메뉴 건너뛰기




Volumn 1830, Issue 12, 2013, Pages 5435-5443

Albumin-drug interaction and its clinical implication

Author keywords

Binding site; Displacement; Extracorporeal albumin dialysis; Human serum albumin; Structure function relationship

Indexed keywords


EID: 84885375036     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.05.005     Document Type: Review
Times cited : (396)

References (125)
  • 3
    • 0036599564 scopus 로고    scopus 로고
    • Practical aspects of the ligand-binding and enzymatic properties of human serum albumin
    • DOI 10.1248/bpb.25.695
    • U. Kragh-Hansen, V.T.G. Chuang, and M. Otagiri Practical aspects of the ligand-binding and enzymatic properties of human serum albumin Biol. Pharm. Bull. 25 2002 695 704 (Pubitemid 40036701)
    • (2002) Biological and Pharmaceutical Bulletin , vol.25 , Issue.6 , pp. 695-704
    • Krach-Hansen, U.1    Chuang, V.T.G.2    Otagiri, M.3
  • 5
    • 33644687674 scopus 로고    scopus 로고
    • A molecular functional study on the interactions of drugs with plasma proteins
    • M. Otagiri A molecular functional study on the interactions of drugs with plasma proteins Drug Metab. Pharmacokinet. 20 2005 309 323
    • (2005) Drug Metab. Pharmacokinet. , vol.20 , pp. 309-323
    • Otagiri, M.1
  • 8
    • 0017229891 scopus 로고
    • Binding of drugs to serum albumin (first of two parts)
    • J. Koch-Weser, and E.M. Sellers Binding of drugs to serum albumin (first of two parts) N. Engl. J. Med. 294 1976 311 316
    • (1976) N. Engl. J. Med. , vol.294 , pp. 311-316
    • Koch-Weser, J.1    Sellers, E.M.2
  • 9
    • 78649706279 scopus 로고    scopus 로고
    • The effect of plasma protein binding on in vivo efficacy: Misconceptions in drug discovery
    • D.A. Smith, L. Di, and E.H. Kerns The effect of plasma protein binding on in vivo efficacy: misconceptions in drug discovery Nat. Rev. Drug Discov. 9 2010 929 939
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 929-939
    • Smith, D.A.1    Di, L.2    Kerns, E.H.3
  • 10
    • 0017481335 scopus 로고
    • Binding of drugs by albumin and plasma protein
    • J.J. Vallner Binding of drugs by albumin and plasma protein J. Pharm. Sci. 66 1977 447 465
    • (1977) J. Pharm. Sci. , vol.66 , pp. 447-465
    • Vallner, J.J.1
  • 11
    • 0014296306 scopus 로고
    • The binding of drugs by plasma proteins
    • M.C. Meyer, and D.E. Guttman The binding of drugs by plasma proteins J. Pharm. Sci. 57 1968 895 918
    • (1968) J. Pharm. Sci. , vol.57 , pp. 895-918
    • Meyer, M.C.1    Guttman, D.E.2
  • 12
    • 0017099526 scopus 로고
    • Plasma and tissue protein binding of drugs in pharmacokinetics
    • W.J. Jusko, and M. Gretch Plasma and tissue protein binding of drugs in pharmacokinetics Drug Metab. Rev. 5 1976 43 140
    • (1976) Drug Metab. Rev. , vol.5 , pp. 43-140
    • Jusko, W.J.1    Gretch, M.2
  • 13
    • 70350455500 scopus 로고    scopus 로고
    • Lessons from the crystallographic analysis of small molecule binding to human serum albumin
    • S. Curry Lessons from the crystallographic analysis of small molecule binding to human serum albumin Drug Metab. Pharmacokinet. 24 2009 342 357
    • (2009) Drug Metab. Pharmacokinet. , vol.24 , pp. 342-357
    • Curry, S.1
  • 15
    • 33750081513 scopus 로고    scopus 로고
    • Influence of protein binding and use of unbound (free) drug concentrations
    • M.E. Burton, L.M. Shaw, J.J. Schentag, W.E. Evans, fourth ed. Lippincott Williams & Wilkins Philadelphia
    • J.J. MacKichan Influence of protein binding and use of unbound (free) drug concentrations M.E. Burton, L.M. Shaw, J.J. Schentag, W.E. Evans, Applied Pharmacokinetics and Pharmacodynamics: Principles of Therapeutic Drug Monitoring fourth ed. 2005 Lippincott Williams & Wilkins Philadelphia 82 120
    • (2005) Applied Pharmacokinetics and Pharmacodynamics: Principles of Therapeutic Drug Monitoring , pp. 82-120
    • Mackichan, J.J.1
  • 16
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • DOI 10.1038/1869
    • S. Curry, H. Mandelkow, P. Brick, and N. Franks Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites Nat. Struct. Biol. 5 1998 827 835 (Pubitemid 28402087)
    • (1998) Nature Structural Biology , vol.5 , Issue.9 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 18
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • G. Sudlow, D.J. Birkett, and D.N. Wade The characterization of two specific drug binding sites on human serum albumin Mol. Pharmacol. 11 1975 824 832
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 19
    • 0017174391 scopus 로고
    • Further characterization of specific drug binding sites on human serum albumin
    • G. Sudlow, D.J. Birkett, and D.N. Wade Further characterization of specific drug binding sites on human serum albumin Mol. Pharmacol. 12 1976 1052 1061
    • (1976) Mol. Pharmacol. , vol.12 , pp. 1052-1061
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 20
    • 0023743229 scopus 로고
    • Location and characterization of the warfarin binding site of human serum albumin - A comparative study of two large fragments
    • O.J. Bos, J.P. Remijn, M.J. Fischer, J. Wilting, and L.H. Janssen Location and characterization of the warfarin binding site of human serum albumin - a comparative study of two large fragments Biochem. Pharmacol. 37 1988 3905 3909
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 3905-3909
    • Bos, O.J.1    Remijn, J.P.2    Fischer, M.J.3    Wilting, J.4    Janssen, L.H.5
  • 24
    • 0020063750 scopus 로고
    • Characterization of an important drug binding area on human serum albumin including the high-affinity binding sites of warfarin and azapropazone
