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Volumn 11, Issue , 2011, Pages

Dynamical basis for drug resistance of HIV-1 protease

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE INHIBITOR; P16 PROTEASE, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 79959992520     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-11-31     Document Type: Article
Times cited : (15)

References (64)
  • 2
    • 0036176766 scopus 로고    scopus 로고
    • Rational approach to aids drug design through structural biology
    • DOI 10.1146/annurev.med.53.052901.131947
    • Rational approach to AIDS drug design through structural biology. A Wlodawer, Ann Red Med 2002 53 595 614 10.1146/annurev.med.53.052901.131947 (Pubitemid 34177897)
    • (2002) Annual Review of Medicine , vol.53 , pp. 595-614
    • Wlodawer, A.1
  • 3
    • 0041922335 scopus 로고    scopus 로고
    • HIV-1 protease inhibitors: A comparative QSAR analysis
    • DOI 10.2174/0929867033457070
    • HIV-1 protease inhibitors: a comparative QSAR analysis. A Kurup, SB Mekapati, R Garg, C Hansch, Curr Med Chem 2003 10 1679 1688 10.2174/ 0929867033457070 12871116 (Pubitemid 37038593)
    • (2003) Current Medicinal Chemistry , vol.10 , Issue.17 , pp. 1679-1688
    • Kurup, A.1    Mekapati, S.B.2    Garg, R.3    Hansch, C.4
  • 5
    • 0031804609 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 protease: A major success of structure-assisted drug design
    • DOI 10.1146/annurev.biophys.27.1.249
    • Inhibitors of HIV-1 protease: A major success of structureassisted drug design. A Wlodawer, J Vondrasek, Annu Rev Biophys Biomol Struct 1998 27 249 284 10.1146/annurev.biophys.27.1.249 9646869 (Pubitemid 28286016)
    • (1998) Annual Review of Biophysics and Biomolecular Structure , vol.27 , pp. 249-284
    • Wlodawer, A.1    Vondrasek, J.2
  • 6
    • 0034194615 scopus 로고    scopus 로고
    • HIV-1 entry - An expanding portal for drug discovery
    • DOI 10.1016/S1359-6446(00)01484-7, PII S1359644600014847
    • HIV-1 entry- an expanding portal for drug discovery. WS Blair, Drug Discovery Today 2000 5 183 194 10.1016/S1359-6446(00)01484-7 10790262 (Pubitemid 30211615)
    • (2000) Drug Discovery Today , vol.5 , Issue.5 , pp. 183-194
    • Blair, W.S.1    Lin, P.-F.2    Meanwell, N.A.3    Wallace, O.B.4
  • 9
    • 0034974984 scopus 로고    scopus 로고
    • The active site of HIV-1 protease
    • DOI 10.1002/med.1012
    • The active site of HIV-1 protease. PP Mager, Med Res Rev 2001 21 348 353 10.1002/med.1012 11410934 (Pubitemid 32565497)
    • (2001) Medicinal Research Reviews , vol.21 , Issue.4 , pp. 348-353
    • Mager, P.P.1
  • 10
    • 33748514992 scopus 로고    scopus 로고
    • Overcoming HIV-1 resistance to protease inhibitors
    • DOI 10.1016/j.ddmec.2006.06.005, PII S174067650600040X
    • Overcoming HIV-1 resistance to protease inhibitors. E Freire, Drug Discov Today 2006 3 281 286 10.1016/j.ddmec.2006.06.005 (Pubitemid 44356304)
    • (2006) Drug Discovery Today: Disease Mechanisms , vol.3 , Issue.2 , pp. 281-286
    • Freire, E.1
  • 11
    • 0037469148 scopus 로고    scopus 로고
    • A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance
    • DOI 10.1021/bi027019u
    • A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance. S Muzammil, P Ross, E Freire, Biochemistry 2003 42 631 638 10.1021/bi027019u 12534275 (Pubitemid 36133287)
