메뉴 건너뛰기




Volumn 17, Issue 10, 2011, Pages 2693-2705

A comparative study of HIV-1 and HTLV-I protease structure and dynamics reveals a conserved residue interaction network

Author keywords

HIV; HTLV; Molecular dynamics simulation; Protein structure; Protein ligand interactions

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; MOLECULAR SCAFFOLD;

EID: 80255138809     PISSN: 16102940     EISSN: 09485023     Source Type: Journal    
DOI: 10.1007/s00894-011-0971-1     Document Type: Article
Times cited : (8)

References (63)
  • 1
    • 0019254359 scopus 로고
    • Detection and isolation of type C retrovirus particles from fresh and cultured lymphocytes of a patient with cutaneous T-cell lymphoma
    • DOI 10.1073/pnas.77.12.7415
    • BJ Poiesz FW Ruscetti AF Gazdar PA Bunn JD Minna RC Gallo 1980 Detection and isolation of type C retrovirus particles from fresh and cultured lymphocytes of a patient with cutaneous T-cell lymphoma Proc Natl Acad Sci USA 77 7415 7419 10.1073/pnas.77.12.7415 1:CAS:528:DyaL3MXhtlOnt74%3D (Pubitemid 11131140)
    • (1980) Proceedings of the National Academy of Sciences of the United States of America , vol.77 , Issue.12 , pp. 7415-7419
    • Poiesz, B.J.1    Ruscetti, F.W.2    Gazdar, A.F.3
  • 2
    • 0021418424 scopus 로고
    • Monoclonal integration of human T-cell leukemia provirus in all primary tumors of adult T-cell leukemia suggests causative role of human T-cell leukemia virus in the disease
    • 10.1073/pnas.81.8.2534 1:STN:280:DyaL2c7psVSntg%3D%3D
    • M Yoshida M Seiki K Yamaguchi K Takatsuki 1984 Monoclonal integration of human T-cell leukemia provirus in all primary tumors of adult T-cell leukemia suggests causative role of human T-cell leukemia virus in the disease Proc Natl Acad Sci USA 81 2534 2537 10.1073/pnas.81.8.2534 1:STN:280:DyaL2c7psVSntg%3D%3D
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 2534-2537
    • Yoshida, M.1    Seiki, M.2    Yamaguchi, K.3    Takatsuki, K.4
  • 3
    • 0021995980 scopus 로고
    • Antibodies to human T-lymphotropic virus type-I in patients with tropical spastic paraparesis
    • A Gessain F Barin JC Vernant O Gout L Maurs A Calender G de The 1985 Antibodies to human T-lymphotropic virus type-I in patients with tropical spastic paraparesis Lancet 2 8452 407 410 10.1016/S0140-6736(85)92734-5 1:STN:280:DyaL2M3psVyitA%3D%3D (Pubitemid 15231248)
    • (1985) Lancet , vol.2 , Issue.8452 , pp. 407-410
    • Gessain, A.1    Barin, F.2    Vernant, J.C.3
  • 4
    • 0025251824 scopus 로고
    • Infective dermatitis of Jamaican children: A marker for HTLV-I infection
    • 10.1016/0140-6736(90)92896-P 1:STN:280:DyaK3M%2FktFCitA%3D%3D
    • L LaGrenade B Hanchard V Fletcher B Cranston W Blattner 1990 Infective dermatitis of Jamaican children: a marker for HTLV-I infection Lancet 336 8727 1345 1347 10.1016/0140-6736(90)92896-P 1:STN:280:DyaK3M%2FktFCitA%3D%3D
    • (1990) Lancet , vol.336 , Issue.8727 , pp. 1345-1347
    • Lagrenade, L.1    Hanchard, B.2    Fletcher, V.3    Cranston, B.4    Blattner, W.5
  • 6
    • 0024376581 scopus 로고
    • HTLV-1 and polymyositis in Jamaica
    • 10.1016/S0140-6736(89)91793-5 1:STN:280:DyaK3c%2Fkt1yksw%3D%3D
    • OS Morgan P Rodgers-Johnson C Mora G Char 1989 HTLV-1 and polymyositis in Jamaica Lancet 2 8673 1184 1187 10.1016/S0140-6736(89)91793-5 1:STN:280:DyaK3c%2Fkt1yksw%3D%3D
    • (1989) Lancet , vol.2 , Issue.8673 , pp. 1184-1187
    • Morgan, O.S.1    Rodgers-Johnson, P.2    Mora, C.3    Char, G.4
  • 7
    • 0024583643 scopus 로고
    • Chronic inflammatory arthropathy associated with HTLV-I
    • 10.1016/S0140-6736(89)90038-X 1:STN:280:DyaL1M7kt1ygsQ%3D%3D
    • K Nishioka I Maruyama K Sato I Kitajima Y Nakajima M Osame 1989 Chronic inflammatory arthropathy associated with HTLV-I Lancet 1 8635 441 441 10.1016/S0140-6736(89)90038-X 1:STN:280:DyaL1M7kt1ygsQ%3D%3D
    • (1989) Lancet , vol.1 , Issue.8635 , pp. 441-441
    • Nishioka, K.1    Maruyama, I.2    Sato, K.3    Kitajima, I.4    Nakajima, Y.5    Osame, M.6
  • 8
    • 0027156506 scopus 로고
    • An HTLV-I vaccine: Why, how, for whom?
