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Volumn 169, Issue 2, 2012, Pages 388-410

Molecular recognition in the human immunodeficiency virus capsid and antiviral design

Author keywords

Antiviral agent; Capsid; Human immunodeficiency virus; Interfacial inhibitor; Molecular recognition; Peptide

Indexed keywords

ANKYRIN; ANTIVIRUS AGENT; BENZIMIDAZOLE DERIVATIVE; BENZODIAZEPINE DERIVATIVE; CALCIUM BINDING PROTEIN; CALCIUM CHANNEL BLOCKING AGENT; CAPSID PROTEIN; DENDRIMER; GLYCINE DERIVATIVE; HYDRAZONE DERIVATIVE; N (2 METHYLAMINOETHYL) 5 ISOQUINOLINESULFONAMIDE; PEPTIDE DERIVATIVE; PF 3450074; THIOUREA DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84868609925     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2012.06.016     Document Type: Review
Times cited : (35)

References (169)
  • 2
    • 34250347313 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 assembly, release and maturation
    • Adamson C.S., Freed E.O. Human immunodeficiency virus type 1 assembly, release and maturation. Advances in Pharmacology 2007, 55:347-397.
    • (2007) Advances in Pharmacology , vol.55 , pp. 347-397
    • Adamson, C.S.1    Freed, E.O.2
  • 3
    • 1542284115 scopus 로고    scopus 로고
    • The molecular basis of HIV capsid assembly-five years of progress
    • Adamson C.S., Jones I.M. The molecular basis of HIV capsid assembly-five years of progress. Reviews in Medical Virology 2004, 14:107-121.
    • (2004) Reviews in Medical Virology , vol.14 , pp. 107-121
    • Adamson, C.S.1    Jones, I.M.2
  • 5
    • 27144548783 scopus 로고    scopus 로고
    • The retroviral capsid domain dictates virion size, morphology and coassembly of gag into virus-like particles
    • Ako-Adjei D., Johnson M.C., Vogt V.M. The retroviral capsid domain dictates virion size, morphology and coassembly of gag into virus-like particles. Journal of Virology 2005, 79:13463-13472.
    • (2005) Journal of Virology , vol.79 , pp. 13463-13472
    • Ako-Adjei, D.1    Johnson, M.C.2    Vogt, V.M.3
  • 7
    • 34548255898 scopus 로고    scopus 로고
    • Flexibility in HIV-1 assembly subunits: solution structure of the monomeric C-terminal domain of the capsid protein
    • Alcaraz L.A., del álamo M., Barrera F.N., Mateu M.G., Neira J.L. Flexibility in HIV-1 assembly subunits: solution structure of the monomeric C-terminal domain of the capsid protein. Biophysical Journal 2007, 93:1264-1276.
    • (2007) Biophysical Journal , vol.93 , pp. 1264-1276
    • Alcaraz, L.A.1    del Álamo, M.2    Barrera, F.N.3    Mateu, M.G.4    Neira, J.L.5
  • 8
    • 44949165530 scopus 로고    scopus 로고
    • Structural mobility of the monomeric C-terminal domain of the HIV-1 capsid protein
    • Alcaraz L.A., del álamo M., Mateu M.G., Neira J.L. Structural mobility of the monomeric C-terminal domain of the HIV-1 capsid protein. FEBS Journal 2008, 275:3299-3311.
    • (2008) FEBS Journal , vol.275 , pp. 3299-3311
    • Alcaraz, L.A.1    del Álamo, M.2    Mateu, M.G.3    Neira, J.L.4
  • 9
    • 78349297963 scopus 로고    scopus 로고
    • Revisiting HIV-1 uncoating
    • Arhel N. Revisiting HIV-1 uncoating. Retrovirology 2010, 7:96.
    • (2010) Retrovirology , vol.7 , pp. 96
    • Arhel, N.1
  • 10
    • 65149095269 scopus 로고    scopus 로고
    • Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly
    • Bailey G.D., Hyun J.K., Mitra A.K., Kingston R.L. Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly. Structure 2009, 17:737-748.
    • (2009) Structure , vol.17 , pp. 737-748
    • Bailey, G.D.1    Hyun, J.K.2    Mitra, A.K.3    Kingston, R.L.4
  • 11
    • 18744416007 scopus 로고    scopus 로고
    • Highly active antiretroviral therapy: current state of the art, new agents and their pharmacological interactions useful for improving therapeutic outcome
    • Barbaro G., Scozzafava A., Mastrolorenzo A., Supuran C.T. Highly active antiretroviral therapy: current state of the art, new agents and their pharmacological interactions useful for improving therapeutic outcome. Current Pharmaceutical Design 2005, 11:1805-1843.
    • (2005) Current Pharmaceutical Design , vol.11 , pp. 1805-1843
    • Barbaro, G.1    Scozzafava, A.2    Mastrolorenzo, A.3    Supuran, C.T.4
  • 16
    • 47749125805 scopus 로고    scopus 로고
    • Solution structure of a hydrocarbon staple peptide inhibitor in complex with monomeric C-terminal domain of HIV-1 capsid
    • Bhattacharya S., Zhang H., Debnath A.K., Cowburn D. Solution structure of a hydrocarbon staple peptide inhibitor in complex with monomeric C-terminal domain of HIV-1 capsid. Journal of Biological Chemistry 2008, 283:16274-16278.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 16274-16278
    • Bhattacharya, S.1    Zhang, H.2    Debnath, A.K.3    Cowburn, D.4
  • 17
    • 67649407509 scopus 로고    scopus 로고
    • The cell biology of HIV-1 virion genesis
    • Bieniasz P.D. The cell biology of HIV-1 virion genesis. Cell Host & Microbe 2009, 5:550-558.