    • (2003) Biochemistry , vol.42 , Issue.3 , pp. 631-638
    • Muzammil, S.1    Ross, P.2    Freire, E.3
  • 12
    • 10944234802 scopus 로고    scopus 로고
    • Molecular dynamics simulations of 14 HIV protease mutants in complexes with indinavir
    • DOI 10.1007/s00894-004-0205-x
    • Molecular dynamics simulations of 14 HIV protease mutants in complexes with indinavir. XF Chen, IT Weber, RW Harrison, J Mol Model 2004 10 373 381 10.1007/s00894-004-0205-x 15597206 (Pubitemid 40012066)
    • (2004) Journal of Molecular Modeling , vol.10 , Issue.5-6 , pp. 373-381
    • Chen, X.1    Weber, I.T.2    Harrison, R.W.3
  • 13
    • 42449147045 scopus 로고    scopus 로고
    • Evaluating the potency of HIV-1 protease drugs to combat resistance
    • DOI 10.1002/prot.21808
    • Evaluating the potency of HIV-1 protease drugs to combat resistance. TJ Hou, WA McLaughlin, W Wang, Proteins 2008 71 1163 1174 18004760 (Pubitemid 351564043)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.3 , pp. 1163-1174
    • Hou, T.1    McLaughlin, W.A.2    Wang, W.3
  • 14
    • 34248336220 scopus 로고    scopus 로고
    • Unique thermodynamic response of tipranavir to human immunodeficiency virus type 1 protease drug resistance mutations
    • DOI 10.1128/JVI.02706-06
    • Unique thermodynamic response of tipranavir to human immunodeficiency virus type 1 protease drug resistance mutations. S Muzammil, AA Armstrong, LW Kang, A Jakalian, PR Bonneau, V Schmelmer, LM Amzel, E Freire, J Virol 2007 81 5144 5154 10.1128/JVI.02706-06 17360759 (Pubitemid 46744425)
    • (2007) Journal of Virology , vol.81 , Issue.10 , pp. 5144-5154
    • Muzammil, S.1    Armstrong, A.A.2    Kang, L.W.3    Jakalian, A.4    Bonneau, P.R.5    Schmelmer, V.6    Amzel, L.M.7    Freire, E.8
  • 15
    • 0036121219 scopus 로고    scopus 로고
    • Substrate shape determines specificity of recognition for HIV-1 protease: Analysis of crystal structures of six substrate complexes
    • DOI 10.1016/S0969-2126(02)00720-7, PII S0969212602007207
    • Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes. M Prabu-Jeyabalan, E Nalivaika, CA Schiffer, Structure 2002 10 369 381 10.1016/S0969-2126(02)00720-7 12005435 (Pubitemid 34230624)
    • (2002) Structure , vol.10 , Issue.3 , pp. 369-381
    • Prabu-Jeyabalan, M.1    Nalivaika, E.2    Schiffer, C.A.3
  • 16
    • 0033921617 scopus 로고    scopus 로고
    • Phenotypic and genotypic analysis of clinical HIV-1 isolates reveals extensive protease inhibitor cross-resistance: A survey of over 6000 samples
    • DOI 10.1097/00002030-200006160-00018
    • Phenotypic and genotypic analysis of clinical HIV-1 isolates reveals extensive protease inhibitor cross-resistance: a survey of over 6000 samples. K Hertogs, S Bloor, SD Kemp, C Van den Eynde, TM Alcorn, R Pauwels, MV Houtte, S Staszewski, V Miller, BA Larder, AIDS 2000 14 1203 1210 10.1097/00002030- 200006160-00018 10894285 (Pubitemid 30420664)
    • (2000) AIDS , vol.14 , Issue.9 , pp. 1203-1210
    • Hertogs, K.1    Bloor, S.2    Kemp, S.D.3    Van Den Eynde, C.4    Alcorn, T.M.5    Pauwels, R.6    Van Houtte, M.7    Staszewski, S.8    Miller, V.9    Larder, B.A.10
  • 17
    • 0036222716 scopus 로고    scopus 로고