    • K.J. Fehske, U. Schläfer, U. Wollert, and W.E. Müller Characterization of an important drug binding area on human serum albumin including the high-affinity binding sites of warfarin and azapropazone Mol. Pharmacol. 21 1982 387 393 (Pubitemid 12139839)
    • (1982) Molecular Pharmacology , vol.21 , Issue.2 , pp. 387-393
    • Fehske, K.J.1    Schlafer, U.2    Wollert, U.3    Muller, W.E.4
  • 25
    • 0019524375 scopus 로고
    • The location of drug binding sites in human serum albumin
    • DOI 10.1016/0006-2952(81)90151-9
    • K.J. Fehske, W.E. Müller, and U. Wollert The location of drug binding sites in human serum albumin Biochem. Pharmacol. 30 1981 687 692 (Pubitemid 11146814)
    • (1981) Biochemical Pharmacology , vol.30 , Issue.7 , pp. 687-692
    • Fehske, K.J.1    Mueller, W.E.2    Wollert, U.3
  • 27
    • 0020660621 scopus 로고
    • Relations between high-affinity binding sites for l-tryptophan, diazepam, salicylate and phenol red on human serum albumin
    • U. Kragh-Hansen Relations between high-affinity binding sites for l-tryptophan, diazepam, salicylate and phenol red on human serum albumin Biochem. J. 209 1983 135 142
    • (1983) Biochem. J. , vol.209 , pp. 135-142
    • Kragh-Hansen, U.1
  • 28
    • 0021984733 scopus 로고
    • Relations between high-affinity binding sites of markers for binding regions on human serum albumin
    • U. Kragh-Hansen Relations between high-affinity binding sites of markers for binding regions on human serum albumin Biochem. J. 225 1985 629 638 (Pubitemid 15174251)
    • (1985) Biochemical Journal , vol.225 , Issue.3 , pp. 629-638
    • Kragh-Hansen, U.1
  • 29
    • 0023688913 scopus 로고
    • Evidence for a large and flexible region of human serum albumin possessing high affinity binding sites for salicylate, warfarin, and other ligands
    • U. Kragh-Hansen Evidence for a large and flexible region of human serum albumin possessing high affinity binding sites for salicylate, warfarin, and other ligands Mol. Pharmacol. 34 1988 160 171
    • (1988) Mol. Pharmacol. , vol.34 , pp. 160-171
    • Kragh-Hansen, U.1
  • 30
    • 10644282198 scopus 로고    scopus 로고
    • Characterization of site I of human serum albumin using spectroscopic analyses: Locational relations between regions Ib and Ic of site I
    • DOI 10.1002/jps.20203
    • K. Yamasaki, T. Maruyama, A. Takadate, A. Suenaga, U. Kragh-Hansen, and M. Otagiri Characterization of site I of human serum albumin using spectroscopic analyses: locational relations between regions Ib and Ic of site I J. Pharm. Sci. 93 2004 3004 3012 (Pubitemid 39657804)
    • (2004) Journal of Pharmaceutical Sciences , vol.93 , Issue.12 , pp. 3004-3012
    • Yamasaki, K.1    Maruyama, T.2    Takadate, A.3    Suenaga, A.4    Kragh-Hansen, U.5    Otagiri, M.6
  • 31
    • 41849123136 scopus 로고    scopus 로고
    • A new drug binding subsite on human serum albumin and drug-drug interaction studied by X-ray crystallography
    • L. Zhu, F. Yang, L. Chen, E.J. Meehan, and M. Huang A new drug binding subsite on human serum albumin and drug-drug interaction studied by X-ray crystallography J. Struct. Biol. 162 2008 40 49
    • (2008) J. Struct. Biol. , vol.162 , pp. 40-49
    • Zhu, L.1    Yang, F.2    Chen, L.3    Meehan, E.J.4    Huang, M.5
  • 32
    • 0035933789 scopus 로고    scopus 로고
    • Crystal structure analysis of warfarin binding to human serum albumin: Anatomy of drug site i
    • I. Petitpas, A.A. Bhattacharya, S. Twine, M. East, and S. Curry Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I J. Biol. Chem. 276 2001 22804 22809
    • (2001) J. Biol. Chem. , vol.276 , pp. 22804-22809
    • Petitpas, I.1    Bhattacharya, A.A.2    Twine, S.3    East, M.4    Curry, S.5
  • 33
    • 0021030158 scopus 로고
    • Structural requirements for drug binding to site II on human serum albumin
    • S. Wanwimolruk, D.J. Birkett, and P.M. Brooks Structural requirements for drug binding to site II on human serum albumin Mol. Pharmacol. 24 1983 458 463 (Pubitemid 14249842)
    • (1983) Molecular Pharmacology , vol.24 , Issue.3 , pp. 458-463
    • Wanwimolruk, S.1    Birkett, D.J.2    Brooks, P.M.3
  • 34
    • 0030701947 scopus 로고    scopus 로고
    • Stereoselectivity and enantiomer-enantiomer interactions in the binding of ibuprofen to human serum albumin
    • DOI 10.1002/(SICI)1520-636X(1997)9:7<643::AID-CHIR1>3.0.CO;2-8
    • T. Itoh, Y. Saura, Y. Tsuda, and H. Yamada Stereoselectivity and enantiomer-enantiomer interactions in the binding of ibuprofen to human serum albumin Chirality 9 1997 643 649 (Pubitemid 27479370)
    • (1997) Chirality , vol.9 , Issue.7 , pp. 643-649
    • Itoh, T.1    Saura, Y.2    Tsuda, Y.3    Yamada, H.4
  • 35
    • 0035820385 scopus 로고    scopus 로고
    • Flunitrazepam, a 7-nitro-1,4-benzodiazepine that is unable to bind to the indole-benzodiazepine site of human serum albumin
    • DOI 10.1016/S0167-4838(01)00151-0, PII S0167483801001510
    • V.T. Chuang, and M. Otagiri Flunitrazepam, a 7-nitro-1,4-benzodiazepine that is unable to bind to the indole-benzodiazepine site of human serum albumin Biochim. Biophys. Acta 1546 2001 337 345 (Pubitemid 32280829)
    • (2001) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1546 , Issue.2 , pp. 337-345
    • Chuang, V.T.G.1    Otagiri, M.2
  • 36
    • 79955118487 scopus 로고    scopus 로고
    • Crystallographic analysis reveals the structural basis of the high-affinity binding of iophenoxic acid to human serum albumin
