메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages

Identification of Bartonella Trw host-specific receptor on erythrocytes

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MULTIPROTEIN COMPLEX; TRW PROTEIN; TRWH PROTEIN; TRWJ1 PROTEIN; TRWJ2 PROTEIN; TRWL PROTEIN; UNCLASSIFIED DRUG;

EID: 84864386808     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0041447     Document Type: Article
Times cited : (18)

References (53)
  • 1
    • 67949107950 scopus 로고    scopus 로고
    • Ecological fitness and strategies of adaptation of Bartonella species to their hosts and vectors
    • Chomel BB, Boulouis HJ, Breitschwerdt EB, Kasten RW, Vayssier-Taussat M, et al. (2009) Ecological fitness and strategies of adaptation of Bartonella species to their hosts and vectors. Vet Res 40: 29.
    • (2009) Vet Res , vol.40 , pp. 29
    • Chomel, B.B.1    Boulouis, H.J.2    Breitschwerdt, E.B.3    Kasten, R.W.4    Vayssier-Taussat, M.5
  • 2
    • 44449138960 scopus 로고    scopus 로고
    • Persistent Bartonella infection: epidemiological and clinical implications
    • Discussion 1047-1039
    • Boulouis HJ, Haddad N, Vayssier-Taussat M, Maillard R, Chomel B, (2007) [Persistent Bartonella infection: epidemiological and clinical implications]. Bull Acad Natl Med 191: 1037-1044; discussion 1047-1039.
    • (2007) Bull Acad Natl Med , vol.191 , pp. 1037-1044
    • Boulouis, H.J.1    Haddad, N.2    Vayssier-Taussat, M.3    Maillard, R.4    Chomel, B.5
  • 4
    • 0033772639 scopus 로고    scopus 로고
    • Antigenic variation in vector-borne pathogens
    • Barbour AG, Restrepo BI, (2000) Antigenic variation in vector-borne pathogens. Emerg Infect Dis 6: 449-457.
    • (2000) Emerg Infect Dis , vol.6 , pp. 449-457
    • Barbour, A.G.1    Restrepo, B.I.2
  • 5
    • 0343831897 scopus 로고    scopus 로고
    • Invasion and persistent intracellular colonization of erythrocytes. A unique parasitic strategy of the emerging pathogen Bartonella
    • Schulein R, Seubert A, Gille C, Lanz C, Hansmann Y, et al. (2001) Invasion and persistent intracellular colonization of erythrocytes. A unique parasitic strategy of the emerging pathogen Bartonella. J Exp Med 193: 1077-1086.
    • (2001) J Exp Med , vol.193 , pp. 1077-1086
    • Schulein, R.1    Seubert, A.2    Gille, C.3    Lanz, C.4    Hansmann, Y.5
  • 6
    • 0030865798 scopus 로고    scopus 로고
    • Interaction of Bartonella henselae with endothelial cells results in bacterial aggregation on the cell surface and the subsequent engulfment and internalisation of the bacterial aggregate by a unique structure, the invasome
    • Dehio C, Meyer M, Berger J, Schwarz H, Lanz C, (1997) Interaction of Bartonella henselae with endothelial cells results in bacterial aggregation on the cell surface and the subsequent engulfment and internalisation of the bacterial aggregate by a unique structure, the invasome. J Cell Sci 110 (Pt 18): 2141-2154.
    • (1997) J Cell Sci , vol.110 , Issue.Pt 18 , pp. 2141-2154
    • Dehio, C.1    Meyer, M.2    Berger, J.3    Schwarz, H.4    Lanz, C.5
  • 7
    • 0032997071 scopus 로고    scopus 로고
    • Interactions of Bartonella henselae with vascular endothelial cells
    • Dehio C, (1999) Interactions of Bartonella henselae with vascular endothelial cells. Curr Opin Microbiol 2: 78-82.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 78-82
    • Dehio, C.1
  • 8
    • 0035371051 scopus 로고    scopus 로고
    • Bartonella interactions with endothelial cells and erythrocytes
    • Dehio C, (2001) Bartonella interactions with endothelial cells and erythrocytes. Trends Microbiol 9: 279-285.
