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Volumn 5, Issue 11, 2009, Pages

Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding

Author keywords

[No Author keywords available]

Indexed keywords

5 HELIX; ANTIVIRUS AGENT; C 37; C PEPTIDE; CD4 ANTIGEN; CHEMOKINE RECEPTOR; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; 5 HELIX PROTEIN, SYNTHETIC; 5-HELIX PROTEIN, SYNTHETIC; CARRIER PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; PEPTIDE;

EID: 73549091727     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1000674     Document Type: Article
Times cited : (52)

References (49)
  • 1
    • 17244362388 scopus 로고    scopus 로고
    • Mechanistic basis of enzyme-targeted drugs
    • Robertson JG (2005) Mechanistic basis of enzyme-targeted drugs. Biochemistry 44: 5561-5571.
    • (2005) Biochemistry , vol.44 , pp. 5561-5571
    • Robertson, J.G.1
  • 2
    • 34250356440 scopus 로고    scopus 로고
    • Exploitation of structural and regulatory diversity in glutamate racemases
    • Lundqvist T, Fisher SL, Kern G, Folmer RH, Xue Y, et al. (2007) Exploitation of structural and regulatory diversity in glutamate racemases. Nature 447: 817-822.
    • (2007) Nature , vol.447 , pp. 817-822
    • Lundqvist, T.1    Fisher, S.L.2    Kern, G.3    Folmer, R.H.4    Xue, Y.5
  • 3
    • 33748741296 scopus 로고    scopus 로고
    • Kinetic dependence to HIV-1 entry inhibition
    • Steger HK, Root MJ (2006) Kinetic dependence to HIV-1 entry inhibition. J Biol Chem 281: 25813-25821.
    • (2006) J Biol Chem , vol.281 , pp. 25813-25821
    • Steger, H.K.1    Root, M.J.2
  • 4
    • 2442625211 scopus 로고    scopus 로고
    • HIV-1 gp41 as a target for viral entry inhibition
    • Root MJ, Steger HK (2004) HIV-1 gp41 as a target for viral entry inhibition. Curr Pharm Des 10: 1805-1825.
    • (2004) Curr Pharm Des , vol.10 , pp. 1805-1825
    • Root, M.J.1    Steger, H.K.2
  • 5
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS (1997) Core structure of gp41 from the HIV envelope glycoprotein. Cell 89: 263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 7
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M, Blacklow SC, Kim PS (1995) A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat Struct Biol 2: 1075-1082.
    • (1995) Nat Struct Biol , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 8
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild CT, Shugars DC, Greenwell TK, McDanal CB, Matthews TJ (1994) Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc Natl Acad Sci U S A 91: 9770-9774.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 10
    • 0038467539 scopus 로고    scopus 로고
    • Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope
    • Kilgore NR, Salzwedel K, Reddick M, Allaway GP, Wild CT (2003) Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope. J Virol 77: 7669-7672.
    • (2003) J Virol , vol.77 , pp. 7669-7672
    • Kilgore, N.R.1    Salzwedel, K.2    Reddick, M.3    Allaway, G.P.4    Wild, C.T.5
  • 11
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • Chan DC, Chutkowski CT, Kim PS (1998) Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc Natl Acad Sci U S A 95: 15613-15617.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 12
    • 0038576281 scopus 로고    scopus 로고
    • Enfuvirtide, an HIV-1 fusion inhibitor, for drug-resistant HIV infection in North and South America
    • Lalezari JP, Henry K, O'Hearn M, Montaner JS, Piliero PJ, et al. (2003) Enfuvirtide, an HIV-1 fusion inhibitor, for drug-resistant HIV infection in North and South America. N Engl J Med 348: 2175-2185.