    • (2009) Cell Host & Microbe , vol.5 , pp. 550-558
    • Bieniasz, P.D.1
  • 21
    • 21244446315 scopus 로고    scopus 로고
    • The cysteine residues of HIV-1 capsid regulate oligomerization and cyclophilin A-induced changes
    • Bon Homme M., Carter C., Scarlata S. The cysteine residues of HIV-1 capsid regulate oligomerization and cyclophilin A-induced changes. Biophysical Journal 2005, 88:2078-2088.
    • (2005) Biophysical Journal , vol.88 , pp. 2078-2088
    • Bon Homme, M.1    Carter, C.2    Scarlata, S.3
  • 22
    • 79953170194 scopus 로고    scopus 로고
    • Dissecting protein-protein interactions using directed evolution
    • Bonsor D.A., Sundberg E.J. Dissecting protein-protein interactions using directed evolution. Biochemistry 2011, 50:2394-2402.
    • (2011) Biochemistry , vol.50 , pp. 2394-2402
    • Bonsor, D.A.1    Sundberg, E.J.2
  • 23
    • 0031680643 scopus 로고    scopus 로고
    • The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly
    • Borsetti A., öhagen å., Göttlinger H.G. The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly. Journal of Virology 1998, 72:9313-9317.
    • (1998) Journal of Virology , vol.72 , pp. 9313-9317
    • Borsetti, A.1    Öhagen, Å.2    Göttlinger, H.G.3
  • 26
    • 33644806492 scopus 로고    scopus 로고
    • The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions
    • Briggs J.A.G., Riches J.D., Glass B., Forster F., Kräusslich H.-G., Fuller S. The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions. Structure 2006, 14:15-20.
    • (2006) Structure , vol.14 , pp. 15-20
    • Briggs, J.A.G.1    Riches, J.D.2    Glass, B.3    Forster, F.4    Kräusslich, H.-G.5    Fuller, S.6
  • 30
    • 78549260676 scopus 로고    scopus 로고
    • A new functional role of HIV-1 integrase during uncoating of the viral core
    • Briones M.S., Chow S.A. A new functional role of HIV-1 integrase during uncoating of the viral core. Immunologic Research 2010, 48:14-26.
    • (2010) Immunologic Research , vol.48 , pp. 14-26
    • Briones, M.S.1    Chow, S.A.2
  • 31
    • 73549103358 scopus 로고    scopus 로고
    • The development of antiretroviral therapy and its impact on the HIV-1/AIDS pandemic
    • Broder S. The development of antiretroviral therapy and its impact on the HIV-1/AIDS pandemic. Antiviral Research 2010, 85:1-18.
    • (2010) Antiviral Research , vol.85 , pp. 1-18
    • Broder, S.1
  • 32
  • 33
    • 0033027711 scopus 로고    scopus 로고
    • In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain
    • Campbell S., Rein A. In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain. Journal of Virology 1999, 73:2270-2279.
    • (1999) Journal of Virology , vol.73 , pp. 2270-2279
    • Campbell, S.1    Rein, A.2
  • 34
    • 0029103178 scopus 로고
    • Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
    • Campbell S., Vogt V.M. Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1. Journal of Virology 1995, 69:6487-6497.
    • (1995) Journal of Virology , vol.69 , pp. 6487-6497
    • Campbell, S.1    Vogt, V.M.2
  • 36
    • 24144468961 scopus 로고    scopus 로고
    • High-throughput human immunodeficiency virus type 1 (HIV-1) full replication assay that includes Vif as an antiviral target
    • Cao J., Isaacson J., Patick A.K., Blair W.S. High-throughput human immunodeficiency virus type 1 (HIV-1) full replication assay that includes Vif as an antiviral target. Antimicrobial Agents and Chemotherapy 2005, 49:3833-3841.
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , pp. 3833-3841
    • Cao, J.1    Isaacson, J.2    Patick, A.K.3    Blair, W.S.4
  • 37
    • 59649084913 scopus 로고    scopus 로고
    • Visualization of a missing link in retrovirus capsid assembly
    • Cardone G., Purdy J.G., Cheng N., Craven R.C., Steven A.C. Visualization of a missing link in retrovirus capsid assembly. Nature 2009, 457:694-699.
    • (2009) Nature , vol.457 , pp. 694-699
    • Cardone, G.1    Purdy, J.G.2    Cheng, N.3    Craven, R.C.4    Steven, A.C.5
  • 39
    • 77950282072 scopus 로고    scopus 로고
    • Structural and dynamical characterization of tubular HIV-1 capsid protein assemblies by solid state nuclear magnetic resonance and electron microscopy
    • Chen B., Tycko R. Structural and dynamical characterization of tubular HIV-1 capsid protein assemblies by solid state nuclear magnetic resonance and electron microscopy. Protein Science 2010, 19:716-730.
    • (2010) Protein Science , vol.19 , pp. 716-730
    • Chen, B.1    Tycko, R.2
  • 40
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T., Wells J.A. A hot spot of binding energy in a hormone-receptor interface. Science 1995, 267:383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 42
    • 80051768952 scopus 로고    scopus 로고
    • A retroviral chimeric capsid protein reveals the role of the N-terminal β-hairpin in mature core assembly
    • Cortines J.R., Monroe E.B., Kang S., Prevelige P.E. A retroviral chimeric capsid protein reveals the role of the N-terminal β-hairpin in mature core assembly. Journal of Molecular Biology 2011, 410:641-652.
