메뉴 건너뛰기




Volumn 28, Issue 11, 2012, Pages 479-485

Host actin remodeling and protection from malaria by hemoglobinopathies

Author keywords

Actin remodeling; Cryo electrontomography; Cytoadhesion; Hemoglobinopathies; Malaria; Maurer's clefts; Protein trafficking

Indexed keywords

ACTIN; CD36 ANTIGEN; ERYTHROCYTE MEMBRANE PROTEIN 1; HEMOGLOBIN S;

EID: 84867870011     PISSN: 14714922     EISSN: 14715007     Source Type: Journal    
DOI: 10.1016/j.pt.2012.08.003     Document Type: Review
Times cited : (38)

References (57)
  • 1
    • 22544441601 scopus 로고    scopus 로고
    • How malaria has affected the human genome and what human genetics can teach us about malaria
    • Kwiatkowski D.P. How malaria has affected the human genome and what human genetics can teach us about malaria. Am. J. Hum. Genet. 2005, 77:171-192.
    • (2005) Am. J. Hum. Genet. , vol.77 , pp. 171-192
    • Kwiatkowski, D.P.1
  • 2
    • 34648815616 scopus 로고    scopus 로고
    • The ABO blood group system and Plasmodium falciparum malaria
    • Cserti C.M., Dzik W.H. The ABO blood group system and Plasmodium falciparum malaria. Blood 2007, 110:2250-2258.
    • (2007) Blood , vol.110 , pp. 2250-2258
    • Cserti, C.M.1    Dzik, W.H.2
  • 3
    • 84993770069 scopus 로고    scopus 로고
    • World Health Organization World Malaria Report 2010
    • World Health Organization
    • World Health Organization (2010) World Malaria Report 2010, World Health Organization.
    • (2010)
  • 4
    • 0037070775 scopus 로고    scopus 로고
    • Protective effects of the sickle cell gene against malaria morbidity and mortality
    • Aidoo M., et al. Protective effects of the sickle cell gene against malaria morbidity and mortality. Lancet 2002, 359:1311-1312.
    • (2002) Lancet , vol.359 , pp. 1311-1312
    • Aidoo, M.1
  • 6
    • 0035891266 scopus 로고    scopus 로고
    • Haemoglobin C protects against clinical Plasmodium falciparum malaria
    • Modiano D., et al. Haemoglobin C protects against clinical Plasmodium falciparum malaria. Nature 2001, 414:305-308.
    • (2001) Nature , vol.414 , pp. 305-308
    • Modiano, D.1
  • 7
    • 84861344450 scopus 로고    scopus 로고
    • Haemoglobinopathies and the clinical epidemiology of malaria: a systematic review and meta-analysis
    • Taylor S.M., et al. Haemoglobinopathies and the clinical epidemiology of malaria: a systematic review and meta-analysis. Lancet Infect. Dis. 2012, 12:457-468.
    • (2012) Lancet Infect. Dis. , vol.12 , pp. 457-468
    • Taylor, S.M.1
  • 8
    • 64749100258 scopus 로고    scopus 로고
    • Malaria parasite proteins that remodel the host erythrocyte
    • Maier A.G., et al. Malaria parasite proteins that remodel the host erythrocyte. Nat. Rev. Microbiol. 2009, 7:341-354.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 341-354
    • Maier, A.G.1
  • 9
    • 79957553908 scopus 로고    scopus 로고
    • Malaria parasite clag3 genes determine channel-mediated nutrient uptake by infected red blood cells
    • Nguitragool W., et al. Malaria parasite clag3 genes determine channel-mediated nutrient uptake by infected red blood cells. Cell 2011, 145:665-677.
    • (2011) Cell , vol.145 , pp. 665-677
    • Nguitragool, W.1
  • 10
    • 77955596444 scopus 로고    scopus 로고
    • Moving in and renovating: exporting proteins from Plasmodium into host erythrocytes
    • Goldberg D.E., Cowman A.F. Moving in and renovating: exporting proteins from Plasmodium into host erythrocytes. Nat. Rev. Microbiol. 2010, 8:617-621.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 617-621
    • Goldberg, D.E.1    Cowman, A.F.2
  • 11
    • 1642431673 scopus 로고    scopus 로고
    • Var genes, PfEMP1 and the human host
    • Flick K., Chen Q. var genes, PfEMP1 and the human host. Mol. Biochem. Parasitol. 2004, 134:3-9.