    • 10.1089/aid.1993.9.381
    • G de The R Bomford 1993 An HTLV-I vaccine: why, how, for whom? AIDS Res Hum Retroviruses 9 381 386 10.1089/aid.1993.9.381
    • (1993) AIDS Res Hum Retroviruses , vol.9 , pp. 381-386
    • De The, G.1    Bomford, R.2
  • 9
    • 0029846448 scopus 로고    scopus 로고
    • Virological aspects of tropical spastic paraparesis/HTLV-I associated myelopathy and HTLV-I infection
    • A Gessain 1996 Virological aspects of tropical spastic paraparesis/HTLV-I associated myelopathy and HTLV-I infection J Neurovirol 2 299 306 10.3109/13550289609146894 1:STN:280:DyaK2s%2FmvFSiug%3D%3D (Pubitemid 26372455)
    • (1996) Journal of NeuroVirology , vol.2 , Issue.5 , pp. 299-306
    • Gessain, A.1
  • 10
    • 0031742857 scopus 로고    scopus 로고
    • Human T-cell lymphotropic virus type 1 tax among American blood donors
    • D Zucker-Franklin BA Pancake 1998 Human T-cell lymphotropic virus type 1 tax among American blood donors Clin Diagn Lab Immunol 5 831 835 1:STN:280:DyaK1M%2FhvFOruw%3D%3D (Pubitemid 28519261)
    • (1998) Clinical and Diagnostic Laboratory Immunology , vol.5 , Issue.6 , pp. 831-835
    • Zucker-Franklin, D.1    Pancake, B.A.2
  • 12
    • 0021261510 scopus 로고
    • Frequent detection and isolation of cytopathic retroviruses (HTLV-III) from patients with AIDS and at risk for AIDS
    • RC Gallo SZ Salahuddin M Popovic GM Shearer M Kaplan BF Haynes TJ Palker R Redfield J Oleske S Bea 1984 Frequent detection and isolation of cytopathic retroviruses (HTLV-III) from patients with AIDS and at risk for AIDS Science 224 500 503 10.1126/science.6200936 1:STN:280:DyaL2c7nt1aisA%3D%3D (Pubitemid 14134741)
    • (1984) Science , vol.224 , Issue.4648 , pp. 500-503
    • Gallo, R.C.1    Salahuddin, S.Z.2    Popovic, M.3
  • 14
    • 39149111265 scopus 로고    scopus 로고
    • Treatment of adult T-cell leukemia/lymphoma: Past, present, and future
    • DOI 10.1111/j.1600-0609.2007.01016.x
    • K Ishitsuka K Tamura 2008 Treatment of adult T-cell leukemia/lymphoma: past, present, and future Eur J Haematol 80 185 196 10.1111/j.1600-0609.2007. 01016.x 1:CAS:528:DC%2BD1cXktVKisr8%3D (Pubitemid 351253463)
    • (2008) European Journal of Haematology , vol.80 , Issue.3 , pp. 185-196
    • Ishitsuka, K.1    Tamura, K.2
  • 15
    • 0033525874 scopus 로고    scopus 로고
    • Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase
    • DOI 10.1074/jbc.274.10.6660
    • JM Louis S Oroszlan J Tozser 1999 Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase J Biol Chem 274 6660 6666 10.1074/jbc.274.10.6660 1:CAS:528:DyaK1MXhs1Cgs74%3D (Pubitemid 29111086)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.10 , pp. 6660-6666
    • Louis, J.M.1    Oroszlan, S.2    Tozser, J.3
  • 19
    • 25844449712 scopus 로고    scopus 로고
    • Molecular dynamics simulations of HIV-1 protease suggest different mechanisms contributing to drug resistance
    • Wartha F, Horn AHC, Meiselbach H, Sticht H (2005) Molecular dynamics simulations of HIV-1 protease suggest different mechanisms contributing to drug resistance. J Chem Theory Comput 1:315-324
    • (2005) J Chem Theory Comput , vol.1 , pp. 315-324
    • Wartha, F.1    Ahc, H.2    Meiselbach, H.3    Sticht, H.4
  • 20
    • 77958053240 scopus 로고    scopus 로고