    • (2011) Journal of Molecular Biology , vol.410 , pp. 641-652
    • Cortines, J.R.1    Monroe, E.B.2    Kang, S.3    Prevelige, P.E.4
  • 43
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine scanning mutagenesis
    • Cunningham B.C., Wells J.A. High-resolution epitope mapping of hGH-receptor interactions by alanine scanning mutagenesis. Science 1989, 244:1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 45
    • 34250665073 scopus 로고    scopus 로고
    • Colony filtration blotting for screening soluble expression in Escherichia coli
    • Dahlroth S.L., Nordlund P., Cornvik T. Colony filtration blotting for screening soluble expression in Escherichia coli. Nature Protocols 2006, 1:253-258.
    • (2006) Nature Protocols , vol.1 , pp. 253-258
    • Dahlroth, S.L.1    Nordlund, P.2    Cornvik, T.3
  • 46
    • 34250682229 scopus 로고    scopus 로고
    • Properties, functions and drug targeting of the multifunctional nucleocapsid protein of the human immunodeficiency virus
    • Darlix J.-L., Garrido J.L., Morellet N., Mély Y., de Rocquigny H. Properties, functions and drug targeting of the multifunctional nucleocapsid protein of the human immunodeficiency virus. Advances in Pharmacology 2007, 55:299-346.
    • (2007) Advances in Pharmacology , vol.55 , pp. 299-346
    • Darlix, J.-L.1    Garrido, J.L.2    Morellet, N.3    Mély, Y.4    de Rocquigny, H.5
  • 47
    • 0036050539 scopus 로고    scopus 로고
    • Strategies in the design of antiviral drugs
    • De Clercq E. Strategies in the design of antiviral drugs. Nature Reviews Drug Discovery 2002, 1:13-25.
    • (2002) Nature Reviews Drug Discovery , vol.1 , pp. 13-25
    • De Clercq, E.1
  • 48
    • 2342531101 scopus 로고    scopus 로고
    • Antiviral drugs in current clinical use
    • De Clercq E. Antiviral drugs in current clinical use. Journal of Clinical Virology 2004, 30:115-133.
    • (2004) Journal of Clinical Virology , vol.30 , pp. 115-133
    • De Clercq, E.1
  • 52
    • 10044231838 scopus 로고    scopus 로고
    • Electrostatic repulsion, compensatory mutations, and long-range non-additive effects at the dimerization interface of the HIV capsid protein
    • del álamo M., Mateu M.G. Electrostatic repulsion, compensatory mutations, and long-range non-additive effects at the dimerization interface of the HIV capsid protein. Journal of Molecular Biology 2005, 345:893-906.
    • (2005) Journal of Molecular Biology , vol.345 , pp. 893-906
    • del Álamo, M.1    Mateu, M.G.2
  • 53
    • 0041845304 scopus 로고    scopus 로고
    • Thermodynamic dissection of a low affinity protein-protein interface involved in human immunodeficiency virus assembly
    • del álamo M., Neira J.L., Mateu M.G. Thermodynamic dissection of a low affinity protein-protein interface involved in human immunodeficiency virus assembly. Journal of Biological Chemistry 2003, 278:27923-27929.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 27923-27929
    • del Álamo, M.1    Neira, J.L.2    Mateu, M.G.3
  • 54
    • 27644552564 scopus 로고    scopus 로고
    • Effect of macromolecular crowding agents on human immunodeficiency virus type 1 capsid protein assembly in vitro
    • del álamo M., Rivas G., Mateu M.G. Effect of macromolecular crowding agents on human immunodeficiency virus type 1 capsid protein assembly in vitro. Journal of Virology 2005, 79:14271-14281.
    • (2005) Journal of Virology , vol.79 , pp. 14271-14281
    • del Álamo, M.1    Rivas, G.2    Mateu, M.G.3
  • 55
    • 84870465893 scopus 로고    scopus 로고
    • DeLano Scientific LLC, San Carlos, CA, USA. PyMOL molecular graphics system on World Wide Web URL: .
    • DeLano, W.L., 2002. DeLano Scientific LLC, San Carlos, CA, USA. PyMOL molecular graphics system on World Wide Web URL: http://www.pymol.org/.
    • (2002)
    • DeLano, W.L.1
  • 57
    • 80052763033 scopus 로고    scopus 로고
    • Larger helical populations in peptides derived from the dimerization helix of capsid protein of HIV-1 results in peptide binding toward regions other than the " hotspot" interface
    • Doménech R., Bocanegra R., González-Muñiz R., Gómez J., Mateu M.G., Neira J.L. Larger helical populations in peptides derived from the dimerization helix of capsid protein of HIV-1 results in peptide binding toward regions other than the " hotspot" interface. Biomacromolecules 2011, 12:3252-3264.
    • (2011) Biomacromolecules , vol.12 , pp. 3252-3264
    • Doménech, R.1    Bocanegra, R.2    González-Muñiz, R.3    Gómez, J.4    Mateu, M.G.5    Neira, J.L.6
  • 58
    • 79960487669 scopus 로고    scopus 로고
    • The isolated major homology region of the HIV-1 capsid protein is mainly unfolded in solution and binds to the intact protein
    • Doménech R., Bocanegra R., Velázquez-Campoy A., Neira J.L. The isolated major homology region of the HIV-1 capsid protein is mainly unfolded in solution and binds to the intact protein. Biochimica et Biophysica Acta 2011, 1814:1269-1278.
    • (2011) Biochimica et Biophysica Acta , vol.1814 , pp. 1269-1278
    • Doménech, R.1    Bocanegra, R.2    Velázquez-Campoy, A.3    Neira, J.L.4
  • 59
    • 0024342524 scopus 로고
    • RNA virus evolution and the control of viral disease
    • Domingo E. RNA virus evolution and the control of viral disease. Progress in Drug Research 1989, 33:93-133.