    • (2003) N Engl J Med , vol.348 , pp. 2175-2185
    • Lalezari, J.P.1    Henry, K.2    O'Hearn, M.3    Montaner, J.S.4    Piliero, P.J.5
  • 13
    • 0037849954 scopus 로고    scopus 로고
    • Efficacy of enfuvirtide in patients infected with drug-resistant HIV-1 in Europe and Australia
    • Lazzarin A, Clotet B, Cooper D, Reynes J, Arasteh K, et al. (2003) Efficacy of enfuvirtide in patients infected with drug-resistant HIV-1 in Europe and Australia. N Engl J Med 348: 2186-2195.
    • (2003) N Engl J Med , vol.348 , pp. 2186-2195
    • Lazzarin, A.1    Clotet, B.2    Cooper, D.3    Reynes, J.4    Arasteh, K.5
  • 14
    • 0035949493 scopus 로고    scopus 로고
    • Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
    • Eckert DM, Kim PS (2001) Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. Proc Natl Acad Sci U S A 98: 11187-11192.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11187-11192
    • Eckert, D.M.1    Kim, P.S.2
  • 15
    • 0035800816 scopus 로고    scopus 로고
    • Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity
    • Louis JM, Bewley CA, Clore GM (2001) Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity. J Biol Chem 276: 29485-29489.
    • (2001) J Biol Chem , vol.276 , pp. 29485-29489
    • Louis, J.M.1    Bewley, C.A.2    Clore, G.M.3
  • 16
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root MJ, Kay MS, Kim PS (2001) Protein design of an HIV-1 entry inhibitor. Science 291: 884-888.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 17
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta RA, Wild CT, Weng Y, Weiss CD (1998) Capture of an early fusion-active conformation of HIV-1 gp41. Nat Struct Biol 5: 276-279.
    • (1998) Nat Struct Biol , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 18
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan GB, Markosyan RM, Hemmati H, Delmedico MK, Lambert DM, et al. (2000) Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J Cell Biol 151: 413-423.
    • (2000) J Cell Biol , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5
  • 19
    • 0037059049 scopus 로고    scopus 로고
    • Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics
    • Reeves JD, Gallo SA, Ahmad N, Miamidian JL, Harvey PE, et al. (2002) Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics. Proc Natl Acad Sci U S A 99: 16249-16254.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16249-16254
    • Reeves, J.D.1    Gallo, S.A.2    Ahmad, N.3    Miamidian, J.L.4    Harvey, P.E.5
  • 20
    • 10644267548 scopus 로고    scopus 로고
    • The cytoplasmic tail slows the folding of human immunodeficiency virus type 1 Env from a late prebundle configuration into the six-helix bundle
    • Abrahamyan LG, Mkrtchyan SR, Binley J, Lu M, Melikyan GB, et al. (2005) The cytoplasmic tail slows the folding of human immunodeficiency virus type 1 Env from a late prebundle configuration into the six-helix bundle. J Virol 79: 106-115.
    • (2005) J Virol , vol.79 , pp. 106-115
    • Abrahamyan, L.G.1    Mkrtchyan, S.R.2    Binley, J.3    Lu, M.4    Melikyan, G.B.5
  • 21
    • 15244356599 scopus 로고    scopus 로고
    • Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus
    • Platt EJ, Durnin JP, Kabat D (2005) Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus. J Virol 79: 4347-4356.
    • (2005) J Virol , vol.79 , pp. 4347-4356
    • Platt, E.J.1    Durnin, J.P.2    Kabat, D.3
  • 22
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Munoz-Barroso I, Durell S, Sakaguchi K, Appella E, Blumenthal R (1998) Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J Cell Biol 140: 315-323.
    • (1998) J Cell Biol , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 23
    • 24644449058 scopus 로고    scopus 로고
    • Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection
    • Bianchi E, Finotto M, Ingallinella P, Hrin R, Carella AV, et al. (2005) Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection. Proc Natl Acad Sci U S A 102: 12903-12908.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12903-12908
    • Bianchi, E.1    Finotto, M.2    Ingallinella, P.3    Hrin, R.4    Carella, A.V.5
  • 25
    • 33746810900 scopus 로고    scopus 로고
    • Structural basis for HIV-1 neutralization by a gp41 fusion intermediate-directed antibody
    • Luftig MA, Mattu M, Di Giovine P, Geleziunas R, Hrin R, et al. (2006) Structural basis for HIV-1 neutralization by a gp41 fusion intermediate-directed antibody. Nat Struct Mol Biol 13: 740-747.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 740-747
    • Luftig, M.A.1    Mattu, M.2    Di Giovine, P.3    Geleziunas, R.4    Hrin, R.5
  • 26
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky LT, Shugars DC, Matthews TJ (1998) Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J Virol 72: 986-993.