    • A.J. Ryan, C.-W. Chung, and S. Curry Crystallographic analysis reveals the structural basis of the high-affinity binding of iophenoxic acid to human serum albumin BMC Struct. Biol. 11 2011 18
    • (2011) BMC Struct. Biol. , vol.11 , pp. 18
    • Ryan, A.J.1    Chung, C.-W.2    Curry, S.3
  • 37
    • 0034634370 scopus 로고    scopus 로고
    • Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin
    • A.A. Bhattacharya, T. Grüne, and S. Curry Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin J. Mol. Biol. 303 2000 721 732
    • (2000) J. Mol. Biol. , vol.303 , pp. 721-732
    • Bhattacharya, A.A.1    Grüne, T.2    Curry, S.3
  • 38
    • 0018596292 scopus 로고
    • Binding of drugs to human serum albumin: XI. The specificity of three binding sites as studied with albumin immobilized in microparticles
    • I. Sjöholm, B. Ekman, A. Kober, I. Ljungstedt-Påhlman, B. Seiving, and T. Sjödin Binding of drugs to human serum albumin: XI. The specificity of three binding sites as studied with albumin immobilized in microparticles Mol. Pharmacol. 16 1979 767 777
    • (1979) Mol. Pharmacol. , vol.16 , pp. 767-777
    • Sjöholm, I.1    Ekman, B.2    Kober, A.3    Ljungstedt-Påhlman, I.4    Seiving, B.5    Sjödin, T.6
  • 39
    • 0034624021 scopus 로고    scopus 로고
    • Binding of the general anesthetics propofol and halothane to human serum albumin: High resolution crystal structures
    • DOI 10.1074/jbc.M005460200
    • A.A. Bhattacharya, S. Curry, and N.P. Franks Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures J. Biol. Chem. 275 2000 38731 38738 (Pubitemid 32009208)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.49 , pp. 38731-38738
    • Bhattacharya, A.A.1    Curry, S.2    Franks, N.P.3
  • 40
    • 47049119049 scopus 로고    scopus 로고
    • Crystallographic analysis of human serum albumin complexed with 4Z, 15E-bilirubin-IXα
    • P.A. Zunszain, J. Ghuman, A.F. McDonagh, and S. Curry Crystallographic analysis of human serum albumin complexed with 4Z, 15E-bilirubin-IXα J. Mol. Biol. 381 2008 394 406
    • (2008) J. Mol. Biol. , vol.381 , pp. 394-406
    • Zunszain, P.A.1    Ghuman, J.2    McDonagh, A.F.3    Curry, S.4
  • 42
    • 34347324020 scopus 로고    scopus 로고
    • Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties
    • DOI 10.1038/sj.bjp.0707251, PII 0707251
    • K. Oettl, and R.E. Stauber Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties Br. J. Pharmacol. 151 2007 580 590 (Pubitemid 47016287)
    • (2007) British Journal of Pharmacology , vol.151 , Issue.5 , pp. 580-590
    • Oettl, K.1    Stauber, R.E.2
  • 43
    • 0029905841 scopus 로고    scopus 로고
    • Covalent binding between bucillamine derivatives and human serum albumin
    • DOI 10.1023/A:1016057513490
    • R. Narazaki, M. Hamada, K. Harada, and M. Otagiri Covalent binding between bucillamine derivatives and human serum albumin Pharm. Res. 13 1996 1317 1321 (Pubitemid 26344974)
    • (1996) Pharmaceutical Research , vol.13 , Issue.9 , pp. 1317-1321
    • Narazaki, R.1    Hamada, M.2    Harada, K.3    Otagiri, M.4
  • 44
    • 84885377739 scopus 로고
    • Gold-induced structural switch of cys34 in albumin: Comparison of auranofin with aurothiomalate
    • J. Christodoulou, P.J. Sadler, and S. Tucker Gold-induced structural switch of cys34 in albumin: comparison of auranofin with aurothiomalate Metal-Based Drugs 1 1994 527
    • (1994) Metal-Based Drugs , vol.1 , pp. 527
    • Christodoulou, J.1    Sadler, P.J.2    Tucker, S.3
  • 45
    • 0027328485 scopus 로고
    • Nuclear magnetic resonance studies of the binding of captopril and penicillamine by serum albumin
    • DOI 10.1016/0006-2952(93)90671-I
    • D.A. Keire, S.V. Mariappan, J. Peng, and D.L. Rabenstein Nuclear magnetic resonance studies of the binding of captopril and penicillamine by serum albumin Biochem. Pharmacol. 46 1993 1059 1069 (Pubitemid 23280548)
    • (1993) Biochemical Pharmacology , vol.46 , Issue.6 , pp. 1059-1069
    • Keire, D.A.1    Mariappan, S.V.S.2    Peng, J.3    Rabenstein, D.L.4
  • 46
    • 0031041370 scopus 로고    scopus 로고
    • Kinetic analysis of the covalent binding of captopril to human serum albumin
    • DOI 10.1021/js960234+
    • R. Narazaki, K. Harada, A. Sugii, and M. Otagiri Kinetic analysis of the covalent binding of captopril to human serum albumin J. Pharm. Sci. 86 1997 215 219 (Pubitemid 27078387)
    • (1997) Journal of Pharmaceutical Sciences , vol.86 , Issue.2 , pp. 215-219
    • Narazaki, R.1    Harada, K.2    Sugii, A.3    Otagiri, M.4
  • 47
    • 0031768811 scopus 로고    scopus 로고
    • 34 by ethacrynic acid: Structural characterisation and binding properties
    • DOI 10.1016/S0731-7085(98)00163-0, PII S0731708598001630
    • C. Bertucci, B. Nanni, A. Raffaelli, and P. Salvadori Chemical modification of human albumin at cys34 by ethacrynic acid: structural characterisation and binding properties J. Pharm. Biomed. Anal. 18 1998 127 136 (Pubitemid 28529329)
    • (1998) Journal of Pharmaceutical and Biomedical Analysis , vol.18 , Issue.1-2 , pp. 127-136
    • Bertucci, C.1    Nanni, B.2    Raffaelli, A.3    Salvadori, P.4
  • 49
    • 0036210212 scopus 로고    scopus 로고
    • Covalent binding of nitrogen mustards to the cysteine-34 residue in human serum albumin
    • DOI 10.1007/s00204-001-0318-2
    • D. Noort, A.G. Hulst, and R. Jansen Covalent binding of nitrogen mustards to the cysteine-34 residue in human serum albumin Arch. Toxicol. 76 2002 83 88 (Pubitemid 34251559)
    • (2002) Archives of Toxicology , vol.76 , Issue.2 , pp. 83-88
    • Noort, D.1    Hulst, A.G.2    Jansen, R.3
  • 50
    • 34547141383 scopus 로고    scopus 로고