    • Genotypic testing for human immunodeficiency virus type 1 drug resistance
    • DOI 10.1128/CMR.15.2.247-277.2002
    • Genotypic testing for human immunodeficiency virus type 1 drug resistance. RW Shafer, Clin Microbiol Rev 2002 15 247 277 10.1128/CMR.15.2.247- 277.2002 11932232 (Pubitemid 34303765)
    • (2002) Clinical Microbiology Reviews , vol.15 , Issue.2 , pp. 247-277
    • Shafer, R.W.1
  • 18
    • 1842509978 scopus 로고    scopus 로고
    • Positive Selection Detection in 40,000 Human Immunodeficiency Virus (HIV) Type 1 Sequences Automatically Identifies Drug Resistance and Positive Fitness Mutations in HIV Protease and Reverse Transcriptase
    • DOI 10.1128/JVI.78.7.3722-3732.2004
    • Positive selection detection in 40,000 human immunodeficiency virus (HIV) type 1 sequences automatically identifies drug resistance and positive fitness mutations in HIV protease and reverse transcriptase. L Chen, A Perlina, CJ Lee, J Virol 2004 78 3722 3732 10.1128/JVI.78.7.3722-3732.2004 15016892 (Pubitemid 38568311)
    • (2004) Journal of Virology , vol.78 , Issue.7 , pp. 3722-3732
    • Chen, L.1    Perlina, A.2    Lee, C.J.3
  • 20
    • 33747150776 scopus 로고    scopus 로고
    • Algorithms for the interpretation of HIV-1 genotypic drug resistance information
    • DOI 10.1016/j.antiviral.2006.05.003, PII S0166354206001306
    • Algorithms for the interpretation of HIV-1 genotypic drug resistance information. J Vercauteren, AM Vandamme, Antivir Res 2006 71 335 342 10.1016/j.antiviral.2006.05.003 16782210 (Pubitemid 44223769)
    • (2006) Antiviral Research , vol.71 , Issue.SPEC. ISS. 2-3 , pp. 335-342
    • Vercauteren, J.1    Vandamme, A.-M.2
  • 23
    • 49049087284 scopus 로고    scopus 로고
    • Relating sequence evolution of HIV1-protease to its underlying molecular mechanics
    • 10.1016/j.gene.2008.06.007 18590806
    • Relating sequence evolution of HIV1-protease to its underlying molecular mechanics. K Hamacher, Gene 2008 422 30 36 10.1016/j.gene.2008.06.007 18590806
    • (2008) Gene , vol.422 , pp. 30-36
    • Hamacher, K.1
  • 24
    • 76549102880 scopus 로고    scopus 로고
    • Detecting and understanding combinatorial mutation patterns responsible for HIV drug resistance
    • 10.1073/pnas.0907304107 20080674
    • Detecting and understanding combinatorial mutation patterns responsible for HIV drug resistance. J Zhang, T Hou, W Wang, JS Liu, Proc Natl Acad Sci USA 2010 107 1321 1326 10.1073/pnas.0907304107 20080674
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1321-1326
    • Zhang, J.1    Hou, T.2    Wang, W.3    Liu, J.S.4
  • 25
    • 17044404749 scopus 로고    scopus 로고
    • Computer prediction of drug resistance mutations in proteins
    • 10.1016/S1359-6446(05)03377-5 15809198
    • Computer prediction of drug resistance mutations in proteins. ZW Cao, LY Han, CJ Zheng, ZL Ji, X Chen, HH Lin, YZ Chen, Drug Discov Today 2005 10 521 529 10.1016/S1359-6446(05)03377-5 15809198
    • (2005) Drug Discov Today , vol.10 , pp. 521-529
    • Cao, Z.W.1    Han, L.Y.2    Zheng, C.J.3    Ji, Z.L.4    Chen, X.5    Lin, H.H.6    Chen, Y.Z.7
  • 26
    • 34548720347 scopus 로고    scopus 로고
    • Mining complex genotypic features for predicting HIV-1 drug resistance
    • DOI 10.1093/bioinformatics/btm353
