메뉴 건너뛰기




Volumn 6, Issue 7, 2015, Pages 795-826

Delivery of drugs bound to erythrocytes: New avenues for an old intravascular carrier

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT; DRUG CARRIER; ERYTHROCYTE BAND 3 PROTEIN; GLUCOSE TRANSPORTER 1; GLYCOPHORIN; HYBRID PROTEIN; NANOPARTICLE; RHESUS D ANTIBODY; DRUG; LIGAND; MACROGOL DERIVATIVE; MEMBRANE PROTEIN; PROTEIN BINDING;

EID: 84938393719     PISSN: 20415990     EISSN: 20416008     Source Type: Journal    
DOI: 10.4155/tde.15.34     Document Type: Review
Times cited : (99)

References (305)
  • 1
    • 0017388651 scopus 로고
    • Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase
    • Abuchowski A, McCoy JR, Palczuk NC, van Es T, Davis FF. Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase. J. Biol. Chem. 252(11), 3582-3586 (1977).
    • (1977) J. Biol. Chem. , vol.252 , Issue.11 , pp. 3582-3586
    • Abuchowski, A.1    Mccoy, J.R.2    Palczuk, N.C.3    Van Es, T.4    Davis, F.F.5
  • 2
    • 2942588977 scopus 로고    scopus 로고
    • Human red blood cells: Rheological aspects, uptake, and release of cytotoxic drugs
    • Dumez H, Reinhart WH, Guetens G, de Bruijn EA. Human red blood cells: rheological aspects, uptake, and release of cytotoxic drugs. Crit. Rev. Clin. Lab. Sci. 41(2), 159-188 (2004).
    • (2004) Crit. Rev. Clin. Lab. Sci. , vol.41 , Issue.2 , pp. 159-188
    • Dumez, H.1    Reinhart, W.H.2    Guetens, G.3    De Bruijn, E.A.4
  • 3
    • 0026063037 scopus 로고
    • Blood-brain barrier glucose transporter is asymmetrically distributed on brain capillary endothelial lumenal and ablumenal membranes: An electron microscopic immunogold study
    • Farrell CL, Pardridge WM. Blood-brain barrier glucose transporter is asymmetrically distributed on brain capillary endothelial lumenal and ablumenal membranes: an electron microscopic immunogold study. Proc. Natl Acad. Sci. USA 88(13), 5779-5783 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , Issue.13 , pp. 5779-5783
    • Farrell, C.L.1    Pardridge, W.M.2
  • 4
    • 0032951946 scopus 로고    scopus 로고
    • Effects of barbiturates on facilitative glucose transporters are pharmacologically specific and isoform selective
    • Haspel HC, Stephenson KN, Davies-Hill T et al. Effects of barbiturates on facilitative glucose transporters are pharmacologically specific and isoform selective. J. Membr. Biol. 169(1), 45-53 (1999).
    • (1999) J. Membr. Biol. , vol.169 , Issue.1 , pp. 45-53
    • Haspel, H.C.1    Stephenson, K.N.2    Davies-Hill, T.3
  • 5
    • 84861406720 scopus 로고    scopus 로고
    • Nanoscale drug delivery systems for enhanced drug penetration into solid tumors: Current progress and opportunities
    • Waite CL, Roth CM. Nanoscale drug delivery systems for enhanced drug penetration into solid tumors: current progress and opportunities. Crit. Rev. Biomed. Eng. 40(1), 21-41 (2012).
    • (2012) Crit. Rev. Biomed. Eng. , vol.40 , Issue.1 , pp. 21-41
    • Waite, C.L.1    Roth, C.M.2
  • 6
    • 11144223212 scopus 로고    scopus 로고
    • Glut-1 deficiency syndrome: Clinical, genetic, and therapeutic aspects
    • Wang D, Pascual JM, Yang H et al. Glut-1 deficiency syndrome: clinical, genetic, and therapeutic aspects. Ann. Neurol. 57(1), 111-118 (2005).
    • (2005) Ann. Neurol. , vol.57 , Issue.1 , pp. 111-118
    • Wang, D.1    Pascual, J.M.2    Yang, H.3
  • 7
    • 84255194777 scopus 로고    scopus 로고
    • Glut1 deficiency syndrome and erythrocyte glucose uptake assay
    • Yang H, Wang D, Engelstad K et al. Glut1 deficiency syndrome and erythrocyte glucose uptake assay. Ann. Neurol. 70(6), 996-1005 (2011).
    • (2011) Ann. Neurol. , vol.70 , Issue.6 , pp. 996-1005
    • Yang, H.1    Wang, D.2    Engelstad, K.3
  • 8
    • 77949673546 scopus 로고    scopus 로고
    • Signaling, delivery and age as emerging issues in the benefit/risk ratio outcome of TPA for treatment of CNS ischemic disorders
    • Armstead WM, Ganguly K, Kiessling JW et al. Signaling, delivery and age as emerging issues in the benefit/risk ratio outcome of tPA For treatment of CNS ischemic disorders. J. Neurochem. 113(2), 303-312 (2010).
    • (2010) J. Neurochem. , vol.113 , Issue.2 , pp. 303-312
    • Armstead, W.M.1    Ganguly, K.2    Kiessling, J.W.3
  • 9
    • 16844364343 scopus 로고    scopus 로고
    • Thrombolytic agents
    • Collen D, Lijnen HR. Thrombolytic agents. Thromb. Haemost. 93(4), 627-630 (2005).
    • (2005) Thromb. Haemost , vol.93 , Issue.4 , pp. 627-630
    • Collen, D.1    Lijnen, H.R.2
  • 10
    • 61849153021 scopus 로고    scopus 로고
    • Impact of nanotechnology on drug delivery
    • Farokhzad OC, Langer R. Impact of nanotechnology on drug delivery. ACS Nano 3(1), 16-20 (2009).
    • (2009) ACS Nano , vol.3 , Issue.1 , pp. 16-20
    • Farokhzad, O.C.1    Langer, R.2
  • 11
    • 48349116380 scopus 로고    scopus 로고
    • Control of endothelial targeting and intracellular delivery of therapeutic enzymes by modulating the size and shape of ICAM-1-targeted carriers
    • Muro S, Garnacho C, Champion JA et al. Control of endothelial targeting and intracellular delivery of therapeutic enzymes by modulating the size and shape of ICAM-1-targeted carriers. Mol. Ther. J. Am. Soc. Gene Ther. 16(8), 1450-1458 (2008).
    • (2008) Mol. Ther. J. Am. Soc. Gene Ther. , vol.16 , Issue.8 , pp. 1450-1458
    • Muro, S.1    Garnacho, C.2    Champion, J.A.3
  • 12
    • 0142209155 scopus 로고    scopus 로고
    • Thrombolysis: Newer thrombolytic agents and their role in clinical medicine
    • Nordt TK, Bode C. Thrombolysis: newer thrombolytic agents and their role in clinical medicine. Heart Br. Card. Soc. 89(11), 1358-1362 (2003).
    • (2003) Heart Br. Card. Soc. , vol.89 , Issue.11 , pp. 1358-1362
    • Nordt, T.K.1    Bode, C.2
  • 13
    • 77955175216 scopus 로고    scopus 로고
    • Strategies in the design of nanoparticles for therapeutic applications
    • Petros RA, DeSimone JM. Strategies in the design of nanoparticles for therapeutic applications. Nat. Rev. Drug Discov. 9(8), 615-627 (2010).
    • (2010) Nat. Rev. Drug Discov. , vol.9 , Issue.8 , pp. 615-627
    • Petros, R.A.1    DeSimone, J.M.2
  • 14
    • 80053303931 scopus 로고    scopus 로고
    • Endothelial targeting of antibody-decorated polymeric filomicelles
    • Shuvaev VV, Ilies MA, Simone E et al. Endothelial targeting of antibody-decorated polymeric filomicelles. ACS Nano 5(9), 6991-6999 (2011).
    • (2011) ACS Nano , vol.5 , Issue.9 , pp. 6991-6999
    • Shuvaev, V.V.1    Ilies, M.A.2    Simone, E.3
  • 15
    • 84855690182 scopus 로고    scopus 로고
    • Erythrocytes as carriers for drugs: The transition from the laboratory to the clinic is approaching
    • Magnani M. Erythrocytes as carriers for drugs: the transition from the laboratory to the clinic is approaching. Expert Opin. Biol. Ther. 12(2), 137-138 (2012).
    • (2012) Expert Opin. Biol. Ther. , vol.12 , Issue.2 , pp. 137-138
    • Magnani, M.1
  • 16
    • 77949878932 scopus 로고    scopus 로고
    • Drug delivery by red blood cells: Vascular carriers designed by mother nature
    • Muzykantov VR. Drug delivery by red blood cells: vascular carriers designed by mother nature. Expert Opin. Drug Deliv. 7(4), 403-427 (2010).
    • (2010) Expert Opin. Drug Deliv. , vol.7 , Issue.4 , pp. 403-427
    • Muzykantov, V.R.1
  • 17
    • 0026594781 scopus 로고
    • Thromboerythrocytes. in vitro studies of a potential autologous, semi-artificial alternative to platelet transfusions
    • Coller BS, Springer KT, Beer JH et al. Thromboerythrocytes. In vitro studies of a potential autologous, semi-artificial alternative to platelet transfusions. J. Clin. Invest. 89(2), 546-555 (1992).
    • (1992) J. Clin. Invest. , vol.89 , Issue.2 , pp. 546-555
    • Coller, B.S.1    Springer, K.T.2    Beer, J.H.3
  • 18
    • 2642606351 scopus 로고
    • Incorporation of glucocerebrosidase into Gaucher's disease monocytes in vitro
    • Dale GL, Kuhl W, Beutler E. Incorporation of glucocerebrosidase into Gaucher's disease monocytes in vitro. Proc. Natl Acad. Sci. USA 76(1), 473-475 (1979).
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , Issue.1 , pp. 473-475
    • Dale, G.L.1    Kuhl, W.2    Beutler, E.3
  • 22
    • 0342526720 scopus 로고    scopus 로고
    • Heterogeneity of hypotonically loaded rat erythrocyte populations as detected by countercurrent distribution in aqueous polymer two-phase systems
    • Pérez MT, Alvarez FJ, García-Pérez AI, Lucas L, Tejedor MC, Sancho P. Heterogeneity of hypotonically loaded rat erythrocyte populations as detected by countercurrent distribution in aqueous polymer two-phase systems. J. Chromatogr. B Biomed. Appl. 677(1), 45-51 (1996).
    • (1996) J. Chromatogr. B Biomed. Appl. , vol.677 , Issue.1 , pp. 45-51
    • Pérez, M.T.1    Alvarez, F.J.2    García-Pérez, A.I.3    Lucas, L.4    Tejedor, M.C.5    Sancho, P.6
  • 23
    • 0027104487 scopus 로고
    • Immunological response to L-asparaginase loaded into red blood cells
    • Ktavtzoff R, Desbois I, Doinel C et al. Immunological response to L-asparaginase loaded into red blood cells. Adv. Exp. Med. Biol. 326, 175-182 (1992).
    • (1992) Adv. Exp. Med. Biol. , vol.326 , pp. 175-182
    • Ktavtzoff, R.1    Desbois, I.2    Doinel, C.3
  • 24
    • 0034986978 scopus 로고    scopus 로고
    • Erythrocytemediated delivery of a new homodinucleotide active against human immunodeficiency virus and herpes simplex virus
    • Rossi L, Serafini S, Cappellacci L et al. Erythrocytemediated delivery of a new homodinucleotide active against human immunodeficiency virus and herpes simplex virus. J. Antimicrob. Chemother. 47(6), 819-827 (2001).
    • (2001) J. Antimicrob. Chemother , vol.47 , Issue.6 , pp. 819-827
    • Rossi, L.1    Serafini, S.2    Cappellacci, L.3
  • 25
    • 0025635979 scopus 로고
    • Construction and characterization of adriamycin-loaded canine red blood cells as a potential slow delivery system
    • Tonetti M, Astroff B, Satterfield W, De Flora A, Benatti U, DeLoach JR. Construction and characterization of adriamycin-loaded canine red blood cells as a potential slow delivery system. Biotechnol. Appl. Biochem. 12(6), 621-629 (1990).
    • (1990) Biotechnol. Appl. Biochem. , vol.12 , Issue.6 , pp. 621-629
    • Tonetti, M.1    Astroff, B.2    Satterfield, W.3    De Flora, A.4    Benatti, U.5    DeLoach, J.R.6
  • 26
    • 57549118342 scopus 로고    scopus 로고
    • Opsonized erythrocyte ghosts for liver-targeted delivery of antisense oligodeoxynucleotides
    • Kim S-H, Kim E-J, Hou J-H et al. Opsonized erythrocyte ghosts for liver-targeted delivery of antisense oligodeoxynucleotides. Biomaterials 30(5), 959-967 (2009).
    • (2009) Biomaterials , vol.30 , Issue.5 , pp. 959-967
    • Kim, S.-H.1    Kim, E.-J.2    Hou, J.-H.3
  • 27
    • 0023432973 scopus 로고
    • Long-term physiological effects of enhanced O2 release by inositol hexaphosphate-loaded erythrocytes
    • Teisseire B, Ropars C, Villeréal MC, Nicolau C. Long-term physiological effects of enhanced O2 release by inositol hexaphosphate-loaded erythrocytes. Proc. Natl Acad. Sci. USA 84(19), 6894-6898 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , Issue.19 , pp. 6894-6898
    • Teisseire, B.1    Ropars, C.2    Villeréal, M.C.3    Nicolau, C.4
  • 28
    • 0034044058 scopus 로고    scopus 로고
    • Vitro and in vivo studies with human carrier erythrocytes loaded with polyethylene glycol-conjugated and native adenosine deaminase
    • Bax BE, Bain MD, Fairbanks LD, Webster AD, Chalmers RA. In vitro and in vivo studies with human carrier erythrocytes loaded with polyethylene glycol-conjugated and native adenosine deaminase. Br. J. Haematol. 109(3), 549-554 (2000).
    • (2000) Br. J. Haematol. , vol.109 , Issue.3 , pp. 549-554
    • Bax, B.E.1    Bain, M.D.2    Fairbanks, L.D.3    Webster, A.D.4    Chalmers, R.A.5
  • 30
    • 0345768477 scopus 로고    scopus 로고
    • Tolerance evaluation of L-asparaginase loaded in red blood cells
    • Kravtzoff R, Colombat PH, Desbois I et al. Tolerance evaluation of L-asparaginase loaded in red blood cells. Eur. J. Clin. Pharmacol. 51(3-4), 221-225 (1996).
    • (1996) Eur. J. Clin. Pharmacol. , vol.51 , Issue.3-4 , pp. 221-225
    • Kravtzoff, R.1    Colombat, P.H.2    Desbois, I.3
  • 31
    • 0029995124 scopus 로고    scopus 로고
    • Improved pharmacodynamics of L-asparaginase-loaded in human red blood cells
    • Kravtzoff R, Desbois I, Lamagnere JP et al. Improved pharmacodynamics of L-asparaginase-loaded in human red blood cells. Eur. J. Clin. Pharmacol. 49(6), 465-470 (1996).
    • (1996) Eur. J. Clin. Pharmacol , vol.49 , Issue.6 , pp. 465-470
    • Kravtzoff, R.1    Desbois, I.2    Lamagnere, J.P.3
  • 32
    • 33847314729 scopus 로고    scopus 로고
    • Applications of carrier erythrocytes in delivery of biopharmaceuticals
    • Hamidi M, Zarrin A, Foroozesh M, Mohammadi-Samani S. Applications of carrier erythrocytes in delivery of biopharmaceuticals. J. Control. Release 118(2), 145-160 (2007).
    • (2007) J. Control. Release , vol.118 , Issue.2 , pp. 145-160
    • Hamidi, M.1    Zarrin, A.2    Foroozesh, M.3    Mohammadi-Samani, S.4
  • 33
    • 0030878357 scopus 로고    scopus 로고
    • Red cell-mediated therapy: Opportunities and challenges
    • Krantz A. Red cell-mediated therapy: opportunities and challenges. Blood Cells Mol. Dis. 23(1), 58-68 (1997).
    • (1997) Blood Cells Mol. Dis. , vol.23 , Issue.1 , pp. 58-68
    • Krantz, A.1
  • 34
    • 39449126839 scopus 로고    scopus 로고
    • Drug loaded erythrocytes: As novel drug delivery system
    • Patel PD, Dand N, Hirlekar RS, Kadam VJ. Drug loaded erythrocytes: as novel drug delivery system. Curr. Pharm. Des. 14(1), 63-70 (2008).
    • (2008) Curr. Pharm. Des. , vol.14 , Issue.1 , pp. 63-70
    • Patel, P.D.1    Dand, N.2    Hirlekar, R.S.3    Kadam, V.J.4
  • 37
    • 34548593279 scopus 로고    scopus 로고
    • A 9-yr evaluation of carrier erythrocyte encapsulated adenosine deaminase (ADA) therapy in a patient with adult-type ADA deficiency
    • Bax BE, Bain MD, Fairbanks LD et al. A 9-yr evaluation of carrier erythrocyte encapsulated adenosine deaminase (ADA) therapy in a patient with adult-type ADA deficiency. Eur. J. Haematol. 79(4), 338-348 (2007).
    • (2007) Eur. J. Haematol. , vol.79 , Issue.4 , pp. 338-348
    • Bax, B.E.1    Bain, M.D.2    Fairbanks, L.D.3
  • 38
    • 84888316673 scopus 로고    scopus 로고
    • Clinical and biochemical improvements in a patient with MNGIE following enzyme replacement
    • Bax BE, Bain MD, Scarpelli M, Filosto M, Tonin P, Moran N. Clinical and biochemical improvements in a patient with MNGIE following enzyme replacement. Neurology 81(14), 1269-1271 (2013).
    • (2013) Neurology , vol.81 , Issue.14 , pp. 1269-1271
    • Bax, B.E.1    Bain, M.D.2    Scarpelli, M.3    Filosto, M.4    Tonin, P.5    Moran, N.6
  • 39
    • 84055193022 scopus 로고    scopus 로고
    • International seminar on the red blood cells as vehicles for drugs
    • Godfrin Y, Horand F, Franco R et al. International seminar on the red blood cells as vehicles for drugs. Expert Opin. Biol. Ther. 12(1), 127-133 (2012).