    • (2001) Trends Microbiol , vol.9 , pp. 279-285
    • Dehio, C.1
  • 9
    • 1942520221 scopus 로고    scopus 로고
    • The VirB type IV secretion system of Bartonella henselae mediates invasion, proinflammatory activation and antiapoptotic protection of endothelial cells
    • Schmid MC, Schulein R, Dehio M, Denecker G, Carena I, et al. (2004) The VirB type IV secretion system of Bartonella henselae mediates invasion, proinflammatory activation and antiapoptotic protection of endothelial cells. Mol Microbiol 52: 81-92.
    • (2004) Mol Microbiol , vol.52 , pp. 81-92
    • Schmid, M.C.1    Schulein, R.2    Dehio, M.3    Denecker, G.4    Carena, I.5
  • 10
    • 58149289838 scopus 로고    scopus 로고
    • Bartonella henselae: subversion of vascular endothelial cell functions by translocated bacterial effector proteins
    • Pulliainen AT, Dehio C, (2009) Bartonella henselae: subversion of vascular endothelial cell functions by translocated bacterial effector proteins. Int J Biochem Cell Biol 41: 507-510.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 507-510
    • Pulliainen, A.T.1    Dehio, C.2
  • 11
    • 23744442067 scopus 로고    scopus 로고
    • Infection of human CD34+ progenitor cells with Bartonella henselae results in intraerythrocytic presence of B. henselae
    • Mandle T, Einsele H, Schaller M, Neumann D, Vogel W, et al. (2005) Infection of human CD34+ progenitor cells with Bartonella henselae results in intraerythrocytic presence of B. henselae. Blood 106: 1215-1222.
    • (2005) Blood , vol.106 , pp. 1215-1222
    • Mandle, T.1    Einsele, H.2    Schaller, M.3    Neumann, D.4    Vogel, W.5
  • 12
    • 0019506216 scopus 로고
    • Bartonella bacilliformis: colonial types and erythrocyte adherence
    • Walker TS, Winkler HH, (1981) Bartonella bacilliformis: colonial types and erythrocyte adherence. Infect Immun 31: 480-486.
    • (1981) Infect Immun , vol.31 , pp. 480-486
    • Walker, T.S.1    Winkler, H.H.2
  • 13
    • 0028234682 scopus 로고
    • Identification of outer membrane proteins of Bartonella bacilliformis
    • Minnick MF, (1994) Identification of outer membrane proteins of Bartonella bacilliformis. Infect Immun 62: 2644-2648.
    • (1994) Infect Immun , vol.62 , pp. 2644-2648
    • Minnick, M.F.1
  • 15
    • 0036840135 scopus 로고    scopus 로고
    • Bartonella: new explanations for old diseases
    • Greub G, Raoult D, (2002) Bartonella: new explanations for old diseases. J Med Microbiol 51: 915-923.
    • (2002) J Med Microbiol , vol.51 , pp. 915-923
    • Greub, G.1    Raoult, D.2
  • 16
    • 0027359265 scopus 로고
    • Characterization of Bartonella bacilliformis flagella and effect of antiflagellin antibodies on invasion of human erythrocytes
    • Scherer DC, DeBuron-Connors I, Minnick MF, (1993) Characterization of Bartonella bacilliformis flagella and effect of antiflagellin antibodies on invasion of human erythrocytes. Infect Immun 61: 4962-4971.
    • (1993) Infect Immun , vol.61 , pp. 4962-4971
    • Scherer, D.C.1    DeBuron-Connors, I.2    Minnick, M.F.3
  • 17
  • 18
    • 0032771397 scopus 로고    scopus 로고
    • Development of a system for genetic manipulation of Bartonella bacilliformis
    • Battisti JM, Minnick MF, (1999) Development of a system for genetic manipulation of Bartonella bacilliformis. Appl Environ Microbiol 65: 3441-3448.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3441-3448
    • Battisti, J.M.1    Minnick, M.F.2
  • 19
    • 0033834434 scopus 로고    scopus 로고
    • Interaction of Bartonella bacilliformis with human erythrocyte membrane proteins
    • Buckles EL, McGinnis Hill E, (2000) Interaction of Bartonella bacilliformis with human erythrocyte membrane proteins. Microb Pathog 29: 165-174.