    • Liquid chromatography/tandem mass spectrometry detection of covalent binding of acetaminophen to human serum albumin
    • DOI 10.1124/dmd.106.014233
    • M.C. Damsten, J.N.M. Commandeur, A. Fidder, A.G. Hulst, D. Touw, D. Noort, and N.P.E. Vermeulen Liquid chromatography/tandem mass spectrometry detection of covalent binding of acetaminophen to human serum albumin Drug Metab. Dispos. 35 2007 1408 1417 (Pubitemid 47121783)
    • (2007) Drug Metabolism and Disposition , vol.35 , Issue.8 , pp. 1408-1417
    • Damsten, M.C.1    Commandeur, J.N.M.2    Fidder, A.3    Hulst, A.G.4    Touw, D.5    Noort, D.6    Vermeulen, N.P.E.7
  • 51
    • 0026081563 scopus 로고
    • The pharmacokinetics of albumin conjugates of d-penicillamine in humans
    • D.A. Joyce, R.O. Day, and B.R. Murphy The pharmacokinetics of albumin conjugates of d-penicillamine in humans Drug Metab. Dispos. 19 1991 309 311
    • (1991) Drug Metab. Dispos. , vol.19 , pp. 309-311
    • Joyce, D.A.1    Day, R.O.2    Murphy, B.R.3
  • 52
    • 0030890007 scopus 로고    scopus 로고
    • Covalent binding of a bucillamine derivative with albumin in sera from healthy subjects and patients with various diseases
    • DOI 10.1023/A:1012006306915
    • R. Narazaki, and M. Otagiri Covalent binding of a bucillamine derivative with albumin in sera from healthy subjects and patients with various diseases Pharm. Res. 14 1997 351 353 (Pubitemid 27160948)
    • (1997) Pharmaceutical Research , vol.14 , Issue.3 , pp. 351-353
    • Narazaki, R.1    Otagiri, M.2
  • 54
    • 15344349012 scopus 로고    scopus 로고
    • Bucolome, a potent binding inhibitor for furosemide, alters the pharmacokinetics and diuretic effect of furosemide: Potential for use of bucolome to restore diuretic response in nephrotic syndrome
    • DOI 10.1124/dmd.104.002782
    • N. Takamura, T. Maruyama, E. Chosa, K. Kawai, Y. Tsutsumi, Y. Uryu, K. Yamasaki, T. Deguchi, and M. Otagiri Bucolome, a potent binding inhibitor for furosemide, alters the pharmacokinetics and diuretic effect of furosemide: potential for use of bucolome to restore diuretic response in nephrotic syndrome Drug Metab. Dispos. 33 2005 596 602 (Pubitemid 40393204)
    • (2005) Drug Metabolism and Disposition , vol.33 , Issue.4 , pp. 596-602
    • Takamura, N.1    Maruyama, T.2    Chosa, E.3    Kawai, K.4    Tsutsumi, Y.5    Uryu, Y.6    Yamasaki, K.7    Deguchi, T.8    Otagiri, M.9
  • 55
    • 0015758809 scopus 로고
    • Drug-protein binding. IV. Modulation of binding Increasing activity of sulfonamides with displacing agents: A review
    • A.H. Anton Drug-protein binding. IV. Modulation of binding Increasing activity of sulfonamides with displacing agents: a review Ann. N. Y. Acad. Sci. 226 1973 273 292
    • (1973) Ann. N. Y. Acad. Sci. , vol.226 , pp. 273-292
    • Anton, A.H.1
  • 56
    • 0018916858 scopus 로고
    • Plasma protein binding and interaction studies with diflunisal, a new salicylate analgesic
    • DOI 10.1016/0006-2952(80)90378-0
    • R.K. Verbeeck, A. Boel, A. Buntinx, and P.J. De Schepper Plasma protein binding and interaction studies with diflunisal, a new salicylate analgesic Biochem. Pharmacol. 29 1980 571 576 (Pubitemid 10212897)
    • (1980) Biochemical Pharmacology , vol.29 , Issue.4 , pp. 571-576
    • Verbeeck, R.K.1    Boel, A.2    Buntinx, A.3    De Schepper, P.J.4
  • 58
    • 0021353799 scopus 로고
    • Albumin binding of anti-inflammatory drugs. Utility of site-oriented versus a stoichiometric analysis
    • B. Honoré, and R. Brodersen Albumin binding of anti-inflammatory drugs Utility of a site-oriented versus a stoichiometric analysis Mol. Pharmacol. 25 1984 137 150 (Pubitemid 14223264)
    • (1984) Molecular Pharmacology , vol.25 , Issue.1 , pp. 137-150
    • Honore, B.1    Brodersen, R.2
  • 59
    • 84874737376 scopus 로고    scopus 로고
    • A diclofenac suppository-nabumetone combination therapy for arthritic pain relief and a monitoring method for the diclofenac binding capacity of HSA site II in rheumatoid arthritis
    • 10.1002/bdd.1829
    • N. Setoguchi, N. Takamura, K. Fujita, K. Ogata, J. Tokunaga, T. Nishio, E. Chosa, K. Arimori, K. Kawai, and R. Yamamoto A diclofenac suppository-nabumetone combination therapy for arthritic pain relief and a monitoring method for the diclofenac binding capacity of HSA site II in rheumatoid arthritis Biopharm. Drug Dispos. 2012 10.1002/bdd.1829
    • (2012) Biopharm. Drug Dispos.
    • Setoguchi, N.1    Takamura, N.2    Fujita, K.3    Ogata, K.4    Tokunaga, J.5    Nishio, T.6    Chosa, E.7    Arimori, K.8    Kawai, K.9    Yamamoto, R.10
  • 60
    • 0029769656 scopus 로고    scopus 로고
    • Albumin binding sites for etodolac enantiomers
    • DOI 10.1002/(SICI)1520-636X(1996)8:3<271::AID-CHIR7>3.0.CO;2-K
    • I. Mignot, N. Presle, F. Lapicque, C. Monot, R. Dropsy, and P. Netter Albumin binding sites for etodolac enantiomers Chirality 8 1996 271 280 (Pubitemid 26259331)
    • (1996) Chirality , vol.8 , Issue.3 , pp. 271-280
    • Mignot, I.1    Presle, N.2    Lapicque, F.3    Monot, C.4    Dropsy, R.5    Netter, P.6
  • 61
    • 0017880691 scopus 로고
    • Competitive binding of long-chain free fatty acids, octanoate, and chlorophenoxyisobutyrate to albumin
    • H. Meisner, and K. Neet Competitive binding of long-chain free fatty acids, octanoate, and chlorophenoxyisobutyrate to albumin Mol. Pharmacol. 14 1978 337 346 (Pubitemid 8305834)
    • (1978) Molecular Pharmacology , vol.14 , Issue.2 , pp. 337-346
    • Meisner, H.1    Neet, K.2
  • 62
    • 0028303820 scopus 로고
    • Plasma protein binding displacement interactions - Why are they still regarded as clinically important?