    • (2012) Expert Opin. Biol. Ther. , vol.12 , Issue.1 , pp. 127-133
    • Godfrin, Y.1    Horand, F.2    Franco, R.3
  • 40
    • 79952607367 scopus 로고    scopus 로고
    • L-asparaginase loaded red blood cells in refractory or relapsing acute lymphoblastic leukaemia in children and adults: Results of the graspall 2005-01 randomized trial
    • Domenech C, Thomas X, Chabaud S et al. l-asparaginase loaded red blood cells in refractory or relapsing acute lymphoblastic leukaemia in children and adults: results of the GRASPALL 2005-01 randomized trial. Br. J. Haematol. 153(1), 58-65 (2011).
    • (2011) Br. J. Haematol. , vol.153 , Issue.1 , pp. 58-65
    • Domenech, C.1    Thomas, X.2    Chabaud, S.3
  • 41
    • 53149124013 scopus 로고    scopus 로고
    • Erythrocyte-mediated delivery of dexamethasone in patients with mild-tomoderate ulcerative colitis, refractory to mesalamine: A randomized, controlled study
    • Bossa F, Latiano A, Rossi L et al. Erythrocyte-mediated delivery of dexamethasone in patients with mild-tomoderate ulcerative colitis, refractory to mesalamine: a randomized, controlled study. Am. J. Gastroenterol. 103(10), 2509-2516 (2008).
    • (2008) Am. J. Gastroenterol. , vol.103 , Issue.10 , pp. 2509-2516
    • Bossa, F.1    Latiano, A.2    Rossi, L.3
  • 42
    • 84884606301 scopus 로고    scopus 로고
    • Erythrocytesmediated delivery of dexamethasone 21-phosphate in steroid-dependent ulcerative colitis: A randomized, doubleblind Sham-controlled study
    • Bossa F, Annese V, Valvano MR et al. Erythrocytesmediated delivery of dexamethasone 21-phosphate in steroid-dependent ulcerative colitis: a randomized, doubleblind Sham-controlled study. Inflamm. Bowel Dis. 19(9), 1872-1879 (2013).
    • (2013) Inflamm. Bowel Dis. , vol.19 , Issue.9 , pp. 1872-1879
    • Bossa, F.1    Annese, V.2    Valvano, M.R.3
  • 43
    • 58149158216 scopus 로고    scopus 로고
    • Red cell membrane: Past, present, and future
    • Mohandas N, Gallagher PG. Red cell membrane: past, present, and future. Blood 112(10), 3939-3948 (2008).
    • (2008) Blood , vol.112 , Issue.10 , pp. 3939-3948
    • Mohandas, N.1    Gallagher, P.G.2
  • 44
    • 84907030234 scopus 로고    scopus 로고
    • The relationship between red blood cell deformability metrics and perfusion of an artificial microvascular network
    • Sosa JM, Nielsen ND, Vignes SM, Chen TG, Shevkoplyas SS. The relationship between red blood cell deformability metrics and perfusion of an artificial microvascular network. Clin. Hemorheol. Microcirc. 57(3), 275-289 (2013).
    • (2013) Clin. Hemorheol. Microcirc. , vol.57 , Issue.3 , pp. 275-289
    • Sosa, J.M.1    Nielsen, N.D.2    Vignes, S.M.3    Chen, T.G.4    Shevkoplyas, S.S.5
  • 45
    • 33846664696 scopus 로고    scopus 로고
    • Physiology and pathophysiology of heme: Implications for kidney disease
    • Tracz MJ, Alam J, Nath KA. Physiology and pathophysiology of heme: implications for kidney disease. J. Am. Soc. Nephrol. 18(2), 414-420 (2007).
    • (2007) J. Am. Soc. Nephrol. , vol.18 , Issue.2 , pp. 414-420
    • Tracz, M.J.1    Alam, J.2    Nath, K.A.3
  • 46
    • 84874439878 scopus 로고    scopus 로고
    • Hemolysis and free hemoglobin revisited: Exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins
    • Schaer DJ, Buehler PW, Alayash AI, Belcher JD, Vercellotti GM. Hemolysis and free hemoglobin revisited: exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins. Blood 121(8), 1276-1284 (2013).
    • (2013) Blood , vol.121 , Issue.8 , pp. 1276-1284
    • Schaer, D.J.1    Buehler, P.W.2    Alayash, A.I.3    Belcher, J.D.4    Vercellotti, G.M.5
  • 48
    • 33746616420 scopus 로고    scopus 로고
    • In-depth analysis of the membrane and cytosolic proteome of red blood cells
    • Pasini EM, Kirkegaard M, Mortensen P, Lutz HU, Thomas AW, Mann M. In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood 108(3), 791-801 (2006).
    • (2006) Blood , vol.108 , Issue.3 , pp. 791-801
    • Pasini, E.M.1    Kirkegaard, M.2    Mortensen, P.3    Lutz, H.U.4    Thomas, A.W.5    Mann, M.6
  • 49
    • 33845243747 scopus 로고    scopus 로고
    • Rac GT pases regulate the morphology and deformability of the erythrocyte cytoskeleton
    • Kalfa TA, Pushkaran S, Mohandas N et al. Rac GTPases regulate the morphology and deformability of the erythrocyte cytoskeleton. Blood 108(12), 3637-3645 (2006).
    • (2006) Blood , vol.108 , Issue.12 , pp. 3637-3645
    • Kalfa, T.A.1    Pushkaran, S.2    Mohandas, N.3
  • 50
    • 0029797605 scopus 로고    scopus 로고
    • Identification of distinct luminal domains for macromolecules, erythrocytes, and leukocytes within mammalian capillaries
    • Vink H, Duling BR. Identification of distinct luminal domains for macromolecules, erythrocytes, and leukocytes within mammalian capillaries. Circ. Res. 79(3), 581-589 (1996).
    • (1996) Circ. Res. , vol.79 , Issue.3 , pp. 581-589
    • Vink, H.1    Duling, B.R.2
  • 51
    • 81255184413 scopus 로고    scopus 로고
    • Native ultrastructure of the red cell cytoskeleton by cryo-electron tomography
    • Nans A, Mohandas N, Stokes DL. Native ultrastructure of the red cell cytoskeleton by cryo-electron tomography. Biophys. J. 101(10), 2341-2350 (2011).
    • (2011) Biophys. J , vol.101 , Issue.10 , pp. 2341-2350
    • Nans, A.1    Mohandas, N.2    Stokes, D.L.3
  • 53
    • 0019454521 scopus 로고
    • Abnormalities in membrane phospholipid organization in sickled erythrocytes
    • Lubin B, Chiu D, Bastacky J, Roelofsen B, Van Deenen LL. Abnormalities in membrane phospholipid organization in sickled erythrocytes. J. Clin. Invest. 67(6), 1643-1649 (1981).
    • (1981) J. Clin. Invest. , vol.67 , Issue.6 , pp. 1643-1649
    • Lubin, B.1    Chiu, D.2    Bastacky, J.3    Roelofsen, B.4    Van Deenen, L.L.5
  • 54
    • 42049115740 scopus 로고    scopus 로고
    • Disorders of red cell membrane
    • An X, Mohandas N. Disorders of red cell membrane. Br. J. Haematol. 141(3), 367-375 (2008).
    • (2008) Br. J. Haematol. , vol.141 , Issue.3 , pp. 367-375
    • An, X.1    Mohandas, N.2
  • 55
    • 79960695890 scopus 로고    scopus 로고
    • Hereditary red cell membrane defects: Diagnostic and clinical aspects
    • Barcellini W, Bianchi P, Fermo E et al. Hereditary red cell membrane defects: diagnostic and clinical aspects. Blood Transfus. Trasfus. Sangue. 9(3), 274-277 (2011).
    • (2011) Blood Transfus. Trasfus. Sangue. , vol.9 , Issue.3 , pp. 274-277
    • Barcellini, W.1    Bianchi, P.2    Fermo, E.3
  • 56
    • 0037105613 scopus 로고    scopus 로고
    • Splenectomy prolongs in vivo survival of erythrocytes differently in spectrin/ankyrinand band 3-deficient hereditary spherocytosis
    • Reliene R, Mariani M, Zanella A et al. Splenectomy prolongs in vivo survival of erythrocytes differently in spectrin/ankyrinand band 3-deficient hereditary spherocytosis. Blood 100(6), 2208-2215 (2002).
    • (2002) Blood , vol.100 , Issue.6 , pp. 2208-2215
    • Reliene, R.1    Mariani, M.2    Zanella, A.3
  • 58
    • 84860188200 scopus 로고    scopus 로고
    • From artificial red blood cells, oxygen carriers, and oxygen therapeutics to artificial cells, nanomedicine, and beyond
    • Chang TMS. From artificial red blood cells, oxygen carriers, and oxygen therapeutics to artificial cells, nanomedicine, and beyond. Artif. Cells Blood Substit. Immobil. Biotechnol. 40(3), 197-199 (2012).
    • (2012) Artif. Cells Blood Substit. Immobil. Biotechnol. , vol.40 , Issue.3 , pp. 197-199
    • Chang, T.M.S.1
  • 59
    • 24044477899 scopus 로고    scopus 로고
    • Artificial oxygen carriers as an alternative to red blood cell transfusion
    • Habler O, Pape A, Meier J, Zwissler B. [Artificial oxygen carriers as an alternative to red blood cell transfusion]. Anaesthesist 54(8), 741-754 (2005).
    • (2005) Anaesthesist , vol.54 , Issue.8 , pp. 741-754
    • Habler, O.1    Pape, A.2    Meier, J.3    Zwissler, B.4
  • 60
    • 0029026224 scopus 로고
    • Enhanced complement susceptibility of avidin-biotintreated human erythrocytes is a consequence of neutralization of the complement regulators CD59 and decay accelerating factor
    • Zaltzman AB, Van den Berg CW, Muzykantov VR, Morgan BP. Enhanced complement susceptibility of avidin-biotintreated human erythrocytes is a consequence of neutralization of the complement regulators CD59 and decay accelerating factor. Biochem. J. 307(Pt 3), 651-656 (1995).
    • (1995) Biochem. J. , vol.307 , pp. 651-656
    • Zaltzman, A.B.1    Van Den Berg, C.W.2    Muzykantov, V.R.3    Morgan, B.P.4
  • 62
    • 30144445383 scopus 로고    scopus 로고
    • SHPS-1 promotes the survival of circulating erythrocytes through inhibition of phagocytosis by splenic macrophages
    • Ishikawa-Sekigami T, Kaneko Y, Okazawa H et al. SHPS-1 promotes the survival of circulating erythrocytes through inhibition of phagocytosis by splenic macrophages. Blood 107(1), 341-348 (2006).
    • (2006) Blood , vol.107 , Issue.1 , pp. 341-348
    • Ishikawa-Sekigami, T.1    Kaneko, Y.2    Okazawa, H.3
  • 64
    • 84868624308 scopus 로고    scopus 로고
    • Engulfment of hematopoietic stem cells caused by down-regulation of CD47 is critical in the pathogenesis of hemophagocytic lymphohistiocytosis
    • Kuriyama T, Takenaka K, Kohno K et al. Engulfment of hematopoietic stem cells caused by down-regulation of CD47 is critical in the pathogenesis of hemophagocytic lymphohistiocytosis. Blood 120(19), 4058-4067 (2012).
    • (2012) Blood , vol.120 , Issue.19 , pp. 4058-4067
    • Kuriyama, T.1    Takenaka, K.2    Kohno, K.3
  • 65
    • 0021802626 scopus 로고
    • Distribution of decay-accelerating factor in the peripheral blood of normal individuals and patients with paroxysmal nocturnal hemoglobinuria
    • Kinoshita T, Medof ME, Silber R, Nussenzweig V. Distribution of decay-accelerating factor in the peripheral blood of normal individuals and patients with paroxysmal nocturnal hemoglobinuria. J. Exp. Med. 162(1), 75-92 (1985).
    • (1985) J. Exp. Med. , vol.162 , Issue.1 , pp. 75-92
    • Kinoshita, T.1    Medof, M.E.2    Silber, R.3    Nussenzweig, V.4
  • 66
    • 0021713655 scopus 로고
    • Inhibition of complement activation on the surface of cells after incorporation of decay-accelerating factor (DAF) into their membranes
    • Medof ME, Kinoshita T, Nussenzweig V. Inhibition of complement activation on the surface of cells after incorporation of decay-accelerating factor (DAF) into their membranes. J. Exp. Med. 160(5), 1558-1578 (1984).
    • (1984) J. Exp. Med. , vol.160 , Issue.5 , pp. 1558-1578
    • Medof, M.E.1    Kinoshita, T.2    Nussenzweig, V.3
  • 67
    • 0037800971 scopus 로고
    • Affected erythrocytes of patients with paroxysmal nocturnal hemoglobinuria are deficient in the complement regulatory protein, decay accelerating factor
    • Nicholson-Weller A, March JP, Rosenfeld SI, Austen KF. Affected erythrocytes of patients with paroxysmal nocturnal hemoglobinuria are deficient in the complement regulatory protein, decay accelerating factor. Proc. Natl Acad. Sci. USA 80(16), 5066-5070 (1983).
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , Issue.16 , pp. 5066-5070
    • Nicholson-Weller, A.1    March, J.P.2    Rosenfeld, S.I.3    Austen, K.F.4
  • 68
    • 0006386057 scopus 로고
    • Deficiency of an erythrocyte membrane protein with complement regulatory activity in paroxysmal nocturnal hemoglobinuria
    • Pangburn MK, Schreiber RD, Müller-Eberhard HJ. Deficiency of an erythrocyte membrane protein with complement regulatory activity in paroxysmal nocturnal hemoglobinuria. Proc. Natl Acad. Sci. USA 80(17), 5430-5434 (1983).
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , Issue.17 , pp. 5430-5434
    • Pangburn, M.K.1    Schreiber, R.D.2    Müller-Eberhard, H.J.3
  • 69
    • 0024732632 scopus 로고
    • Erythrocyte membrane protein deficiencies in paroxysmal nocturnal hemoglobinuria
    • Schultz DR. Erythrocyte membrane protein deficiencies in paroxysmal nocturnal hemoglobinuria. Am. J. Med. 87(3N), 22N-29N (1989).
    • (1989) Am. J. Med. , vol.87 , Issue.3 N , pp. 22N-29N
    • Schultz, D.R.1
  • 70
    • 0027936442 scopus 로고
    • Recombinant soluble CD59 inhibits reactive haemolysis with complement
    • Sugita Y, Ito K, Shiozuka K et al. Recombinant soluble CD59 inhibits reactive haemolysis with complement. Immunology 82(1), 34-41 (1994).
    • (1994) Immunology , vol.82 , Issue.1 , pp. 34-41
    • Sugita, Y.1    Ito, K.2    Shiozuka, K.3
  • 71
    • 0025213377 scopus 로고
    • Binding of anti-band 3 autoantibody to oxidatively damaged erythrocytes. Formation of senescent antigen on erythrocyte surface by an oxidative mechanism
    • Beppu M, Mizukami A, Nagoya M, Kikugawa K. Binding of anti-band 3 autoantibody to oxidatively damaged erythrocytes. Formation of senescent antigen on erythrocyte surface by an oxidative mechanism. J. Biol. Chem. 265(6), 3226-3233 (1990).
    • (1990) J. Biol. Chem. , vol.265 , Issue.6 , pp. 3226-3233
    • Beppu, M.1    Mizukami, A.2    Nagoya, M.3    Kikugawa, K.4
  • 72
    • 0022656044 scopus 로고
    • The natural anti-alpha-galactosyl IgG on human normal senescent red blood cells
    • Galili U, Flechner I, Knyszynski A, Danon D, Rachmilewitz EA. The natural anti-alpha-galactosyl IgG on human normal senescent red blood cells. Br. J. Haematol. 62(2), 317-324 (1986).
    • (1986) Br. J. Haematol. , vol.62 , Issue.2 , pp. 317-324
    • Galili, U.1    Flechner, I.2    Knyszynski, A.3    Danon, D.4    Rachmilewitz, E.A.5
  • 73
    • 0028954970 scopus 로고
    • Naturally occurring human anti-band 3 autoantibodies accelerate clearance of erythrocytes in Guinea pigs
    • Giger U, Sticher B, Naef R, Burger R, Lutz HU. Naturally occurring human anti-band 3 autoantibodies accelerate clearance of erythrocytes in Guinea pigs. Blood 85(7), 1920-1928 (1995).
    • (1995) Blood , vol.85 , Issue.7 , pp. 1920-1928
    • Giger, U.1    Sticher, B.2    Naef, R.3    Burger, R.4    Lutz, H.U.5
  • 74
    • 0019872977 scopus 로고
    • Isolation of the phagocytosis-inducing IgG-binding antigen on senescent somatic cells
    • Kay MM. Isolation of the phagocytosis-inducing IgG-binding antigen on senescent somatic cells. Nature 289(5797), 491-494 (1981).
    • (1981) Nature , vol.289 , Issue.5797 , pp. 491-494
    • Kay, M.M.1
  • 75
    • 79251569904 scopus 로고    scopus 로고
    • Robust erythrophagocytosis leads to macrophage apoptosis via a hemin-mediated redox imbalance: Role in hemolytic disorders
    • Cambos M, Scorza T. Robust erythrophagocytosis leads to macrophage apoptosis via a hemin-mediated redox imbalance: role in hemolytic disorders. J. Leukoc. Biol. 89(1), 159-171 (2011).
    • (2011) J. Leukoc. Biol. , vol.89 , Issue.1 , pp. 159-171
    • Cambos, M.1    Scorza, T.2
  • 76
    • 0023280601 scopus 로고
    • Effect of Kupffer cell phagocytosis of erythrocytes and erythrocyte ghosts on susceptibility to endotoxemia and bacteremia
    • Loegering DJ, Commins LM, Minnear FL, Gary LA, Hill LA. Effect of Kupffer cell phagocytosis of erythrocytes and erythrocyte ghosts on susceptibility to endotoxemia and bacteremia. Infect. Immun. 55(9), 2074-2080 (1987).
    • (1987) Infect. Immun. , vol.55 , Issue.9 , pp. 2074-2080
    • Loegering, D.J.1    Commins, L.M.2    Minnear, F.L.3    Gary, L.A.4    Hill, L.A.5
  • 77
    • 23444437972 scopus 로고    scopus 로고
    • Structure and function of the spleen
    • Mebius RE, Kraal G. Structure and function of the spleen. Nat. Rev. Immunol. 5(8), 606-616 (2005).
