메뉴 건너뛰기




Volumn 110, Issue 41, 2013, Pages 16426-16431

Structural insight on the recognition of surface-bound opsonins by the integrin i domain of complement receptor 3

Author keywords

Innate immunity; Integrin receptor; Phagocytosis; Structural biology

Indexed keywords

ASPARTIC ACID; CD11B ANTIGEN; COMPLEMENT; COMPLEMENT COMPONENT C3B; COMPLEMENT COMPONENT C3D; COMPLEMENT RECEPTOR; COMPLEMENT RECEPTOR 2; GLUTAMIC ACID; INTEGRIN 1 DOMAIN OF COMPLEMENT RECEPTOR 3; METAL ION; OPSONIN; UNCLASSIFIED DRUG;

EID: 84885333791     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1311261110     Document Type: Article
Times cited : (109)

References (53)
  • 1
  • 2
    • 0033836315 scopus 로고    scopus 로고
    • Regulation of the adhesion versus cytotoxic functions of the Mac-1/ CR3/alphaMbeta2-integrin glycoprotein
    • Ross GD (2000) Regulation of the adhesion versus cytotoxic functions of the Mac-1/ CR3/alphaMbeta2-integrin glycoprotein. Crit Rev Immunol 20(3):197-222.
    • (2000) Crit Rev Immunol , vol.20 , Issue.3 , pp. 197-222
    • Ross, G.D.1
  • 3
    • 0027530684 scopus 로고
    • The i domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands
    • Diamond MS, Garcia-Aguilar J, Bickford JK, Corbi AL, Springer TA (1993) The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands. J Cell Biol 120(4):1031-1043.
    • (1993) J Cell Biol , vol.120 , Issue.4 , pp. 1031-1043
    • Diamond, M.S.1    Garcia-Aguilar, J.2    Bickford, J.K.3    Corbi, A.L.4    Springer, T.A.5
  • 4
    • 84857688656 scopus 로고    scopus 로고
    • Integrin inside-out signaling and the immunological synapse
    • Springer TA, Dustin ML (2012) Integrin inside-out signaling and the immunological synapse. Curr Opin Cell Biol 24(1):107-115.
    • (2012) Curr Opin Cell Biol , vol.24 , Issue.1 , pp. 107-115
    • Springer, T.A.1    Dustin, M.L.2
  • 5
    • 77949758937 scopus 로고    scopus 로고
    • Outside-in signal transmission by conformational changes in integrin Mac-1
    • Lefort CT, et al. (2009) Outside-in signal transmission by conformational changes in integrin Mac-1. J Immunol 183(10):6460-6468.
    • (2009) J Immunol , vol.183 , Issue.10 , pp. 6460-6468
    • Lefort, C.T.1
  • 6
    • 46749138342 scopus 로고    scopus 로고
    • Integrin-dependent phagocytosis: Spreading from microadhesion to new concepts
    • Dupuy AG, Caron E (2008) Integrin-dependent phagocytosis: Spreading from microadhesion to new concepts. J Cell Sci 121(Pt 11):1773-1783.
    • (2008) J Cell Sci , vol.121 , Issue.PART. 11 , pp. 1773-1783
    • Dupuy, A.G.1    Caron, E.2
  • 8
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: Complexity in action
    • Underhill DM, Ozinsky A (2002) Phagocytosis of microbes: Complexity in action. Annu Rev Immunol 20:825-852.
    • (2002) Annu Rev Immunol , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 9
    • 0022573996 scopus 로고
    • Phorbol esters cause sequential activation and deactivation of complement receptors on polymorphonuclear leukocytes
    • Wright SD, Meyer BC (1986) Phorbol esters cause sequential activation and deactivation of complement receptors on polymorphonuclear leukocytes. J Immunol 136(5):1759-1764.
    • (1986) J Immunol , vol.136 , Issue.5 , pp. 1759-1764
    • Wright, S.D.1    Meyer, B.C.2
  • 10
    • 34548044827 scopus 로고    scopus 로고
    • Subcapsular encounter and complement-dependent transport of immune complexes by lymph node B cells
    • Phan TG, Grigorova I, Okada T, Cyster JG (2007) Subcapsular encounter and complement-dependent transport of immune complexes by lymph node B cells. Nat Immunol 8(9):992-1000.