    • (1989) Progress in Drug Research , vol.33 , pp. 93-133
    • Domingo, E.1
  • 62
    • 4043142786 scopus 로고    scopus 로고
    • Investigation of N-terminal domain charged residues on the assembly and stability of HIV-1 CA
    • Douglas C.C., Thomas D., Lanman J., Prevelige P.E. Investigation of N-terminal domain charged residues on the assembly and stability of HIV-1 CA. Biochemistry 2004, 43:10435-10441.
    • (2004) Biochemistry , vol.43 , pp. 10435-10441
    • Douglas, C.C.1    Thomas, D.2    Lanman, J.3    Prevelige, P.E.4
  • 63
    • 79551683191 scopus 로고    scopus 로고
    • Structure of the HIV-1 full-length capsid protein in a conformationally trapped unassembled state induced by small-molecule binding
    • Du S., Betts L., Yang R., Shi H., Concel J., Ahn J., Aiken C., Zhang P., Yeh J.I. Structure of the HIV-1 full-length capsid protein in a conformationally trapped unassembled state induced by small-molecule binding. Journal of Molecular Biology 2010, 406:371-386.
    • (2010) Journal of Molecular Biology , vol.406 , pp. 371-386
    • Du, S.1    Betts, L.2    Yang, R.3    Shi, H.4    Concel, J.5    Ahn, J.6    Aiken, C.7    Zhang, P.8    Yeh, J.I.9
  • 64
    • 80052039764 scopus 로고    scopus 로고
    • Helix-mediated protein-protein interactions as targets for intervention using foldamers
    • Edwards T.A., Wilson A.J. Helix-mediated protein-protein interactions as targets for intervention using foldamers. Amino Acids 2011, 41:743-754.
    • (2011) Amino Acids , vol.41 , pp. 743-754
    • Edwards, T.A.1    Wilson, A.J.2
  • 65
    • 0026762403 scopus 로고
    • Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
    • Ehrlich L.S., Agresta B.E., Carter C.A. Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro. Journal of Virology 1992, 66:4874-4883.
    • (1992) Journal of Virology , vol.66 , pp. 4874-4883
    • Ehrlich, L.S.1    Agresta, B.E.2    Carter, C.A.3
  • 66
    • 0034950321 scopus 로고    scopus 로고
    • HIV-1 capsid protein forms spherical (immature-like) and tubular (mature-like) particles in vitro: structure switching by pH-induced conformational changes
    • Ehrlich L.S., Liu T., Scarlata S., Chu B., Carter C. HIV-1 capsid protein forms spherical (immature-like) and tubular (mature-like) particles in vitro: structure switching by pH-induced conformational changes. Biophysical Journal 2001, 81:586-594.
    • (2001) Biophysical Journal , vol.81 , pp. 586-594
    • Ehrlich, L.S.1    Liu, T.2    Scarlata, S.3    Chu, B.4    Carter, C.5
  • 68
    • 33645827371 scopus 로고    scopus 로고
    • Targeting protein-protein interactions by rational design: mimicry of protein surfaces
    • Fletcher S., Hamilton A.D. Targeting protein-protein interactions by rational design: mimicry of protein surfaces. Journal of the Royal Society Interface 2006, 3:215-233.
    • (2006) Journal of the Royal Society Interface , vol.3 , pp. 215-233
    • Fletcher, S.1    Hamilton, A.D.2
  • 69
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey B.M., von Schwedler U., Sundquist W.I., Aiken C. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. Journal of Virology 2002, 76:5667-5677.
    • (2002) Journal of Virology , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 70
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
    • Fuller S.D., Wilk T., Gowen B.E., Kräusslich H.-G., Vogt V.M. Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle. Current Biology 1997, 7:729-738.
    • (1997) Current Biology , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Kräusslich, H.-G.4    Vogt, V.M.5
  • 73
    • 34848866243 scopus 로고    scopus 로고
    • Structure of full-length HIV-1 CA: a model for the mature capsid lattice
    • Ganser-Pornillos B.K., Cheng A., Yeager M. Structure of full-length HIV-1 CA: a model for the mature capsid lattice. Cell 2007, 131:70-79.
    • (2007) Cell , vol.131 , pp. 70-79
    • Ganser-Pornillos, B.K.1    Cheng, A.2    Yeager, M.3
  • 77
    • 84857983099 scopus 로고    scopus 로고
    • The distribution of ligand-binding pockets around protein-protein interfaces suggests a general mechanism for pocket formation
    • Gao M., Skolnick J. The distribution of ligand-binding pockets around protein-protein interfaces suggests a general mechanism for pocket formation. Proceedings of the National Academy of Sciences of United States of America 2012, 109:3784-3789.
    • (2012) Proceedings of the National Academy of Sciences of United States of America , vol.109 , pp. 3784-3789
    • Gao, M.1    Skolnick, J.2
  • 78
    • 2442689040 scopus 로고    scopus 로고
    • The dimerization domain of the HIV-1 capsid protein binds a capsid protein-derived peptide: a biophysical characterization
    • Garzón M.T., Lidón-Moya M.C., Barrera F.N., Prieto A., Gómez J., Mateu M.G., Neira J.L. The dimerization domain of the HIV-1 capsid protein binds a capsid protein-derived peptide: a biophysical characterization. Protein Science 2004, 13:1512-1523.
    • (2004) Protein Science , vol.13 , pp. 1512-1523
    • Garzón, M.T.1    Lidón-Moya, M.C.2    Barrera, F.N.3    Prieto, A.4    Gómez, J.5    Mateu, M.G.6    Neira, J.L.7
  • 80
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Analytical Biochemistry 1989, 182:319-326.
    • (1989) Analytical Biochemistry , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 81
    • 0029794123 scopus 로고    scopus 로고
    • Structure of the amino-terminal core domain of the HIV-1 capsid protein
    • Gitti R.K., Lee B.M., Walker J., Summers M.F., Yoo S., Sundquist W.I. Structure of the amino-terminal core domain of the HIV-1 capsid protein. Science 1996, 273:231-235.