    • (2005) Nat. Rev. Immunol. , vol.5 , Issue.8 , pp. 606-616
    • Mebius, R.E.1    Kraal, G.2
  • 78
    • 0007047966 scopus 로고    scopus 로고
    • Cross-linking treatment of loaded erythrocytes increases delivery of encapsulated substance to macrophages
    • Alvarez FJ, Jordán JA, Calleja P et al. Cross-linking treatment of loaded erythrocytes increases delivery of encapsulated substance to macrophages. Biotechnol. Appl. Biochem. 27(Pt 2), 139-143 (1998).
    • (1998) Biotechnol. Appl. Biochem. , vol.27 , pp. 139-143
    • Alvarez, F.J.1    Jordán, J.A.2    Calleja, P.3
  • 79
    • 0028908093 scopus 로고
    • Modulated red blood cell survival by membrane protein clustering
    • Chiarantini L, Rossi L, Fraternale A, Magnani M. Modulated red blood cell survival by membrane protein clustering. Mol. Cell. Biochem. 144(1), 53-59 (1995).
    • (1995) Mol. Cell. Biochem. , vol.144 , Issue.1 , pp. 53-59
    • Chiarantini, L.1    Rossi, L.2    Fraternale, A.3    Magnani, M.4
  • 80
    • 0029014486 scopus 로고
    • Perturbation of red blood cell membrane rigidity by extracellular ligands
    • Paulitschke M, Nash GB, Anstee DJ, Tanner MJ, Gratzer WB. Perturbation of red blood cell membrane rigidity by extracellular ligands. Blood 86(1), 342-348 (1995).
    • (1995) Blood , vol.86 , Issue.1 , pp. 342-348
    • Paulitschke, M.1    Nash, G.B.2    Anstee, D.J.3    Tanner, M.J.4    Gratzer, W.B.5
  • 81
    • 0031938658 scopus 로고    scopus 로고
    • Endothelial cell vehicles for delivery of cytotoxic genes as a gene therapy approach for carcinoma of the ovary
    • Rancourt C, Robertson MW, Wang M et al. Endothelial cell vehicles for delivery of cytotoxic genes as a gene therapy approach for carcinoma of the ovary. Clin. Cancer Res. Off. J. Am. Assoc. Cancer Res. 4(2), 265-270 (1998).
    • (1998) Clin. Cancer Res. Off. J. Am. Assoc. Cancer Res. , vol.4 , Issue.2 , pp. 265-270
    • Rancourt, C.1    Robertson, M.W.2    Wang, M.3
  • 82
    • 0026343738 scopus 로고
    • Clustering of integral membrane proteins of the human erythrocyte membrane stimulates autologous IgG binding, complement deposition, and phagocytosis
    • Turrini F, Arese P, Yuan J, Low PS. Clustering of integral membrane proteins of the human erythrocyte membrane stimulates autologous IgG binding, complement deposition, and phagocytosis. J. Biol. Chem. 266(35), 23611-23617 (1991).
    • (1991) J. Biol. Chem. , vol.266 , Issue.35 , pp. 23611-23617
    • Turrini, F.1    Arese, P.2    Yuan, J.3    Low, P.S.4
  • 84
    • 0027288165 scopus 로고
    • Characterization of the autologous antibodies that opsonize erythrocytes with clustered integral membrane proteins
    • Turrini F, Mannu F, Arese P, Yuan J, Low PS. Characterization of the autologous antibodies that opsonize erythrocytes with clustered integral membrane proteins. Blood 81(11), 3146-3152 (1993).
    • (1993) Blood , vol.81 , Issue.11 , pp. 3146-3152
    • Turrini, F.1    Mannu, F.2    Arese, P.3    Yuan, J.4    Low, P.S.5
  • 85
    • 0033614457 scopus 로고    scopus 로고
    • Detection of phosphatidylserine surface exposure on human erythrocytes using annexin V-ferrofluid
    • Geldwerth D, Helley D, de Jong K et al. Detection of phosphatidylserine surface exposure on human erythrocytes using annexin V-ferrofluid. Biochem. Biophys. Res. Commun. 258(1), 199-203 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , Issue.1 , pp. 199-203
    • Geldwerth, D.1    Helley, D.2    De Jong, K.3
  • 86
    • 0032748399 scopus 로고    scopus 로고
    • Phosphatidylserinerelated adhesion of human erythrocytes to vascular endothelium
    • Closse C, Dachary-Prigent J, Boisseau MR. Phosphatidylserinerelated adhesion of human erythrocytes to vascular endothelium. Br. J. Haematol. 107(2), 300-302 (1999).
    • (1999) Br. J. Haematol. , vol.107 , Issue.2 , pp. 300-302
    • Closse, C.1    Dachary-Prigent, J.2    Boisseau, M.R.3
  • 87
    • 0025787548 scopus 로고
    • Optimized recirculation survival of mouse carrier erythrocytes
    • discussion 618-622
    • Chiarantini L, Johnson J, Deloach JR. Optimized recirculation survival of mouse carrier erythrocytes. Blood Cells 17(3), 607-617; discussion 618-622 (1991).
    • (1991) Blood Cells , vol.17 , Issue.3 , pp. 607-617
    • Chiarantini, L.1    Johnson, J.2    DeLoach, J.R.3
  • 88
    • 0022553643 scopus 로고
    • In vivo clearance of antibody-sensitized human drug carrier erythrocytes
    • Eichler HG, Gasic S, Bauer K, Korn A, Bacher S. In vivo clearance of antibody-sensitized human drug carrier erythrocytes. Clin. Pharmacol. Ther. 40(3), 300-303 (1986).
    • (1986) Clin. Pharmacol. Ther. , vol.40 , Issue.3 , pp. 300-303
    • Eichler, H.G.1    Gasic, S.2    Bauer, K.3    Korn, A.4    Bacher, S.5
  • 89
    • 0021208253 scopus 로고
    • Effect of red blood cell stroma on the reticuloendothelial system clearance and killing of streptococcus pneumoniae
    • Grover GJ, Loegering DJ. Effect of red blood cell stroma on the reticuloendothelial system clearance and killing of Streptococcus pneumoniae. Circ. Shock 14(1), 39-47 (1984).
    • (1984) Circ. Shock , vol.14 , Issue.1 , pp. 39-47
    • Grover, G.J.1    Loegering, D.J.2
  • 90
    • 28844488320 scopus 로고    scopus 로고
    • The energy-less red blood cell is lost: Erythrocyte enzyme abnormalities of glycolysis
    • Van Wijk R, van Solinge WW. The energy-less red blood cell is lost: erythrocyte enzyme abnormalities of glycolysis. Blood 106(13), 4034-4042 (2005).
    • (2005) Blood , vol.106 , Issue.13 , pp. 4034-4042
    • Van Wijk, R.1    Van Solinge, W.W.2
  • 91
    • 22144443537 scopus 로고    scopus 로고
    • Erythrocytes are the major intravascular storage sites of nitrite in human blood
    • Dejam A, Hunter CJ, Pelletier MM et al. Erythrocytes are the major intravascular storage sites of nitrite in human blood. Blood 106(2), 734-739 (2005).
    • (2005) Blood , vol.106 , Issue.2 , pp. 734-739
    • Dejam, A.1    Hunter, C.J.2    Pelletier, M.M.3
  • 92
    • 0031951625 scopus 로고    scopus 로고
    • Hypotonically loaded rat erythrocytes deliver encapsulated substances into peritoneal macrophages
    • Alvarez FJ, Jordán JA, Herráez A, Díez JC, Tejedor MC. Hypotonically loaded rat erythrocytes deliver encapsulated substances into peritoneal macrophages. J. Biochem. (Tokyo) 123(2), 233-239 (1998).
    • (1998) J. Biochem. (Tokyo) , vol.123 , Issue.2 , pp. 233-239
    • Alvarez, F.J.1    Jordán, J.A.2    Herráez, A.3    Díez, J.C.4    Tejedor, M.C.5
  • 93
    • 0018954749 scopus 로고
    • Enhanced stability of erythrocyteentrapped glucocerebrosidase activity
    • Humphreys JD, Ihler G. Enhanced stability of erythrocyteentrapped glucocerebrosidase activity. J. Lab. Clin. Med. 96(4), 682-692 (1980).
    • (1980) J. Lab. Clin. Med. , vol.96 , Issue.4 , pp. 682-692
    • Humphreys, J.D.1    Ihler, G.2
  • 95
    • 36849017392 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication in macrophages by red blood cell-mediated delivery of a heterodinucleotide of lamivudine and tenofovir
    • Franchetti P, Cappellacci L, Petrelli R et al. Inhibition of HIV-1 replication in macrophages by red blood cell-mediated delivery of a heterodinucleotide of lamivudine and tenofovir. Nucleosides Nucleotides Nucleic Acids 26(8-9), 953-957 (2007).
    • (2007) Nucleosides Nucleotides Nucleic Acids , vol.26 , Issue.8-9 , pp. 953-957
    • Franchetti, P.1    Cappellacci, L.2    Petrelli, R.3
  • 97
    • 0033004359 scopus 로고    scopus 로고
    • Heterodimer-loaded erythrocytes as bioreactors for slow delivery of the antiviral drug azidothymidine and the antimycobacterial drug ethambutol
    • Rossi L, Brandi G, Schiavano GF et al. Heterodimer-loaded erythrocytes as bioreactors for slow delivery of the antiviral drug azidothymidine and the antimycobacterial drug ethambutol. AIDS Res. Hum. Retroviruses 15(4), 345-353 (1999).
    • (1999) AIDS Res. Hum. Retroviruses , vol.15 , Issue.4 , pp. 345-353
    • Rossi, L.1    Brandi, G.2    Schiavano, G.F.3
  • 98
    • 0026846440 scopus 로고
    • Vitro targeting of erythrocytes to cytotoxic t-cells by coupling of thy-1. 2 monoclonal antibody
    • Chiarantini L, Droleskey R, Magnani M, DeLoach JR. In vitro targeting of erythrocytes to cytotoxic T-cells by coupling of Thy-1. 2 monoclonal antibody. Biotechnol. Appl. Biochem. 15(2), 171-184 (1992).
    • (1992) Biotechnol. Appl. Biochem. , vol.15 , Issue.2 , pp. 171-184
    • Chiarantini, L.1    Droleskey, R.2    Magnani, M.3    DeLoach, J.R.4
  • 99
    • 0036268007 scopus 로고    scopus 로고
    • Erythrocyte-mediated delivery of drugs, peptides and modified oligonucleotides
    • Magnani M, Rossi L, Fraternale A et al. Erythrocyte-mediated delivery of drugs, peptides and modified oligonucleotides. Gene Ther. 9(11), 749-751 (2002).
    • (2002) Gene Ther. , vol.9 , Issue.11 , pp. 749-751
    • Magnani, M.1    Rossi, L.2    Fraternale, A.3
  • 100
    • 84898782723 scopus 로고    scopus 로고
    • Targeting and depletion of circulating leukocytes and cancer cells by lipophilic antibody-modified erythrocytes
    • Mukthavaram R, Shi G, Kesari S, Simberg D. Targeting and depletion of circulating leukocytes and cancer cells by lipophilic antibody-modified erythrocytes. J. Control. Release 183, 146-153 (2014).
    • (2014) J. Control. Release , vol.183 , pp. 146-153
    • Mukthavaram, R.1    Shi, G.2    Kesari, S.3    Simberg, D.4
  • 101
    • 0029879401 scopus 로고    scopus 로고
    • Target-sensitive immunoerythrocytes: Interaction of biotinylated red blood cells with immobilized avidin induces their lysis by complement
    • Muzykantov VR, Zaltsman AB, Smirnov MD, Samokhin GP, Morgan BP. Target-sensitive immunoerythrocytes: interaction of biotinylated red blood cells with immobilized avidin induces their lysis by complement. Biochim. Biophys. Acta 1279(2), 137-143 (1996).
    • (1996) Biochim. Biophys. Acta , vol.1279 , Issue.2 , pp. 137-143
    • Muzykantov, V.R.1    Zaltsman, A.B.2    Smirnov, M.D.3    Samokhin, G.P.4    Morgan, B.P.5
  • 102
    • 0027089743 scopus 로고
    • Comparison of uricase-bound and uricase-loaded erythrocytes as bioreactors for uric acid degradation
    • Magnani M, Mancini U, Bianchi M, Fazi A. Comparison of uricase-bound and uricase-loaded erythrocytes as bioreactors for uric acid degradation. Adv. Exp. Med. Biol. 326, 189-194 (1992).
    • (1992) Adv. Exp. Med. Biol. , vol.326 , pp. 189-194
    • Magnani, M.1    Mancini, U.2    Bianchi, M.3    Fazi, A.4
  • 103
    • 0023222030 scopus 로고
    • Directed targeting of immunoerythrocytes provides local protection of endothelial cells from damage by hydrogen peroxide
    • Muzykantov VR, Sakharov DV, Domogatsky SP, Goncharov NV, Danilov SM. Directed targeting of immunoerythrocytes provides local protection of endothelial cells from damage by hydrogen peroxide. Am. J. Pathol. 128(2), 276-285 (1987).
    • (1987) Am. J. Pathol. , vol.128 , Issue.2 , pp. 276-285
    • Muzykantov, V.R.1    Sakharov, D.V.2    Domogatsky, S.P.3    Goncharov, N.V.4    Danilov, S.M.5
  • 104
    • 0027477790 scopus 로고
    • Tannin-mediated attachment of avidin provides complement-resistant immunoerythrocytes that can be lysed in the presence of activator of complement
    • Muzykantov VR, Smirnov MD, Zaltzman AB, Samokhin GP. Tannin-mediated attachment of avidin provides complement-resistant immunoerythrocytes that can be lysed in the presence of activator of complement. Anal. Biochem. 208(2), 338-342 (1993).
    • (1993) Anal. Biochem. , vol.208 , Issue.2 , pp. 338-342
    • Muzykantov, V.R.1    Smirnov, M.D.2    Zaltzman, A.B.3    Samokhin, G.P.4
  • 105
    • 0019852044 scopus 로고
    • Affinity targeting of membrane vesicles to cell surfaces
    • Godfrey W, Doe B, Wallace EF, Bredt B, Wofsy L. Affinity targeting of membrane vesicles to cell surfaces. Exp. Cell Res. 135(1), 137-145 (1981).
    • (1981) Exp. Cell Res. , vol.135 , Issue.1 , pp. 137-145
    • Godfrey, W.1    Doe, B.2    Wallace, E.F.3    Bredt, B.4    Wofsy, L.5
  • 106
    • 0019462171 scopus 로고
    • The use of the 2-iminobiotin-avidin interaction for the selective retrieval of labeled plasma membrane components
    • Orr GA. The use of the 2-iminobiotin-avidin interaction for the selective retrieval of labeled plasma membrane components. J. Biol. Chem. 256(2), 761-766 (1981).
    • (1981) J. Biol. Chem. , vol.256 , Issue.2 , pp. 761-766
    • Orr, G.A.1
  • 107
    • 0022475076 scopus 로고
    • Selective labeling of functional groups on membrane proteins or glycoproteins using reactive biotin derivatives and 125I-streptavidin
    • Roffman E, Meromsky L, Ben-Hur H, Bayer EA, Wilchek M. Selective labeling of functional groups on membrane proteins or glycoproteins using reactive biotin derivatives and 125I-streptavidin. Biochem. Biophys. Res. Commun. 136(1), 80-85 (1986).
    • (1986) Biochem. Biophys. Res. Commun. , vol.136 , Issue.1 , pp. 80-85
    • Roffman, E.1    Meromsky, L.2    Ben-Hur, H.3    Bayer, E.A.4    Wilchek, M.5
  • 108
    • 0023124293 scopus 로고
    • Selective labeling of sulfhydryls and disulfides on blot transfers using avidinbiotin technology: Studies on purified proteins and erythrocyte membranes
    • Bayer EA, Safars M, Wilchek M. Selective labeling of sulfhydryls and disulfides on blot transfers using avidinbiotin technology: studies on purified proteins and erythrocyte membranes. Anal. Biochem. 161(2), 262-271 (1987).
    • (1987) Anal. Biochem. , vol.161 , Issue.2 , pp. 262-271
    • Bayer, E.A.1    Safars, M.2    Wilchek, M.3
  • 109
    • 0022446214 scopus 로고
    • P-Diazobenzoyl biocytin-a new biotinylating reagent for the labeling of tyrosines and histidines in proteins
    • Wilchek M, Ben-Hur H, Bayer EA. p-Diazobenzoyl biocytin-a new biotinylating reagent for the labeling of tyrosines and histidines in proteins. Biochem. Biophys. Res. Commun. 138(2), 872-879 (1986).
    • (1986) Biochem. Biophys. Res. Commun. , vol.138 , Issue.2 , pp. 872-879
    • Wilchek, M.1    Ben-Hur, H.2    Bayer, E.A.3
  • 110
    • 0027397735 scopus 로고
    • Avidin attachment to red blood cells via a phospholipid derivative of biotin provides complement-resistant immunoerythrocytes
    • Muzykantov VR, Smirnov MD, Klibanov AL. Avidin attachment to red blood cells via a phospholipid derivative of biotin provides complement-resistant immunoerythrocytes. J. Immunol. Methods 158(2), 183-190 (1993).
    • (1993) J. Immunol. Methods , vol.158 , Issue.2 , pp. 183-190
    • Muzykantov, V.R.1    Smirnov, M.D.2    Klibanov, A.L.3
  • 113
    • 0028674870 scopus 로고
    • Preparation and characterization of biotinylated red blood cells
    • Magnani M, Chiarantini L, Mancini U. Preparation and characterization of biotinylated red blood cells. Biotechnol. Appl. Biochem. 20(Pt 3), 335-345 (1994).
    • (1994) Biotechnol. Appl. Biochem. , vol.20 , pp. 335-345
    • Magnani, M.1    Chiarantini, L.2    Mancini, U.3
  • 117
    • 0025965387 scopus 로고
    • Streptavidininduced lysis of homologous biotinylated erythrocytes,Evidence against the key role of the avidin charge in complement activation via the alternative pathway
    • Muzykantov VR, Smirnov MD, Samokhin GP. Streptavidininduced lysis of homologous biotinylated erythrocytes. Evidence against the key role of the avidin charge in complement activation via the alternative pathway. FEBS Lett. 280(1), 112-114 (1991).
    • (1991) FEBS Lett. , vol.280 , Issue.1 , pp. 112-114
    • Muzykantov, V.R.1    Smirnov, M.D.2    Samokhin, G.P.3
  • 118
    • 0027058124 scopus 로고
    • On red blood cells, hemolysis and resealed ghosts
    • Hoffman JF. On red blood cells, hemolysis and resealed ghosts. Adv. Exp. Med. Biol. 326, 1-15 (1992).