    • Effects of the V82A and I54V mutations on the dynamics and ligand binding properties of HIV-1 protease
    • 10.1007/s00894-010-0677-9 1:CAS:528:DC%2BC3cXht1Kjt7rO
    • P Dirauf H Meiselbach H Sticht 2010 Effects of the V82A and I54V mutations on the dynamics and ligand binding properties of HIV-1 protease J Mol Model 16 1577 1583 10.1007/s00894-010-0677-9 1:CAS:528:DC%2BC3cXht1Kjt7rO
    • (2010) J Mol Model , vol.16 , pp. 1577-1583
    • Dirauf, P.1    Meiselbach, H.2    Sticht, H.3
  • 21
    • 33846690468 scopus 로고    scopus 로고
    • Insights into amprenavir resistance in E35D HIV-1 protease mutation from molecular dynamics and binding free-energy calculations
    • DOI 10.1007/s00894-006-0121-3, Special Issue
    • H Meiselbach AH Horn T Harrer H Sticht 2007 Insights into amprenavir resistance in E35D HIV-1 protease mutation from molecular dynamics and binding free-energy calculations J Mol Model 13 297 304 10.1007/s00894-006-0121-3 1:CAS:528:DC%2BD2sXisFantLw%3D (Pubitemid 46189159)
    • (2007) Journal of Molecular Modeling , vol.13 , Issue.2 , pp. 297-304
    • Meiselbach, H.1    Horn, A.H.C.2    Harrer, T.3    Sticht, H.4
  • 23
    • 0029859529 scopus 로고    scopus 로고
    • Ionization states of the catalytic residues in HIV-1 protease
    • DOI 10.1038/nsb1196-946
    • R Smith IM Brereton RY Chai SB Kent 1996 Ionization states of the catalytic residues in HIV-1 protease Nat Struct Biol 3 946 950 10.1038/nsb1196-946 1:CAS:528:DC%2BD38Xms1Clsbk%3D (Pubitemid 26398328)
    • (1996) Nature Structural Biology , vol.3 , Issue.11 , pp. 946-950
    • Smith, R.1    Brereton, I.M.2    Chai, R.Y.3    Kent, S.B.H.4
  • 26
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman DA, Case DA, Caldwell JW, Ross WS, Cheatham TE 3rd, DeBolt S, Ferguson D, Seibel G, Kollman P (1995) AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comp Phys Commun 91:1-41
    • (1995) Comp Phys Commun , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham Iii, T.E.5    Debolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 27
    • 0032922174 scopus 로고    scopus 로고
    • A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat
    • TE Cheatham 3rd P Cieplak PA Kollman 1999 A modified version of the Cornell, et al.. force field with improved sugar pucker phases and helical repeat J Biomol Struct Dyn 16 845 862 1:CAS:528:DyaK1MXitF2jsb8%3D (Pubitemid 29157655)
    • (1999) Journal of Biomolecular Structure and Dynamics , vol.16 , Issue.4 , pp. 845-862
    • Cheatham III, T.E.1    Cieplak, P.2    Kollman, P.A.3
  • 29
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • 10.1063/1.445869 1:CAS:528:DyaL3sXksF2htL4%3D
    • WL Jorgensen J Chandrasekhar JD Madura RW Impey ML Klein 1983 Comparison of simple potential functions for simulating liquid water J Chem Phys 79 926 935 10.1063/1.445869 1:CAS:528:DyaL3sXksF2htL4%3D
    • (1983) J Chem Phys , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3    Impey, R.W.4    Klein, M.L.5
  • 30
    • 2942532422 scopus 로고    scopus 로고
    • Development and testing of a general amber force field
    • 10.1002/jcc.20035 1:CAS:528:DC%2BD2cXksFakurc%3D
    • J Wang RM Wolf JW Caldwell PA Kollman DA Case 2004 Development and testing of a general amber force field J Comput Chem 25 1157 1174 10.1002/jcc.20035 1:CAS:528:DC%2BD2cXksFakurc%3D