    • (2004) Mol. Biochem. Parasitol. , vol.134 , pp. 3-9
    • Flick, K.1    Chen, Q.2
  • 12
    • 84863836958 scopus 로고    scopus 로고
    • Abnormal PfEMP1/knob display on Plasmodium falciparum-infected erythrocytes containing hemoglobin variants: fresh insights into malaria pathogenesis and protection
    • Fairhurst R.M., et al. Abnormal PfEMP1/knob display on Plasmodium falciparum-infected erythrocytes containing hemoglobin variants: fresh insights into malaria pathogenesis and protection. Microbes Infect. 2012, 14:851-862.
    • (2012) Microbes Infect. , vol.14 , pp. 851-862
    • Fairhurst, R.M.1
  • 13
    • 84859105640 scopus 로고    scopus 로고
    • Cerebral malaria: what is known and what is on research
    • Gay F., et al. Cerebral malaria: what is known and what is on research. Rev. Neurol. (Paris) 2012, 168:239-256.
    • (2012) Rev. Neurol. (Paris) , vol.168 , pp. 239-256
    • Gay, F.1
  • 14
    • 0028046041 scopus 로고
    • An immunohistochemical study of the pathology of fatal malaria. Evidence for widespread endothelial activation and a potential role for intercellular adhesion molecule-1 in cerebral sequestration
    • Turner G.D., et al. An immunohistochemical study of the pathology of fatal malaria. Evidence for widespread endothelial activation and a potential role for intercellular adhesion molecule-1 in cerebral sequestration. Am. J. Pathol. 1994, 145:1057-1069.
    • (1994) Am. J. Pathol. , vol.145 , pp. 1057-1069
    • Turner, G.D.1
  • 15
    • 2642644550 scopus 로고    scopus 로고
    • Systemic endothelial activation occurs in both mild and severe malaria. Correlating dermal microvascular endothelial cell phenotype and soluble cell adhesion molecules with disease severity
    • Turner G.D., et al. Systemic endothelial activation occurs in both mild and severe malaria. Correlating dermal microvascular endothelial cell phenotype and soluble cell adhesion molecules with disease severity. Am. J. Pathol. 1998, 152:1477-1487.
    • (1998) Am. J. Pathol. , vol.152 , pp. 1477-1487
    • Turner, G.D.1
  • 16
    • 0018726630 scopus 로고
    • The role of hemoglobins C, S, and Nbalt in the inhibition of malaria parasite development in vitro
    • Friedman M.J., et al. The role of hemoglobins C, S, and Nbalt in the inhibition of malaria parasite development in vitro. Am. J. Trop. Med. Hyg. 1979, 28:777-780.
    • (1979) Am. J. Trop. Med. Hyg. , vol.28 , pp. 777-780
    • Friedman, M.J.1
  • 17
    • 38949087305 scopus 로고    scopus 로고
    • Impaired cytoadherence of Plasmodium falciparum-infected erythrocytes containing sickle hemoglobin
    • Cholera R., et al. Impaired cytoadherence of Plasmodium falciparum-infected erythrocytes containing sickle hemoglobin. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:991-996.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 991-996
    • Cholera, R.1
  • 18
    • 84862062566 scopus 로고    scopus 로고
    • α-Thalassemia impairs the cytoadherence of Plasmodium falciparum-infected erythrocytes
    • Krause M.A., et al. α-Thalassemia impairs the cytoadherence of Plasmodium falciparum-infected erythrocytes. PLoS ONE 2012, 7:e37214.
    • (2012) PLoS ONE , vol.7
    • Krause, M.A.1
  • 19
    • 21344463107 scopus 로고    scopus 로고
    • Abnormal display of PfEMP-1 on erythrocytes carrying haemoglobin C may protect against malaria
    • Fairhurst R.M., et al. Abnormal display of PfEMP-1 on erythrocytes carrying haemoglobin C may protect against malaria. Nature 2005, 435:1117-1121.