    • P.E. Rolan, and L. Court Plasma protein binding displacement interactions-why are they still regarded as clinically important? Br. J. Clin. Pharmacol. 37 1994 125 128 (Pubitemid 24213753)
    • (1994) British Journal of Clinical Pharmacology , vol.37 , Issue.2 , pp. 125-128
    • Rolan, P.E.1
  • 64
    • 76649085489 scopus 로고    scopus 로고
    • Significance of protein binding in pharmacokinetics and pharmacodynamics
    • S. Schmidt, D. Gonzalez, and H. Derendorf Significance of protein binding in pharmacokinetics and pharmacodynamics J. Pharm. Sci. 99 2010 1107 1122
    • (2010) J. Pharm. Sci. , vol.99 , pp. 1107-1122
    • Schmidt, S.1    Gonzalez, D.2    Derendorf, H.3
  • 65
    • 0020420149 scopus 로고
    • Drug interactions involving the displacement of drugs from plasma protein and tissue binding sites
    • DOI 10.1016/0163-7258(82)90012-2
    • P.F. D'Arcy, and J.C. McElnay Drug interactions involving the displacement of drugs from plasma protein and tissue binding sites Pharmacol. Ther. 17 1982 211 220 (Pubitemid 13236429)
    • (1982) Pharmacology and Therapeutics , vol.17 , Issue.2 , pp. 211-220
    • D'Arcy, P.F.1    McElnay, J.C.2
  • 66
    • 0017297918 scopus 로고
    • Drug therapy. Binding of drugs to serum albumin (second of two parts)
    • J. Koch-Weser, and E.M. Sellers Drug therapy. Binding of drugs to serum albumin (second of two parts) N. Engl. J. Med. 294 1976 526 531
    • (1976) N. Engl. J. Med. , vol.294 , pp. 526-531
    • Koch-Weser, J.1    Sellers, E.M.2
  • 67
    • 0008801154 scopus 로고
    • Potentiation of anticoagulants caused by pyrazole compounds
    • S.L. Fox Potentiation of anticoagulants caused by pyrazole compounds JAMA 188 1964 320 321
    • (1964) JAMA , vol.188 , pp. 320-321
    • Fox, S.L.1
  • 68
    • 0014190465 scopus 로고
    • Potentiation of anticoagulant effect of warfarin by phenylbutazone
    • P.M. Aggeler, R.A. O'Reilly, L. Leong, and P.E. Kowitz Potentiation of anticoagulant effect of warfarin by phenylbutazone N. Engl. J. Med. 276 1967 496 501
    • (1967) N. Engl. J. Med. , vol.276 , pp. 496-501
    • Aggeler, P.M.1    O'Reilly, R.A.2    Leong, L.3    Kowitz, P.E.4
  • 69
    • 0029886356 scopus 로고    scopus 로고
    • Clinically important drug interactions with anticoagulants. An update
    • S. Harder, and P. Thürmann Clinically important drug interactions with anticoagulants. An update Clin. Pharmacokinet. 30 1996 416 444
    • (1996) Clin. Pharmacokinet. , vol.30 , pp. 416-444
    • Harder, S.1    Thürmann, P.2
  • 70
    • 78650622166 scopus 로고    scopus 로고
    • Risks and benefits of combined use of bucolome and warfarin in anticoagulation therapy
    • Y. Hatakeyama, S. Niwano, H. Niwano, T. Kosukegawa, and T. Izumi Risks and benefits of combined use of bucolome and warfarin in anticoagulation therapy Int. Heart J. 51 2010 399 403
    • (2010) Int. Heart J. , vol.51 , pp. 399-403
    • Hatakeyama, Y.1    Niwano, S.2    Niwano, H.3    Kosukegawa, T.4    Izumi, T.5
  • 72
    • 0013814186 scopus 로고
    • Displacement of one drug by another from carrier or receptor sites
    • B.B. Brodie Displacement of one drug by another from carrier or receptor sites Proc. R. Soc. Med. 58 1965 946 955
    • (1965) Proc. R. Soc. Med. , vol.58 , pp. 946-955
    • Brodie, B.B.1
  • 73
    • 0015854058 scopus 로고
    • Effect of phenylbutazone on the binding of vitamin K antagonists to albumin
    • J.P. Tillement, R. Zini, C. Mattei, and E. Singlas Effect of phenylbutazone on the binding of vitamin K antagonists to albumin Eur. J. Clin. Pharmacol. 6 1973 15 18
    • (1973) Eur. J. Clin. Pharmacol. , vol.6 , pp. 15-18
    • Tillement, J.P.1    Zini, R.2    Mattei, C.3    Singlas, E.4
  • 74
    • 0345229053 scopus 로고
    • Evaluation of co-administration of bucolome for warfarin therapy from the view point of protein binding
    • H. Abe, M. Sawada, T. Toda, N. Kurosawa, E. Owada, I. Tazawa, and S. Sakuma Evaluation of co-administration of bucolome for warfarin therapy from the view point of protein binding Jpn. J. Ther. Drug Monit. 12 1995 293 298
    • (1995) Jpn. J. Ther. Drug Monit. , vol.12 , pp. 293-298
    • Abe, H.1    Sawada, M.2    Toda, T.3    Kurosawa, N.4    Owada, E.5    Tazawa, I.6    Sakuma, S.7
  • 75
    • 15044352593 scopus 로고
    • Thrombosis therapy
    • M. Matsuoka Thrombosis therapy Geriatr. Med. 15 1977 505 512
    • (1977) Geriatr. Med. , vol.15 , pp. 505-512
    • Matsuoka, M.1
  • 76
    • 15044359577 scopus 로고
    • A new method of anticoagulant therapy used by combination warfarin and bucolome
    • A. Majima, T. Hosono, and K. Kawabe A new method of anticoagulant therapy used by combination warfarin and bucolome Niigata Igaku Kai Zasshi 88 1982 95 119
    • (1982) Niigata Igaku Kai Zasshi , vol.88 , pp. 95-119
    • Majima, A.1    Hosono, T.2    Kawabe, K.3
  • 77
    • 0031841377 scopus 로고    scopus 로고
    • Cytochrome P4502C9: An enzyme of major importance in human drug metabolism
    • DOI 10.1046/j.1365-2125.1998.00721.x
    • J.O. Miners, and D.J. Birkett Cytochrome P4502C9: an enzyme of major importance in human drug metabolism Br. J. Clin. Pharmacol. 45 1998 525 538 (Pubitemid 28270907)
    • (1998) British Journal of Clinical Pharmacology , vol.45 , Issue.6 , pp. 525-538
    • Miners, J.O.1    Birkett, D.J.2
  • 78
    • 0032875675 scopus 로고    scopus 로고
    • Pharmacokinetic interaction between warfarin and a uricosuric agent, bucolome: Application of in vitro approaches to predicting in vivo reduction of (S)-warfarin clearance
    • H. Takahashi, T. Kashima, S. Kimura, N. Murata, T. Takaba, K. Iwade, T. Abe, H. Tainaka, T. Yasumori, and a H. Echizen Pharmacokinetic interaction between warfarin and a uricosuric agent, bucolome: application of in vitro approaches to predicting In vivo reduction of (S)-warfarin clearance Drug Metab. Dispos. 27 1999 1179 1186 (Pubitemid 29463605)
    • (1999) Drug Metabolism and Disposition , vol.27 , Issue.10 , pp. 1179-1186
    • Takahashi, H.1    Kashima, T.2    Kimura, S.3    Murata, N.4    Takaba, T.5    Iwade, K.6    Abe, T.7    Tainaka, H.8    Yasumori, T.9    Echizen, H.10
  • 79
    • 0017691491 scopus 로고
    • Mechanisms of inhibition of tolbutamide metabolism: Phenylbutazone, oxyphenbutazone, sulfaphenazole
    • S.M. Pond, D.J. Birkett, and D.N. Wade Mechanisms of inhibition of tolbutamide metabolism: phenylbutazone, oxyphenbutazone, sulfaphenazole Clin. Pharmacol. Ther. 22 1977 573 579 (Pubitemid 8225573)
    • (1977) Clinical Pharmacology and Therapeutics , vol.22 , Issue.5 , pp. 573-579
    • Pond, S.M.1    Birkett, D.J.2    Wade, D.N.3
  • 81
    • 77956974134 scopus 로고    scopus 로고
    • Effects of CYP2C93 and CYP2C913 on diclofenac metabolism and inhibition-based drug-drug interactions
    • J. Zi, D. Liu, P. Ma, H. Huang, J. Zhu, D. Wei, J. Yang, and C. Chen Effects of CYP2C93 and CYP2C913 on diclofenac metabolism and inhibition-based drug-drug interactions Drug Metab. Pharmacokinet. 25 2010 343 350
    • (2010) Drug Metab. Pharmacokinet. , vol.25 , pp. 343-350
    • Zi, J.1    Liu, D.2    Ma, P.3    Huang, H.4    Zhu, J.5    Wei, D.6    Yang, J.7    Chen, C.8
  • 82
    • 38349179783 scopus 로고    scopus 로고
    • Dosage plan of a flurbiprofen injection product using inhibition of protein binding by lipid emulsion in rats
    • K. Ogata, N. Takamura, J. Tokunaga, and K. Kawai Dosage plan of a flurbiprofen injection product using inhibition of protein binding by lipid emulsion in rats J. Pharm. Pharmacol. 60 2008 15 20
    • (2008) J. Pharm. Pharmacol. , vol.60 , pp. 15-20
    • Ogata, K.1    Takamura, N.2    Tokunaga, J.3    Kawai, K.4
  • 84
    • 84875260007 scopus 로고    scopus 로고
    • Pharmacokinetic alteration of (99 m)Tc-MAG3 using serum protein binding displacement method
    • 10.1016/j.nucmedbio.2012.12.002
    • K. Nishi, M. Kobayashi, R. Nishii, N. Shikano, N. Takamura, and N. Kuga Pharmacokinetic alteration of (99 m)Tc-MAG3 using serum protein binding displacement method Nucl. Med. Biol. 2013 10.1016/j.nucmedbio.2012.12.002
    • (2013) Nucl. Med. Biol.