    • (2004) J Comput Chem , vol.25 , pp. 1157-1174
    • Wang, J.1    Wolf, R.M.2    Caldwell, J.W.3    Kollman, P.A.4    Case, D.A.5
  • 31
    • 33846823909 scopus 로고
    • Particle mesh Ewald. An N.log(N) method for Ewald sums in large systems
    • 10.1063/1.464397 1:CAS:528:DyaK3sXks1Ohsr0%3D
    • TA Darden DM York LG Pedersen 1993 Particle mesh Ewald. An N.log(N) method for Ewald sums in large systems J Chem Phys 98 10089 10092 10.1063/1.464397 1:CAS:528:DyaK3sXks1Ohsr0%3D
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.A.1    York, D.M.2    Pedersen, L.G.3
  • 32
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • 10.1016/0021-9991(77)90098-5 1:CAS:528:DyaE2sXktVGhsL4%3D
    • JP Ryckaert G Ciccotti HJC Berendsen 1977 Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J Comput Phys 23 327 341 10.1016/0021-9991(77)90098-5 1:CAS:528:DyaE2sXktVGhsL4%3D
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 33
    • 80255123252 scopus 로고    scopus 로고
    • Tripos (1991-2008) Sybyl 7.3. Tripos, St. Louis
    • Tripos (1991-2008) Sybyl 7.3. Tripos, St. Louis
  • 34
    • 33846654886 scopus 로고    scopus 로고
    • Accelrys Accelrys, San Diego
    • Accelrys (2005) DS ViewerPro Suite 6.0. Accelrys, San Diego
    • (2005) DS ViewerPro Suite 6.0
  • 35
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8:127-134
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 36
    • 0029143262 scopus 로고
    • Analysis of cross reactivity of retrovirus proteases using a vaccinia virus-T7 RNA polymerase-based expression system
    • 10.1099/0022-1317-76-9-2169
    • BG Luukkonen W Tan EM Fenyo S Schwartz 1995 Analysis of cross reactivity of retrovirus proteases using a vaccinia virus-T7 RNA polymerase-based expression system J Gen Virol 76 2169 2180 10.1099/0022-1317-76-9-2169
    • (1995) J Gen Virol , vol.76 , pp. 2169-2180
    • Luukkonen, B.G.1    Tan, W.2    Fenyo, E.M.3    Schwartz, S.4
  • 37
    • 2442712423 scopus 로고    scopus 로고
    • Development of a microtiter plate fluorescent assay for inhibition studies on the HTLV-1 and HIV-1 proteinases
    • DOI 10.1016/j.jviromet.2004.03.001, PII S0166093404000680
    • P Bagossi J Kadas G Miklossy P Boross IT Weber J Tozser 2004 Development of a microtiter plate fluorescent assay for inhibition studies on the HTLV-1 and HIV-1 proteinases J Virol Methods 119 87 93 10.1016/j.jviromet.2004.03.001 1:CAS:528:DC%2BD2cXkt1Smurg%3D (Pubitemid 38670399)
    • (2004) Journal of Virological Methods , vol.119 , Issue.2 , pp. 87-93
    • Bagossi, P.1    Kadas, J.2    Miklossy, G.3    Boross, P.4    Weber, I.T.5    Tozser, J.6
  • 38
    • 3042648441 scopus 로고    scopus 로고
    • Narrow substrate specificity and sensitivity toward ligand-binding site mutations of human T-cell leukemia virus type 1 protease
    • DOI 10.1074/jbc.M401868200
    • Kadas J, Weber IT, Bagossi P, Miklossy G, Boross P, Oroszlan S, Tozser J (2004) Narrow substrate specificity and sensitivity toward ligand-binding site mutations of human T-cell leukemia virus type 1 protease. J Biol Chem 279:27148-27157 (Pubitemid 38812551)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27148-27157
    • Kadas, J.1    Weber, I.T.2    Bagossi, P.3    Miklossy, G.4    Boross, P.5    Oroszlan, S.6    Tozser, J.7