    • (1998) J Virol , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 27
    • 0042706375 scopus 로고    scopus 로고
    • HIV-1 resistance to the gp41-dependent fusion inhibitor C-34
    • Armand-Ugon M, Gutierrez A, Clotet B, Este JA (2003) HIV-1 resistance to the gp41-dependent fusion inhibitor C-34. Antiviral Res 59: 137-142.
    • (2003) Antiviral Res , vol.59 , pp. 137-142
    • Armand-Ugon, M.1    Gutierrez, A.2    Clotet, B.3    Este, J.A.4
  • 28
    • 45749135859 scopus 로고    scopus 로고
    • Selection of T1249-resistant human immunodeficiency virus type 1 variants
    • Eggink D, Baldwin CE, Deng Y, Langedijk JP, Lu M, et al. (2008) Selection of T1249-resistant human immunodeficiency virus type 1 variants. J Virol 82: 6678-6688.
    • (2008) J Virol , vol.82 , pp. 6678-6688
    • Eggink, D.1    Baldwin, C.E.2    Deng, Y.3    Langedijk, J.P.4    Lu, M.5
  • 29
    • 28844443476 scopus 로고    scopus 로고
    • Arf, Sec7 and Brefeldin A: A model towards the therapeutic inhibition of guanine nucleotide-exchange factors
    • Zeghouf M, Guibert B, Zeeh JC, Cherfils J (2005) Arf, Sec7 and Brefeldin A: a model towards the therapeutic inhibition of guanine nucleotide-exchange factors. Biochem Soc Trans 33: 1265-1268.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1265-1268
    • Zeghouf, M.1    Guibert, B.2    Zeeh, J.C.3    Cherfils, J.4
  • 30
    • 55049103844 scopus 로고    scopus 로고
    • Intravenous anesthetics inhibit human paraoxonase-1 (PON1) activity in vitro and in vivo
    • Alici HA, Ekinci D, Beydemir S (2008) Intravenous anesthetics inhibit human paraoxonase-1 (PON1) activity in vitro and in vivo. Clin Biochem 41: 1384-1390.
    • (2008) Clin Biochem , vol.41 , pp. 1384-1390
    • Alici, H.A.1    Ekinci, D.2    Beydemir, S.3
  • 31
    • 73549116713 scopus 로고    scopus 로고
    • Copeland R (2000) Enzymes (John Wiley and Sons, Inc., New York).
    • Copeland R (2000) Enzymes (John Wiley and Sons, Inc., New York).
  • 32
    • 26844448487 scopus 로고    scopus 로고
    • A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitope
    • Miller MD, Geleziunas R, Bianchi E, Lennard S, Hrin R, et al. (2005) A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitope. Proc Natl Acad Sci U S A 102: 14759-14764.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14759-14764
    • Miller, M.D.1    Geleziunas, R.2    Bianchi, E.3    Lennard, S.4    Hrin, R.5
  • 33
    • 63649151400 scopus 로고    scopus 로고
    • Interactions of HIV-1 inhibitory peptide T20 with the gp41 N-HR coiled coil
    • Champagne K, Shishido A, Root MJ (2009) Interactions of HIV-1 inhibitory peptide T20 with the gp41 N-HR coiled coil. J Biol Chem 284: 3619-3627.
