhibitors of protein disulfide isomerase (PDI) prevent cleavage of disulfide-bonds in receptor-bound gp120 and prevent HIV-1 entry. J. Biol. Chem. 277:2002;50579-50588.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50579-50588
    • Gallina, A.1
  • 39
    • 0037474328 scopus 로고    scopus 로고
    • Protein disulfide isomerase-mediated reduction of two disulfide-bonds of HIV Env gp120 occurs post CXCR4 binding and is required for fusion
    • Barbouche R., et al. Protein disulfide isomerase-mediated reduction of two disulfide-bonds of HIV Env gp120 occurs post CXCR4 binding and is required for fusion. J. Biol. Chem. 278:2003;3131-3136.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3131-3136
    • Barbouche, R.1
  • 40
    • 0028257964 scopus 로고
    • Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction
    • Ryser H.J., et al. Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction. Proc. Natl. Acad. Sci. U. S. A. 91:1994;4559-4563.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 4559-4563
    • Ryser, H.J.1
  • 41
    • 0035282999 scopus 로고    scopus 로고
    • The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding
    • Fenouillet E., et al. The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding. J. Infect. Dis. 183:2001;744-752.
    • (2001) J. Infect. Dis. , vol.183 , pp. 744-752
    • Fenouillet, E.1
  • 42
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes R. Integrins: bidirectional, allosteric signaling machines. Cell. 110:2002;673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.1
  • 43
    • 0035979337 scopus 로고    scopus 로고
    • Mechanism of integrin activation by disulfide-bond reduction
    • Yan B., Smith J.W. Mechanism of integrin activation by disulfide-bond reduction. Biochemistry. 40:2001;8861-8867.
    • (2001) Biochemistry , vol.40 , pp. 8861-8867
    • Yan, B.1    Smith, J.W.2
  • 44
    • 0034704162 scopus 로고    scopus 로고
    • A redox site involved in integrin activation
    • Yan B., Smith J.W. A redox site involved in integrin activation. J. Biol. Chem. 275:2000;39964-39972.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39964-39972
    • Yan, B.1    Smith, J.W.2
  • 45
    • 0034711264 scopus 로고    scopus 로고
    • 3 has an endogenous thiol isomerase activity
    • 3 has an endogenous thiol isomerase activity. J. Biol. Chem. 275:2000;36984-36990.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36984-36990
    • O'Neill, S.1
  • 46
    • 0036786353 scopus 로고    scopus 로고
    • Sustained integrin ligation involves extracellular free sulfhydryls and enzymatically catalyzed disulfide exchange
    • Lahav J., et al. Sustained integrin ligation involves extracellular free sulfhydryls and enzymatically catalyzed disulfide exchange. Blood. 100:2002;2472-2478.
    • (2002) Blood , vol.100 , pp. 2472-2478
    • Lahav, J.1
  • 47
    • 0035918587 scopus 로고    scopus 로고
    • Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation
    • Essex D.W., et al. Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation. Biochemistry. 40:2001;6070-6075.
    • (2001) Biochemistry , vol.40 , pp. 6070-6075
    • Essex, D.W.1
  • 48
  • 49
    • 0036220127 scopus 로고    scopus 로고
    • Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
    • Beglova N., et al. Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation. Nat. Struct. Biol. 9:2002;282-287.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 282-287
    • Beglova, N.1
  • 50
    • 0036198797 scopus 로고    scopus 로고
    • Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
    • Freedman R.B., et al. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep. 3:2002;136-140.
    • (2002) EMBO Rep. , vol.3 , pp. 136-140
    • Freedman, R.B.1
  • 51
    • 0037067649 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages
    • Gagnon E., et al. Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages. Cell. 110:2002;119-131.
    • (2002) Cell , vol.110 , pp. 119-131
    • Gagnon, E.1
  • 52
    • 0033923221 scopus 로고    scopus 로고
    • High-capacity redox control at the plasma membrane of mammalian cells: Trans-membrane, cell surface, and serum NADH-oxidases
    • Berridge M.V., Tan A.S. High-capacity redox control at the plasma membrane of mammalian cells: trans-membrane, cell surface, and serum NADH-oxidases. Antioxid. Redox Signal. 2:2000;231-242.
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 231-242
    • Berridge, M.V.1    Tan, A.S.2
  • 53
    • 0033118238 scopus 로고    scopus 로고
    • A molecular mechanism for the cleavage of a disulfide-bond as the primary function of agonist binding to G-protein-coupled receptors based on theoretical calculations supported by experiments
    • Brandt W., et al. A molecular mechanism for the cleavage of a disulfide-bond as the primary function of agonist binding to G-protein-coupled receptors based on theoretical calculations supported by experiments. Eur. J. Biochem. 261:1999;89-97.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 89-97
    • Brandt, W.1
  • 54
    • 0032502267 scopus 로고    scopus 로고
    • Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen
    • Chang Y., et al. Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen. Biochemistry. 37:1998;3258-3271.
    • (1998) Biochemistry , vol.37 , pp. 3258-3271
    • Chang, Y.1
  • 56
    • 0021757436 scopus 로고
    • A new force field for molecular mechanical simulation of nucleic acids and proteins
    • Weiner S.J., et al. A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Am. Chem. Soc. 106:1984;765-784.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 765-784
    • Weiner, S.J.1
  • 57
    • 0023034995 scopus 로고
    • The crystallographically determined structures of atypical strained disulfides engineered into subtilisin
    • Katz B.A., Kossiakoff A. The crystallographically determined structures of atypical strained disulfides engineered into subtilisin. J. Biol. Chem. 261:1986;15480-15485.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15480-15485
    • Katz, B.A.1    Kossiakoff, A.2
  • 58
    • 0022998684 scopus 로고
    • In vivo formation and stability of engineered disulfide-bonds in subtilisin
    • Wells J.A., Power D.B. In vivo formation and stability of engineered disulfide-bonds in subtilisin. J. Biol. Chem. 261:1986;6564-6570.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6564-6570
    • Wells, J.A.1    Power, D.B.2
  • 59
    • 0036752945 scopus 로고    scopus 로고
    • Cysteine regulation of protein function - as exemplified by NMDA-receptor modulation
    • Lipton S.A., et al. Cysteine regulation of protein function - as exemplified by NMDA-receptor modulation. Trends Neurosci. 25:2002;474-480.
    • (2002) Trends Neurosci. , vol.25 , pp. 474-480
    • Lipton, S.A.1
  • 60
    • 0028177807 scopus 로고
    • Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices
    • Ryu S.E., et al. Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices. Structure. 2:1994;59-74.
    • (1994) Structure , vol.2 , pp. 59-74
    • Ryu, S.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.