    • (1996) Science , vol.273 , pp. 231-235
    • Gitti, R.K.1    Lee, B.M.2    Walker, J.3    Summers, M.F.4    Yoo, S.5    Sundquist, W.I.6
  • 84
    • 0030682425 scopus 로고    scopus 로고
    • In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus
    • Gross I., Hohenberg H., Kräusslich H.-G. In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus. European Journal of Biochemistry 1997, 249:592-600.
    • (1997) European Journal of Biochemistry , vol.249 , pp. 592-600
    • Gross, I.1    Hohenberg, H.2    Kräusslich, H.-G.3
  • 86
    • 0033080359 scopus 로고    scopus 로고
    • Interaction of the capsid protein p24 (HIV-1) with sequence-derived peptides: influence on p24 dimerization
    • Hilpert K., Behlke J., Scholz C., Misselwitz R., Schneider-Mergener J., Höhne W. Interaction of the capsid protein p24 (HIV-1) with sequence-derived peptides: influence on p24 dimerization. Virology 1999, 254:6-10.
    • (1999) Virology , vol.254 , pp. 6-10
    • Hilpert, K.1    Behlke, J.2    Scholz, C.3    Misselwitz, R.4    Schneider-Mergener, J.5    Höhne, W.6
  • 90
    • 84857910140 scopus 로고    scopus 로고
    • Chemical modulators working at pharmacological interface of target proteins
    • Jeon Y.H., Lee J.Y., Kim S. Chemical modulators working at pharmacological interface of target proteins. Bioorganic and Medicinal Chemistry 2012, 10.1016/i.bmc.2011.12.016.
    • (2012) Bioorganic and Medicinal Chemistry
    • Jeon, Y.H.1    Lee, J.Y.2    Kim, S.3
  • 91
    • 78751519855 scopus 로고    scopus 로고
    • New therapeutic approaches targeted at the late stages of the HIV-1 replication cycle
    • Jiang Y., Liu X., De Clercq E. New therapeutic approaches targeted at the late stages of the HIV-1 replication cycle. Current Medicinal Chemistry 2011, 18:16-28.
    • (2011) Current Medicinal Chemistry , vol.18 , pp. 16-28
    • Jiang, Y.1    Liu, X.2    De Clercq, E.3
  • 95
    • 0141960816 scopus 로고    scopus 로고
    • Generation of a phagemid mouse recombinant antibody fragment library by multisite-directed mutagenesis
    • Kelley L.L., Momany C. Generation of a phagemid mouse recombinant antibody fragment library by multisite-directed mutagenesis. Biotechniques 2003, 35:750-752.
    • (2003) Biotechniques , vol.35 , pp. 750-752
    • Kelley, L.L.1    Momany, C.2
  • 96
    • 33749009745 scopus 로고    scopus 로고
    • Implications for viral capsid assembly from crystal structures of HIV-1 Gag (1-278) and CA(N) (133-278)
    • Kelly B.N., Howard B.R., Wang H., Robinson H., Sundquist W.I., Hill C.P. Implications for viral capsid assembly from crystal structures of HIV-1 Gag (1-278) and CA(N) (133-278). Biochemistry 2006, 45:11257-11266.
    • (2006) Biochemistry , vol.45 , pp. 11257-11266
    • Kelly, B.N.1    Howard, B.R.2    Wang, H.3    Robinson, H.4    Sundquist, W.I.5    Hill, C.P.6
  • 98
    • 67749142080 scopus 로고    scopus 로고
    • High-affinity recognition of Lanthanide (III) Chelate Complexes by a Reprogrammed Human Lipocalin 2
    • Kim H.J., Eichinger A., Skerra A. High-affinity recognition of Lanthanide (III) Chelate Complexes by a Reprogrammed Human Lipocalin 2. Journal of the American Chemical Society 2009, 131:3565-3576.
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 3565-3576
    • Kim, H.J.1    Eichinger, A.2    Skerra, A.3
  • 102
    • 0036634466 scopus 로고    scopus 로고
    • Kinetic analysis of the role of intersubunit interactions in human immunodeficiency virus type 1 capsid protein assembly in vitro
    • Lanman J., Sexton J., Sakalian M., Prevelige P.E. Kinetic analysis of the role of intersubunit interactions in human immunodeficiency virus type 1 capsid protein assembly in vitro. Journal of Virology 2002, 76:6900-6908.
    • (2002) Journal of Virology , vol.76 , pp. 6900-6908
    • Lanman, J.1    Sexton, J.2    Sakalian, M.3    Prevelige, P.E.4
  • 104
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 capsid protein
    • Li S., Hill C.P., Sundquist W.I., Finch J.T. Image reconstructions of helical assemblies of the HIV-1 capsid protein. Nature 2000, 407:409-413.
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 105
    • 64049088223 scopus 로고    scopus 로고
    • Discovery of dual inhibitors targeting both HIV-1 capsid and human cyclopyllin A to inhibit the assembly and uncoating of the viral capsid
    • Li J., Tan Z., Tang S., Hewlett I., Pang R., He M., He S., Tian B., Chen K., Yang M. Discovery of dual inhibitors targeting both HIV-1 capsid and human cyclopyllin A to inhibit the assembly and uncoating of the viral capsid. Bioorganic and Medicinal Chemistry 2009, 17:3177-3188.