    • (1992) Adv. Exp. Med. Biol , vol.326 , pp. 1-15
    • Hoffman, J.F.1
  • 119
    • 0025789842 scopus 로고
    • Avidin attachment to biotinylated erythrocytes induces homologous lysis via the alternative pathway of complement
    • Muzykantov VR, Smirnov MD, Samokhin GP. Avidin attachment to biotinylated erythrocytes induces homologous lysis via the alternative pathway of complement. Blood 78(10), 2611-2618 (1991).
    • (1991) Blood , vol.78 , Issue.10 , pp. 2611-2618
    • Muzykantov, V.R.1    Smirnov, M.D.2    Samokhin, G.P.3
  • 120
    • 0026486950 scopus 로고
    • Fast lysis by complement and uptake by liver of avidin-carrying biotinylated erythrocytes
    • Muzykantov VR, Seregina N, Smirnov MD. Fast lysis by complement and uptake by liver of avidin-carrying biotinylated erythrocytes. Int. J. Artif. Organs 15(10), 622-627 (1992).
    • (1992) Int. J. Artif. Organs , vol.15 , Issue.10 , pp. 622-627
    • Muzykantov, V.R.1    Seregina, N.2    Smirnov, M.D.3
  • 121
    • 0027398834 scopus 로고
    • Avidin attachment to biotinylated amino groups of the erythrocyte membrane eliminates homologous restriction of both classical and alternative pathways of the complement
    • Muzykantov VR, Smirnov MD, Klibanov AL. Avidin attachment to biotinylated amino groups of the erythrocyte membrane eliminates homologous restriction of both classical and alternative pathways of the complement. FEBS Lett. 318(2), 108-112 (1993).
    • (1993) FEBS Lett. , vol.318 , Issue.2 , pp. 108-112
    • Muzykantov, V.R.1    Smirnov, M.D.2    Klibanov, A.L.3
  • 122
    • 0029900816 scopus 로고    scopus 로고
    • Attachment of antibody to biotinylated red blood cells: Immuno-red blood cells display high affinity to immobilized antigen and normal biodistribution in rats
    • Muzykantov VR, Murciano JC. Attachment of antibody to biotinylated red blood cells: immuno-red blood cells display high affinity to immobilized antigen and normal biodistribution in rats. Biotechnol. Appl. Biochem. 24(Pt 1), 41-45 (1996).
    • (1996) Biotechnol. Appl. Biochem. , vol.24 , pp. 41-45
    • Muzykantov, V.R.1    Murciano, J.C.2
  • 123
    • 0027942688 scopus 로고
    • Attachment of biotinylated antibody to red blood cells: Antigen-binding capacity of immunoerythrocytes and their susceptibility to lysis by complement
    • Muzykantov VR, Taylor RP. Attachment of biotinylated antibody to red blood cells: antigen-binding capacity of immunoerythrocytes and their susceptibility to lysis by complement. Anal. Biochem. 223(1), 142-148 (1994).
    • (1994) Anal. Biochem , vol.223 , Issue.1 , pp. 142-148
    • Muzykantov, V.R.1    Taylor, R.P.2
  • 124
    • 0026069567 scopus 로고
    • Avidin acylation prevents the complement-dependent lysis of avidincarrying erythrocytes
    • Muzykantov VR, Smirnov MD, Samokhin GP. Avidin acylation prevents the complement-dependent lysis of avidincarrying erythrocytes. Biochem. J. 273(Pt 2), 393-397 (1991).
    • (1991) Biochem. J , vol.273 , pp. 393-397
    • Muzykantov, V.R.1    Smirnov, M.D.2    Samokhin, G.P.3
  • 125
    • 0026647494 scopus 로고
    • Avidininduced lysis of biotinylated erythrocytes by homologous complement via the alternative pathway depends on avidin's ability of multipoint binding with biotinylated membrane
    • Muzykantov VR, Smirnov MD, Samokhin GP. Avidininduced lysis of biotinylated erythrocytes by homologous complement via the alternative pathway depends on avidin's ability of multipoint binding with biotinylated membrane. Biochim. Biophys. Acta 1107(1), 119-125 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1107 , Issue.1 , pp. 119-125
    • Muzykantov, V.R.1    Smirnov, M.D.2    Samokhin, G.P.3
  • 126
    • 0030272519 scopus 로고    scopus 로고
    • Regulation of the complement-mediated elimination of red blood cells modified with biotin and streptavidin
    • Muzykantov VR, Murciano JC, Taylor RP, Atochina EN, Herraez A. Regulation of the complement-mediated elimination of red blood cells modified with biotin and streptavidin. Anal. Biochem. 241(1), 109-119 (1996).
    • (1996) Anal. Biochem , vol.241 , Issue.1 , pp. 109-119
    • Muzykantov, V.R.1    Murciano, J.C.2    Taylor, R.P.3    Atochina, E.N.4    Herraez, A.5
  • 127
    • 0030932273 scopus 로고    scopus 로고
    • Red blood cells as delivery system for recombinant HSV-1 glycoprotein B: Immunogenicity and protection in mice
    • Chiarantini L, Argnani R, Zucchini S et al. Red blood cells as delivery system for recombinant HSV-1 glycoprotein B: immunogenicity and protection in mice. Vaccine 15(3), 276-280 (1997).
    • (1997) Vaccine , vol.15 , Issue.3 , pp. 276-280
    • Chiarantini, L.1    Argnani, R.2    Zucchini, S.3
  • 128
    • 0022974712 scopus 로고
    • Carrierdirected targeting of liposomes and erythrocytes to denuded areas of vessel wall
    • Smirnov VN, Domogatsky SP, Dolgov VV et al. Carrierdirected targeting of liposomes and erythrocytes to denuded areas of vessel wall. Proc. Natl Acad. Sci. USA 83(17), 6603-6607 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , Issue.17 , pp. 6603-6607
    • Smirnov, V.N.1    Domogatsky, S.P.2    Dolgov, V.V.3
  • 129
    • 4544311496 scopus 로고    scopus 로고
    • Staphylococcus aureus bound to complement receptor 1 on human erythrocytes by bispecific monoclonal antibodies is phagocytosed by acceptor macrophages
    • Gyimesi E, Bankovich AJ, Schuman TA, Goldberg JB, Lindorfer MA, Taylor RP. Staphylococcus aureus bound to complement receptor 1 on human erythrocytes by bispecific monoclonal antibodies is phagocytosed by acceptor macrophages. Immunol. Lett. 95(2), 185-192 (2004).
    • (2004) Immunol. Lett. , vol.95 , Issue.2 , pp. 185-192
    • Gyimesi, E.1    Bankovich, A.J.2    Schuman, T.A.3    Goldberg, J.B.4    Lindorfer, M.A.5    Taylor, R.P.6
  • 130
    • 0032525002 scopus 로고    scopus 로고
    • Escherichia coli bound to the primate erythrocyte complement receptor via bispecific monoclonal antibodies are transferred to and phagocytosed by human monocytes in an in vitro model
    • Kuhn SE, Nardin A, Klebba PE, Taylor RP. Escherichia coli bound to the primate erythrocyte complement receptor via bispecific monoclonal antibodies are transferred to and phagocytosed by human monocytes in an in vitro model. J. Immunol. 160(10), 5088-5097 (1998).
    • (1998) J. Immunol , vol.160 , Issue.10 , pp. 5088-5097
    • Kuhn, S.E.1    Nardin, A.2    Klebba, P.E.3    Taylor, R.P.4
  • 131
    • 0026317879 scopus 로고
    • Use of heteropolymeric monoclonal antibodies to attach antigens to the C3b receptor of human erythrocytes: A potential therapeutic treatment
    • Taylor RP, Sutherland WM, Reist CJ, Webb DJ, Wright EL, Labuguen RH. Use of heteropolymeric monoclonal antibodies to attach antigens to the C3b receptor of human erythrocytes: a potential therapeutic treatment. Proc. Natl Acad. Sci. USA 88(8), 3305-3309 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , Issue.8 , pp. 3305-3309
    • Taylor, R.P.1    Sutherland, W.M.2    Reist, C.J.3    Webb, D.J.4    Wright, E.L.5    Labuguen, R.H.6
  • 132
    • 0346023953 scopus 로고    scopus 로고
    • ScFv-mediated in vivo targeting of DAF to erythrocytes inhibits lysis by complement
    • Spitzer D, Unsinger J, Bessler M, Atkinson JP. ScFv-mediated in vivo targeting of DAF to erythrocytes inhibits lysis by complement. Mol. Immunol. 40(13), 911-919 (2004).
    • (2004) Mol. Immunol. , vol.40 , Issue.13 , pp. 911-919
    • Spitzer, D.1    Unsinger, J.2    Bessler, M.3    Atkinson, J.P.4
  • 133
    • 0034622520 scopus 로고    scopus 로고
    • GPI-linked proteins do not transfer spontaneously from erythrocytes to liposomes. New aspects of reorganization of the cell membrane
    • Suzuki K, Okumura Y. GPI-linked proteins do not transfer spontaneously from erythrocytes to liposomes. New aspects of reorganization of the cell membrane. Biochemistry (Mosc. ) 39(31), 9477-9485 (2000).
    • (2000) Biochemistry (Mosc. ) , vol.39 , Issue.31 , pp. 9477-9485
    • Suzuki, K.1    Okumura, Y.2
  • 134
    • 0032030679 scopus 로고    scopus 로고
    • Vitro incorporation of GPI-anchored proteins into human erythrocytes and their fate in the membrane
    • Civenni G, Test ST, Brodbeck U, Bütikofer P. In vitro incorporation of GPI-anchored proteins into human erythrocytes and their fate in the membrane. Blood 91(5), 1784-1792 (1998).
    • (1998) Blood , vol.91 , Issue.5 , pp. 1784-1792
    • Civenni, G.1    Test, S.T.2    Brodbeck, U.3    Bütikofer, P.4
  • 135
    • 0029940522 scopus 로고    scopus 로고
    • Cell-surface engineering with GPI-anchored proteins
    • Medof ME, Nagarajan S, Tykocinski ML. Cell-surface engineering with GPI-anchored proteins. FASEB J. 10(5), 574-586 (1996).
    • (1996) FASEB J , vol.10 , Issue.5 , pp. 574-586
    • Medof, M.E.1    Nagarajan, S.2    Tykocinski, M.L.3
  • 136
    • 33344462311 scopus 로고    scopus 로고
    • Protection of erythrocytes from human complement-mediated lysis by membranetargeted recombinant soluble CD59: A new approach to PNH therapy
    • Hill A, Ridley SH, Esser D et al. Protection of erythrocytes from human complement-mediated lysis by membranetargeted recombinant soluble CD59: a new approach to PNH therapy. Blood 107(5), 2131-2137 (2006).
    • (2006) Blood , vol.107 , Issue.5 , pp. 2131-2137
    • Hill, A.1    Ridley, S.H.2    Esser, D.3
  • 137
    • 0032482957 scopus 로고    scopus 로고
    • Mammalian glycophosphatidylinositol anchor transfer to proteins and posttransfer deacylation
    • Chen R, Walter EI, Parker G et al. Mammalian glycophosphatidylinositol anchor transfer to proteins and posttransfer deacylation. Proc. Natl Acad. Sci. USA 95(16), 9512-9517 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , Issue.16 , pp. 9512-9517
    • Chen, R.1    Walter, E.I.2    Parker, G.3
  • 138
    • 0029001840 scopus 로고
    • Vivo transfer of GPI-linked complement restriction factors from erythrocytes to the endothelium
    • Kooyman DL, Byrne GW, McClellan S et al. In vivo transfer of GPI-linked complement restriction factors from erythrocytes to the endothelium. Science 269(5220), 89-92 (1995).
    • (1995) Science , vol.269 , Issue.5220 , pp. 89-92
    • Kooyman, D.L.1    Byrne, G.W.2    McClellan, S.3
  • 139
    • 0343415680 scopus 로고    scopus 로고
    • Preparation and characterization of "heparinocytes": Erythrocytes with covalently bound low molecular weight heparin
    • Müller M, Büchi L, Woodtli K, Haeberli A, Beer JH. Preparation and characterization of "heparinocytes": erythrocytes with covalently bound low molecular weight heparin. FEBS Lett. 468(2-3), 115-119 (2000).
    • (2000) FEBS Lett. , vol.468 , Issue.2-3 , pp. 115-119
    • Müller, M.1    Büchi, L.2    Woodtli, K.3    Haeberli, A.4    Beer, J.H.5
  • 140
    • 0027473646 scopus 로고
    • Pharmacokinetic and thrombolytic properties of chimeric plasminogen activators consisting of a single-chain FV fragment of a fibrin-specific antibody fused to single-chain urokinase
    • Holvoet P, Laroche Y, Stassen JM et al. Pharmacokinetic and thrombolytic properties of chimeric plasminogen activators consisting of a single-chain Fv fragment of a fibrin-specific antibody fused to single-chain urokinase. Blood 81(3), 696-703 (1993).
    • (1993) Blood , vol.81 , Issue.3 , pp. 696-703
    • Holvoet, P.1    Laroche, Y.2    Stassen, J.M.3
  • 141
    • 0023179843 scopus 로고
    • A multicenter, randomized, placebo-controlled trial of a new form of intravenous recombinant tissue-type plasminogen activator (activase) in acute myocardial infarction
    • Topol EJ, Morris DC, Smalling RW et al. A multicenter, randomized, placebo-controlled trial of a new form of intravenous recombinant tissue-type plasminogen activator (activase) in acute myocardial infarction. J. Am. Coll. Cardiol. 9(6), 1205-1213 (1987).
    • (1987) J. Am. Coll. Cardiol. , vol.9 , Issue.6 , pp. 1205-1213
    • Topol, E.J.1    Morris, D.C.2    Smalling, R.W.3
  • 142
    • 0029084057 scopus 로고
    • Two receptor systems are involved in the plasma clearance of tissue-type plasminogen activator (t-PA) in vivo
    • Narita M, Bu G, Herz J, Schwartz AL. Two receptor systems are involved in the plasma clearance of tissue-type plasminogen activator (t-PA) in vivo. J. Clin. Invest. 96(2), 1164-1168 (1995).
    • (1995) J. Clin. Invest. , vol.96 , Issue.2 , pp. 1164-1168
    • Narita, M.1    Bu, G.2    Herz, J.3    Schwartz, A.L.4
  • 143
    • 0027226178 scopus 로고
    • Mechanisms of activation of mammalian plasma fibrinolytic systems with streptokinase and with recombinant staphylokinase
    • Collen D, Van Hoef B, Schlott B, Hartmann M, Gührs KH, Lijnen HR. Mechanisms of activation of mammalian plasma fibrinolytic systems with streptokinase and with recombinant staphylokinase. Eur. J. Biochem. FEBS 216(1), 307-314 (1993).
    • (1993) Eur. J. Biochem. FEBS , vol.216 , Issue.1 , pp. 307-314
    • Collen, D.1    Van Hoef, B.2    Schlott, B.3    Hartmann, M.4    Gührs, K.H.5    Lijnen, H.R.6
  • 144
    • 0027535088 scopus 로고
    • Thrombolytic profiles of clot-targeted plasminogen activators. Parameters determining potency and initial and maximal rates
    • Holvoet P, Dewerchin M, Stassen JM et al. Thrombolytic profiles of clot-targeted plasminogen activators. Parameters determining potency and initial and maximal rates. Circulation 87(3), 1007-1016 (1993).
    • (1993) Circulation , vol.87 , Issue.3 , pp. 1007-1016
    • Holvoet, P.1    Dewerchin, M.2    Stassen, J.M.3
  • 146
    • 9544229716 scopus 로고    scopus 로고
    • Enhanced thrombolytic and antithrombotic potency of a fibrin-targeted plasminogen activator in baboons
    • Runge MS, Harker LA, Bode C et al. Enhanced thrombolytic and antithrombotic potency of a fibrin-targeted plasminogen activator in baboons. Circulation 94(6), 1412-1422 (1996).
    • (1996) Circulation , vol.94 , Issue.6 , pp. 1412-1422
    • Runge, M.S.1    Harker, L.A.2    Bode, C.3
  • 147
    • 0031951510 scopus 로고    scopus 로고
    • Tissue plasminogen activator (tPA) increases neuronal damage after focal cerebral ischemia in wild-type and tPA-deficient mice
    • Wang YF, Tsirka SE, Strickland S, Stieg PE, Soriano SG, Lipton SA. Tissue plasminogen activator (tPA) increases neuronal damage after focal cerebral ischemia in wild-type and tPA-deficient mice. Nat. Med. 4(2), 228-231 (1998).
    • (1998) Nat. Med. , vol.4 , Issue.2 , pp. 228-231
    • Wang, Y.F.1    Tsirka, S.E.2    Strickland, S.3    Stieg, P.E.4    Soriano, S.G.5    Lipton, S.A.6
  • 148
    • 77953732621 scopus 로고    scopus 로고
    • The spatial dynamics of fibrin clot dissolution catalyzed by erythrocyte-bound vs. Free fibrinolytics
    • Gersh KC, Zaitsev S, Muzykantov V, Cines DB, Weisel JW. The spatial dynamics of fibrin clot dissolution catalyzed by erythrocyte-bound vs. free fibrinolytics. J. Thromb. Haemost. JTH 8(5), 1066-1074 (2010).
    • (2010) J. Thromb. Haemost. JTH , vol.8 , Issue.5 , pp. 1066-1074
    • Gersh, K.C.1    Zaitsev, S.2    Muzykantov, V.3    Cines, D.B.4    Weisel, J.W.5
  • 149
    • 79955951798 scopus 로고    scopus 로고
    • Flow-dependent channel formation in clots by an erythrocyte-bound fibrinolytic agent
    • Gersh KC, Zaitsev S, Cines DB, Muzykantov V, Weisel JW. Flow-dependent channel formation in clots by an erythrocyte-bound fibrinolytic agent. Blood 117(18), 4964-4967 (2011).
    • (2011) Blood , vol.117 , Issue.18 , pp. 4964-4967
    • Gersh, K.C.1    Zaitsev, S.2    Cines, D.B.3    Muzykantov, V.4    Weisel, J.W.5
  • 150
    • 14344252453 scopus 로고    scopus 로고
    • Blood clearance and activity of erythrocyte-coupled fibrinolytics
    • Ganguly K, Krasik T, Medinilla S et al. Blood clearance and activity of erythrocyte-coupled fibrinolytics. J. Pharmacol. Exp. Ther. 312(3), 1106-1113 (2005).