    • Mining complex genotypic features for predicting HIV-1 drug resistance. H Saigo, T Uno, K Tsuda, Bioinformatics 2007 23 2455 2462 10.1093/bioinformatics/ btm353 17698858 (Pubitemid 47423844)
    • (2007) Bioinformatics , vol.23 , Issue.18 , pp. 2455-2462
    • Saigo, H.1    Uno, T.2    Tsuda, K.3
  • 27
    • 3042812835 scopus 로고    scopus 로고
    • Simple linear model provides highly accurate genotypic predictions of HIV-1 drug resistance
    • Simple linear model provides highly accurate genotypic predictions of HIV-1 drug resistance. K Wang, E Jenwitheesuk, R Samudrala, JE Mittler, Antivir Ther 2004 9 343 352 15259897 (Pubitemid 38878750)
    • (2004) Antiviral Therapy , vol.9 , Issue.3 , pp. 343-352
    • Wang, K.1    Jenwitheesuk, E.2    Samudrala, R.3    Mittler, J.E.4
  • 30
    • 0034851803 scopus 로고    scopus 로고
    • Can an optimization/scoring procedure in ligand-protein docking be employed to probe drug-resistant mutations in proteins?
    • DOI 10.1016/S1093-3263(01)00091-2, PII S1093326301000912
    • Can an optimization/scoring procedure in ligand protein docking be employed to probe drug resistant mutations in proteins? YZ Chen, XL Gu, ZW Cao, J Mol Graph Model 2001 19 560 570 10.1016/S1093-3263(01)00091-2 11552685 (Pubitemid 32823260)
    • (2001) Journal of Molecular Graphics and Modelling , vol.19 , Issue.6 , pp. 560-570
    • Chen, Y.Z.1    Gu, X.L.2    Cao, Z.W.3
  • 31
    • 0041341885 scopus 로고    scopus 로고
    • Structure-based phenotyping predicts HIV-1 protease inhibitor resistance
    • DOI 10.1110/ps.0301103
    • Structure-based phenotyping predicts HIV-1 protease inhibitor resistance. MD Shenderovich, RM Kagan, PNR Heseltine, K Ramnarayan, Protein Sci 2003 12 1706 1718 10.1110/ps.0301103 12876320 (Pubitemid 36910051)
    • (2003) Protein Science , vol.12 , Issue.8 , pp. 1706-1718
    • Shenderovich, M.D.1    Kagan, R.M.2    Heseltine, P.N.R.3    Ramnarayan, K.4
  • 32
    • 61449101624 scopus 로고    scopus 로고
    • Predicting drug resistance of the HIV-1 protease using molecular interaction energy components
    • 10.1002/prot.22192 18704937
    • Predicting drug resistance of the HIV-1 protease using molecular interaction energy components. T Hou, W Zhang, J Wang, W Wang, Proteins 2009 74 837 846 10.1002/prot.22192 18704937
    • (2009) Proteins , vol.74 , pp. 837-846
    • Hou, T.1    Zhang, W.2    Wang, J.3    Wang, W.4
  • 35
    • 77952938726 scopus 로고    scopus 로고
    • Global dynamics of proteins: Bridging between structure and function
    • 10.1146/annurev.biophys.093008.131258 20192781
    • Global dynamics of proteins: bridging between structure and function. I Bahar, TR Lezon, LW Yang, E Eyal, Annu Rev Biophys 2010 39 23 42 10.1146/annurev.biophys.093008.131258 20192781
    • (2010) Annu Rev Biophys , vol.39 , pp. 23-42
    • Bahar, I.1    Lezon, T.R.2    Yang, L.W.3    Eyal, E.4
  • 36
    • 68149163617 scopus 로고    scopus 로고
    • Large-scale evaluation of dynamically important residues in proteins predicted by the perturbation analysis of a coarse-grained elastic model
    • 10.1186/1472-6807-9-45 19591676
    • Large-scale evaluation of dynamically important residues in proteins predicted by the perturbation analysis of a coarse-grained elastic model. W Zheng, M Tekpinar, BMC Struct Biol 2009 9 45 10.1186/1472-6807-9-45 19591676