    • (2007) Nat Immunol , vol.8 , Issue.9 , pp. 992-1000
    • Phan, T.G.1    Grigorova, I.2    Okada, T.3    Cyster, J.G.4
  • 11
    • 84866046885 scopus 로고    scopus 로고
    • Lymph node macrophages
    • Gray EE, Cyster JG (2012) Lymph node macrophages. J Innate Immun 4(5-6):424-436.
    • (2012) J Innate Immun , vol.4 , Issue.5-6 , pp. 424-436
    • Gray, E.E.1    Cyster, J.G.2
  • 12
    • 79953033726 scopus 로고    scopus 로고
    • Trafficking of B cell antigen in lymph nodes
    • Gonzalez SF, et al. (2011) Trafficking of B cell antigen in lymph nodes. Annu Rev Immunol 29:215-233.
    • (2011) Annu Rev Immunol , vol.29 , pp. 215-233
    • Gonzalez, S.F.1
  • 13
    • 84863348094 scopus 로고    scopus 로고
    • Molecular basis for complement recognition by integrin αxβ2
    • Chen X, Yu Y, Mi LZ, Walz T, Springer TA (2012) Molecular basis for complement recognition by integrin αXβ2. Proc Natl Acad Sci USA 109(12):4586-4591.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.12 , pp. 4586-4591
    • Chen, X.1    Yu, Y.2    Mi, L.Z.3    Walz, T.4    Springer, T.A.5
  • 14
    • 0019953149 scopus 로고
    • Anti-Mac-1 selectively inhibits the mouse and human type three complement receptor
    • Beller DI, Springer TA, Schreiber RD (1982) Anti-Mac-1 selectively inhibits the mouse and human type three complement receptor. J Exp Med 156(4):1000-1009.
    • (1982) J Exp Med , vol.156 , Issue.4 , pp. 1000-1009
    • Beller, D.I.1    Springer, T.A.2    Schreiber, R.D.3
  • 15
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee JO, Rieu P, Arnaout MA, Liddington R (1995) Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 80(4):631-638.
    • (1995) Cell , vol.80 , Issue.4 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 16
    • 13444294243 scopus 로고    scopus 로고
    • Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin alphaXbeta2
    • Vorup-Jensen T, et al. (2005) Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin alphaXbeta2. Proc Natl Acad Sci USA 102(5):1614-1619.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.5 , pp. 1614-1619
    • Vorup-Jensen, T.1
  • 17
    • 80054741216 scopus 로고    scopus 로고
    • Surface plasmon resonance biosensing in studies of the binding between β integrin i domains and their ligands
    • Vorup-Jensen T (2012) Surface plasmon resonance biosensing in studies of the binding between β integrin I domains and their ligands. Methods Mol Biol 757:55-71.
    • (2012) Methods Mol Biol , vol.757 , pp. 55-71
    • Vorup-Jensen, T.1
  • 18
    • 0020438716 scopus 로고
    • C3 convertase of human complement: Enhanced formation and stability of the enzyme generated with nickel instead of magnesium
    • Fishelson Z, Müller-Eberhard HJ (1982) C3 convertase of human complement: Enhanced formation and stability of the enzyme generated with nickel instead of magnesium. J Immunol 129(6):2603-2607.
    • (1982) J Immunol , vol.129 , Issue.6 , pp. 2603-2607
    • Fishelson, Z.1    Müller-Eberhard, H.J.2
  • 19
    • 0032557324 scopus 로고    scopus 로고
    • X-ray crystal structure of C3d:AC3fragmentandligand for complement receptor 2
    • Nagar B, Jones RG, Diefenbach RJ, Isenman DE, Rini JM (1998) X-ray crystal structure of C3d:AC3fragmentandligand for complement receptor 2. Science 280(5367):1277-1281.