    • (2009) J Biol Chem , vol.284 , pp. 3619-3627
    • Champagne, K.1    Shishido, A.2    Root, M.J.3
  • 34
    • 34547854349 scopus 로고    scopus 로고
    • Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus
    • Dwyer JJ, Wilson KL, Davison DK, Freel SA, Seedorff JE, et al. (2007) Design of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virus. Proc Natl Acad Sci U S A 104: 12772-12777.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 12772-12777
    • Dwyer, J.J.1    Wilson, K.L.2    Davison, D.K.3    Freel, S.A.4    Seedorff, J.E.5
  • 35
    • 55849137299 scopus 로고    scopus 로고
    • Potent HIV fusion inhibitors against Enfuvirtide-resistant HIV-1 strains
    • He Y, Cheng J, Lu H, Li J, Hu J, et al. (2008) Potent HIV fusion inhibitors against Enfuvirtide-resistant HIV-1 strains. Proc Natl Acad Sci U S A 105: 16332-16337.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 16332-16337
    • He, Y.1    Cheng, J.2    Lu, H.3    Li, J.4    Hu, J.5
  • 36
    • 45549093277 scopus 로고    scopus 로고
    • Design and evaluation of sifuvirtide, a novel HIV-1 fusion inhibitor
    • He Y, Xiao Y, Song H, Liang Q, Ju D, et al. (2008) Design and evaluation of sifuvirtide, a novel HIV-1 fusion inhibitor. J Biol Chem 283: 11126-11134.
    • (2008) J Biol Chem , vol.283 , pp. 11126-11134
    • He, Y.1    Xiao, Y.2    Song, H.3    Liang, Q.4    Ju, D.5
  • 37
    • 45749112585 scopus 로고    scopus 로고
    • Identification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure: Implications for designing novel anti-HIV fusion inhibitors
    • He Y, Cheng J, Li J, Qi Z, Lu H, et al. (2008) Identification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure: implications for designing novel anti-HIV fusion inhibitors. J Virol 82: 6349-6358.
    • (2008) J Virol , vol.82 , pp. 6349-6358
    • He, Y.1    Cheng, J.2    Li, J.3    Qi, Z.4    Lu, H.5
  • 38
    • 65249085618 scopus 로고    scopus 로고
    • Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency
    • Ingallinella P, Bianchi E, Ladwa NA, Wang YJ, Hrin R, et al. (2009) Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency. Proc Natl Acad Sci U S A 106: 5801-5806.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 5801-5806
    • Ingallinella, P.1    Bianchi, E.2    Ladwa, N.A.3    Wang, Y.J.4    Hrin, R.5
  • 39
    • 25144489604 scopus 로고    scopus 로고
    • Impact of human immunodeficiency virus type 1 gp41 amino acid substitutions selected during enfuvirtide treatment on gp41 binding and antiviral potency of enfuvirtide in vitro
    • Mink M, Mosier SM, Janumpalli S, Davison D, Jin L, et al. (2005) Impact of human immunodeficiency virus type 1 gp41 amino acid substitutions selected during enfuvirtide treatment on gp41 binding and antiviral potency of enfuvirtide in vitro. J Virol 79: 12447-12454.
    • (2005) J Virol , vol.79 , pp. 12447-12454
    • Mink, M.1    Mosier, S.M.2    Janumpalli, S.3    Davison, D.4    Jin, L.5
  • 40
    • 33646868062 scopus 로고    scopus 로고
    • Characterization of envelope glycoprotein gp41 genotype and phenotypic susceptibility to enfuvirtide at baseline and on treatment in the phase III clinical trials TORO-1 and TORO-2
    • Melby T, Sista P, DeMasi R, Kirkland T, Roberts N, et al. (2006) Characterization of envelope glycoprotein gp41 genotype and phenotypic susceptibility to enfuvirtide at baseline and on treatment in the phase III clinical trials TORO-1 and TORO-2. AIDS Res Hum Retroviruses 22: 375-385.