    • (2000) Microb Pathog , vol.29 , pp. 165-174
    • Buckles, E.L.1    McGinnis Hill, E.2
  • 20
    • 0031416196 scopus 로고    scopus 로고
    • Comparison of the abilities of proteins from Bartonella bacilliformis and Bartonella henselae to deform red cell membranes and to bind to red cell ghost proteins
    • Iwaki-Egawa S, Ihler GM, (1997) Comparison of the abilities of proteins from Bartonella bacilliformis and Bartonella henselae to deform red cell membranes and to bind to red cell ghost proteins. FEMS Microbiol Lett 157: 207-217.
    • (1997) FEMS Microbiol Lett , vol.157 , pp. 207-217
    • Iwaki-Egawa, S.1    Ihler, G.M.2
  • 21
    • 0034255091 scopus 로고    scopus 로고
    • Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells
    • Christie PJ, Vogel JP, (2000) Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells. Trends Microbiol 8: 354-360.
    • (2000) Trends Microbiol , vol.8 , pp. 354-360
    • Christie, P.J.1    Vogel, J.P.2
  • 22
    • 36548999782 scopus 로고    scopus 로고
    • Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors
    • Saenz HL, Engel P, Stoeckli MC, Lanz C, Raddatz G, et al. (2007) Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors. Nat Genet 39: 1469-1476.
    • (2007) Nat Genet , vol.39 , pp. 1469-1476
    • Saenz, H.L.1    Engel, P.2    Stoeckli, M.C.3    Lanz, C.4    Raddatz, G.5
  • 23
    • 77954687617 scopus 로고    scopus 로고
    • The Trw type IV secretion system of Bartonella mediates host-specific adhesion to erythrocytes
    • Vayssier-Taussat M, Le Rhun D, Deng HK, Biville F, Cescau S, et al. (2010) The Trw type IV secretion system of Bartonella mediates host-specific adhesion to erythrocytes. PLoS Pathog 6: e1000946.
    • (2010) PLoS Pathog , vol.6
    • Vayssier-Taussat, M.1    Le Rhun, D.2    Deng, H.K.3    Biville, F.4    Cescau, S.5
  • 24
    • 47549106865 scopus 로고    scopus 로고
    • Infection-associated type IV secretion systems of Bartonella and their diverse roles in host cell interaction
    • Dehio C, (2008) Infection-associated type IV secretion systems of Bartonella and their diverse roles in host cell interaction. Cell Microbiol 10: 1591-1598.
    • (2008) Cell Microbiol , vol.10 , pp. 1591-1598
    • Dehio, C.1
  • 27
    • 21244462648 scopus 로고    scopus 로고
    • Virulence-associated type IV secretion systems of Bartonella
    • Schroder G, Dehio C, (2005) Virulence-associated type IV secretion systems of Bartonella. Trends Microbiol 13: 336-342.
    • (2005) Trends Microbiol , vol.13 , pp. 336-342
    • Schroder, G.1    Dehio, C.2
  • 28
    • 0032762640 scopus 로고    scopus 로고
    • Vir proteins stabilize VirB5 and mediate its association with the T pilus of Agrobacterium tumefaciens
    • Schmidt-Eisenlohr H, Domke N, Angerer C, Wanner G, Zambryski PC, et al. (1999) Vir proteins stabilize VirB5 and mediate its association with the T pilus of Agrobacterium tumefaciens. J Bacteriol 181: 7485-7492.
    • (1999) J Bacteriol , vol.181 , pp. 7485-7492
    • Schmidt-Eisenlohr, H.1    Domke, N.2    Angerer, C.3    Wanner, G.4    Zambryski, P.C.5
  • 29
    • 36448994400 scopus 로고    scopus 로고
    • The VirB5 protein localizes to the T-pilus tips in Agrobacterium tumefaciens
    • Aly KA, Baron C, (2007) The VirB5 protein localizes to the T-pilus tips in Agrobacterium tumefaciens. Microbiology 153: 3766-3775.