    • (1998) Science , vol.280 , Issue.5367 , pp. 1277-1281
    • Nagar, B.1    Jones, R.G.2    Diefenbach, R.J.3    Isenman, D.E.4    Rini, J.M.5
  • 20
    • 79953772478 scopus 로고    scopus 로고
    • Structural basis for engagement by complement factor H of C3b on a self surface
    • Morgan HP, et al. (2011) Structural basis for engagement by complement factor H of C3b on a self surface. Nat Struct Mol Biol 18(4):463-470.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.4 , pp. 463-470
    • Morgan, H.P.1
  • 21
    • 79955533554 scopus 로고    scopus 로고
    • A crystal structure of the complex between human complement receptor 2 and its ligand C3d
    • van den Elsen JM, Isenman DE (2011) A crystal structure of the complex between human complement receptor 2 and its ligand C3d. Science 332(6029):608-611.
    • (2011) Science , vol.332 , Issue.6029 , pp. 608-611
    • Van Den Elsen, J.M.1    Isenman, D.E.2
  • 22
    • 84869201214 scopus 로고    scopus 로고
    • On the roles of polyvalent binding in immune recognition: Perspectives in the nanoscience of immunology and the immune response to nanomedicines
    • Vorup-Jensen T (2012) On the roles of polyvalent binding in immune recognition: Perspectives in the nanoscience of immunology and the immune response to nanomedicines. Adv Drug Deliv Rev 64(15):1759-1781.
    • (2012) Adv Drug Deliv Rev , vol.64 , Issue.15 , pp. 1759-1781
    • Vorup-Jensen, T.1
  • 23
    • 15544389174 scopus 로고    scopus 로고
    • Identity of the amino acid residues involved in C3bi binding to the I-domain supports a mosaic model to explain the broad ligand repertoire of integrin alpha M beta 2
    • Ustinov VA, Plow EF (2005) Identity of the amino acid residues involved in C3bi binding to the I-domain supports a mosaic model to explain the broad ligand repertoire of integrin alpha M beta 2. Biochemistry 44(11):4357-4364.
    • (2005) Biochemistry , vol.44 , Issue.11 , pp. 4357-4364
    • Ustinov, V.A.1    Plow, E.F.2
  • 24
    • 84866558185 scopus 로고    scopus 로고
    • Structural basis for activation of the complement system by component C4 cleavage
    • Kidmose RT, et al. (2012) Structural basis for activation of the complement system by component C4 cleavage. Proc Natl Acad Sci USA 109(38):15425-15430.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.38 , pp. 15425-15430
    • Kidmose, R.T.1
  • 25
    • 0022273901 scopus 로고
    • Membrane complement receptors specific for bound fragments of C3
    • Ross GD, Medof ME (1985) Membrane complement receptors specific for bound fragments of C3. Adv Immunol 37:217-267.
    • (1985) Adv Immunol , vol.37 , pp. 217-267
    • Ross, G.D.1    Medof, M.E.2
  • 26
    • 33745899624 scopus 로고    scopus 로고
    • The structure of bovine complement component 3 reveals the basis for thioester function
    • Fredslund F, et al. (2006) The structure of bovine complement component 3 reveals the basis for thioester function. J Mol Biol 361(1):115-127.
    • (2006) J Mol Biol , vol.361 , Issue.1 , pp. 115-127
    • Fredslund, F.1
  • 27
    • 25644452794 scopus 로고    scopus 로고
    • Structures of complement component C3 provide insights into the function and evolution of immunity
    • Janssen BJ, et al. (2005) Structures of complement component C3 provide insights into the function and evolution of immunity. Nature 437(7058):505-511.
    • (2005) Nature , vol.437 , Issue.7058 , pp. 505-511
    • Janssen, B.J.1
  • 28
    • 79952612300 scopus 로고    scopus 로고
    • Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement
    • Kajander T, et al. (2011) Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement. Proc Natl Acad Sci USA 108(7): 2897-2902.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.7 , pp. 2897-2902
    • Kajander, T.1
  • 29
    • 0028898528 scopus 로고
    • Mutation of residues in the C3dg region of human complement component C3 corresponding to a proposed binding site for complement receptor type 2 (CR2, CD21) does not abolish binding of iC3b or C3dg to CR2
    • Diefenbach RJ, Isenman DE (1995) Mutation of residues in the C3dg region of human complement component C3 corresponding to a proposed binding site for complement receptor type 2 (CR2, CD21) does not abolish binding of iC3b or C3dg to CR2. J Immunol 154(5):2303-2320.