    • (2009) BMC Struct Biol , vol.9 , pp. 45
    • Zheng, W.1    Tekpinar, M.2
  • 37
    • 33749029273 scopus 로고    scopus 로고
    • Pump-probe molecular dynamics as a tool for studying protein motion and long range coupling
    • DOI 10.1002/prot.21146
    • Pump-probe molecular dynamics as a tool for studying protein motion and long range coupling. K Sharp, JJ Skinner, Proteins 2006 65 347 361 10.1002/prot.21146 16933296 (Pubitemid 44454109)
    • (2006) Proteins: Structure, Function and Genetics , vol.65 , Issue.2 , pp. 347-361
    • Sharp, K.1    Skinner, J.J.2
  • 38
    • 58949102247 scopus 로고    scopus 로고
    • Signaling pathways of PDZ2 domain: A molecular dynamics interaction correlation analysis
    • 10.1002/prot.22139 18618698
    • Signaling pathways of PDZ2 domain: A molecular dynamics interaction correlation analysis. Y Kong, M Karplus, Proteins 2009 74 145 154 10.1002/prot.22139 18618698
    • (2009) Proteins , vol.74 , pp. 145-154
    • Kong, Y.1    Karplus, M.2
  • 39
    • 55849106575 scopus 로고    scopus 로고
    • Efficient identification of critical residues based only on protein structure by network analysis
    • 10.1371/journal.pone.0000421 17502913
    • Efficient identification of critical residues based only on protein structure by network analysis. MP Cusack, B Thibert, DE Bredesen, G del Rio, PLoS ONE 2007 2 421 10.1371/journal.pone.0000421 17502913
    • (2007) PLoS ONE , vol.2 , pp. 5421
    • Cusack, M.P.1    Thibert, B.2    Bredesen, D.E.3    Del Rio, G.4
  • 40
    • 65949104571 scopus 로고    scopus 로고
    • Frequency-resolved communication maps for proteins and other nanoscale materials
    • 10.1063/1.3130149 19466865
    • Frequency-resolved communication maps for proteins and other nanoscale materials. DM Leitner, J Chem Phys 2009 130 195101 195109 10.1063/1.3130149 19466865
    • (2009) J Chem Phys , vol.130 , pp. 195101-195109
    • Leitner, D.M.1
  • 41
    • 79952681074 scopus 로고    scopus 로고
    • Dynamics studies of luciferase using elastic network model: How the sequence distribution of luciferase determines its color
    • 10.1093/protein/gzq109 21159621
    • Dynamics studies of luciferase using elastic network model: how the sequence distribution of luciferase determines its color. Y Mao, Protein Eng Des Sel 2011 24 341 349 10.1093/protein/gzq109 21159621
    • (2011) Protein Eng des Sel , vol.24 , pp. 341-349
    • Mao, Y.1
  • 42
    • 1942519782 scopus 로고    scopus 로고
    • Finite Element Solution of the Steady-State Smoluchowski Equation for Rate Constant Calculations
    • Finite element solution of the steady-state Smoluchowski equation for rate constant calculations. Y Song, Y Zhang, T Shen, CL Bajaj, JA McCammon, NA Baker, Biophys J 2004 86 2017 2029 10.1016/S0006-3495(04)74263-0 15041644 (Pubitemid 38524394)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 2017-2029
    • Song, Y.1    Zhang, Y.2    Shen, T.3    Bajaj, C.L.4    McCammon, J.A.5    Baker, N.A.6
  • 43
    • 33644948688 scopus 로고    scopus 로고
    • HIV-1 protease flaps spontaneously close to the correct structure in simulations following manual placement of an inhibitor into the open state
    • 10.1021/ja058211x 16506755