    • (2007) Microbiology , vol.153 , pp. 3766-3775
    • Aly, K.A.1    Baron, C.2
  • 30
    • 0031923138 scopus 로고    scopus 로고
    • Processed VirB2 is the major subunit of the promiscuous pilus of Agrobacterium tumefaciens
    • Lai EM, Kado CI, (1998) Processed VirB2 is the major subunit of the promiscuous pilus of Agrobacterium tumefaciens. J Bacteriol 180: 2711-2717.
    • (1998) J Bacteriol , vol.180 , pp. 2711-2717
    • Lai, E.M.1    Kado, C.I.2
  • 31
    • 0037143720 scopus 로고    scopus 로고
    • Detergent extraction identifies different VirB protein subassemblies of the type IV secretion machinery in the membranes of Agrobacterium tumefaciens
    • Krall L, Wiedemann U, Unsin G, Weiss S, Domke N, et al. (2002) Detergent extraction identifies different VirB protein subassemblies of the type IV secretion machinery in the membranes of Agrobacterium tumefaciens. Proc Natl Acad Sci U S A 99: 11405-11410.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11405-11410
    • Krall, L.1    Wiedemann, U.2    Unsin, G.3    Weiss, S.4    Domke, N.5
  • 32
    • 0034819855 scopus 로고    scopus 로고
    • Intracellular induction of the Bartonella henselae virB operon by human endothelial cells
    • Schmiederer M, Arcenas R, Widen R, Valkov N, Anderson B, (2001) Intracellular induction of the Bartonella henselae virB operon by human endothelial cells. Infect Immun 69: 6495-6502.
    • (2001) Infect Immun , vol.69 , pp. 6495-6502
    • Schmiederer, M.1    Arcenas, R.2    Widen, R.3    Valkov, N.4    Anderson, B.5
  • 33
    • 17644417153 scopus 로고    scopus 로고
    • CD46-independent binding of neisserial type IV pili and the major pilus adhesin, PilC, to human epithelial cells
    • Kirchner M, Heuer D, Meyer TF, (2005) CD46-independent binding of neisserial type IV pili and the major pilus adhesin, PilC, to human epithelial cells. Infect Immun 73: 3072-3082.
    • (2005) Infect Immun , vol.73 , pp. 3072-3082
    • Kirchner, M.1    Heuer, D.2    Meyer, T.F.3
  • 34
    • 0018279059 scopus 로고
    • The anion transport system of the red blood cell. The role of membrane protein evaluated by the use of 'probes
    • Cabantchik ZI, Knauf PA, Rothstein A, (1978) The anion transport system of the red blood cell. The role of membrane protein evaluated by the use of 'probes'. Biochim Biophys Acta 515: 239-302.
    • (1978) Biochim Biophys Acta , vol.515 , pp. 239-302
    • Cabantchik, Z.I.1    Knauf, P.A.2    Rothstein, A.3
  • 36
    • 0021918068 scopus 로고
    • Plasmodium falciparum malaria: band 3 as a possible receptor during invasion of human erythrocytes
    • Okoye VC, Bennett V, (1985) Plasmodium falciparum malaria: band 3 as a possible receptor during invasion of human erythrocytes. Science 227: 169-171.
    • (1985) Science , vol.227 , pp. 169-171
    • Okoye, V.C.1    Bennett, V.2
  • 37
    • 0025836190 scopus 로고
    • Plasmodium falciparum polypeptides interacting with human red cell membranes show high affinity binding to Band-3
    • Jones GL, Edmundson HM, (1991) Plasmodium falciparum polypeptides interacting with human red cell membranes show high affinity binding to Band-3. Biochim Biophys Acta 1097: 71-76.
    • (1991) Biochim Biophys Acta , vol.1097 , pp. 71-76
    • Jones, G.L.1    Edmundson, H.M.2
  • 38
    • 0020603505 scopus 로고
    • A monoclonal antibody to rhesus erythrocyte band 3 inhibits invasion by malaria (Plasmodium knowlesi) merozoites
    • Miller LH, Hudson D, Rener J, Taylor D, Hadley TJ, et al. (1983) A monoclonal antibody to rhesus erythrocyte band 3 inhibits invasion by malaria (Plasmodium knowlesi) merozoites. J Clin Invest 72: 1357-1364.