    • Nishi, K.1    Kobayashi, M.2    Nishii, R.3    Shikano, N.4    Takamura, N.5    Kuga, N.6
  • 85
    • 0017138040 scopus 로고
    • Drug protein binding and the nephrotic syndrome
    • R. Gugler, and D.L. Azarnoff Drug protein binding and the nephrotic syndrome Clin. Pharmacokinet. 1 1976 25 35
    • (1976) Clin. Pharmacokinet. , vol.1 , pp. 25-35
    • Gugler, R.1    Azarnoff, D.L.2
  • 86
    • 0021340719 scopus 로고
    • Alteration of drug-protein binding in renal disease
    • M.M. Reidenberg, and D.E. Drayer Alteration of drug-protein binding in renal disease Clin. Pharmacokinet. 9 Suppl. 1 1984 18 26 (Pubitemid 14179497)
    • (1984) Clinical Pharmacokinetics , vol.9 , Issue.SUPPL. 1 , pp. 18-26
    • Reidenberg, M.M.1    Drayer, D.E.2
  • 87
    • 0031755844 scopus 로고    scopus 로고
    • Elevated free fosphenytoin concentrations in uremic sera: Uremic toxins hippuric acid and indoxyl sulfate do not account for the impaired protein binding of fosphenytoin
    • DOI 10.1097/00007691-199812000-00013
    • A. Dasgupta, and D. Havlik Elevated free fosphenytoin concentrations in uremic sera: uremic toxins hippuric acid and indoxyl sulfate do not account for the impaired protein binding of fosphenytoin Ther. Drug Monit. 20 1998 658 662 (Pubitemid 28544296)
    • (1998) Therapeutic Drug Monitoring , vol.20 , Issue.6 , pp. 658-662
    • Dasgupta, A.1    Havlik, D.2
  • 88
    • 0018889593 scopus 로고
    • Plasma protein carbamylation and decreased acidic drug protein binding in uremia
    • S. Erill, R. Calvo, and R. Carlos Plasma protein carbamylation and decreased acidic drug protein binding in uremia Clin. Pharmacol. Ther. 27 1980 612 618 (Pubitemid 10105592)
    • (1980) Clinical Pharmacology and Therapeutics , vol.27 , Issue.5 , pp. 612-618
    • Erill, S.1    Calvo, R.2    Carlos, R.3
  • 89
    • 0020035172 scopus 로고
    • Effects of carbamylation of plasma proteins and competitive displacers on drug binding in uremia
    • R. Calvo, R. Carlos, and S. Erill Effects of carbamylation of plasma proteins and competitive displacers on drug binding in uremia Pharmacology 24 1982 248 252 (Pubitemid 12153554)
    • (1982) Pharmacology , vol.24 , Issue.4 , pp. 248-252
    • Calvo, R.1    Carlos, R.2    Erill, S.3
  • 91
    • 79960122985 scopus 로고    scopus 로고
    • Update on the pharmacokinetics and redox properties of protein-bound uremic toxins
    • H. Watanabe, Y. Miyamoto, M. Otagiri, and T. Maruyama Update on the pharmacokinetics and redox properties of protein-bound uremic toxins J. Pharm. Sci. 100 2011 3682 3695
    • (2011) J. Pharm. Sci. , vol.100 , pp. 3682-3695
    • Watanabe, H.1    Miyamoto, Y.2    Otagiri, M.3    Maruyama, T.4
  • 92
    • 0029621975 scopus 로고
    • Characterization of binding site of uremic toxins on human serum albumin
    • T. Sakai, A. Takadate, and M. Otagiri Characterization of binding site of uremic toxins on human serum albumin Biol. Pharm. Bull. 18 1995 1755 1761 (Pubitemid 26012996)
    • (1995) Biological and Pharmaceutical Bulletin , vol.18 , Issue.12 , pp. 1755-1761
    • Sakai, T.1    Takadate, A.2    Otagiri, M.3
  • 93
    • 0031283463 scopus 로고    scopus 로고
    • Effects of urernic toxins and fatty acids on serum protein binding of furosemide: Possible mechanism of the binding defect in uremia
    • N. Takamura, T. Maruyama, and M. Otagiri Effects of uremic toxins and fatty acids on serum protein binding of furosemide: possible mechanism of the binding defect in uremia Clin. Chem. 43 1997 2274 2280 (Pubitemid 28022962)
    • (1997) Clinical Chemistry , vol.43 , Issue.12 , pp. 2274-2280
    • Takamura, N.1    Maruyama, T.2    Otagiri, M.3
  • 94
    • 23044444127 scopus 로고    scopus 로고
    • The structure and function of oxidized albumin in hemodialysis patients: Its role in elevated oxidative stress via neutrophil burst
    • DOI 10.1016/j.bbrc.2005.07.035, PII S0006291X05014968
    • K. Mera, M. Anraku, K. Kitamura, K. Nakajou, T. Maruyama, and M. Otagiri The structure and function of oxidized albumin in hemodialysis patients: Its role in elevated oxidative stress via neutrophil burst Biochem. Biophys. Res. Commun. 334 2005 1322 1328 (Pubitemid 41074719)
    • (2005) Biochemical and Biophysical Research Communications , vol.334 , Issue.4 , pp. 1322-1328
    • Mera, K.1    Anraku, M.2    Kitamura, K.3    Nakajou, K.4    Maruyama, T.5    Otagiri, M.6
  • 95
    • 0026041957 scopus 로고
    • The role of albumin in human physiology and pathophysiology, Part III: Albumin and disease states
    • J.P. Doweiko, and D.J. Nompleggi The role of albumin in human physiology and pathophysiology, Part III: albumin and disease states JPEN J. Parenter. Enteral Nutr. 15 1991 476 483
    • (1991) JPEN J. Parenter. Enteral Nutr. , vol.15 , pp. 476-483
    • Doweiko, J.P.1    Nompleggi, D.J.2
  • 96
    • 0030944488 scopus 로고    scopus 로고
    • Pharmacokinetics and safety of tiagabine in subjects with various degrees of hepatic function
    • DOI 10.1111/j.1528-1157.1997.tb01734.x
    • A.H. Lau, L.E. Gustavson, R. Sperelakis, N.P. Lam, T. El-Shourbagy, J.X. Qian, and T. Layden Pharmacokinetics and safety of tiagabine in subjects with various degrees of hepatic function Epilepsia 38 1997 445 451 (Pubitemid 27172025)
    • (1997) Epilepsia , vol.38 , Issue.4 , pp. 445-451
    • Lau, A.H.1    Gustavson, L.E.2    Sperelakis, R.3    Lam, N.P.4    El-Shourbagy, T.5    Qian, J.X.6    Layden, T.7
  • 97
    • 0018169248 scopus 로고
    • Differentiated effects of liver cirrhosis on the albumin binding sites for diazepam, salicylic acid and warfarin