    • HIV-1 protease flaps spontaneously close to the correct structure in simulations following manual placement of an inhibitor into the open state. V Hornak, A Okur, RC Rizzo, C Simmerling, J Am Chem Soc 2006 128 2812 2813 10.1021/ja058211x 16506755
    • (2006) J Am Chem Soc , vol.128 , pp. 2812-2813
    • Hornak, V.1    Okur, A.2    Rizzo, R.C.3    Simmerling, C.4
  • 44
    • 33744730369 scopus 로고    scopus 로고
    • Closing of the flaps of HIV-1 protease induced by substrate binding: A model of a flap closing mechanism in retroviral aspartic proteases
    • DOI 10.1021/bi060188k
    • Closing of the flaps of HIV-1 protease induced by substrate binding: A model of flap closing mechanism in retroviral aspartic proteases. G Toth, A Borics, Biochemistry 2006 45 6606 6614 10.1021/bi060188k 16716071 (Pubitemid 43825361)
    • (2006) Biochemistry , vol.45 , Issue.21 , pp. 6606-6614
    • Toth, G.1    Borics, A.2
  • 45
    • 67249128279 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics of ligands binding into protein: The case of HIV-1 protease inhibitors
    • 10.1063/1.3148022 19508101
    • Coarse-grained molecular dynamics of ligands binding into protein: the case of HIV-1 protease inhibitors. D Li, MS Liu, B Ji, K Hwang, J Chem Phys 2009 130 215102 10.1063/1.3148022 19508101
    • (2009) J Chem Phys , vol.130 , pp. 215102
    • Li, D.1    Liu, M.S.2    Ji, B.3    Hwang, K.4
  • 46
    • 24344438610 scopus 로고    scopus 로고
    • A coarse grained model for the dynamics of flap opening in HIV-1 protease
    • DOI 10.1016/j.cplett.2005.07.075, PII S0009261405010663
    • A coarse grained model for the dynamics of flap opening in HIV-1 protease. V Tozzini, JA McCammon, Chem Phys Lett 2005 413 123 128 10.1016/j.cplett.2005.07.075 (Pubitemid 41252378)
    • (2005) Chemical Physics Letters , vol.413 , Issue.1-3 , pp. 123-128
    • Tozzini, V.1    McCammon, J.A.2
  • 47
    • 33847116895 scopus 로고    scopus 로고
    • Flap opening dynamics in HIV-1 protease explored with a coarse-grained model
    • 10.1016/j.jsb.2006.08.005 17029846
    • Flap opening dynamics in HIV-1 protease explored with a coarse-grained model. V Tozzini, J Trylska, C Chang, JA McCammon, J Struct Biol 2007 157 606 615 10.1016/j.jsb.2006.08.005 17029846
    • (2007) J Struct Biol , vol.157 , pp. 606-615
    • Tozzini, V.1    Trylska, J.2    Chang, C.3    McCammon, J.A.4
  • 48
    • 59349083629 scopus 로고    scopus 로고
    • Residue energy and mobility in sequence to global structure and dynamics of a HIV-1 protease (1DIFA) by a coarse-grained Monte Carlo simulation
    • 10.1063/1.3050106 19191412
    • Residue energy and mobility in sequence to global structure and dynamics of a HIV-1 protease (1DIFA) by a coarse-grained Monte Carlo simulation. RB Pandey, BL Farmer, J Chem Phys 2009 130 044906 10.1063/1.3050106 19191412
    • (2009) J Chem Phys , vol.130 , pp. 044906
    • Pandey, R.B.1    Farmer, B.L.2
  • 49
    • 2442543557 scopus 로고    scopus 로고
    • Accurate and Efficient Description of Protein Vibrational Dynamics: Comparing Molecular Dynamics and Gaussian Models
    • DOI 10.1002/prot.20049
    • Accurate and efficient description of protein vibrational dynamics: comparing molecular dynamics and Gaussian models. C Micheletti, P Carloni, A Maritan, Proteins 2004 55 635 645 10.1002/prot.20049 15103627 (Pubitemid 38620088)