    • (2005) Nature , vol.435 , pp. 1117-1121
    • Fairhurst, R.M.1
  • 20
    • 82855184916 scopus 로고    scopus 로고
    • Hemoglobins S and C interfere with actin remodeling in Plasmodium falciparum-infected erythrocytes
    • Cyrklaff M., et al. Hemoglobins S and C interfere with actin remodeling in Plasmodium falciparum-infected erythrocytes. Science 2011, 334:1283-1286.
    • (2011) Science , vol.334 , pp. 1283-1286
    • Cyrklaff, M.1
  • 21
    • 0038281390 scopus 로고    scopus 로고
    • Aberrant development of Plasmodium falciparum in hemoglobin CC red cells: implications for the malaria protective effect of the homozygous state
    • Fairhurst R.M., et al. Aberrant development of Plasmodium falciparum in hemoglobin CC red cells: implications for the malaria protective effect of the homozygous state. Blood 2003, 101:3309-3315.
    • (2003) Blood , vol.101 , pp. 3309-3315
    • Fairhurst, R.M.1
  • 22
    • 84863296068 scopus 로고    scopus 로고
    • Plasmodium falciparum-induced CD36 clustering rapidly strengthens cytoadherence via p130CAS-mediated actin cytoskeletal rearrangement
    • Davis S.P., et al. Plasmodium falciparum-induced CD36 clustering rapidly strengthens cytoadherence via p130CAS-mediated actin cytoskeletal rearrangement. FASEB J. 2012, 26:1119-1130.
    • (2012) FASEB J. , vol.26 , pp. 1119-1130
    • Davis, S.P.1
  • 23
    • 34848909318 scopus 로고    scopus 로고
    • CD36 signals to the actin cytoskeleton and regulates microglial migration via a p130Cas complex
    • Stuart L.M., et al. CD36 signals to the actin cytoskeleton and regulates microglial migration via a p130Cas complex. J. Biol. Chem. 2007, 282:27392-27401.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27392-27401
    • Stuart, L.M.1
  • 24
    • 38449122179 scopus 로고    scopus 로고
    • Electron tomography of the Maurer's cleft organelles of Plasmodium falciparum-infected erythrocytes reveals novel structural features
    • Hanssen E., et al. Electron tomography of the Maurer's cleft organelles of Plasmodium falciparum-infected erythrocytes reveals novel structural features. Mol. Microbiol. 2008, 67:703-718.
    • (2008) Mol. Microbiol. , vol.67 , pp. 703-718
    • Hanssen, E.1
  • 25
    • 12344305982 scopus 로고    scopus 로고
    • Maurer's cleft organization in the cytoplasm of Plasmodium falciparum-infected erythrocytes: new insights from three-dimensional reconstruction of serial ultrathin sections
    • Wickert H., et al. Maurer's cleft organization in the cytoplasm of Plasmodium falciparum-infected erythrocytes: new insights from three-dimensional reconstruction of serial ultrathin sections. Eur. J. Cell Biol. 2004, 83:567-582.
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 567-582
    • Wickert, H.1
  • 26
    • 68049100010 scopus 로고    scopus 로고
    • 3-D analysis of the Plasmodium falciparum Maurer's clefts using different electron tomographic approaches
    • Henrich P., et al. 3-D analysis of the Plasmodium falciparum Maurer's clefts using different electron tomographic approaches. Biotechnol. J. 2009, 4:888-894.
    • (2009) Biotechnol. J. , vol.4 , pp. 888-894
    • Henrich, P.1
  • 27
    • 30044443910 scopus 로고    scopus 로고
    • Maurer's clefts: a novel multi-functional organelle in the cytoplasm of Plasmodium falciparum-infected erythrocytes
    • Lanzer M., et al. Maurer's clefts: a novel multi-functional organelle in the cytoplasm of Plasmodium falciparum-infected erythrocytes. Int. J. Parasitol. 2006, 36:23-36.