    • (1983) J Clin Invest , vol.72 , pp. 1357-1364
    • Miller, L.H.1    Hudson, D.2    Rener, J.3    Taylor, D.4    Hadley, T.J.5
  • 39
    • 0030581703 scopus 로고    scopus 로고
    • A role for erythrocyte band 3 degradation by the parasite gp76 serine protease in the formation of the parasitophorous vacuole during invasion of erythrocytes by Plasmodium falciparum
    • Roggwiller E, Betoulle ME, Blisnick T, Braun Breton C, (1996) A role for erythrocyte band 3 degradation by the parasite gp76 serine protease in the formation of the parasitophorous vacuole during invasion of erythrocytes by Plasmodium falciparum. Mol Biochem Parasitol 82: 13-24.
    • (1996) Mol Biochem Parasitol , vol.82 , pp. 13-24
    • Roggwiller, E.1    Betoulle, M.E.2    Blisnick, T.3    Braun Breton, C.4
  • 40
    • 0027771176 scopus 로고
    • Proteolytic digestion of band 3 at an external site alters the erythrocyte membrane organisation and may facilitate malarial invasion
    • McPherson RA, Donald DR, Sawyer WH, Tilley L, (1993) Proteolytic digestion of band 3 at an external site alters the erythrocyte membrane organisation and may facilitate malarial invasion. Mol Biochem Parasitol 62: 233-242.
    • (1993) Mol Biochem Parasitol , vol.62 , pp. 233-242
    • McPherson, R.A.1    Donald, D.R.2    Sawyer, W.H.3    Tilley, L.4
  • 41
    • 0033958230 scopus 로고    scopus 로고
    • Functional conservation of the malaria vaccine antigen MSP-119across distantly related Plasmodium species
    • O'Donnell RA, Saul A, Cowman AF, Crabb BS, (2000) Functional conservation of the malaria vaccine antigen MSP-119across distantly related Plasmodium species. Nat Med 6: 91-95.
    • (2000) Nat Med , vol.6 , pp. 91-95
    • O'Donnell, R.A.1    Saul, A.2    Cowman, A.F.3    Crabb, B.S.4
  • 42
    • 0035908009 scopus 로고    scopus 로고
    • Antibodies against merozoite surface protein (MSP)-1(19) are a major component of the invasion-inhibitory response in individuals immune to malaria
    • O'Donnell RA, de Koning-Ward TF, Burt RA, Bockarie M, Reeder JC, et al. (2001) Antibodies against merozoite surface protein (MSP)-1(19) are a major component of the invasion-inhibitory response in individuals immune to malaria. J Exp Med 193: 1403-1412.
    • (2001) J Exp Med , vol.193 , pp. 1403-1412
    • O'Donnell, R.A.1    de Koning-Ward, T.F.2    Burt, R.A.3    Bockarie, M.4    Reeder, J.C.5
  • 43
    • 0038303177 scopus 로고    scopus 로고
    • Band 3 is a host receptor binding merozoite surface protein 1 during the Plasmodium falciparum invasion of erythrocytes
    • Goel VK, Li X, Chen H, Liu SC, Chishti AH, et al. (2003) Band 3 is a host receptor binding merozoite surface protein 1 during the Plasmodium falciparum invasion of erythrocytes. Proc Natl Acad Sci U S A 100: 5164-5169.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5164-5169
    • Goel, V.K.1    Li, X.2    Chen, H.3    Liu, S.C.4    Chishti, A.H.5
  • 44
    • 27844495638 scopus 로고    scopus 로고
    • Two Plasmodium falciparum merozoite proteins binding to erythrocyte band 3 form a direct complex
    • Kariuki MM, Li X, Yamodo I, Chishti AH, Oh SS, (2005) Two Plasmodium falciparum merozoite proteins binding to erythrocyte band 3 form a direct complex. Biochem Biophys Res Commun 338: 1690-1695.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 1690-1695
    • Kariuki, M.M.1    Li, X.2    Yamodo, I.3    Chishti, A.H.4    Oh, S.S.5
  • 45
    • 1242294422 scopus 로고    scopus 로고
    • A co-ligand complex anchors Plasmodium falciparum merozoites to the erythrocyte invasion receptor band 3
    • Li X, Chen H, Oo TH, Daly TM, Bergman LW, et al. (2004) A co-ligand complex anchors Plasmodium falciparum merozoites to the erythrocyte invasion receptor band 3. J Biol Chem 279: 5765-5771.