    • (1995) J Immunol , vol.154 , Issue.5 , pp. 2303-2320
    • Diefenbach, R.J.1    Isenman, D.E.2
  • 30
    • 0034292433 scopus 로고    scopus 로고
    • Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21)
    • Clemenza L, Isenman DE (2000) Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21). J Immunol 165(7):3839-3848.
    • (2000) J Immunol , vol.165 , Issue.7 , pp. 3839-3848
    • Clemenza, L.1    Isenman, D.E.2
  • 31
    • 0028130314 scopus 로고
    • Identification of the complement iC3b binding site in the beta 2 integrin CR3 (CD11b/CD18)
    • Ueda T, Rieu P, Brayer J, Arnaout MA (1994) Identification of the complement iC3b binding site in the beta 2 integrin CR3 (CD11b/CD18). Proc Natl Acad Sci USA 91(22): 10680-10684.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.22 , pp. 10680-10684
    • Ueda, T.1    Rieu, P.2    Brayer, J.3    Arnaout, M.A.4
  • 32
    • 0034698162 scopus 로고    scopus 로고
    • Folding and function of i domaindeleted Mac-1 and lymphocyte function-associated antigen-1
    • Yalamanchili P, Lu C, Oxvig C, Springer TA (2000) Folding and function of I domaindeleted Mac-1 and lymphocyte function-associated antigen-1. J Biol Chem 275(29): 21877-21882.
    • (2000) J Biol Chem , vol.275 , Issue.29 , pp. 21877-21882
    • Yalamanchili, P.1    Lu, C.2    Oxvig, C.3    Springer, T.A.4
  • 33
    • 0141780823 scopus 로고    scopus 로고
    • The fourth blade within the beta-propeller is involved specifically in C3bi recognition by integrin alpha M beta 2
    • Li Y, Zhang L (2003) The fourth blade within the beta-propeller is involved specifically in C3bi recognition by integrin alpha M beta 2. J Biol Chem 278(36):34395-34402.
    • (2003) J Biol Chem , vol.278 , Issue.36 , pp. 34395-34402
    • Li, Y.1    Zhang, L.2
  • 34
    • 79955780870 scopus 로고    scopus 로고
    • A systemic lupus erythematosusassociated R77H substitution in the CD11b chain of the Mac-1 integrin compromises leukocyte adhesion and phagocytosis
    • MacPhersonM, Lek HS, Prescott A, Fagerholm SC (2011)A systemic lupus erythematosusassociated R77H substitution in the CD11b chain of the Mac-1 integrin compromises leukocyte adhesion and phagocytosis. J Biol Chem 286(19):17303-17310.
    • (2011) J Biol Chem , vol.286 , Issue.19 , pp. 17303-17310
    • Macpherson, M.1    Lek, H.S.2    Prescott, A.3    Fagerholm, S.C.4
  • 35
    • 2242466605 scopus 로고    scopus 로고
    • Identification of functional segments within the beta2I-domain of integrin alphaMbeta2
    • Xiong Y-M, Haas TA, Zhang L (2002) Identification of functional segments within the beta2I-domain of integrin alphaMbeta2. J Biol Chem 277(48):46639-46644.
    • (2002) J Biol Chem , vol.277 , Issue.48 , pp. 46639-46644
    • Xiong, Y.-M.1    Haas, T.A.2    Zhang, L.3
  • 36
    • 0028006579 scopus 로고
    • Interactions of human complement component C3 with factor B and with complement receptors type 1 (CR1, CD35) and type 3 (CR3, CD11b/CD18) involve an acidic sequence at the N-terminus of C3 alpha'-chain
    • Taniguchi-Sidle A, Isenman DE (1994) Interactions of human complement component C3 with factor B and with complement receptors type 1 (CR1, CD35) and type 3 (CR3, CD11b/CD18) involve an acidic sequence at the N-terminus of C3 alpha'-chain. J Immunol 153(11):5285-5302.