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , Issue.3 , pp. 1106-1113
    • Ganguly, K.1    Krasik, T.2    Medinilla, S.3
  • 151
    • 0042855871 scopus 로고    scopus 로고
    • Prophylactic fibrinolysis through selective dissolution of nascent clots by tPA-carrying erythrocytes
    • Murciano J-C, Medinilla S, Eslin D, Atochina E, Cines DB, Muzykantov VR. Prophylactic fibrinolysis through selective dissolution of nascent clots by tPA-carrying erythrocytes. Nat. Biotechnol. 21(8), 891-896 (2003).
    • (2003) Nat. Biotechnol , vol.21 , Issue.8 , pp. 891-896
    • Murciano, J.-C.1    Medinilla, S.2    Eslin, D.3    Atochina, E.4    Cines, D.B.5    Muzykantov, V.R.6
  • 152
    • 26444544223 scopus 로고    scopus 로고
    • Plasminogen activators contribute to impairment of hypercapnic and hypotensive cerebrovasodilation after cerebral hypoxia/ ischemia in the newborn pig
    • Armstead WM, Cines DB, Higazi A.A.-R. Plasminogen activators contribute to impairment of hypercapnic and hypotensive cerebrovasodilation after cerebral hypoxia/ ischemia in the newborn pig. Stroke J. Cereb. Circ. 36(10), 2265-2269 (2005).
    • (2005) Stroke J. Cereb. Circ. , vol.36 , Issue.10 , pp. 2265-2269
    • Armstead, W.M.1    Cines, D.B.2    Aa-R, H.3
  • 153
    • 57349131018 scopus 로고    scopus 로고
    • Urokinase plasminogen activator impairs SNP and PGE2 cerebrovasodilation after brain injury through activation of LRP and ERK MAPK
    • Armstead WM, Christine AJ, Higazi AA-R, Cines DB. Urokinase plasminogen activator impairs SNP and PGE2 cerebrovasodilation after brain injury through activation of LRP and ERK MAPK. J. Neurotrauma 25(11), 1375-1381 (2008).
    • (2008) J. Neurotrauma , vol.25 , Issue.11 , pp. 1375-1381
    • Armstead, W.M.1    Christine, A.J.2    Higazi, A.A.-R.3    Cines, D.B.4
  • 154
    • 68249122804 scopus 로고    scopus 로고
    • Red blood cells-coupled tPA prevents impairment of cerebral vasodilatory responses and tissue injury in pediatric cerebral hypoxia/ischemia through inhibition of ERK MAPK activation
    • Armstead WM, Ganguly K, Kiessling JW et al. Red blood cells-coupled tPA prevents impairment of cerebral vasodilatory responses and tissue injury in pediatric cerebral hypoxia/ischemia through inhibition of ERK MAPK activation. J. Cereb. Blood Flow Metab. 29(8), 1463-1474 (2009).
    • (2009) J. Cereb. Blood Flow Metab. , vol.29 , Issue.8 , pp. 1463-1474
    • Armstead, W.M.1    Ganguly, K.2    Kiessling, J.W.3
  • 155
    • 81155138207 scopus 로고    scopus 로고
    • Red blood cellcoupled tissue plasminogen activator prevents impairment of cerebral vasodilatory responses through inhibition of c-Jun-N-terminal kinase and potentiation of p38 mitogen-activated protein kinase after cerebral photothrombosis in the newborn pig
    • Armstead WM, Ganguly K, Riley J et al. Red blood cellcoupled tissue plasminogen activator prevents impairment of cerebral vasodilatory responses through inhibition of c-Jun-N-terminal kinase and potentiation of p38 mitogen-activated protein kinase after cerebral photothrombosis in the newborn pig. Pediatr. Crit. Care Med. 12(6), e369-e375 (2011).
    • (2011) Pediatr. Crit. Care Med. , vol.12 , Issue.6 , pp. e369-e375
    • Armstead, W.M.1    Ganguly, K.2    Riley, J.3
  • 156
    • 70349335374 scopus 로고    scopus 로고
    • Soluble urokinase receptor conjugated to carrier red blood cells binds latent pro-urokinase and alters its functional profile
    • Murciano J-C, Higazi AA-R, Cines DB, Muzykantov VR. Soluble urokinase receptor conjugated to carrier red blood cells binds latent pro-urokinase and alters its functional profile. J. Control. Release 139(3), 190-196 (2009).
    • (2009) J. Control. Release , vol.139 , Issue.3 , pp. 190-196
    • Murciano, J.-C.1    Higazi, A.A.-R.2    Cines, D.B.3    Muzykantov, V.R.4
  • 157
    • 54049147394 scopus 로고    scopus 로고
    • Cerebrovascular thromboprophylaxis in mice by erythrocyte-coupled tissuetype plasminogen activator
    • Danielyan K, Ganguly K, Ding B-S et al. Cerebrovascular thromboprophylaxis in mice by erythrocyte-coupled tissuetype plasminogen activator. Circulation 118(14), 1442-1449 (2008).
    • (2008) Circulation , vol.118 , Issue.14 , pp. 1442-1449
    • Danielyan, K.1    Ganguly, K.2    Ding, B.-S.3
  • 158
    • 84856212785 scopus 로고    scopus 로고
    • Microthrombosis after experimental subarachnoid hemorrhage: Time course and effect of red blood cell-bound thrombin-activated prourokinase and clazosentan
    • Pisapia JM, Xu X, Kelly J et al. Microthrombosis after experimental subarachnoid hemorrhage: time course and effect of red blood cell-bound thrombin-activated prourokinase and clazosentan. Exp. Neurol. 233(1), 357-363 (2012).
    • (2012) Exp. Neurol. , vol.233 , Issue.1 , pp. 357-363
    • Pisapia, J.M.1    Xu, X.2    Kelly, J.3
  • 159
    • 70450184289 scopus 로고    scopus 로고
    • Erythrocytebound tissue plasminogen activator is neuroprotective in experimental traumatic brain injury
    • Stein SC, Ganguly K, Belfield CM et al. Erythrocytebound tissue plasminogen activator is neuroprotective in experimental traumatic brain injury. J. Neurotrauma 26(9), 1585-1592 (2009).
    • (2009) J. Neurotrauma , vol.26 , Issue.9 , pp. 1585-1592
    • Stein, S.C.1    Ganguly, K.2    Belfield, C.M.3
  • 160
    • 0038481255 scopus 로고    scopus 로고
    • Immune adherence revisited: Novel players in an old game
    • Hess C, Schifferli JA. Immune adherence revisited: novel players in an old game. News Physiol. Sci. 18, 104-108 (2003).
    • (2003) News Physiol. Sci. , vol.18 , pp. 104-108
    • Hess, C.1    Schifferli, J.A.2
  • 161
    • 0018875296 scopus 로고
    • Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorphonuclear leukocyte, B lymphocyte, and monocyte
    • Fearon DT. Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorphonuclear leukocyte, B lymphocyte, and monocyte. J. Exp. Med. 152(1), 20-30 (1980).
    • (1980) J. Exp. Med. , vol.152 , Issue.1 , pp. 20-30
    • Fearon, D.T.1
  • 162
    • 0035018479 scopus 로고    scopus 로고
    • Structure-function relationships of complement receptor type 1
    • Krych-Goldberg M, Atkinson JP. Structure-function relationships of complement receptor type 1. Immunol. Rev. 180, 112-122 (2001).
    • (2001) Immunol. Rev. , vol.180 , pp. 112-122
    • Krych-Goldberg, M.1    Atkinson, J.P.2
  • 163
    • 0035668198 scopus 로고    scopus 로고
    • Heteropolymer-mediated clearance of immune complexes via erythrocyte CR1: Mechanisms and applications
    • Lindorfer MA, Hahn CS, Foley PL, Taylor RP. Heteropolymer-mediated clearance of immune complexes via erythrocyte CR1: mechanisms and applications. Immunol. Rev. 183, 10-24 (2001).
    • (2001) Immunol. Rev. , vol.183 , pp. 10-24
    • Lindorfer, M.A.1    Hahn, C.S.2    Foley, P.L.3    Taylor, R.P.4
  • 164
    • 0031982024 scopus 로고    scopus 로고
    • Mapping epitopes for 20 monoclonal antibodies to CR1
    • Nickells M, Hauhart R, Krych M et al. Mapping epitopes for 20 monoclonal antibodies to CR1. Clin. Exp. Immunol. 112(1), 27-33 (1998).
    • (1998) Clin. Exp. Immunol. , vol.112 , Issue.1 , pp. 27-33
    • Nickells, M.1    Hauhart, R.2    Krych, M.3
  • 165
    • 0032004079 scopus 로고    scopus 로고
    • Quantitative studies of heteropolymer-mediated binding of inactivated Marburg virus to the complement receptor on primate erythrocytes
    • Nardin A, Sutherland WM, Hevey M, Schmaljohn A, Taylor RP. Quantitative studies of heteropolymer-mediated binding of inactivated Marburg virus to the complement receptor on primate erythrocytes. J. Immunol. Methods 211(1-2), 21-31 (1998).
    • (1998) J. Immunol. Methods , vol.211 , Issue.1-2 , pp. 21-31
    • Nardin, A.1    Sutherland, W.M.2    Hevey, M.3    Schmaljohn, A.4    Taylor, R.P.5
  • 166
    • 0026560403 scopus 로고
    • In vivo binding and clearance of circulating antigen by bispecific heteropolymermediated binding to primate erythrocyte complement receptor
    • Taylor RP, Reist CJ, Sutherland WM, Otto A, Labuguen RH, Wright EL. In vivo binding and clearance of circulating antigen by bispecific heteropolymermediated binding to primate erythrocyte complement receptor. J. Immunol. 148(8), 2462-2468 (1992).
    • (1992) J. Immunol. , vol.148 , Issue.8 , pp. 2462-2468
    • Taylor, R.P.1    Reist, C.J.2    Sutherland, W.M.3    Otto, A.4    Labuguen, R.H.5    Wright, E.L.6
  • 167
    • 20244373048 scopus 로고    scopus 로고
    • A transgenic mouse model for studying the clearance of blood-borne pathogens via human complement receptor 1 (CR1)
    • Repik A, Pincus SE, Ghiran I et al. A transgenic mouse model for studying the clearance of blood-borne pathogens via human complement receptor 1 (CR1). Clin. Exp. Immunol. 140(2), 230-240 (2005).
    • (2005) Clin. Exp. Immunol. , vol.140 , Issue.2 , pp. 230-240
    • Repik, A.1    Pincus, S.E.2    Ghiran, I.3
  • 168
    • 0030899530 scopus 로고    scopus 로고
    • The primate erythrocyte complement receptor (CR1) as a privileged site: Binding of immunoglobulin G to erythrocyte CR1 does not target erythrocytes for phagocytosis
    • Reinagel ML, Gezen M, Ferguson PJ, Kuhn S, Martin EN, Taylor RP. The primate erythrocyte complement receptor (CR1) as a privileged site: binding of immunoglobulin G to erythrocyte CR1 does not target erythrocytes for phagocytosis. Blood 89(3), 1068-1077 (1997).
    • (1997) Blood , vol.89 , Issue.3 , pp. 1068-1077
    • Reinagel, M.L.1    Gezen, M.2    Ferguson, P.J.3    Kuhn, S.4    Martin, E.N.5    Taylor, R.P.6
  • 169
    • 0033376409 scopus 로고    scopus 로고
    • How are immune complexes bound to the primate erythrocyte complement receptor transferred to acceptor phagocytic cells
    • Nardin A, Lindorfer MA, Taylor RP. How are immune complexes bound to the primate erythrocyte complement receptor transferred to acceptor phagocytic cells? Mol. Immunol. 36(13-14), 827-835 (1999).
    • (1999) Mol. Immunol , vol.36 , Issue.13-14 , pp. 827-835
    • Nardin, A.1    Lindorfer, M.A.2    Taylor, R.P.3
  • 170
    • 0036802373 scopus 로고    scopus 로고
    • Visualization of the transfer reaction: Tracking immune complexes from erythrocyte complement receptor 1 to macrophages
    • Craig ML, Bankovich AJ, Taylor RP. Visualization of the transfer reaction: tracking immune complexes from erythrocyte complement receptor 1 to macrophages. Clin. Immunol. 105(1), 36-47 (2002).
    • (2002) Clin. Immunol. , vol.105 , Issue.1 , pp. 36-47
    • Craig, M.L.1    Bankovich, A.J.2    Taylor, R.P.3
  • 171
    • 14044259330 scopus 로고    scopus 로고
    • Processing of C3bopsonized immune complexes bound to non-complement receptor 1 (CR1) sites on red cells: Phagocytosis, transfer, and associations with CR1
    • Craig ML, Waitumbi JN, Taylor RP. Processing of C3bopsonized immune complexes bound to non-complement receptor 1 (CR1) sites on red cells: phagocytosis, transfer, and associations with CR1. J. Immunol. 174(5), 3059-3066 (2005).
    • (2005) J. Immunol , vol.174 , Issue.5 , pp. 3059-3066
    • Craig, M.L.1    Waitumbi, J.N.2    Taylor, R.P.3
  • 172
    • 0031022953 scopus 로고    scopus 로고
    • Immune complexes bound to the primate erythrocyte complement receptor (CR1) via anti-CR1 mAbs are cleared simultaneously with loss of CR1 in a concerted reaction in a rhesus monkey model
    • Taylor RP, Ferguson PJ, Martin EN et al. Immune complexes bound to the primate erythrocyte complement receptor (CR1) via anti-CR1 mAbs are cleared simultaneously with loss of CR1 in a concerted reaction in a rhesus monkey model. Clin. Immunol. Immunopathol. 82(1), 49-59 (1997).
    • (1997) Clin. Immunol. Immunopathol , vol.82 , Issue.1 , pp. 49-59
    • Taylor, R.P.1    Ferguson, P.J.2    Martin, E.N.3
  • 173
    • 0028997991 scopus 로고
    • Antigenbased heteropolymers facilitate, via primate erythrocyte complement receptor type 1, rapid erythrocyte binding of an autoantibody and its clearance from the circulation in rhesus monkeys
    • Ferguson PJ, Martin EN, Greene KL et al. Antigenbased heteropolymers facilitate, via primate erythrocyte complement receptor type 1, rapid erythrocyte binding of an autoantibody and its clearance from the circulation in rhesus monkeys. J. Immunol. 155(1), 339-347 (1995).
    • (1995) J. Immunol. , vol.155 , Issue.1 , pp. 339-347
    • Ferguson, P.J.1    Martin, E.N.2    Greene, K.L.3
  • 174
    • 0035882036 scopus 로고    scopus 로고
    • Targeting of Pseudomonas aeruginosa in the bloodstream with bispecific monoclonal antibodies
    • Lindorfer MA, Nardin A, Foley PL et al. Targeting of Pseudomonas aeruginosa in the bloodstream with bispecific monoclonal antibodies. J. Immunol. 167(4), 2240-2249 (2001).
    • (2001) J. Immunol , vol.167 , Issue.4 , pp. 2240-2249
    • Lindorfer, M.A.1    Nardin, A.2    Foley, P.L.3
  • 175
    • 0027932831 scopus 로고
    • Cross-linked bispecific monoclonal antibody heteropolymers facilitate the clearance of human IGM from the circulation of squirrel monkeys
    • Reist CJ, Liang HY, Denny D, Martin EN, Scheld WM, Taylor RP. Cross-linked bispecific monoclonal antibody heteropolymers facilitate the clearance of human IgM from the circulation of squirrel monkeys. Eur. J. Immunol. 24(9), 2018-2025 (1994).
    • (1994) Eur. J. Immunol , vol.24 , Issue.9 , pp. 2018-2025
    • Reist, C.J.1    Liang, H.Y.2    Denny, D.3    Martin, E.N.4    Scheld, W.M.5    Taylor, R.P.6
  • 176
    • 24644486865 scopus 로고    scopus 로고
    • The erythrocyte viral trap: Transgenic expression of viral receptor on erythrocytes attenuates coxsackievirus B infection
    • Asher DR, Cerny AM, Finberg RW. The erythrocyte viral trap: transgenic expression of viral receptor on erythrocytes attenuates coxsackievirus B infection. Proc. Natl Acad. Sci. USA 102(36), 12897-12902 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.36 , pp. 12897-12902
    • Asher, D.R.1    Cerny, A.M.2    Finberg, R.W.3
  • 177
    • 0035863785 scopus 로고    scopus 로고
    • Bispecific monoclonal antibodies mediate binding of dengue virus to erythrocytes in a monkey model of passive viremia
    • Hahn CS, French OG, Foley P, Martin EN, Taylor RP. Bispecific monoclonal antibodies mediate binding of dengue virus to erythrocytes in a monkey model of passive viremia. J. Immunol. 166(2), 1057-1065 (2001).
    • (2001) J. Immunol , vol.166 , Issue.2 , pp. 1057-1065
    • Hahn, C.S.1    French, O.G.2    Foley, P.3    Martin, E.N.4    Taylor, R.P.5
  • 178
    • 0031568096 scopus 로고    scopus 로고
    • Bispecific monoclonal antibody complexes bound to primate erythrocyte complement receptor 1 facilitate virus clearance in a monkey model
    • Taylor RP, Sutherland WM, Martin EN et al. Bispecific monoclonal antibody complexes bound to primate erythrocyte complement receptor 1 facilitate virus clearance in a monkey model. J. Immunol. 158(2), 842-850 (1997).
    • (1997) J. Immunol. , vol.158 , Issue.2 , pp. 842-850
    • Taylor, R.P.1    Sutherland, W.M.2    Martin, E.N.3
  • 179
    • 84887003085 scopus 로고    scopus 로고
    • Mechanisms of enhanced neutralization of botulinum neurotoxin by monoclonal antibodies conjugated to antibodies specific for the erythrocyte complement receptor
    • Sharma R, Zhao H, Al-Saleem FH et al. Mechanisms of enhanced neutralization of botulinum neurotoxin by monoclonal antibodies conjugated to antibodies specific for the erythrocyte complement receptor. Mol. Immunol. 57(2), 247-254 (2014).