    • (2006) Int. J. Parasitol. , vol.36 , pp. 23-36
    • Lanzer, M.1
  • 28
    • 0038048449 scopus 로고    scopus 로고
    • Evidence for trafficking of PfEMP1 to the surface of P. falciparum-infected erythrocytes via a complex membrane network
    • Wickert H., et al. Evidence for trafficking of PfEMP1 to the surface of P. falciparum-infected erythrocytes via a complex membrane network. Eur. J. Cell Biol. 2003, 82:271-284.
    • (2003) Eur. J. Cell Biol. , vol.82 , pp. 271-284
    • Wickert, H.1
  • 29
    • 0142008046 scopus 로고    scopus 로고
    • Generation of an erythrocyte vesicle transport system by Plasmodium falciparum malaria parasites
    • Taraschi T.F., et al. Generation of an erythrocyte vesicle transport system by Plasmodium falciparum malaria parasites. Blood 2003, 102:3420-3426.
    • (2003) Blood , vol.102 , pp. 3420-3426
    • Taraschi, T.F.1
  • 30
    • 0033982042 scopus 로고    scopus 로고
    • Evidence for vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in Plasmodium falciparum infected erythrocytes
    • Trelka D.P., et al. Evidence for vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in Plasmodium falciparum infected erythrocytes. Mol. Biochem. Parasitol. 2000, 106:131-145.
    • (2000) Mol. Biochem. Parasitol. , vol.106 , pp. 131-145
    • Trelka, D.P.1
  • 31
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard T.D., Cooper J.A. Actin, a central player in cell shape and movement. Science 2009, 326:1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 32
    • 79251565514 scopus 로고    scopus 로고
    • Development and host cell modifications of Plasmodium falciparum blood stages in four dimensions
    • Gruring C., et al. Development and host cell modifications of Plasmodium falciparum blood stages in four dimensions. Nat. Commun. 2011, 2:165.
    • (2011) Nat. Commun. , vol.2 , pp. 165
    • Gruring, C.1
  • 33
    • 42049115740 scopus 로고    scopus 로고
    • Disorders of red cell membrane
    • An X., Mohandas N. Disorders of red cell membrane. Br. J. Haematol. 2008, 141:367-375.
    • (2008) Br. J. Haematol. , vol.141 , pp. 367-375
    • An, X.1    Mohandas, N.2
  • 34
    • 0023430419 scopus 로고
    • Plasmodium falciparum: fine structural changes in the cytoskeletons of infected erythrocytes
    • Taylor D.W., et al. Plasmodium falciparum: fine structural changes in the cytoskeletons of infected erythrocytes. Exp. Parasitol. 1987, 64:178-187.
    • (1987) Exp. Parasitol. , vol.64 , pp. 178-187
    • Taylor, D.W.1
  • 35
    • 77649273767 scopus 로고    scopus 로고
    • Interaction of the exported malaria protein Pf332 with the red blood cell membrane skeleton
    • Waller K.L., et al. Interaction of the exported malaria protein Pf332 with the red blood cell membrane skeleton. Biochim. Biophys. Acta 2010, 1798:861-871.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 861-871
    • Waller, K.L.1
  • 36
    • 0034105159 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte membrane protein 1 is anchored to the actin-spectrin junction and knob-associated histidine-rich protein in the erythrocyte skeleton
    • Oh S.S., et al. Plasmodium falciparum erythrocyte membrane protein 1 is anchored to the actin-spectrin junction and knob-associated histidine-rich protein in the erythrocyte skeleton. Mol. Biochem. Parasitol. 2000, 108:237-247.
    • (2000) Mol. Biochem. Parasitol. , vol.108 , pp. 237-247
    • Oh, S.S.1
  • 37
    • 59649117682 scopus 로고    scopus 로고
    • Functional alteration of red blood cells by a megadalton protein of Plasmodium falciparum
    • Glenister F.K., et al. Functional alteration of red blood cells by a megadalton protein of Plasmodium falciparum. Blood 2009, 113:919-928.
    • (2009) Blood , vol.113 , pp. 919-928
    • Glenister, F.K.1
  • 38
    • 0025960553 scopus 로고
    • Selective association of a fragment of the knob protein with spectrin, actin and the red cell membrane
    • Kilejian A., et al. Selective association of a fragment of the knob protein with spectrin, actin and the red cell membrane. Mol. Biochem. Parasitol. 1991, 44:175-181.