    • (2009) Bioorganic and Medicinal Chemistry , vol.17 , pp. 3177-3188
    • Li, J.1    Tan, Z.2    Tang, S.3    Hewlett, I.4    Pang, R.5    He, M.6    He, S.7    Tian, B.8    Chen, K.9    Yang, M.10
  • 106
    • 35649023220 scopus 로고    scopus 로고
    • HIV-1 capsid proteins and cyclophilin A as new targets for anti-AIDS therapeutic agents
    • Li J., Tang S., Hewlett I., Yang M. HIV-1 capsid proteins and cyclophilin A as new targets for anti-AIDS therapeutic agents. Infectious Disorders-Drug Targets 2007, 7:238-244.
    • (2007) Infectious Disorders-Drug Targets , vol.7 , pp. 238-244
    • Li, J.1    Tang, S.2    Hewlett, I.3    Yang, M.4
  • 107
    • 0028342554 scopus 로고
    • Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis
    • Mammano F., öhagen å., Höglund S., Göttlinger H.G. Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis. Journal of Virology 1994, 68:4927-4936.
    • (1994) Journal of Virology , vol.68 , pp. 4927-4936
    • Mammano, F.1    Öhagen, Å.2    Höglund, S.3    Göttlinger, H.G.4
  • 108
    • 70349947190 scopus 로고    scopus 로고
    • The capsid protein of human immunodeficiency virus: interactions of HIV-1 capsid with host protein factors
    • Mascarenhas A.P., Musier-Forsyth K. The capsid protein of human immunodeficiency virus: interactions of HIV-1 capsid with host protein factors. FEBS Journal 2009, 276:6118-6127.
    • (2009) FEBS Journal , vol.276 , pp. 6118-6127
    • Mascarenhas, A.P.1    Musier-Forsyth, K.2
  • 109
    • 0029101761 scopus 로고
    • Antibody recognition of picornaviruses and escape from neutralization: a structural view
    • Mateu M.G. Antibody recognition of picornaviruses and escape from neutralization: a structural view. Virus Research 1995, 38:1-24.
    • (1995) Virus Research , vol.38 , pp. 1-24
    • Mateu, M.G.1
  • 110
    • 0036302078 scopus 로고    scopus 로고
    • Conformational stability of dimeric and monomeric forms of the C-terminal domain of human immunodeficiency virus-1 capsid protein
    • Mateu M.G. Conformational stability of dimeric and monomeric forms of the C-terminal domain of human immunodeficiency virus-1 capsid protein. Journal of Molecular Biology 2002, 318:519-531.
    • (2002) Journal of Molecular Biology , vol.318 , pp. 519-531
    • Mateu, M.G.1
  • 111
    • 70349971586 scopus 로고    scopus 로고
    • The capsid protein of human immunodeficiency virus: intersubunit interactions during virus assembly
    • Mateu M.G. The capsid protein of human immunodeficiency virus: intersubunit interactions during virus assembly. FEBS Journal 2009, 276:6098-6109.
    • (2009) FEBS Journal , vol.276 , pp. 6098-6109
    • Mateu, M.G.1
  • 115
    • 81555225908 scopus 로고    scopus 로고
    • The expanding view of protein-protein interactions: complexes involving intrinsically disordered proteins
    • Mészáros B., Simon I., Dosztány S. The expanding view of protein-protein interactions: complexes involving intrinsically disordered proteins. Physical Biology 2011, 8:035003.
    • (2011) Physical Biology , vol.8 , pp. 035003
    • Mészáros, B.1    Simon, I.2    Dosztány, S.3
  • 116
    • 0027829616 scopus 로고
    • Macromolecular crowding and molecular recognition
    • Minton A.P. Macromolecular crowding and molecular recognition. Journal of Molecular Recognition 1993, 6:211-214.
    • (1993) Journal of Molecular Recognition , vol.6 , pp. 211-214
    • Minton, A.P.1
  • 117
    • 84870434069 scopus 로고    scopus 로고
    • (Eds.), 2012. Special issue on Retroviral RNA, protein co-factors and chaperones. Virus Research.
    • Mirambeau, G. Darlix, J.-L., Summers, M.F., Berkhout, B. (Eds.), 2012. Special issue on Retroviral RNA, protein co-factors and chaperones. Virus Research.
    • Mirambeau, G.1    Darlix, J.-L.2    Summers, M.F.3    Berkhout, B.4
  • 118
    • 78751663443 scopus 로고    scopus 로고
    • Features, processing states and heterologous protein interactions in the modulation of the retroviral nucleocapsid protein function
    • Mirambeau G., Lyonnais S., Gorelick R.J. Features, processing states and heterologous protein interactions in the modulation of the retroviral nucleocapsid protein function. RNA Biology 2010, 7:724-734.
    • (2010) RNA Biology , vol.7 , pp. 724-734
    • Mirambeau, G.1    Lyonnais, S.2    Gorelick, R.J.3
  • 120
    • 78149417909 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange analysis of HIV-1 capsid assembly and maturation
    • Monroe E.B., Kang S., Kyere S.K., Li R., Prevelige P.E. Hydrogen/deuterium exchange analysis of HIV-1 capsid assembly and maturation. Structure 2010, 18:1483-1491.
    • (2010) Structure , vol.18 , pp. 1483-1491
    • Monroe, E.B.1    Kang, S.2    Kyere, S.K.3    Li, R.4    Prevelige, P.E.5
  • 121
    • 34548779127 scopus 로고    scopus 로고
    • Hot spots-a review of the protein-protein interface determinant amino acid residues
    • Moreira I.S., Fernandes P.A., Ramos M.J. Hot spots-a review of the protein-protein interface determinant amino acid residues. Proteins 2007, 68:803-812.
    • (2007) Proteins , vol.68 , pp. 803-812
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 122
    • 82055192318 scopus 로고    scopus 로고
    • Targeting protein-protein and protein-nucleic acid interactions for anti-HIV therapy
    • Mori M., Manetti F., Botta M. Targeting protein-protein and protein-nucleic acid interactions for anti-HIV therapy. Current Pharmaceutical Design 2011, 17:3713-3728.