    • (2014) Mol. Immunol. , vol.57 , Issue.2 , pp. 247-254
    • Sharma, R.1    Zhao, H.2    Al-Saleem, F.H.3
  • 180
    • 0032780458 scopus 로고    scopus 로고
    • Infusion of bispecific monoclonal antibody complexes into monkeys provides immunologic protection against later challenge with a model pathogen
    • Craig ML, Reinagel ML, Martin EN, Schlimgen R, Nardin A, Taylor RP. Infusion of bispecific monoclonal antibody complexes into monkeys provides immunologic protection against later challenge with a model pathogen. Clin. Immunol. 92(2), 170-180 (1999).
    • (1999) Clin. Immunol. , vol.92 , Issue.2 , pp. 170-180
    • Craig, M.L.1    Reinagel, M.L.2    Martin, E.N.3    Schlimgen, R.4    Nardin, A.5    Taylor, R.P.6
  • 181
    • 0028859797 scopus 로고
    • Antigen-based heteropolymers. A potential therapy for binding and clearing autoantibodies via erythrocyte CR1
    • Ferguson PJ, Reist CJ, Martin EN et al. Antigen-based heteropolymers. A potential therapy for binding and clearing autoantibodies via erythrocyte CR1. Arthritis Rheum. 38(2), 190-200 (1995).
    • (1995) Arthritis Rheum. , vol.38 , Issue.2 , pp. 190-200
    • Ferguson, P.J.1    Reist, C.J.2    Martin, E.N.3
  • 182
    • 0036865717 scopus 로고    scopus 로고
    • Evaluation of antigen-based heteropolymer for treatment of systemic lupus erythematosus in a nonhuman primate model
    • Pincus SE, Lukacher N, Mohamed N et al. Evaluation of antigen-based heteropolymer for treatment of systemic lupus erythematosus in a nonhuman primate model. Clin. Immunol. 105(2), 141-154 (2002).
    • (2002) Clin. Immunol. , vol.105 , Issue.2 , pp. 141-154
    • Pincus, S.E.1    Lukacher, N.2    Mohamed, N.3
  • 183
    • 0030843417 scopus 로고    scopus 로고
    • Monoclonal antibodymediated, complement-independent binding of human tumor necrosis factor-alpha to primate erythrocytes via complement receptor 1
    • Buster BL, Mattes KA, Scheld WM. Monoclonal antibodymediated, complement-independent binding of human tumor necrosis factor-alpha to primate erythrocytes via complement receptor 1. J. Infect. Dis. 176(4), 1041-1046 (1997).
    • (1997) J. Infect. Dis. , vol.176 , Issue.4 , pp. 1041-1046
    • Buster, B.L.1    Mattes, K.A.2    Scheld, W.M.3
  • 184
    • 33748768760 scopus 로고    scopus 로고
    • Human complement receptor type 1-directed loading of tissue plasminogen activator on circulating erythrocytes for prophylactic fibrinolysis
    • Zaitsev S, Danielyan K, Murciano J-C et al. Human complement receptor type 1-directed loading of tissue plasminogen activator on circulating erythrocytes for prophylactic fibrinolysis. Blood 108(6), 1895-1902 (2006).
    • (2006) Blood , vol.108 , Issue.6 , pp. 1895-1902
    • Zaitsev, S.1    Danielyan, K.2    Murciano, J.-C.3
  • 185
    • 0026801368 scopus 로고
    • Red blood cell glycophorins
    • Chasis JA, Mohandas N. Red blood cell glycophorins. Blood 80(8), 1869-1879 (1992).
    • (1992) Blood , vol.80 , Issue.8 , pp. 1869-1879
    • Chasis, J.A.1    Mohandas, N.2
  • 186
    • 0028447611 scopus 로고
    • Some concepts relating to the molecular genetic basis of certain MNS blood group antigens
    • Reid ME. Some concepts relating to the molecular genetic basis of certain MNS blood group antigens. Transfus. Med. Oxf. Engl. 4(2), 99-111 (1994).
    • (1994) Transfus. Med. Oxf. Engl. , vol.4 , Issue.2 , pp. 99-111
    • Reid, M.E.1
  • 187
    • 0034102056 scopus 로고    scopus 로고
    • Red cell antigens on band 3 and glycophorin A
    • Poole J. Red cell antigens on band 3 and glycophorin A. Blood Rev. 14(1), 31-43 (2000).
    • (2000) Blood Rev. , vol.14 , Issue.1 , pp. 31-43
    • Poole, J.1
  • 188
    • 0027290454 scopus 로고
    • Recombinant miltenberger i and II human blood group antigens: The role of glycosylation in cell surface expression and antigenicity of glycophorin A
    • Ugorski M, Blackall DP, Påhlsson P, Shakin-Eshleman SH, Moore J, Spitalnik SL. Recombinant Miltenberger I and II human blood group antigens: the role of glycosylation in cell surface expression and antigenicity of glycophorin A. Blood 82(6), 1913-1920 (1993).
    • (1993) Blood , vol.82 , Issue.6 , pp. 1913-1920
    • Ugorski, M.1    Blackall, D.P.2    Påhlsson, P.3    Shakin-Eshleman, S.H.4    Moore, J.5    Spitalnik, S.L.6
  • 189
    • 0020679082 scopus 로고
    • The red cell membrane skeleton: Recent progress
    • Marchesi VT. The red cell membrane skeleton: recent progress. Blood 61(1), 1-11 (1983).
    • (1983) Blood , vol.61 , Issue.1 , pp. 1-11
    • Marchesi, V.T.1
  • 192
    • 16544378275 scopus 로고    scopus 로고
    • Purification, crystallization and x-ray diffraction analysis of a recombinant Fab that recognizes a human blood-group antigen
    • Song SC, Xie K, Czerwinski M, Spitalnik SL, Wedekind JE. Purification, crystallization and x-ray diffraction analysis of a recombinant Fab that recognizes a human blood-group antigen. Acta Crystallogr. D Biol. Crystallogr. 60(Pt 4), 788-791 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 788-791
    • Song, S.C.1    Xie, K.2    Czerwinski, M.3    Spitalnik, S.L.4    Wedekind, J.E.5
  • 193
    • 0032926939 scopus 로고    scopus 로고
    • A molecular approach for isolating high-affinity fab fragments that are useful in blood group serology
    • Czerwinski M, Krop-Watorek A, Siegel DL, Spitalnik SL. A molecular approach for isolating high-affinity Fab fragments that are useful in blood group serology. Transfusion 39(4), 364-371 (1999).
    • (1999) Transfusion , vol.39 , Issue.4 , pp. 364-371
    • Czerwinski, M.1    Krop-Watorek, A.2    Siegel, D.L.3    Spitalnik, S.L.4
  • 194
    • 77954687045 scopus 로고    scopus 로고
    • Sustained thromboprophylaxis mediated by an RBC-targeted prourokinase zymogen activated at the site of clot formation
    • Zaitsev S, Spitzer D, Murciano J-C et al. Sustained thromboprophylaxis mediated by an RBC-targeted prourokinase zymogen activated at the site of clot formation. Blood 115(25), 5241-5248 (2010).
    • (2010) Blood , vol.115 , Issue.25 , pp. 5241-5248
    • Zaitsev, S.1    Spitzer, D.2    Murciano, J.-C.3
  • 195
    • 28844498710 scopus 로고    scopus 로고
    • Endothelial targeting of a recombinant construct fusing a PECAM-1 single-chain variable antibody fragment (SCFV) with prourokinase facilitates prophylactic thrombolysis in the pulmonary vasculature
    • Ding B-S, Gottstein C, Grunow A et al. Endothelial targeting of a recombinant construct fusing a PECAM-1 single-chain variable antibody fragment (scFv) with prourokinase facilitates prophylactic thrombolysis in the pulmonary vasculature. Blood 106(13), 4191-4198 (2005).
    • (2005) Blood , vol.106 , Issue.13 , pp. 4191-4198
    • Ding, B.-S.1    Gottstein, C.2    Grunow, A.3
  • 196
    • 0025840611 scopus 로고
    • A recombinant chimeric plasminogen activator with high affinity for fibrin has increased thrombolytic potency in vitro and in vivo
    • Runge MS, Quertermous T, Zavodny PJ et al. A recombinant chimeric plasminogen activator with high affinity for fibrin has increased thrombolytic potency in vitro and in vivo. Proc. Natl Acad. Sci. USA 88(22), 10337-10341 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , Issue.22 , pp. 10337-10341
    • Runge, M.S.1    Quertermous, T.2    Zavodny, P.J.3
  • 197
    • 18244424748 scopus 로고    scopus 로고
    • A soluble recombinant multimeric anti-Rh(D) single-chain Fv/CR1 molecule restores the immune complex binding ability of CR1-deficient erythrocytes
    • Oudin S, Libyh MT, Goossens D et al. A soluble recombinant multimeric anti-Rh(D) single-chain Fv/CR1 molecule restores the immune complex binding ability of CR1-deficient erythrocytes. J. Immunol. 164(3), 1505-1513 (2000).
    • (2000) J. Immunol. , vol.164 , Issue.3 , pp. 1505-1513
    • Oudin, S.1    Libyh, M.T.2    Goossens, D.3
  • 198
    • 0942263632 scopus 로고    scopus 로고
    • The monoclonal antibody TER-119 recognizes a molecule associated with glycophorin A and specifically marks the late stages of murine erythroid lineage
    • Kina T, Ikuta K, Takayama E et al. The monoclonal antibody TER-119 recognizes a molecule associated with glycophorin A and specifically marks the late stages of murine erythroid lineage. Br. J. Haematol. 109(2), 280-287 (2000).
    • (2000) Br. J. Haematol. , vol.109 , Issue.2 , pp. 280-287
    • Kina, T.1    Ikuta, K.2    Takayama, E.3
  • 199
    • 28244463961 scopus 로고    scopus 로고
    • Vivo correction of complement regulatory protein deficiency with an inhibitor targeting the red blood cell membrane
    • Spitzer D, Unsinger J, Mao D, Wu X, Molina H, Atkinson JP. In vivo correction of complement regulatory protein deficiency with an inhibitor targeting the red blood cell membrane. J. Immunol. 175(11), 7763-7770 (2005).
    • (2005) J. Immunol. , vol.175 , Issue.11 , pp. 7763-7770
    • Spitzer, D.1    Unsinger, J.2    Mao, D.3    Wu, X.4    Molina, H.5    Atkinson, J.P.6
  • 200
    • 33749506251 scopus 로고    scopus 로고
    • Cutting edge: Treatment of complement regulatory protein deficiency by retroviral in vivo gene therapy
    • Spitzer D, Wu X, Ma X, Xu L, Ponder KP, Atkinson JP. Cutting edge: treatment of complement regulatory protein deficiency by retroviral in vivo gene therapy. J. Immunol. 177(8), 4953-4956 (2006).
    • (2006) J. Immunol. , vol.177 , Issue.8 , pp. 4953-4956
    • Spitzer, D.1    Wu, X.2    Ma, X.3    Xu, L.4    Ponder, K.P.5    Atkinson, J.P.6
  • 201
    • 77249117354 scopus 로고    scopus 로고
    • Targeting of a mutant plasminogen activator to circulating red blood cells for prophylactic fibrinolysis
    • Zaitsev S, Spitzer D, Murciano J-C et al. Targeting of a Mutant Plasminogen Activator to Circulating Red Blood Cells for Prophylactic Fibrinolysis. J. Pharmacol. Exp. Ther. 332(3), 1022-1031 (2010).
    • (2010) J. Pharmacol. Exp. Ther. , vol.332 , Issue.3 , pp. 1022-1031
    • Zaitsev, S.1    Spitzer, D.2    Murciano, J.-C.3
  • 202
    • 0023924509 scopus 로고
    • A role for thrombomodulin in the pathogenesis of thrombin-induced thromboembolism in mice
    • Kumada T, Dittman WA, Majerus PW. A role for thrombomodulin in the pathogenesis of thrombin-induced thromboembolism in mice. Blood 71(3), 728-733 (1988).
    • (1988) Blood , vol.71 , Issue.3 , pp. 728-733
    • Kumada, T.1    Dittman, W.A.2    Majerus, P.W.3
  • 203
    • 84861206965 scopus 로고    scopus 로고
    • Targeting recombinant thrombomodulin fusion protein to red blood cells provides multifaceted thromboprophylaxis
    • Zaitsev S, Kowalska MA, Neyman M et al. Targeting recombinant thrombomodulin fusion protein to red blood cells provides multifaceted thromboprophylaxis. Blood 119(20), 4779-4785 (2012).
    • (2012) Blood , vol.119 , Issue.20 , pp. 4779-4785
    • Zaitsev, S.1    Kowalska, M.A.2    Neyman, M.3
  • 204
    • 84871965318 scopus 로고    scopus 로고
    • Engineering antigens for in situ erythrocyte binding induces T-cell deletion
    • Kontos S, Kourtis IC, Dane KY, Hubbell JA. Engineering antigens for in situ erythrocyte binding induces T-cell deletion. Proc. Natl Acad. Sci. USA 110(1), E60-E68 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , Issue.1 , pp. E60-E68
    • Kontos, S.1    Kourtis, I.C.2    Dane, K.Y.3    Hubbell, J.A.4
  • 205
    • 1942509539 scopus 로고    scopus 로고
    • Red blood cell blood group antigens: Structure and function
    • Reid ME, Mohandas N. Red blood cell blood group antigens: structure and function. Semin. Hematol. 41(2), 93-117 (2004).
    • (2004) Semin. Hematol. , vol.41 , Issue.2 , pp. 93-117
    • Reid, M.E.1    Mohandas, N.2
  • 207
    • 77954737068 scopus 로고    scopus 로고
    • The relationship between blood groups and disease
    • Anstee DJ. The relationship between blood groups and disease. Blood 115(23), 4635-4643 (2010).
    • (2010) Blood , vol.115 , Issue.23 , pp. 4635-4643
    • Anstee, D.J.1
  • 208
    • 84942477434 scopus 로고
    • AN unusual case of intra-group agglutination
    • Levine P, Stetson RE. AN unusual case of intra-group agglutination. J. Am. Med. Assoc. 113(2), 126-127 (1939).
    • (1939) J. Am. Med. Assoc. , vol.113 , Issue.2 , pp. 126-127
    • Levine, P.1    Stetson, R.E.2
  • 209
    • 84964093882 scopus 로고
    • An agglutinable factor in human blood recognized by immune sera for rhesus blood
    • Landsteiner K, Wiener AS. An agglutinable factor in human blood recognized by immune sera for rhesus blood. Exp. Biol. Med. 43(1), 223-223 (1940).
    • (1940) Exp. Biol. Med. , vol.43 , Issue.1 , pp. 223-223
    • Landsteiner, K.1    Wiener, A.S.2
  • 210
    • 0034651012 scopus 로고    scopus 로고
    • The Rh blood group system: A review
    • Avent ND, Reid ME. The Rh blood group system: a review. Blood 95(2), 375-387 (2000).
    • (2000) Blood , vol.95 , Issue.2 , pp. 375-387
    • Avent, N.D.1    Reid, M.E.2
  • 212
    • 0032527131 scopus 로고    scopus 로고
    • Rhnull disease: The amorph type results from a novel double mutation in RhCe gene on D-negative background
    • Huang CH, Chen Y, Reid ME, Seidl C. Rhnull disease: the amorph type results from a novel double mutation in RhCe gene on D-negative background. Blood 92(2), 664-671 (1998).
    • (1998) Blood , vol.92 , Issue.2 , pp. 664-671
    • Huang, C.H.1    Chen, Y.2    Reid, M.E.3    Seidl, C.4
  • 213
    • 0036682963 scopus 로고    scopus 로고
    • Cell-surface expression of RhD blood group polypeptide is posttranscriptionally regulated by the RhAG glycoprotein
    • Mouro-Chanteloup I, D'Ambrosio AM, Gane P et al. Cell-surface expression of RhD blood group polypeptide is posttranscriptionally regulated by the RhAG glycoprotein. Blood 100(3), 1038-1047 (2002).
    • (2002) Blood , vol.100 , Issue.3 , pp. 1038-1047
    • Mouro-Chanteloup, I.1    D'Ambrosio, A.M.2    Gane, P.3
  • 214
    • 0025024967 scopus 로고
    • Molecular cloning and protein structure of a human blood group Rh polypeptide
    • Chérif-Zahar B, Bloy C, Le Van Kim C et al. Molecular cloning and protein structure of a human blood group Rh polypeptide. Proc. Natl Acad. Sci. USA 87(16), 6243-6247 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , Issue.16 , pp. 6243-6247
    • Chérif-Zahar, B.1    Bloy, C.2    Le Van Kim, C.3
  • 215
    • 0035053248 scopus 로고    scopus 로고
    • New insights into the Rh superfamily of genes and proteins in erythroid cells and nonerythroid tissues
    • Huang C-H, Liu PZ. New insights into the Rh superfamily of genes and proteins in erythroid cells and nonerythroid tissues. Blood Cells. Mol. Dis. 27(1), 90-101 (2001).
    • (2001) Blood Cells. Mol. Dis. , vol.27 , Issue.1 , pp. 90-101
    • Huang, C.-H.1    Liu, P.Z.2
  • 216
    • 84886874276 scopus 로고    scopus 로고
    • High prevalence of red blood cell alloimmunization in sickle cell disease despite transfusion from Rh-matched minority donors
    • Chou ST, Jackson T, Vege S, Smith-Whitley K, Friedman DF, Westhoff CM. High prevalence of red blood cell alloimmunization in sickle cell disease despite transfusion from Rh-matched minority donors. Blood 122(6), 1062-1071 (2013).
    • (2013) Blood , vol.122 , Issue.6 , pp. 1062-1071
    • Chou, S.T.1    Jackson, T.2    Vege, S.3    Smith-Whitley, K.4    Friedman, D.F.5    Westhoff, C.M.6
  • 217
    • 0023890146 scopus 로고
    • Murine monoclonal antibodies associated with Rh17, Rh29, and Rh46 antigens
    • Rouger P, Edelman L. Murine monoclonal antibodies associated with Rh17, Rh29, and Rh46 antigens. Transfusion 28(1), 52-55 (1988).
    • (1988) Transfusion , vol.28 , Issue.1 , pp. 52-55
    • Rouger, P.1    Edelman, L.2
  • 218
    • 0023128759 scopus 로고
    • Hematological aspect of Rh deficiency syndrome: A case report and a review of the literature
    • Nash R, Shojania AM. Hematological aspect of Rh deficiency syndrome: a case report and a review of the literature. Am. J. Hematol. 24(3), 267-275 (1987).