    • (1991) Mol. Biochem. Parasitol. , vol.44 , pp. 175-181
    • Kilejian, A.1
  • 39
    • 0034670103 scopus 로고    scopus 로고
    • Plasmodium falciparum histidine-rich protein 1 associates with the band 3 binding domain of ankyrin in the infected red cell membrane
    • Magowan C., et al. Plasmodium falciparum histidine-rich protein 1 associates with the band 3 binding domain of ankyrin in the infected red cell membrane. Biochim. Biophys. Acta 2000, 1502:461-470.
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 461-470
    • Magowan, C.1
  • 40
    • 24744459649 scopus 로고    scopus 로고
    • Structural and functional studies of interaction between Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) and erythrocyte spectrin
    • Pei X., et al. Structural and functional studies of interaction between Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) and erythrocyte spectrin. J. Biol. Chem. 2005, 280:31166-31171.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31166-31171
    • Pei, X.1
  • 41
    • 34548507477 scopus 로고    scopus 로고
    • Interactions of Plasmodium falciparum erythrocyte membrane protein 3 with the red blood cell membrane skeleton
    • Waller K.L., et al. Interactions of Plasmodium falciparum erythrocyte membrane protein 3 with the red blood cell membrane skeleton. Biochim. Biophys. Acta 2007, 1768:2145-2156.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2145-2156
    • Waller, K.L.1
  • 42
    • 34848884573 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) destabilizes erythrocyte membrane skeleton
    • Pei X., et al. Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) destabilizes erythrocyte membrane skeleton. J. Biol. Chem. 2007, 282:26754-26758.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26754-26758
    • Pei, X.1
  • 43
    • 0030906683 scopus 로고    scopus 로고
    • Defining the minimal domain of the Plasmodium falciparum protein MESA involved in the interaction with the red cell membrane skeletal protein 4.1
    • Bennett B.J., et al. Defining the minimal domain of the Plasmodium falciparum protein MESA involved in the interaction with the red cell membrane skeletal protein 4.1. J. Biol. Chem. 1997, 272:15299-15306.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15299-15306
    • Bennett, B.J.1
  • 44
    • 0041940227 scopus 로고    scopus 로고
    • Mature parasite-infected erythrocyte surface antigen (MESA) of Plasmodium falciparum binds to the 30-kDa domain of protein 4.1 in malaria-infected red blood cells
    • Waller K.L., et al. Mature parasite-infected erythrocyte surface antigen (MESA) of Plasmodium falciparum binds to the 30-kDa domain of protein 4.1 in malaria-infected red blood cells. Blood 2003, 102:1911-1914.
    • (2003) Blood , vol.102 , pp. 1911-1914
    • Waller, K.L.1
  • 45
    • 0028035118 scopus 로고
    • Plasmodium falciparum: mapping the membrane-binding domain in the ring-infected erythrocyte surface antigen
    • Foley M., et al. Plasmodium falciparum: mapping the membrane-binding domain in the ring-infected erythrocyte surface antigen. Exp. Parasitol. 1994, 79:340-350.
    • (1994) Exp. Parasitol. , vol.79 , pp. 340-350
    • Foley, M.1
  • 46
    • 34547959977 scopus 로고    scopus 로고
    • The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion
    • Pei X., et al. The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion. Blood 2007, 110:1036-1042.
    • (2007) Blood , vol.110 , pp. 1036-1042
    • Pei, X.1
  • 47
    • 46149093701 scopus 로고    scopus 로고
    • Exported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytes
    • Maier A.G., et al. Exported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytes. Cell 2008, 134:48-61.
    • (2008) Cell , vol.134 , pp. 48-61
    • Maier, A.G.1
  • 48
    • 0345682080 scopus 로고
    • Quantitative studies of ferritinlike iron in erythrocytes of thalassemia, sickle-cell anemia, and hemoglobin Hammersmith with Mossbauer spectroscopy
    • Bauminger E.R., et al. Quantitative studies of ferritinlike iron in erythrocytes of thalassemia, sickle-cell anemia, and hemoglobin Hammersmith with Mossbauer spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 1979, 76:939-943.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 939-943
    • Bauminger, E.R.1
  • 49
    • 55949098500 scopus 로고    scopus 로고
    • Oxidative process in erythrocytes of individuals with hemoglobin S
    • Chaves M.A., et al. Oxidative process in erythrocytes of individuals with hemoglobin S. Hematology 2008, 13:187-192.