    • (2004) Proteins: Structure, Function and Genetics , vol.55 , Issue.3 , pp. 635-645
    • Micheletti, C.1    Carloni, P.2    Maritan, A.3
  • 50
    • 0037963159 scopus 로고    scopus 로고
    • Cooperative fluctuations of unliganded and substrate-bound HIV-1 protease: A structure-based analysis on a variety of conformations from crystallography and molecular dynamics simulations
    • DOI 10.1002/prot.10350
    • Cooperative fluctuations of unliganded and substrate-bound HIV-1 protease: A structure-based analysis on a variety of conformations from crystallography and molecular dynamics simulations. N Kurt, WR Scott, CA Schiffer, T Haliloglu, Proteins 2003 51 409 422 10.1002/prot.10350 12696052 (Pubitemid 36528826)
    • (2003) Proteins: Structure, Function and Genetics , vol.51 , Issue.3 , pp. 409-422
    • Kurt, N.1    Scott, W.R.P.2    Schiffer, C.A.3    Haliloglu, T.4
  • 51
    • 0036786493 scopus 로고    scopus 로고
    • Drug resistance in HIV-1 protease: Flexibility assisted mechanism of compensatory mutations
    • 12237461
    • Drug resistance in HIV-1 protease: Flexibility assisted mechanism of compensatory mutations. S Piana, P Carloni, U Rothlisberger, Protein Sci 2002 11 2393 2402 12237461
    • (2002) Protein Sci , vol.11 , pp. 2393-2402
    • Piana, S.1    Carloni, P.2    Rothlisberger, U.3
  • 52
    • 1842454635 scopus 로고    scopus 로고
    • HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: Possible contributions to drug resistance and a potential new target site for drugs
    • DOI 10.1110/ps.03468904
    • HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs. AL Perryman, JH Lin, JA McCammon, Protein Sci 2004 13 1108 1123 10.1110/ps.03468904 15044738 (Pubitemid 38429231)
    • (2004) Protein Science , vol.13 , Issue.4 , pp. 1108-1123
    • Perryman, A.L.1    Lin, J.-H.2    McCammon, J.A.3
  • 53
    • 43349093759 scopus 로고    scopus 로고
    • Analysis of correlated mutations in HIV-1 protease using spectral clustering
    • DOI 10.1093/bioinformatics/btn110
    • Analysis of correlated mutations in hiv-1 protease using spectral clustering. Y Liu, E Eyal, I Bahar, Bioinformatics 2008 24 1243 1250 10.1093/bioinformatics/btn110 18375964 (Pubitemid 351659620)
    • (2008) Bioinformatics , vol.24 , Issue.10 , pp. 1243-1250
    • Liu, Y.1    Eyal, E.2    Bahar, I.3
  • 55
    • 34548736034 scopus 로고    scopus 로고
    • Dynamics of firefly luciferase inhibition by general anesthetics: Gaussian and anisotropic network analyses
    • DOI 10.1529/biophysj.106.102780
    • Dynamics of firefly luciferase inhibition by general anesthetics: Gaussian and anisotropic network analyses. A Szarecka, Y Xu, P Tang, Biophys J 2007 93 1895 1905 10.1529/biophysj.106.102780 17513367 (Pubitemid 47437574)
    • (2007) Biophysical Journal , vol.93 , Issue.6 , pp. 1895-1905
    • Szarecka, A.1    Xu, Y.2    Tang, P.3
  • 56
    • 0036298514 scopus 로고    scopus 로고
    • Relation between sequence and structure of HIV-1 protease inhibitor complexes: A model system for the analysis of protein Flexibility
    • DOI 10.1006/jmbi.2001.5173