    • (1987) Am. J. Hematol. , vol.24 , Issue.3 , pp. 267-275
    • Nash, R.1    Shojania, A.M.2
  • 219
    • 74549187471 scopus 로고    scopus 로고
    • A new blood group system, RHAG: Three antigens resulting from amino acid substitutions in the Rh-associated glycoprotein
    • Tilley L, Green C, Poole J et al. A new blood group system, RHAG: three antigens resulting from amino acid substitutions in the Rh-associated glycoprotein. Vox Sang. 98(2), 151-159 (2010).
    • (2010) Vox Sang. , vol.98 , Issue.2 , pp. 151-159
    • Tilley, L.1    Green, C.2    Poole, J.3
  • 220
    • 77953097228 scopus 로고    scopus 로고
    • Function of human Rh based on structure of RhCG at 2. 1 A
    • Gruswitz F, Chaudhary S, Ho JD et al. Function of human Rh based on structure of RhCG at 2. 1 A. Proc. Natl Acad. Sci. USA 107(21), 9638-9643 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , Issue.21 , pp. 9638-9643
    • Gruswitz, F.1    Chaudhary, S.2    Ho, J.D.3
  • 221
    • 0038486939 scopus 로고    scopus 로고
    • The Rh complex exports ammonium from human red blood cells
    • Hemker MB, Cheroutre G, van Zwieten R et al. The Rh complex exports ammonium from human red blood cells. Br. J. Haematol. 122(2), 333-340 (2003).
    • (2003) Br. J. Haematol. , vol.122 , Issue.2 , pp. 333-340
    • Hemker, M.B.1    Cheroutre, G.2    Van Zwieten, R.3
  • 222
    • 23844557874 scopus 로고    scopus 로고
    • Deciphering the function of the Rh family of proteins
    • Westhoff CM. Deciphering the function of the Rh family of proteins. Transfusion 45(2 Suppl. ), S117-S121 (2005).
    • (2005) Transfusion , vol.45 , Issue.2 , pp. S117-S121
    • Westhoff, C.M.1
  • 223
    • 0027616610 scopus 로고
    • Monoclonal antibodies against Kell glycoprotein: Serology, immunochemistry and quantification of antigen sites
    • Parsons SF, Gardner B, Anstee DJ. Monoclonal antibodies against Kell glycoprotein: serology, immunochemistry and quantification of antigen sites. Transfus. Med. Oxf. Engl. 3(2), 137-142 (1993).
    • (1993) Transfus. Med. Oxf. Engl. , vol.3 , Issue.2 , pp. 137-142
    • Parsons, S.F.1    Gardner, B.2    Anstee, D.J.3
  • 224
    • 34547789294 scopus 로고    scopus 로고
    • MCLEOD syndrome: A neurohaematological disorder: MCLEOD syndrome
    • Jung HH, Danek A, Frey BM. McLeod syndrome: a neurohaematological disorder: McLeod syndrome. Vox Sang. 93(2), 112-121 (2007).
    • (2007) Vox Sang. , vol.93 , Issue.2 , pp. 112-121
    • Jung, H.H.1    Danek, A.2    Frey, B.M.3
  • 225
    • 0031466796 scopus 로고    scopus 로고
    • The structure and function of band 3 (AE1): Recent developments (review)
    • Tanner MJ. The structure and function of band 3 (AE1): recent developments (review). Mol. Membr. Biol. 14(4), 155-165 (1997).
    • (1997) Mol. Membr. Biol. , vol.14 , Issue.4 , pp. 155-165
    • Tanner, M.J.1
  • 227
    • 16044367177 scopus 로고    scopus 로고
    • (band 3) is required to prevent erythrocyte membrane surface loss but not to form the membrane skeleton
    • (band 3) is required to prevent erythrocyte membrane surface loss but not to form the membrane skeleton. Cell 86(6), 917-927 (1996).
    • (1996) Cell , vol.86 , Issue.6 , pp. 917-927
  • 229
    • 84891516068 scopus 로고    scopus 로고
    • The Diego blood group system: A review
    • Figueroa D. The Diego blood group system: a review. Immunohematol. Am. Red Cross 29(2), 73-81 (2013).
    • (2013) Immunohematol. Am. Red Cross , vol.29 , Issue.2 , pp. 73-81
    • Figueroa, D.1
  • 230
    • 77649154817 scopus 로고    scopus 로고
    • MNS blood group system: A review
    • Reid ME. MNS blood group system: a review. Immunohematol. Am. Red Cross 25(3), 95-101 (2009).
    • (2009) Immunohematol. Am. Red Cross , vol.25 , Issue.3 , pp. 95-101
    • Reid, M.E.1
  • 231
    • 0022391958 scopus 로고
    • Erythrocyte membrane rigidity induced by glycophorin A-ligand interaction. Evidence for a ligand-induced association between glycophorin A and skeletal proteins
    • Chasis JA, Mohandas N, Shohet SB. Erythrocyte membrane rigidity induced by glycophorin A-ligand interaction. Evidence for a ligand-induced association between glycophorin A and skeletal proteins. J. Clin. Invest. 75(6), 1919-1926 (1985).
    • (1985) J. Clin. Invest , vol.75 , Issue.6 , pp. 1919-1926
    • Chasis, J.A.1    Mohandas, N.2    Shohet, S.B.3
  • 232
    • 0028330803 scopus 로고
    • Cooperative action between band 3 and glycophorin A in human erythrocytes: Immobilization of band 3 induced by antibodies to glycophorin A
    • Knowles DW, Chasis JA, Evans EA, Mohandas N. Cooperative action between band 3 and glycophorin A in human erythrocytes: immobilization of band 3 induced by antibodies to glycophorin A. Biophys. J. 66(5), 1726-1732 (1994).
    • (1994) Biophys. J. , vol.66 , Issue.5 , pp. 1726-1732
    • Knowles, D.W.1    Chasis, J.A.2    Evans, E.A.3    Mohandas, N.4
  • 234
    • 84872104874 scopus 로고    scopus 로고
    • Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains
    • Rungaldier S, Oberwagner W, Salzer U, Csaszar E, Prohaska R. Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Biochim. Biophys. Acta 1828(3), 956-966 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1828 , Issue.3 , pp. 956-966
    • Rungaldier, S.1    Oberwagner, W.2    Salzer, U.3    Csaszar, E.4    Prohaska, R.5
  • 236
    • 84877617414 scopus 로고    scopus 로고
    • Disruption of SMIM1 causes the Vel blood type
    • Ballif BA, Helias V, Peyrard T et al. Disruption of SMIM1 causes the Vel blood type. EMBO Mol. Med. 5(5), 751-761 (2013).
    • (2013) EMBO Mol. Med. , vol.5 , Issue.5 , pp. 751-761
    • Ballif, B.A.1    Helias, V.2    Peyrard, T.3
  • 237
    • 84878603453 scopus 로고    scopus 로고
    • Homozygosity for a null allele of SMIM1 defines the Vel-negative blood group phenotype
    • Storry JR, Jöud M, Christophersen MK et al. Homozygosity for a null allele of SMIM1 defines the Vel-negative blood group phenotype. Nat. Genet. 45(5), 537-541 (2013).
    • (2013) Nat. Genet. , vol.45 , Issue.5 , pp. 537-541
    • Storry, J.R.1    Jöud, M.2    Christophersen, M.K.3
  • 238
    • 84862777314 scopus 로고    scopus 로고
    • ABCB6 is dispensable for erythropoiesis and specifies the new blood group system Langereis
    • Helias V, Saison C, Ballif BA et al. ABCB6 is dispensable for erythropoiesis and specifies the new blood group system Langereis. Nat. Genet. 44(2), 170-173 (2012).
    • (2012) Nat. Genet. , vol.44 , Issue.2 , pp. 170-173
    • Helias, V.1    Saison, C.2    Ballif, B.A.3
  • 239
    • 0021809144 scopus 로고
    • Red cell alloantibodies in thalassemia major. Results of an Italian cooperative study
    • Sirchia G, Zanella A, Parravicini A, Morelati F, Rebulla P, Masera G. Red cell alloantibodies in thalassemia major. Results of an Italian cooperative study. Transfusion 25(2), 110-112 (1985).
    • (1985) Transfusion , vol.25 , Issue.2 , pp. 110-112
    • Sirchia, G.1    Zanella, A.2    Parravicini, A.3    Morelati, F.4    Rebulla, P.5    Masera, G.6
  • 240
  • 241
    • 0017357632 scopus 로고
    • Role of sialic acid in survival of erythrocytes in the circulation: Interaction of neuraminidase-treated and untreated erythrocytes with spleen and liver at the cellular level
    • Aminoff D, Bruegge WF, Bell WC, Sarpolis K, Williams R. Role of sialic acid in survival of erythrocytes in the circulation: interaction of neuraminidase-treated and untreated erythrocytes with spleen and liver at the cellular level. Proc. Natl Acad. Sci. USA 74(4), 1521-1524 (1977).
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , Issue.4 , pp. 1521-1524
    • Aminoff, D.1    Bruegge, W.F.2    Bell, W.C.3    Sarpolis, K.4    Williams, R.5
  • 242
    • 0025735940 scopus 로고
    • Single-unit transfusions of RBC enzymatically converted from group B to group O to A and O normal volunteers
    • Lenny LL, Hurst R, Goldstein J, Benjamin LJ, Jones RL. Single-unit transfusions of RBC enzymatically converted from group B to group O to A and O normal volunteers. Blood 77(6), 1383-1388 (1991).
    • (1991) Blood , vol.77 , Issue.6 , pp. 1383-1388
    • Lenny, L.L.1    Hurst, R.2    Goldstein, J.3    Benjamin, L.J.4    Jones, R.L.5
  • 243
    • 0028213906 scopus 로고
    • Transfusions to group O subjects of 2 units of red cells enzymatically converted from group B to group O
    • Lenny LL, Hurst R, Goldstein J, Galbraith RA. Transfusions to group O subjects of 2 units of red cells enzymatically converted from group B to group O. Transfusion 34(3), 209-214 (1994).
    • (1994) Transfusion , vol.34 , Issue.3 , pp. 209-214
    • Lenny, L.L.1    Hurst, R.2    Goldstein, J.3    Galbraith, R.A.4
  • 244
    • 0029555428 scopus 로고
    • Multiple-unit and second transfusions of red cells enzymatically converted from group B to group O: Report on the end of phase 1 trials
    • Lenny LL, Hurst R, Zhu A, Goldstein J, Galbraith RA. Multiple-unit and second transfusions of red cells enzymatically converted from group B to group O: report on the end of phase 1 trials. Transfusion 35(11), 899-902 (1995).
    • (1995) Transfusion , vol.35 , Issue.11 , pp. 899-902
    • Lenny, L.L.1    Hurst, R.2    Zhu, A.3    Goldstein, J.4    Galbraith, R.A.5
  • 245
    • 0033725180 scopus 로고    scopus 로고
    • Transfusion to blood group A and O patients of group B RBCs that have been enzymatically converted to group O
    • Kruskall MS, AuBuchon JP, Anthony KY et al. Transfusion to blood group A and O patients of group B RBCs that have been enzymatically converted to group O. Transfusion 40(11), 1290-1298 (2000).
    • (2000) Transfusion , vol.40 , Issue.11 , pp. 1290-1298
    • Kruskall, M.S.1    AuBuchon, J.P.2    Anthony, K.Y.3
  • 246
    • 0025939630 scopus 로고
    • Deantigenation of human erythrocytes by bacterial glycosidases-evidence for the noninvolvement of mediumsized glycosphingolipids in the dolichos biflorus lectin hemagglutination
    • Falk P, Hoskins LC, Lindstedt R, Svanborg C, Larson G. Deantigenation of human erythrocytes by bacterial glycosidases-evidence for the noninvolvement of mediumsized glycosphingolipids in the Dolichos biflorus lectin hemagglutination. Arch. Biochem. Biophys. 290(2), 312-319 (1991).
    • (1991) Arch. Biochem. Biophys. , vol.290 , Issue.2 , pp. 312-319
    • Falk, P.1    Hoskins, L.C.2    Lindstedt, R.3    Svanborg, C.4    Larson, G.5
  • 247
    • 0021726464 scopus 로고
    • Preparation of transfusable red cells by enzymatic conversion
    • Goldstein J. Preparation of transfusable red cells by enzymatic conversion. Prog. Clin. Biol. Res. 165, 139-157 (1984).
    • (1984) Prog. Clin. Biol. Res. , vol.165 , pp. 139-157
    • Goldstein, J.1
  • 248
    • 0024702064 scopus 로고
    • Conversion of ABO blood groups
    • Goldstein J. Conversion of ABO blood groups. Transfus. Med. Rev. 3(3), 206-212 (1989).
    • (1989) Transfus. Med. Rev. , vol.3 , Issue.3 , pp. 206-212
    • Goldstein, J.1
  • 249
    • 0026746041 scopus 로고
    • Purification and characterization of N-acetyl-alpha-D-galactosaminidase from Gallus domesticus
    • Hata J, Dhar M, Mitra M et al. Purification and characterization of N-acetyl-alpha-D-galactosaminidase from Gallus domesticus. Biochem. Int. 28(1), 77-86 (1992).
    • (1992) Biochem. Int. , vol.28 , Issue.1 , pp. 77-86
    • Hata, J.1    Dhar, M.2    Mitra, M.3
  • 250
    • 0034934003 scopus 로고    scopus 로고
    • Changes in immunologic properties of group A RBCS during treatment with an A-degrading exo-N-acetylgalactosaminidase
    • Hoskins LC, Boulding ET. Changes in immunologic properties of group A RBCs during treatment with an A-degrading exo-N-acetylgalactosaminidase. Transfusion 41(7), 908-916 (2001).
    • (2001) Transfusion , vol.41 , Issue.7 , pp. 908-916
    • Hoskins, L.C.1    Boulding, E.T.2
  • 251
    • 0031003711 scopus 로고    scopus 로고
    • Purification and characterization of blood group A-degrading isoforms of alpha-N-acetylgalactosaminidase from Ruminococcus torques strain IX-70
    • Hoskins LC, Boulding ET, Larson G. Purification and characterization of blood group A-degrading isoforms of alpha-N-acetylgalactosaminidase from Ruminococcus torques strain IX-70. J. Biol. Chem. 272(12), 7932-7939 (1997).
    • (1997) J. Biol. Chem. , vol.272 , Issue.12 , pp. 7932-7939
    • Hoskins, L.C.1    Boulding, E.T.2    Larson, G.3
  • 252
    • 0037384867 scopus 로고    scopus 로고
    • Clostridium perfringens alpha-N-acetylgalactosaminidase blood group A2-degrading activity
    • Hsieh H-Y, Smith D. Clostridium perfringens alpha-N-acetylgalactosaminidase blood group A2-degrading activity. Biotechnol. Appl. Biochem. 37(2), 157-163 (2003).
    • (2003) Biotechnol. Appl. Biochem. , vol.37 , Issue.2 , pp. 157-163
    • Hsieh, H.-Y.1    Smith, D.2
  • 253
    • 0026504157 scopus 로고
    • Blood substitutes, present and future perspectives [internet] nacetylgalactosaminidase from acremonium SP
    • Izumi K, Yamamoto K, Tochikura T, Hirabayashi Y. Blood substitutes, present and future perspectives [Internet] Nacetylgalactosaminidase from Acremonium sp. Biochim. Biophys. Acta 1116(1), 72-74 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1116 , Issue.1 , pp. 72-74
    • Izumi, K.1    Yamamoto, K.2    Tochikura, T.3    Hirabayashi, Y.4
  • 254
    • 0030444332 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant alpha-Nacetylgalactosaminidase produced in the yeast Pichia pastoris
    • Zhu A, Monahan C, Wang ZK, Goldstein J. Expression, purification, and characterization of recombinant alpha-Nacetylgalactosaminidase produced in the yeast Pichia pastoris. Protein Expr. Purif. 8(4), 456-462 (1996).
    • (1996) Protein Expr. Purif. , vol.8 , Issue.4 , pp. 456-462
    • Zhu, A.1    Monahan, C.2    Wang, Z.K.3    Goldstein, J.4
  • 255
    • 34147142476 scopus 로고    scopus 로고
    • Bacterial glycosidases for the production of universal red blood cells
    • Liu QP, Sulzenbacher G, Yuan H et al. Bacterial glycosidases for the production of universal red blood cells. Nat. Biotechnol. 25(4), 454-464 (2007).
    • (2007) Nat. Biotechnol. , vol.25 , Issue.4 , pp. 454-464
    • Liu, Q.P.1    Sulzenbacher, G.2    Yuan, H.3
  • 256
    • 36849021005 scopus 로고    scopus 로고
    • Modifying the red cell surface: Towards an ABO-universal blood supply
    • Olsson ML, Clausen H. Modifying the red cell surface: towards an ABO-universal blood supply. Br. J. Haematol. 140(1), 3-12 (2008).
    • (2008) Br. J. Haematol. , vol.140 , Issue.1 , pp. 3-12
    • Olsson, M.L.1    Clausen, H.2
  • 257
    • 85153867400 scopus 로고    scopus 로고
    • Blood substitutes, present and future perspectives [Internet]
    • Tsuchida E. Blood Substitutes, Present and Future Perspectives [Internet]. Elsevier Science http://books. google. com/books?id=IvnREjqUiKIC
    • Elsevier Science
    • Tsuchida, E.1
  • 258
    • 0030987476 scopus 로고    scopus 로고
    • Covalent binding of poly(ethylene glycol) (PEG) to the surface of red blood cells inhibits aggregation and reduces low shear blood viscosity
    • Armstrong JK, Meiselman HJ, Fisher TC. Covalent binding of poly(ethylene glycol) (PEG) to the surface of red blood cells inhibits aggregation and reduces low shear blood viscosity. Am. J. Hematol. 56(1), 26-28 (1997).
    • (1997) Am. J. Hematol , vol.56 , Issue.1 , pp. 26-28
    • Armstrong, J.K.1    Meiselman, H.J.2    Fisher, T.C.3
  • 259
    • 0033559323 scopus 로고    scopus 로고
    • Structural and functional consequences of antigenic modulation of red blood cells with methoxypoly(ethylene glycol)
    • Murad KL, Mahany KL, Brugnara C, Kuypers FA, Eaton JW, Scott MD. Structural and functional consequences of antigenic modulation of red blood cells with methoxypoly(ethylene glycol). Blood 93(6), 2121-2127 (1999).