    • A. Kober, A. Jenner, and I. Sjöholm Differentiated effects of liver cirrhosis on the albumin binding sites for diazepam, salicylic acid and warfarin Biochem. Pharmacol. 27 1978 2729 2735
    • (1978) Biochem. Pharmacol. , vol.27 , pp. 2729-2735
    • Kober, A.1    Jenner, A.2    Sjöholm, I.3
  • 98
    • 51349134669 scopus 로고    scopus 로고
    • Improvement of impaired albumin binding capacity in acute-on-chronic liver failure by albumin dialysis
    • S. Klammt, S.R. Mitzner, J. Stange, J. Loock, and U. Heemann Improvement of impaired albumin binding capacity in acute-on-chronic liver failure by albumin dialysis Liver Transpl. 14 2008 1333 1339
    • (2008) Liver Transpl. , vol.14 , pp. 1333-1339
    • Klammt, S.1    Mitzner, S.R.2    Stange, J.3    Loock, J.4    Heemann, U.5
  • 99
    • 0021707165 scopus 로고
    • Abnormal serum protein binding of acidic drugs in diabetes mellitus
    • F. Ruiz-Cabello, and S. Erill Abnormal serum protein binding of acidic drugs in diabetes mellitus Clin. Pharmacol. Ther. 36 1984 691 695 (Pubitemid 15224675)
    • (1984) Clinical Pharmacology and Therapeutics , vol.36 , Issue.5 , pp. 691-695
    • Ruiz-Cabello, F.1    Erill, S.2
  • 100
    • 84864246770 scopus 로고    scopus 로고
    • Impaired drug-binding capacities of in vitro and in vivo glycated albumin
    • J. Baraka-Vidot, A. Guerin-Dubourg, E. Bourdon, and P. Rondeau Impaired drug-binding capacities of in vitro and in vivo glycated albumin Biochimie 94 2012 1960 1967
    • (2012) Biochimie , vol.94 , pp. 1960-1967
    • Baraka-Vidot, J.1    Guerin-Dubourg, A.2    Bourdon, E.3    Rondeau, P.4
  • 103
    • 33745862972 scopus 로고    scopus 로고
    • Clinical pharmacokinetics
    • L.Y. Young, M.A. Koda-Kimble, sixth ed. Applied Therapeutic, Inc. Washington
    • M.E. Winter Clinical pharmacokinetics L.Y. Young, M.A. Koda-Kimble, Applied Therapeutics: The Clinical Use of Drugs sixth ed. 1998 Applied Therapeutic, Inc. Washington 2-1 2-21
    • (1998) Applied Therapeutics: The Clinical Use of Drugs , pp. 21-221
    • Winter, M.E.1
  • 104
  • 105
    • 79956060014 scopus 로고    scopus 로고
    • Extracorporeal liver support-albumin dialysis with the molecular adsorbent recirculating system
    • S.R. Mitzner Extracorporeal liver support-albumin dialysis with the molecular adsorbent recirculating system Ann. Hepatol. 10 2011 S21 S28
    • (2011) Ann. Hepatol. , vol.10
    • Mitzner, S.R.1
  • 107
    • 4344699867 scopus 로고    scopus 로고
    • Equipment review: The molecular adsorbents recirculating system (MARS®)
    • DOI 10.1186/cc2895
    • M. Boyle, J. Kurtovic, D. Bihari, S. Riordan, and C. Steiner Equipment review: the molecular adsorbents recirculating system (MARS) Crit. Care 8 2004 280 286 (Pubitemid 39144718)
    • (2004) Critical Care , vol.8 , Issue.4 , pp. 280-286
    • Boyle, M.1    Kurtovic, J.2    Bihari, D.3    Riordan, S.4    Steiner, C.5
  • 108
    • 0035144238 scopus 로고    scopus 로고
    • Extracorporeal detoxification using the molecular adsorbent recirculating system for critically ill patients with liver failure
    • S.R. Mitzner, J.A.N. Stange, S. Klammt, P. Peszynski, R. Schmidt, and G. Nöldge-schomburg Extracorporeal detoxification using the molecular adsorbent recirculating system for critically ill patients with liver failure J. Am. Soc. Nephrol. 12 2001 S75 S82
    • (2001) J. Am. Soc. Nephrol. , vol.12
    • Mitzner, S.R.1    Stange, J.A.N.2    Klammt, S.3    Peszynski, P.4    Schmidt, R.5    Nöldge-Schomburg, G.6
  • 109
    • 70349782869 scopus 로고    scopus 로고
    • Albumin dialysis in liver failure: Comparison of molecular adsorbent recirculating system and single pass albumin dialysis - A retrospective analysis
    • A. Kortgen, F. Rauchfuss, M. Götz, U. Settmacher, M. Bauer, and C. Sponholz Albumin dialysis in liver failure: comparison of molecular adsorbent recirculating system and single pass albumin dialysis - a retrospective analysis Ther. Apher. 13 2009 419 425
    • (2009) Ther. Apher. , vol.13 , pp. 419-425
    • Kortgen, A.1    Rauchfuss, F.2    Götz, M.3    Settmacher, U.4    Bauer, M.5    Sponholz, C.6
  • 110
    • 34247550788 scopus 로고    scopus 로고
    • Effect of the molecular adsorbent recirculating system and Prometheus devices on systemic haemodynamics and vasoactive agents in patients with acute-on-chronic alcoholic liver failure
    • W. Laleman, A. Wilmer, P. Evenepoel, I. Elst, M. Zeegers, Z. Zaman, C. Verslype, J. Fevery, and F. Nevens Effect of the molecular adsorbent recirculating system and Prometheus devices on systemic haemodynamics and vasoactive agents in patients with acute-on-chronic alcoholic liver failure Crit. Care 10 2006 R108
    • (2006) Crit. Care , vol.10 , pp. 108
    • Laleman, W.1    Wilmer, A.2    Evenepoel, P.3    Elst, I.4    Zeegers, M.5    Zaman, Z.6    Verslype, C.7    Fevery, J.8    Nevens, F.9
  • 111
    • 4544368484 scopus 로고    scopus 로고
    • Pathophysiological effects of albumin dialysis in acute-on-chronic liver failure: A randomized controlled study
    • DOI 10.1002/lt.20236
    • S. Sen, N.A. Davies, R.P. Mookerjee, L.M. Cheshire, S.J. Hodges, R. Williams, and R. Jalan Pathophysiological effects of albumin dialysis in acute-on-chronic liver failure: a randomized controlled study Liver Transpl. 10 2004 1109 1119 (Pubitemid 39248408)
    • (2004) Liver Transplantation , vol.10 , Issue.9 , pp. 1109-1119
    • Sen, S.1    Davies, N.A.2    Mookerjee, R.P.3    Cheshire, L.M.4    Hodges, S.J.5    Williams, R.6    Jalan, R.7
  • 113
    • 79961185995 scopus 로고    scopus 로고
    • Clearing of toxic substances: Are there differences between the available liver support devices?