    • Relation between sequence and structure of HIV-1 protease inhibitor complexes: a model system for the analysis of protein flexibility. V Zoete, O Michielin, M Karplus, J Mol Biol 2002 315 21 52 10.1006/jmbi.2001.5173 11771964 (Pubitemid 34722109)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.1 , pp. 21-52
    • Zoete, V.1    Michielin, O.2    Karplus, M.3
  • 58
    • 77952387383 scopus 로고    scopus 로고
    • Computational study of the resistance shown by the subtype B/HIV-1 protease to currently known inhibitors
    • 10.1021/bi100569u 20415450
    • Computational study of the resistance shown by the subtype B/HIV-1 protease to currently known inhibitors. A Genoni, G Morra, KM Merz Jr, G Colombo, Biochemistry 2010 49 4283 4295 10.1021/bi100569u 20415450
    • (2010) Biochemistry , vol.49 , pp. 4283-4295
    • Genoni, A.1    Morra, G.2    Merz Jr., K.M.3    Colombo, G.4
  • 60
    • 25844440811 scopus 로고    scopus 로고
    • Elastic network models for understanding biomolecular machinery: From enzymes to supramolecular assemblies
    • DOI 10.1088/1478-3975/2/4/S12, PII S1478397505050612
    • Elastic network models for understanding biomolecular machinery: from enzymes to supramolecular assemblies. C Chennubhotla, AJ Rader, LW Yang, I Bahar, Phys Biol 2005 2 173 S180 10.1088/1478-3975/2/4/S12 16280623 (Pubitemid 41609444)
    • (2005) Physical Biology , vol.2 , Issue.4
    • Chennubhotla, C.1    Rader, A.J.2    Yang, L.-W.3    Bahar, I.4
  • 61
    • 0035132230 scopus 로고    scopus 로고
    • Anisotropy of fluctuation dynamics of proteins with an elastic network model
    • 10.1016/S0006-3495(01)76033-X 11159421
    • Anisotropy of fluctuation dynamics of proteins with an elastic network model. AR Atilgan, SR Durrel, RL Jernigan, MC Demirel, O Keskin, I Bahar, Biophys J 2001 80 505 515 10.1016/S0006-3495(01)76033-X 11159421
    • (2001) Biophys J , vol.80 , pp. 505-515
    • Atilgan, A.R.1    Durrel, S.R.2    Jernigan, R.L.3    Demirel, M.C.4    Keskin, O.5    Bahar, I.6
  • 62
    • 0036529479 scopus 로고    scopus 로고
    • An efficient algorithm for large-scale detection of protein families
    • An efficient algorithm for large-scale detection of protein families. AJ Enright, S Van Dongen, CA Ouzounis, Nucleic Acids Res 2002 30 1575 1584 10.1093/nar/30.7.1575 11917018 (Pubitemid 34679732)
    • (2002) Nucleic Acids Research , vol.30 , Issue.7 , pp. 1575-1584
    • Enright, A.J.1    Van Dongen, S.2    Ouzounis, C.A.3
  • 63
    • 65849100458 scopus 로고    scopus 로고
    • Markov clustering versus affinity propagation for the partitioning of protein interaction graphs
    • 10.1186/1471-2105-10-99 19331680
    • Markov clustering versus affinity propagation for the partitioning of protein interaction graphs. J Vlasblom, SJ Wodak, BMC Bioinformatics 2009 10 99 10.1186/1471-2105-10-99 19331680
    • (2009) BMC Bioinformatics , vol.10 , pp. 99
    • Vlasblom, J.1    Wodak, S.J.2
  • 64
    • 33751255087 scopus 로고    scopus 로고
    • Evaluation of clustering algorithms for protein-protein interaction networks
    • DOI 10.1186/1471-2105-7-488
    • Evaluation of clustering algorithms for protein-protein interaction networks. S Brohee, J van Helden, BMC Bioinformatics 2006 7 488 10.1186/1471-2105-7-488 17087821 (Pubitemid 44782347)
    • (2006) BMC Bioinformatics , vol.7 , pp. 488
    • Brohee, S.1    Van Helden, J.2


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