    • (2004) J Biol Chem , vol.279 , pp. 5765-5771
    • Li, X.1    Chen, H.2    Oo, T.H.3    Daly, T.M.4    Bergman, L.W.5
  • 46
    • 0022510884 scopus 로고
    • Invasion of erythrocytes by Plasmodium falciparum malaria parasites: evidence for receptor heterogeneity and two receptors
    • Mitchell GH, Hadley TJ, McGinniss MH, Klotz FW, Miller LH, (1986) Invasion of erythrocytes by Plasmodium falciparum malaria parasites: evidence for receptor heterogeneity and two receptors. Blood 67: 1519-1521.
    • (1986) Blood , vol.67 , pp. 1519-1521
    • Mitchell, G.H.1    Hadley, T.J.2    McGinniss, M.H.3    Klotz, F.W.4    Miller, L.H.5
  • 47
    • 0025113460 scopus 로고
    • Evidence for a switching mechanism in the invasion of erythrocytes by Plasmodium falciparum
    • Dolan SA, Miller LH, Wellems TE, (1990) Evidence for a switching mechanism in the invasion of erythrocytes by Plasmodium falciparum. J Clin Invest 86: 618-624.
    • (1990) J Clin Invest , vol.86 , pp. 618-624
    • Dolan, S.A.1    Miller, L.H.2    Wellems, T.E.3
  • 48
    • 68749119337 scopus 로고    scopus 로고
    • Molecular basis of binding of the Plasmodium falciparum receptor BAEBL to erythrocyte receptor glycophorin C
    • Jiang L, Duriseti S, Sun P, Miller LH, (2009) Molecular basis of binding of the Plasmodium falciparum receptor BAEBL to erythrocyte receptor glycophorin C. Mol Biochem Parasitol. 168: 49-54.
    • (2009) Mol Biochem Parasitol , vol.168 , pp. 49-54
    • Jiang, L.1    Duriseti, S.2    Sun, P.3    Miller, L.H.4
  • 49
    • 0021240398 scopus 로고
    • Surface proteins of Plasmodium falciparum merozoites binding to the erythrocyte receptor, glycophorin
    • Perkins ME, (1984) Surface proteins of Plasmodium falciparum merozoites binding to the erythrocyte receptor, glycophorin. J Exp Med 160: 788-798.
    • (1984) J Exp Med , vol.160 , pp. 788-798
    • Perkins, M.E.1
  • 50
    • 65249096690 scopus 로고    scopus 로고
    • Glycophorin B is the erythrocyte receptor of Plasmodium falciparum erythrocyte-binding ligand, EBL-1
    • Mayer DC, Cofie J, Jiang L, Hartl DL, Tracy E, et al. (2009) Glycophorin B is the erythrocyte receptor of Plasmodium falciparum erythrocyte-binding ligand, EBL-1. Proc Natl Acad Sci U S A 106: 5348-5352.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 5348-5352
    • Mayer, D.C.1    Cofie, J.2    Jiang, L.3    Hartl, D.L.4    Tracy, E.5
  • 51
    • 0038142364 scopus 로고    scopus 로고
    • Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl)
    • Lobo CA, Rodriguez M, Reid M, Lustigman S, (2003) Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl). Blood 101: 4628-4631.
    • (2003) Blood , vol.101 , pp. 4628-4631
    • Lobo, C.A.1    Rodriguez, M.2    Reid, M.3    Lustigman, S.4
  • 52
    • 0023959619 scopus 로고
    • Receptor binding domain of glycophorin A for Plasmodium falciparum surface proteins
    • Davidson EA, Perkins ME, (1988) Receptor binding domain of glycophorin A for Plasmodium falciparum surface proteins. Indian J Biochem Biophys 25: 90-94.
    • (1988) Indian J Biochem Biophys , vol.25 , pp. 90-94
    • Davidson, E.A.1    Perkins, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.