    • (2006) AIDS Res Hum Retroviruses , vol.22 , pp. 375-385
    • Melby, T.1    Sista, P.2    DeMasi, R.3    Kirkland, T.4    Roberts, N.5
  • 41
    • 65349113010 scopus 로고    scopus 로고
    • Mutations in gp120 contribute to the resistance of human immunodeficiency virus type 1 to membrane-anchored C-peptide maC46
    • Hermann FG, Egerer L, Brauer F, Gerum C, Schwalbe H, et al. (2009) Mutations in gp120 contribute to the resistance of human immunodeficiency virus type 1 to membrane-anchored C-peptide maC46. J Virol 83: 4844-4853.
    • (2009) J Virol , vol.83 , pp. 4844-4853
    • Hermann, F.G.1    Egerer, L.2    Brauer, F.3    Gerum, C.4    Schwalbe, H.5
  • 42
    • 38649091973 scopus 로고    scopus 로고
    • Peptide mimic of the HIV envelope gp120-gp41 interface
    • Kim S, Pang HB, Kay MS (2008) Peptide mimic of the HIV envelope gp120-gp41 interface. J Mol Biol 376: 786-797.
    • (2008) J Mol Biol , vol.376 , pp. 786-797
    • Kim, S.1    Pang, H.B.2    Kay, M.S.3
  • 43
    • 15844419153 scopus 로고    scopus 로고
    • Identification of a major co-receptor for primary isolates of HIV-1
    • Deng H, Liu R, Ellmeier W, Choe S, Unutmaz D, et al. (1996) Identification of a major co-receptor for primary isolates of HIV-1. Nature 381: 661-666.
    • (1996) Nature , vol.381 , pp. 661-666
    • Deng, H.1    Liu, R.2    Ellmeier, W.3    Choe, S.4    Unutmaz, D.5
  • 44
    • 0026562720 scopus 로고
    • Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene
    • Kimpton J, Emerman M (1992) Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene. J Virol 66: 2232-2239.
    • (1992) J Virol , vol.66 , pp. 2232-2239
    • Kimpton, J.1    Emerman, M.2
  • 45
    • 0031954686 scopus 로고    scopus 로고
    • Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1
    • Platt EJ, Wehrly K, Kuhmann SE, Chesebro B, Kabat D (1998) Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1. J Virol 72: 2855-2864.
    • (1998) J Virol , vol.72 , pp. 2855-2864
    • Platt, E.J.1    Wehrly, K.2    Kuhmann, S.E.3    Chesebro, B.4    Kabat, D.5
  • 46
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6: 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 47
    • 0028009774 scopus 로고
    • Distinct modes of human immunodeficiency virus type 1 proviral latency revealed by superinfection of nonproductively infected cell lines with recombinant luciferase-encoding viruses
    • Chen BK, Saksela K, Andino R, Baltimore D (1994) Distinct modes of human immunodeficiency virus type 1 proviral latency revealed by superinfection of nonproductively infected cell lines with recombinant luciferase-encoding viruses. J Virol 68: 654-660.
    • (1994) J Virol , vol.68 , pp. 654-660
    • Chen, B.K.1    Saksela, K.2    Andino, R.3    Baltimore, D.4
  • 48
    • 0033609149 scopus 로고    scopus 로고
    • Quantification of CD4, CCR5, and CXCR4 levels on lymphocyte subsets, dendritic cells, and differentially conditioned monocyte-derived macrophages
    • Lee B, Sharron M, Montaner LJ, Weissman D, Doms RW (1999) Quantification of CD4, CCR5, and CXCR4 levels on lymphocyte subsets, dendritic cells, and differentially conditioned monocyte-derived macrophages. Proc Natl Acad Sci U S A 96: 5215-5220.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 5215-5220
    • Lee, B.1    Sharron, M.2    Montaner, L.J.3    Weissman, D.4    Doms, R.W.5
  • 49
    • 0021118703 scopus 로고
    • Quantitative analysis of dose-effect relationships: The combined effects of multiple drugs or enzyme inhibitors
    • Chou TC, Talalay P (1984) Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors. Adv Enzyme Regul 22: 27-55.
    • (1984) Adv Enzyme Regul , vol.22 , pp. 27-55
    • Chou, T.C.1    Talalay, P.2


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