    • (1994) J Immunol , vol.153 , Issue.11 , pp. 5285-5302
    • Taniguchi-Sidle, A.1    Isenman, D.E.2
  • 38
    • 0020039086 scopus 로고
    • Identification of a C3bi-specific membrane complement receptor that is expressed on lymphocytes, monocytes, neutrophils, and erythrocytes
    • Ross GD, Lambris JD (1982) Identification of a C3bi-specific membrane complement receptor that is expressed on lymphocytes, monocytes, neutrophils, and erythrocytes. J Exp Med 155(1):96-110.
    • (1982) J Exp Med , vol.155 , Issue.1 , pp. 96-110
    • Ross, G.D.1    Lambris, J.D.2
  • 39
    • 0023519603 scopus 로고
    • The complement fragment C3d facilitates phagocytosis by monocytes
    • Gaither TA, Vargas I, Inada S, Frank MM (1987) The complement fragment C3d facilitates phagocytosis by monocytes. Immunology 62(3):405-411.
    • (1987) Immunology , vol.62 , Issue.3 , pp. 405-411
    • Gaither, T.A.1    Vargas, I.2    Inada, S.3    Frank, M.M.4
  • 40
    • 33750859976 scopus 로고    scopus 로고
    • Structure of C3b reveals conformational changes that underlie complement activity
    • Janssen BJ, Christodoulidou A, McCarthy A, Lambris JD, Gros P (2006) Structure of C3b reveals conformational changes that underlie complement activity. Nature 444(7116): 213-216.
    • (2006) Nature , vol.444 , Issue.7116 , pp. 213-216
    • Janssen, B.J.1    Christodoulidou, A.2    McCarthy, A.3    Lambris, J.D.4    Gros, P.5
  • 41
    • 33750873601 scopus 로고    scopus 로고
    • Structure of C3b in complex with CRIg gives insights into regulation of complement activation
    • Wiesmann C, et al. (2006) Structure of C3b in complex with CRIg gives insights into regulation of complement activation. Nature 444(7116):217-220.
    • (2006) Nature , vol.444 , Issue.7116 , pp. 217-220
    • Wiesmann, C.1
  • 42
    • 0038506990 scopus 로고    scopus 로고
    • Effects of a selective CD11b/CD18 antagonist and recombinant human tissue plasminogen activator treatment alone and in combination in a rat embolic model of stroke
    • Zhang L, et al. (2003) Effects of a selective CD11b/CD18 antagonist and recombinant human tissue plasminogen activator treatment alone and in combination in a rat embolic model of stroke. Stroke 34(7):1790-1795.
    • (2003) Stroke , vol.34 , Issue.7 , pp. 1790-1795
    • Zhang, L.1
  • 43
    • 84872598183 scopus 로고    scopus 로고
    • MRI assessment of the intra-carotid route for macrophage delivery after transient cerebral ischemia
    • Riou A, et al. (2013) MRI assessment of the intra-carotid route for macrophage delivery after transient cerebral ischemia. NMR Biomed 26(2):115-123.
    • (2013) NMR Biomed , vol.26 , Issue.2 , pp. 115-123
    • Riou, A.1
  • 44
    • 0037438495 scopus 로고    scopus 로고
    • Internalization of circulating apoptotic cells by splenic marginal zone dendritic cells: Dependence on complement receptors and effect on cytokine production
    • Morelli AE, et al. (2003) Internalization of circulating apoptotic cells by splenic marginal zone dendritic cells: dependence on complement receptors and effect on cytokine production. Blood 101(2):611-620.
    • (2003) Blood , vol.101 , Issue.2 , pp. 611-620
    • Morelli, A.E.1
  • 45
    • 0025678813 scopus 로고
    • ICAM-1 (CD54): A counter-receptor for Mac-1 (CD11b/ CD18)
    • Diamond MS, et al. (1990) ICAM-1 (CD54): A counter-receptor for Mac-1 (CD11b/ CD18). J Cell Biol 111(6 Pt 2):3129-3139.