    • (2011) Current Pharmaceutical Design , vol.17 , pp. 3713-3728
    • Mori, M.1    Manetti, F.2    Botta, M.3
  • 123
    • 4644301808 scopus 로고    scopus 로고
    • High-resolution structure of a retroviral capsid hexameric amino-terminal domain
    • Mortuza G.B., Haire L.F., Stevens A., Smerdon S.J., Stoye J.P., Taylor I.A. High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature 2004, 431:481-485.
    • (2004) Nature , vol.431 , pp. 481-485
    • Mortuza, G.B.1    Haire, L.F.2    Stevens, A.3    Smerdon, S.J.4    Stoye, J.P.5    Taylor, I.A.6
  • 124
    • 78751670345 scopus 로고    scopus 로고
    • Properties and functions of the nucleocapsid protein in virus assembly
    • Muriaux D., Darlix J.-L. Properties and functions of the nucleocapsid protein in virus assembly. RNA Biology 2010, 7:744-753.
    • (2010) RNA Biology , vol.7 , pp. 744-753
    • Muriaux, D.1    Darlix, J.-L.2
  • 125
    • 6944223885 scopus 로고    scopus 로고
    • Targeting the assembly of the human immunodeficiency virus type 1
    • Muriaux D., Darlix J.-L., Cimarelli A. Targeting the assembly of the human immunodeficiency virus type 1. Current Pharmaceutical Design 2004, 10:3725-3739.
    • (2004) Current Pharmaceutical Design , vol.10 , pp. 3725-3739
    • Muriaux, D.1    Darlix, J.-L.2    Cimarelli, A.3
  • 127
    • 70349967810 scopus 로고    scopus 로고
    • The capsid protein of human immunodeficiency virus: designing inhibitors of capsid assembly
    • Neira J.L. The capsid protein of human immunodeficiency virus: designing inhibitors of capsid assembly. FEBS Journal 2009, 276:6110-6117.
    • (2009) FEBS Journal , vol.276 , pp. 6110-6117
    • Neira, J.L.1
  • 128
    • 67649361866 scopus 로고    scopus 로고
    • Biophysical and structural studies on the capsid protein of the human immunodeficiency virus type 1: a new drug target?
    • Neira J.L. Biophysical and structural studies on the capsid protein of the human immunodeficiency virus type 1: a new drug target?. The Scientific World Journal 2009, 9:404-419.
    • (2009) The Scientific World Journal , vol.9 , pp. 404-419
    • Neira, J.L.1
  • 129
    • 0028292220 scopus 로고
    • Fullerene-like organization of HIV gag-protein shell in virus-like particles produced by recombinant baculovirus
    • Nermut M.V., Hockley D.J., Jowett J.B., Jones I.M., Garreau M., Thomas D. Fullerene-like organization of HIV gag-protein shell in virus-like particles produced by recombinant baculovirus. Virology 1994, 198:288-296.
    • (1994) Virology , vol.198 , pp. 288-296
    • Nermut, M.V.1    Hockley, D.J.2    Jowett, J.B.3    Jones, I.M.4    Garreau, M.5    Thomas, D.6
  • 131
    • 84855347756 scopus 로고    scopus 로고
    • Interfacial inhibitors: targeting macromolecular complexes
    • Pommier Y., Marchand C. Interfacial inhibitors: targeting macromolecular complexes. Nature Reviews 2012, 11:25-36.
    • (2012) Nature Reviews , vol.11 , pp. 25-36
    • Pommier, Y.1    Marchand, C.2
  • 135
    • 84868629559 scopus 로고    scopus 로고
    • (inventor), Small molecule inhibitors of HIV-1 capsid assembly. U.S. Patent application number 20,090,176,776.
    • Prevelige, P. (inventor), 2006. Small molecule inhibitors of HIV-1 capsid assembly. U.S. Patent application number 20,090,176,776.
    • (2006)
    • Prevelige, P.1
  • 136
    • 80051752946 scopus 로고    scopus 로고
    • New approaches for antiviral targeting of HIV assembly
    • Prevelige P.E. New approaches for antiviral targeting of HIV assembly. Journal of Molecular Biology 2011, 410:634-640.
    • (2011) Journal of Molecular Biology , vol.410 , pp. 634-640
    • Prevelige, P.E.1
  • 139
    • 0029961364 scopus 로고    scopus 로고
    • The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle
    • Reicin A.S., öhagen å., Yin L., Höglund S., Goff S.P. The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle. Journal of Virology 1996, 70:8645-8652.
    • (1996) Journal of Virology , vol.70 , pp. 8645-8652
    • Reicin, A.S.1    Öhagen, Å.2    Yin, L.3    Höglund, S.4    Goff, S.P.5
  • 141
    • 79551676332 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on the inhibition of virus assembly and virus-cell receptor recognition
    • Rincón V., Bocanegra R., Rodríguez-Huete A., Rivas G., Mateu M.G. Effects of macromolecular crowding on the inhibition of virus assembly and virus-cell receptor recognition. Biophysical Journal 2011, 100:738-746.
    • (2011) Biophysical Journal , vol.100 , pp. 738-746
    • Rincón, V.1    Bocanegra, R.2    Rodríguez-Huete, A.3    Rivas, G.4    Mateu, M.G.5
  • 142
    • 33644943804 scopus 로고    scopus 로고
    • Nuclear transport of trimeric assembly intermediates exerts a morphogenetic control on the icosahedral parvovirus capsid
    • Riolobos L., Reguera J., Mateu M.G., Almendral J.M. Nuclear transport of trimeric assembly intermediates exerts a morphogenetic control on the icosahedral parvovirus capsid. Journal of Molecular Biology 2006, 357:1026-1038.