    • (2008) Hematology , vol.13 , pp. 187-192
    • Chaves, M.A.1
  • 50
    • 0026099699 scopus 로고
    • Beyond hemoglobin polymerization: the red blood cell membrane and sickle disease pathophysiology
    • Hebbel R.P. Beyond hemoglobin polymerization: the red blood cell membrane and sickle disease pathophysiology. Blood 1991, 77:214-237.
    • (1991) Blood , vol.77 , pp. 214-237
    • Hebbel, R.P.1
  • 51
    • 0025242925 scopus 로고
    • Effect of hemoglobin oxidation products on the stability of red cell membrane skeletons and the associations of skeletal proteins: correlation with a release of hemin
    • Jarolim P., et al. Effect of hemoglobin oxidation products on the stability of red cell membrane skeletons and the associations of skeletal proteins: correlation with a release of hemin. Blood 1990, 76:2125-2131.
    • (1990) Blood , vol.76 , pp. 2125-2131
    • Jarolim, P.1
  • 52
    • 79959351431 scopus 로고    scopus 로고
    • Diverse protective roles of the actin cytoskeleton during oxidative stress
    • Farah M.E., et al. Diverse protective roles of the actin cytoskeleton during oxidative stress. Cytoskeleton (Hoboken) 2011, 68:340-354.
    • (2011) Cytoskeleton (Hoboken) , vol.68 , pp. 340-354
    • Farah, M.E.1
  • 53
    • 16844378031 scopus 로고    scopus 로고
    • Band 3 modifications in Plasmodium falciparum-infected AA and CC erythrocytes assayed by autocorrelation analysis using quantum dots
    • Tokumasu F., et al. Band 3 modifications in Plasmodium falciparum-infected AA and CC erythrocytes assayed by autocorrelation analysis using quantum dots. J. Cell Sci. 2005, 118:1091-1098.
    • (2005) J. Cell Sci. , vol.118 , pp. 1091-1098
    • Tokumasu, F.1
  • 54
    • 78650293510 scopus 로고    scopus 로고
    • Reorganization of the host cytoskeleton by the intracellular pathogen Chlamydia trachomatis
    • Kumar Y., Valdivia R.H. Reorganization of the host cytoskeleton by the intracellular pathogen Chlamydia trachomatis. Commun. Integr. Biol. 2008, 1:175-177.
    • (2008) Commun. Integr. Biol. , vol.1 , pp. 175-177
    • Kumar, Y.1    Valdivia, R.H.2
  • 55
    • 81255136861 scopus 로고    scopus 로고
    • A glance at Listeria and Salmonella cell invasion: different strategies to promote host actin polymerization
    • da Silva C.V., et al. A glance at Listeria and Salmonella cell invasion: different strategies to promote host actin polymerization. Int. J. Med. Microbiol. 2012, 302:19-32.
    • (2012) Int. J. Med. Microbiol. , vol.302 , pp. 19-32
    • da Silva, C.V.1
  • 56
    • 77958507493 scopus 로고    scopus 로고
    • Quantitative analysis of actin turnover in Listeria comet tails: evidence for catastrophic filament turnover
    • Kueh H.Y., et al. Quantitative analysis of actin turnover in Listeria comet tails: evidence for catastrophic filament turnover. Biophys. J. 2010, 99:2153-2162.
    • (2010) Biophys. J. , vol.99 , pp. 2153-2162
    • Kueh, H.Y.1
  • 57
    • 84855461427 scopus 로고    scopus 로고
    • Highly dynamic host actin reorganization around developing Plasmodium inside hepatocytes
    • Gomes-Santos C.S., et al. Highly dynamic host actin reorganization around developing Plasmodium inside hepatocytes. PLoS ONE 2012, 7:e29408.
    • (2012) PLoS ONE , vol.7
    • Gomes-Santos, C.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.