    • (1990) J Cell Biol , vol.111 , Issue.6 PART. 2 , pp. 3129-3139
    • Diamond, M.S.1
  • 46
    • 10744229528 scopus 로고    scopus 로고
    • The pattern recognition receptor (RAGE) is a counterreceptor for leukocyte integrins: A novel pathway for inflammatory cell recruitment
    • Chavakis T, et al. (2003) The pattern recognition receptor (RAGE) is a counterreceptor for leukocyte integrins: A novel pathway for inflammatory cell recruitment. J Exp Med 198(10):1507-1515.
    • (2003) J Exp Med , vol.198 , Issue.10 , pp. 1507-1515
    • Chavakis, T.1
  • 47
    • 11144304343 scopus 로고    scopus 로고
    • The junctional adhesion molecule-C promotes neutrophil transendothelial migration in vitro and in vivo
    • Chavakis T, et al. (2004) The junctional adhesion molecule-C promotes neutrophil transendothelial migration in vitro and in vivo. J Biol Chem 279(53):55602-55608.
    • (2004) J Biol Chem , vol.279 , Issue.53 , pp. 55602-55608
    • Chavakis, T.1
  • 48
    • 84874290850 scopus 로고    scopus 로고
    • Phagocytosis is themain CR3-mediated function affected by the lupus-associated variant of CD11b in human myeloid cells
    • Fossati-Jimack L, et al. (2013) Phagocytosis is themain CR3-mediated function affected by the lupus-associated variant of CD11b in human myeloid cells. PLoS ONE 8(2):e57082.
    • (2013) PLoS ONE , vol.8 , Issue.2
    • Fossati-Jimack, L.1
  • 49
    • 84934442096 scopus 로고    scopus 로고
    • CR2-mediated targeting of complement inhibitors: Bench-to-bedside using a novel strategy for site-specific complement modulation
    • Holers VM, Rohrer B, Tomlinson S (2013) CR2-mediated targeting of complement inhibitors: Bench-to-bedside using a novel strategy for site-specific complement modulation. Adv Exp Med Biol 735:137-154.
    • (2013) Adv Exp Med Biol , vol.735 , pp. 137-154
    • Holers, V.M.1    Rohrer, B.2    Tomlinson, S.3
  • 51
    • 0034624058 scopus 로고    scopus 로고
    • An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain
    • Xiong JP, Li R, Essafi M, Stehle T, Arnaout MA (2000) An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain. J Biol Chem 275(49):38762-38767.
    • (2000) J Biol Chem , vol.275 , Issue.49 , pp. 38762-38767
    • Xiong, J.P.1    Li, R.2    Essafi, M.3    Stehle, T.4    Arnaout, M.A.5
  • 52
    • 0038778441 scopus 로고    scopus 로고
    • Combined affinity and rate constant distributions of ligand populations from experimental surface binding kinetics and equilibria
    • Svitel J, Balbo A, Mariuzza RA, Gonzales NR, Schuck P (2003) Combined affinity and rate constant distributions of ligand populations from experimental surface binding kinetics and equilibria. Biophys J 84(6):4062-4077.
    • (2003) Biophys J , vol.84 , Issue.6 , pp. 4062-4077
    • Svitel, J.1    Balbo, A.2    Mariuzza, R.A.3    Gonzales, N.R.4    Schuck, P.5
  • 53
    • 55549104031 scopus 로고    scopus 로고
    • Bayesian analysis of heterogeneity in the distribution of binding properties of immobilized surface sites
    • Gorshkova II, Svitel J, Razjouyan F, Schuck P (2008) Bayesian analysis of heterogeneity in the distribution of binding properties of immobilized surface sites. Langmuir 24(20):11577-11586.
    • (2008) Langmuir , vol.24 , Issue.20 , pp. 11577-11586
    • Gorshkova, I.I.1    Svitel, J.2    Razjouyan, F.3    Schuck, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.