    • (2006) Journal of Molecular Biology , vol.357 , pp. 1026-1038
    • Riolobos, L.1    Reguera, J.2    Mateu, M.G.3    Almendral, J.M.4
  • 143
    • 33846010537 scopus 로고    scopus 로고
    • Identification of human scFvs targeting atherosclerotic lesions. Selection by single round in vivo phage display
    • Robert R., Jacobin-Valat M.-J., Daret D., Miraux S., Nurden A.T. Identification of human scFvs targeting atherosclerotic lesions. Selection by single round in vivo phage display. Journal of Biological Chemistry 2006, 281:40135-40143.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 40135-40143
    • Robert, R.1    Jacobin-Valat, M.-J.2    Daret, D.3    Miraux, S.4    Nurden, A.T.5
  • 144
    • 35548986260 scopus 로고    scopus 로고
    • Maturation inhibitors: a new therapeutic class targets the virus structure
    • Salzwedel K., Martin D.E., Sakalian M. Maturation inhibitors: a new therapeutic class targets the virus structure. AIDS Reviews 2007, 9:162-172.
    • (2007) AIDS Reviews , vol.9 , pp. 162-172
    • Salzwedel, K.1    Martin, D.E.2    Sakalian, M.3
  • 145
    • 0034646561 scopus 로고    scopus 로고
    • A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin
    • Schlehuber S., Beste G., Skerra A. A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin. Journal of Molecular Biology 2000, 297:1105-1120.
    • (2000) Journal of Molecular Biology , vol.297 , pp. 1105-1120
    • Schlehuber, S.1    Beste, G.2    Skerra, A.3
  • 146
    • 78650064115 scopus 로고    scopus 로고
    • Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization
    • Shi J., Zhou J., Shah V.B., Aiken C., Whitby K. Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization. Journal of Virology 2011, 85:542-549.
    • (2011) Journal of Virology , vol.85 , pp. 542-549
    • Shi, J.1    Zhou, J.2    Shah, V.B.3    Aiken, C.4    Whitby, K.5
  • 147
    • 80155138647 scopus 로고    scopus 로고
    • Structure of a monomeric mutant of the HIV-1 capsid protein
    • Shin R., Tzou Y.-M., Krishna N.R. Structure of a monomeric mutant of the HIV-1 capsid protein. Biochemistry 2011, 50:9457-9467.
    • (2011) Biochemistry , vol.50 , pp. 9457-9467
    • Shin, R.1    Tzou, Y.-M.2    Krishna, N.R.3
  • 150
    • 9644289511 scopus 로고    scopus 로고
    • The use of cell-penetrating peptides for drug delivery
    • Temsamani J., Vidal P. The use of cell-penetrating peptides for drug delivery. Drug Discovery Today 2004, 9:1012-1019.
    • (2004) Drug Discovery Today , vol.9 , pp. 1012-1019
    • Temsamani, J.1    Vidal, P.2
  • 153
    • 0018369485 scopus 로고
    • Study of protein subunit association equilibria by elution gel chromatography
    • Valdes R., Ackers G.K. Study of protein subunit association equilibria by elution gel chromatography. Methods in Enzymology 1979, 61:125-142.
    • (1979) Methods in Enzymology , vol.61 , pp. 125-142
    • Valdes, R.1    Ackers, G.K.2
  • 157
  • 161
    • 70450169243 scopus 로고    scopus 로고
    • Inhibition of protein-protein interactions using designed molecules
    • Wilson A.J. Inhibition of protein-protein interactions using designed molecules. Chemical Society Reviews 2009, 38:3289-3300.
    • (2009) Chemical Society Reviews , vol.38 , pp. 3289-3300
    • Wilson, A.J.1
  • 162
    • 39749133643 scopus 로고    scopus 로고
    • Solution structure of a double mutant of the carboxy-terminal dimerization domain of the HIV-1 capsid protein
    • Wong H.C., Shin R., Krishna N.R. Solution structure of a double mutant of the carboxy-terminal dimerization domain of the HIV-1 capsid protein. Biochemistry 2008, 47:2289-2297.
    • (2008) Biochemistry , vol.47 , pp. 2289-2297
    • Wong, H.C.1    Shin, R.2    Krishna, N.R.3
  • 165
    • 80051756121 scopus 로고    scopus 로고
    • Design of in vitro symmetric complexes and analysis of hybrid methods reveal mechanisms of HIV capsid assembly
    • Yeager M. Design of in vitro symmetric complexes and analysis of hybrid methods reveal mechanisms of HIV capsid assembly. Journal of Molecular Biology 2011, 410:534-552.
    • (2011) Journal of Molecular Biology , vol.410 , pp. 534-552
    • Yeager, M.1
  • 168
    • 67549133427 scopus 로고    scopus 로고
    • Capsid (CA) protein as a novel drug target: recent progress in the research of HIV-1 CA inhibitors
    • Zhang J., Liu X., De Clercq E. Capsid (CA) protein as a novel drug target: recent progress in the research of HIV-1 CA inhibitors. Mini-Reviews in Medicinal Chemistry 2009, 9:510-518.
    • (2009) Mini-Reviews in Medicinal Chemistry , vol.9 , pp. 510-518
    • Zhang, J.1    Liu, X.2    De Clercq, E.3
  • 169
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: biochemical, biophysical and potential physiological consequences
    • Zhou H.X., Rivas G., Minton A.P. Macromolecular crowding and confinement: biochemical, biophysical and potential physiological consequences. Annual Review of Biophysics 2008, 37:375-397.
    • (2008) Annual Review of Biophysics , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3


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