    • (1999) Blood , vol.93 , Issue.6 , pp. 2121-2127
    • Murad, K.L.1    Mahany, K.L.2    Brugnara, C.3    Kuypers, F.A.4    Eaton, J.W.5    Scott, M.D.6
  • 261
    • 79960109503 scopus 로고    scopus 로고
    • Polymer-mediated immunocamouflage of red blood cells: Effects of polymer size on antigenic and immunogenic recognition of allogeneic donor blood cells
    • Wang D, Kyluik DL, Murad KL, Toyofuku WM, Scott MD. Polymer-mediated immunocamouflage of red blood cells: effects of polymer size on antigenic and immunogenic recognition of allogeneic donor blood cells. Sci. China Life Sci. 54(7), 589-598 (2011).
    • (2011) Sci. China Life Sci. , vol.54 , Issue.7 , pp. 589-598
    • Wang, D.1    Kyluik, D.L.2    Murad, K.L.3    Toyofuku, W.M.4    Scott, M.D.5
  • 262
    • 0037066591 scopus 로고    scopus 로고
    • Biophysical consequences of linker chemistry and polymer size on stealth erythrocytes: Size does matter
    • Bradley AJ, Murad KL, Regan KL, Scott MD. Biophysical consequences of linker chemistry and polymer size on stealth erythrocytes: size does matter. Biochim. Biophys. Acta 1561(2), 147-158 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1561 , Issue.2 , pp. 147-158
    • Bradley, A.J.1    Murad, K.L.2    Regan, K.L.3    Scott, M.D.4
  • 263
    • 0035736794 scopus 로고    scopus 로고
    • Electrophoretic mobility of human red blood cells coated with poly(ethylene glycol)
    • Neu B, Armstrong JK, Fisher TC, Bäumler H, Meiselman HJ. Electrophoretic mobility of human red blood cells coated with poly(ethylene glycol). Biorheology 38(5-6), 389-403 (2001).
    • (2001) Biorheology , vol.38 , Issue.5-6 , pp. 389-403
    • Neu, B.1    Armstrong, J.K.2    Fisher, T.C.3    Bäumler, H.4    Meiselman, H.J.5
  • 265
    • 76749104653 scopus 로고    scopus 로고
    • Adsorption of amphiphilic hyperbranched polyglycerol derivatives onto human red blood cells
    • Liu Z, Janzen J, Brooks DE. Adsorption of amphiphilic hyperbranched polyglycerol derivatives onto human red blood cells. Biomaterials 31(12), 3364-3373 (2010).
    • (2010) Biomaterials , vol.31 , Issue.12 , pp. 3364-3373
    • Liu, Z.1    Janzen, J.2    Brooks, D.E.3
  • 266
    • 84871663837 scopus 로고    scopus 로고
    • Effects of amphiphilic star-shaped poly(ethylene glycol) polymers with a cholic acid core on human red blood cell aggregation
    • Janvier F, Zhu JXX, Armstrong J, Meiselman HJ, Cloutier G. Effects of amphiphilic star-shaped poly(ethylene glycol) polymers with a cholic acid core on human red blood cell aggregation. J. Mech. Behav. Biomed. Mater. 18, 100-107 (2013).
    • (2013) J. Mech. Behav. Biomed. Mater. , vol.18 , pp. 100-107
    • Janvier, F.1    Zhu, J.X.X.2    Armstrong, J.3    Meiselman, H.J.4    Cloutier, G.5
  • 267
    • 2942679255 scopus 로고    scopus 로고
    • Causative factors behind poloxamer 188 (pluronic f68, flocor)-induced complement activation in human sera. A protective role against poloxamer-mediated complement activation by elevated serum lipoprotein levels
    • Moghimi SM, Hunter AC, Dadswell CM, Savay S, Alving CR, Szebeni J. Causative factors behind poloxamer 188 (Pluronic F68, Flocor)-induced complement activation in human sera. A protective role against poloxamer-mediated complement activation by elevated serum lipoprotein levels. Biochim. Biophys. Acta 1689(2), 103-113 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1689 , Issue.2 , pp. 103-113
    • Moghimi, S.M.1    Hunter, A.C.2    Dadswell, C.M.3    Savay, S.4    Alving, C.R.5    Szebeni, J.6
  • 268
    • 28244466864 scopus 로고    scopus 로고
    • Complement activation-related pseudoallergy: A new class of drug-induced acute immune toxicity
    • Szebeni J. Complement activation-related pseudoallergy: a new class of drug-induced acute immune toxicity. Toxicology 216(2-3), 106-121 (2005).
    • (2005) Toxicology , vol.216 , Issue.2-3 , pp. 106-121
    • Szebeni, J.1
  • 269
    • 84887020966 scopus 로고    scopus 로고
    • Comparative efficacy of blood cell immunocamouflage by membrane grafting of methoxypoly(ethylene glycol) and polyethyloxazoline
    • Kyluik-Price DL, Li L, Scott MD. Comparative efficacy of blood cell immunocamouflage by membrane grafting of methoxypoly(ethylene glycol) and polyethyloxazoline. Biomaterials 35(1), 412-422 (2014).
    • (2014) Biomaterials , vol.35 , Issue.1 , pp. 412-422
    • Kyluik-Price, D.L.1    Li, L.2    Scott, M.D.3
  • 270
    • 34250800861 scopus 로고    scopus 로고
    • Antibody against poly(ethylene glycol) adversely affects PEG-asparaginase therapy in acute lymphoblastic leukemia patients
    • Armstrong JK, Hempel G, Koling S et al. Antibody against poly(ethylene glycol) adversely affects PEG-asparaginase therapy in acute lymphoblastic leukemia patients. Cancer 110(1), 103-111 (2007).
    • (2007) Cancer , vol.110 , Issue.1 , pp. 103-111
    • Armstrong, J.K.1    Hempel, G.2    Koling, S.3
  • 271
    • 7544224443 scopus 로고    scopus 로고
    • Prolonged circulation of large polymeric nanoparticles by non-covalent adsorption on erythrocytes
    • Chambers E, Mitragotri S. Prolonged circulation of large polymeric nanoparticles by non-covalent adsorption on erythrocytes. J. Control. Release 100(1), 111-119 (2004).
    • (2004) J. Control. Release , vol.100 , Issue.1 , pp. 111-119
    • Chambers, E.1    Mitragotri, S.2
  • 272
    • 84891358668 scopus 로고    scopus 로고
    • Delivering nanoparticles to lungs while avoiding liver and spleen through adsorption on red blood cells
    • Anselmo AC, Gupta V, Zern BJ et al. Delivering nanoparticles to lungs while avoiding liver and spleen through adsorption on red blood cells. ACS Nano 7(12), 11129-11137 (2013).
    • (2013) ACS Nano , vol.7 , Issue.12 , pp. 11129-11137
    • Anselmo, A.C.1    Gupta, V.2    Zern, B.J.3
  • 273
    • 84866126975 scopus 로고    scopus 로고
    • Low modulus biomimetic microgel particles with high loading of hemoglobin
    • Chen K, Merkel TJ, Pandya A et al. Low modulus biomimetic microgel particles with high loading of hemoglobin. Biomacromolecules 13(9), 2748-2759 (2012).
    • (2012) Biomacromolecules , vol.13 , Issue.9 , pp. 2748-2759
    • Chen, K.1    Merkel, T.J.2    Pandya, A.3
  • 275
    • 79551679772 scopus 로고    scopus 로고
    • Using mechanobiological mimicry of red blood cells to extend circulation times of hydrogel microparticles
    • Merkel TJ, Jones SW, Herlihy KP et al. Using mechanobiological mimicry of red blood cells to extend circulation times of hydrogel microparticles. Proc. Natl. Acad. Sci. 108(2), 586-591 (2011).
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , Issue.2 , pp. 586-591
    • Merkel, T.J.1    Jones, S.W.2    Herlihy, K.P.3
  • 276
    • 84874169973 scopus 로고    scopus 로고
    • Minimal "self " peptides that inhibit phagocytic clearance and enhance delivery of nanoparticles
    • Rodriguez PL, Harada T, Christian DA, Pantano DA, Tsai RK, Discher DE. Minimal "self " peptides that inhibit phagocytic clearance and enhance delivery of nanoparticles. Science 339(6122), 971-975 (2013).
    • (2013) Science , vol.339 , Issue.6122 , pp. 971-975
    • Rodriguez, P.L.1    Harada, T.2    Christian, D.A.3    Pantano, D.A.4    Tsai, R.K.5    Discher, D.E.6
  • 277
    • 74849108786 scopus 로고    scopus 로고
    • Prevalence of human anti-mouse antibodies (HAMAS) in routine examinations
    • Koshida S, Asanuma K, Kuribayashi K et al. Prevalence of human anti-mouse antibodies (HAMAs) in routine examinations. Clin. Chim. Acta 411(5-6), 391-394 (2010).
    • (2010) Clin. Chim. Acta , vol.411 , Issue.5-6 , pp. 391-394
    • Koshida, S.1    Asanuma, K.2    Kuribayashi, K.3
  • 278
    • 0032814344 scopus 로고    scopus 로고
    • Human anti-animal antibody interferences in immunological assays
    • Kricka LJ. Human anti-animal antibody interferences in immunological assays. Clin. Chem. 45(7), 942-956 (1999).
    • (1999) Clin. Chem. , vol.45 , Issue.7 , pp. 942-956
    • Kricka, L.J.1
  • 279
    • 0025978976 scopus 로고
    • Man-made antibodies
    • Winter G, Milstein C. Man-made antibodies. Nature 349(6307), 293-299 (1991).
    • (1991) Nature , vol.349 , Issue.6307 , pp. 293-299
    • Winter, G.1    Milstein, C.2
  • 280
    • 77949886815 scopus 로고    scopus 로고
    • Progress in phage display: Evolution of the technique and its application
    • Bratkovic T. Progress in phage display: evolution of the technique and its application. Cell. Mol. Life Sci. CMLS 67(5), 749-767 (2010).
    • (2010) Cell. Mol. Life Sci. CMLS , vol.67 , Issue.5 , pp. 749-767
    • Bratkovic, T.1
  • 282
    • 34250616607 scopus 로고    scopus 로고
    • Phage display-based molecular methods in immunohematology
    • Siegel DL. Phage display-based molecular methods in immunohematology. Transfusion 47(1 Suppl. ), S89-S94 (2007).
    • (2007) Transfusion , vol.47 , pp. S89-S94
    • Siegel, D.L.1
  • 287
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith GP. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228(4705), 1315-1317 (1985).
    • (1985) Science , vol.228 , Issue.4705 , pp. 1315-1317
    • Smith, G.P.1
  • 288
    • 0025838698 scopus 로고
    • A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals
    • Burton DR, Barbas CF, Persson MA, Koenig S, Chanock RM, Lerner RA. A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. Proc. Natl Acad. Sci. USA 88(22), 10134-10137 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , Issue.22 , pp. 10134-10137
    • Burton, D.R.1    Barbas, C.F.2    Persson, M.A.3    Koenig, S.4    Chanock, R.M.5    Lerner, R.A.6
  • 289
    • 0026057989 scopus 로고
    • Generation of diverse high-affinity human monoclonal antibodies by repertoire cloning
    • Persson MA, Caothien RH, Burton DR. Generation of diverse high-affinity human monoclonal antibodies by repertoire cloning. Proc. Natl Acad. Sci. USA 88(6), 2432-2436 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , Issue.6 , pp. 2432-2436
    • Persson, M.A.1    Caothien, R.H.2    Burton, D.R.3
  • 290
    • 0032523202 scopus 로고    scopus 로고
    • Genetic and immunological properties of phage-displayed human anti-Rh(D) antibodies: Implications for Rh(D) epitope topology
    • Chang TY, Siegel DL. Genetic and immunological properties of phage-displayed human anti-Rh(D) antibodies: implications for Rh(D) epitope topology. Blood 91(8), 3066-3078 (1998).
    • (1998) Blood , vol.91 , Issue.8 , pp. 3066-3078
    • Chang, T.Y.1    Siegel, D.L.2
  • 291
    • 0035125517 scopus 로고    scopus 로고
    • Isolation of an IgG anti-B from a human Fab-phage display library
    • Chang TY, Siegel DL. Isolation of an IgG anti-B from a human Fab-phage display library. Transfusion 41(1), 6-12 (2001).
    • (2001) Transfusion , vol.41 , Issue.1 , pp. 6-12
    • Chang, T.Y.1    Siegel, D.L.2
  • 292
    • 0030766333 scopus 로고    scopus 로고
    • Isolation of cell surface-specific human monoclonal antibodies using phage display and magnetically-activated cell sorting: Applications in immunohematology
    • Siegel DL, Chang TY, Russell SL, Bunya VY. Isolation of cell surface-specific human monoclonal antibodies using phage display and magnetically-activated cell sorting: applications in immunohematology. J. Immunol. Methods 206(1-2), 73-85 (1997).
    • (1997) J. Immunol. Methods , vol.206 , Issue.1-2 , pp. 73-85
    • Siegel, D.L.1    Chang, T.Y.2    Russell, S.L.3    Bunya, V.Y.4
  • 293
    • 0028205271 scopus 로고
    • Expression and characterization of recombinant anti-Rh(D) antibodies on filamentous phage: A model system for isolating human red blood cell antibodies by repertoire cloning
    • Siegel DL, Silberstein LE. Expression and characterization of recombinant anti-Rh(D) antibodies on filamentous phage: a model system for isolating human red blood cell antibodies by repertoire cloning. Blood 83(8), 2334-2344 (1994).
    • (1994) Blood , vol.83 , Issue.8 , pp. 2334-2344
    • Siegel, D.L.1    Silberstein, L.E.2
  • 295
    • 60749123372 scopus 로고    scopus 로고
    • Modelling the human immune response: Performance of a 1011 human antibody repertoire against a broad panel of therapeutically relevant antigens
    • Lloyd C, Lowe D, Edwards B et al. Modelling the human immune response: performance of a 1011 human antibody repertoire against a broad panel of therapeutically relevant antigens. Protein Eng. Des. Sel. PEDS 22(3), 159-168 (2009).
    • (2009) Protein Eng. Des. Sel. PEDS , vol.22 , Issue.3 , pp. 159-168
    • Lloyd, C.1    Lowe, D.2    Edwards, B.3
  • 296
    • 38849154606 scopus 로고    scopus 로고
    • Application of phage display to high throughput antibody generation and characterization
    • Schofield DJ, Pope AR, Clementel V et al. Application of phage display to high throughput antibody generation and characterization. Genome Biol. 8(11), R254 (2007).
    • (2007) Genome Biol. , vol.8 , Issue.11 , pp. R254
    • Schofield, D.J.1    Pope, A.R.2    Clementel, V.3
  • 297
    • 0036364847 scopus 로고    scopus 로고
    • Error-prone polymerase chain reaction for modification of SCFVS
    • Martineau P. Error-prone polymerase chain reaction for modification of scFvs. In: Methods Mol. Biol. Clifton NJ. 178, 287-294 (2002).
    • (2002) Methods Mol. Biol. Clifton NJ , vol.178 , pp. 287-294
    • Martineau, P.1
  • 299
    • 28944441839 scopus 로고    scopus 로고
    • Humanization of chicken monoclonal antibody using phagedisplay system
    • Nishibori N, Horiuchi H, Furusawa S, Matsuda H. Humanization of chicken monoclonal antibody using phagedisplay system. Mol. Immunol. 43(6), 634-642 (2006).
    • (2006) Mol. Immunol , vol.43 , Issue.6 , pp. 634-642
    • Nishibori, N.H.1    Furusawa, S.2    Matsuda, H.3
  • 300
    • 0037225412 scopus 로고    scopus 로고
    • Rabbit immune repertoires as sources for therapeutic monoclonal antibodies: The impact of kappa allotype-correlated variation in cysteine content on antibody libraries selected by phage display
    • Popkov M, Mage RG, Alexander CB, Thundivalappil S, Barbas CF, Rader C. Rabbit immune repertoires as sources for therapeutic monoclonal antibodies: the impact of kappa allotype-correlated variation in cysteine content on antibody libraries selected by phage display. J. Mol. Biol. 325(2), 325-335 (2003).
    • (2003) J. Mol. Biol. , vol.325 , Issue.2 , pp. 325-335
    • Popkov, M.1    Mage, R.G.2    Alexander, C.B.3    Thundivalappil, S.4    Barbas, C.F.5    Rader, C.6
  • 301
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRS randomized with trinucleotides
    • Knappik A, Ge L, Honegger A et al. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J. Mol. Biol. 296(1), 57-86 (2000).
    • (2000) J. Mol. Biol. , vol.296 , Issue.1 , pp. 57-86
    • Knappik, A.1    Ge, L.2    Honegger, A.3
  • 302
    • 0035427605 scopus 로고    scopus 로고
    • High-throughput generation and engineering of recombinant human antibodies
    • Krebs B, Rauchenberger R, Reiffert S et al. High-throughput generation and engineering of recombinant human antibodies. J. Immunol. Methods 254(1-2), 67-84 (2001).
    • (2001) J. Immunol. Methods , vol.254 , Issue.1-2 , pp. 67-84
    • Krebs, B.1    Rauchenberger, R.2    Reiffert, S.3
  • 303
    • 0028141993 scopus 로고
    • Guiding the selection of human antibodies from phage display repertoires to a single epitope of an antigen
    • Jespers LS, Roberts A, Mahler SM, Winter G, Hoogenboom HR. Guiding the selection of human antibodies from phage display repertoires to a single epitope of an antigen. Biotechnol. Nat. Publ. Co. 12(9), 899-903 (1994).
    • (1994) Biotechnol. Nat. Publ. Co. , vol.12 , Issue.9 , pp. 899-903
    • Jespers, L.S.1    Roberts, A.2    Mahler, S.M.3    Winter, G.4    Hoogenboom, H.R.5
  • 304
    • 17644406997 scopus 로고    scopus 로고
    • From rodent reagents to human therapeutics using antibody guided selection
    • Osbourn J, Groves M, Vaughan T. From rodent reagents to human therapeutics using antibody guided selection. Methods San Diego Calif. 36(1), 61-68 (2005).
    • (2005) Methods San Diego Calif. , vol.36 , Issue.1 , pp. 61-68
    • Osbourn, J.1    Groves, M.2    Vaughan, T.3
  • 305
    • 84904284885 scopus 로고    scopus 로고
    • Engineered red blood cells as carriers for systemic delivery of a wide array of functional probes
    • Shi J, Kundrat L, Pishesha N et al. Engineered red blood cells as carriers for systemic delivery of a wide array of functional probes. Proc. Natl Acad. Sci. USA 111(28), 10131-10136 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , Issue.28 , pp. 10131-10136
    • Shi, J.1    Kundrat, L.2    Pishesha, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.