    • P. Krisper, V. Stadlbauer, and R.E. Stauber Clearing of toxic substances: are there differences between the available liver support devices? Liver Int. 31 2011 5 8
    • (2011) Liver Int. , vol.31 , pp. 5-8
    • Krisper, P.1    Stadlbauer, V.2    Stauber, R.E.3
  • 114
    • 33646231998 scopus 로고    scopus 로고
    • Albumin regeneration in liver support-comparison of different methods
    • S. Mitzner, S. Klammt, J. Stange, and R. Schmidt Albumin regeneration in liver support-comparison of different methods Ther. Apher. Dial. 10 2006 108 117
    • (2006) Ther. Apher. Dial. , vol.10 , pp. 108-117
    • Mitzner, S.1    Klammt, S.2    Stange, J.3    Schmidt, R.4
  • 115
    • 33646238474 scopus 로고    scopus 로고
    • How can liver toxins be removed? Filtration and adsorption with the Prometheus system
    • J. Vienken, and H. Christmann How can liver toxins be removed? Filtration and adsorption with the Prometheus system Ther. Apher. Dial. 10 2006 125 131
    • (2006) Ther. Apher. Dial. , vol.10 , pp. 125-131
    • Vienken, J.1    Christmann, H.2
  • 116
    • 37349101400 scopus 로고    scopus 로고
    • Bench-to-bedside review: Current evidence for extracorporeal albumin dialysis systems in liver failure
    • C.J. Karvellas, N. Gibney, D. Kutsogiannis, J. Wendon, and V.G. Bain Bench-to-bedside review: current evidence for extracorporeal albumin dialysis systems in liver failure Crit. Care 11 2007 215
    • (2007) Crit. Care , vol.11 , pp. 215
    • Karvellas, C.J.1    Gibney, N.2    Kutsogiannis, D.3    Wendon, J.4    Bain, V.G.5
  • 118
    • 33847669639 scopus 로고    scopus 로고
    • Treatment of severe theophylline poisoning with the molecular adsorbent recirculating system (MARS) [22]
    • DOI 10.1093/ndt/gfl640
    • S. Korsheed, N.M. Selby, and R.J. Fluck Treatment of severe theophylline poisoning with the molecular adsorbent recirculating system (MARS) Nephrol. Dial. Transplant. 22 2007 969 970 (Pubitemid 46351739)
    • (2007) Nephrology Dialysis Transplantation , vol.22 , Issue.3 , pp. 969-970
    • Korsheed, S.1    Selby, N.M.2    Fluck, R.J.3
  • 119
    • 0037319024 scopus 로고    scopus 로고
    • Treatment of phenytoin toxicity by the molecular adsorbents recirculating system (MARS)
    • DOI 10.1046/j.1528-1157.2003.31402.x
    • S. Sen, N. Ratnaraj, N.A. Davies, R.P. Mookerjee, C.E. Cooper, P.N. Patsalos, R. Williams, and R. Jalan Treatment of phenytoin toxicity by the molecular adsorbents recirculating system (MARS) Epilepsia 44 2003 265 267 (Pubitemid 36206034)
    • (2003) Epilepsia , vol.44 , Issue.2 , pp. 265-267
    • Sen, S.1    Ratnaraj, N.2    Davies, N.A.3    Mookerjee, R.P.4    Cooper, C.E.5    Patsalos, P.N.6    Williams, R.7    Jalan, R.8
  • 120
    • 35848970744 scopus 로고    scopus 로고
    • Extracorporeal treatment of intoxications
    • A.C. de Pont Extracorporeal treatment of intoxications Curr. Opin. Crit. Care 13 2007 668 673
    • (2007) Curr. Opin. Crit. Care , vol.13 , pp. 668-673
    • De Pont, A.C.1
  • 121
    • 33645999327 scopus 로고    scopus 로고
    • Albumin dialysis: A new therapeutic alternative for severe diltiazem intoxication [2]
    • DOI 10.1080/15563650500516041, PII K041363653874783
    • N. Pichon, B. François, C. Chevreuil, and J.M. Gaulier Albumin dialysis: a new therapeutic alternative for severe diltiazem intoxication Clin. Toxicol. (Phila.) 44 2006 195 196 (Pubitemid 44112957)
    • (2006) Clinical Toxicology , vol.44 , Issue.2 , pp. 195-196
    • Pichon, N.1    Francois, B.2    Clavel, M.3    Vignon, P.4    Chevreuil, C.5    Michel Gaulier, J.6
  • 122
    • 84861529439 scopus 로고    scopus 로고
    • Extracorporeal albumin dialysis in three cases of acute calcium channel blocker poisoning with life-threatening refractory cardiogenic shock
    • N. Pichon, A. Dugard, M. Clavel, J.B. Amiel, and B. François Extracorporeal albumin dialysis in three cases of acute calcium channel blocker poisoning with life-threatening refractory cardiogenic shock Ann. Emerg. Med. 59 2012 540 544
    • (2012) Ann. Emerg. Med. , vol.59 , pp. 540-544
    • Pichon, N.1    Dugard, A.2    Clavel, M.3    Amiel, J.B.4    François, B.5
  • 124
    • 15944381174 scopus 로고    scopus 로고
    • How tightly can a drug be bound to a protein and still be removable by charcoal hemoperfusion in overdose cases?
    • C.I. Kawasaki, R. Nishi, S. Uekihara, S. Hayano, U. Kragh-Hansen, and M. Otagiri How tightly can a drug be bound to a protein and still be removable by charcoal hemoperfusion in overdose cases? Clin. Toxicol. (Phila.) 43 2005 95 99
    • (2005) Clin. Toxicol. (Phila.) , vol.43 , pp. 95-99
    • Kawasaki, C.I.1    Nishi, R.2    Uekihara, S.3    Hayano, S.4    Kragh-Hansen, U.5    Otagiri, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.