  • 39
    • 0033780526 scopus 로고    scopus 로고
    • Comparison of the substrate specificity of the human T-cell leukemia virus and human immunodeficiency virus proteinases
    • 10.1046/j.1432-1327.2000.01714.x 1:CAS:528:DC%2BD3cXnsVygtro%3D
    • J Tozser G Zahuczky P Bagossi JM Louis TD Copeland S Oroszlan RW Harrison IT Weber 2000 Comparison of the substrate specificity of the human T-cell leukemia virus and human immunodeficiency virus proteinases Eur J Biochem 267 6287 6295 10.1046/j.1432-1327.2000.01714.x 1:CAS:528:DC%2BD3cXnsVygtro%3D
    • (2000) Eur J Biochem , vol.267 , pp. 6287-6295
    • Tozser, J.1    Zahuczky, G.2    Bagossi, P.3    Louis, J.M.4    Copeland, T.D.5    Oroszlan, S.6    Harrison, R.W.7    Weber, I.T.8
  • 40
    • 0025924419 scopus 로고
    • Studies on the role of the S4 substrate binding site of HIV proteinases
    • 10.1016/0014-5793(91)80186-7 1:CAS:528:DyaK3MXkt1Gjsrs%3D
    • J Tozser A Gustchina IT Weber I Blaha EM Wondrak S Oroszlan 1991 Studies on the role of the S4 substrate binding site of HIV proteinases FEBS Lett 279 356 360 10.1016/0014-5793(91)80186-7 1:CAS:528:DyaK3MXkt1Gjsrs%3D
    • (1991) FEBS Lett , vol.279 , pp. 356-360
    • Tozser, J.1    Gustchina, A.2    Weber, I.T.3    Blaha, I.4    Wondrak, E.M.5    Oroszlan, S.6
  • 41
    • 0025122828 scopus 로고
    • Comparison of inhibitor binding in HIV-1 protease and in non-viral aspartic proteases: The role of the flap
    • DOI 10.1016/0014-5793(90)81171-J
    • A Gustchina IT Weber 1990 Comparison of inhibitor binding in HIV-1 protease and in non-viral aspartic proteases: the role of the flap FEBS Lett 269 269 272 10.1016/0014-5793(90)81171-J 1:CAS:528:DyaK3cXlvVOjurw%3D (Pubitemid 20245369)
    • (1990) FEBS Letters , vol.269 , Issue.1 , pp. 269-272
    • Gustchina, A.1    Weber, I.T.2
  • 42
    • 0026702928 scopus 로고
    • Two-step binding mechanism for HIV protease inhibitors
    • 10.1021/bi00149a020 1:CAS:528:DyaK38XltVeltro%3D
    • ES Furfine E D'Souza KJ Ingold JJ Leban T Spector DJ Porter 1992 Two-step binding mechanism for HIV protease inhibitors Biochemistry 31 7886 7891 10.1021/bi00149a020 1:CAS:528:DyaK38XltVeltro%3D
    • (1992) Biochemistry , vol.31 , pp. 7886-7891
    • Furfine, E.S.1    D'Souza, E.2    Ingold, K.J.3    Leban, J.J.4    Spector, T.5    Porter, D.J.6
  • 43
    • 0027309442 scopus 로고
    • Inhibitor binding to the Phe53Trp mutant of HIV-1 protease promotes conformational changes detectable by spectrofluorometry
    • EJ Rodriguez C Debouck IC Deckman H Abu-Soud FM Raushel TD Meek 1993 Inhibitor binding to the Phe53Trp mutant of HIV-1 protease promotes conformational changes detectable by spectrofluorometry Biochemistry 32 3557 3563 10.1021/bi00065a006 1:CAS:528:DyaK3sXisFSmt7o%3D (Pubitemid 23126929)
    • (1993) Biochemistry , vol.32 , Issue.14 , pp. 3557-3563
    • Rodriguez, E.J.1    Debouck, C.2    Deckman, I.C.3    Abu-Soud, H.4    Raushel, F.M.5    Meek, T.D.6
  • 45
    • 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
    • AL Perryman JH Lin JA McCammon 2004 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 Protein Sci 13 1108 1123 10.1110/ps.03468904 1:CAS:528:DC%2BD2cXivFaktbY%3D (Pubitemid 38429231)
    • (2004) Protein Science , vol.13 , Issue.4 , pp. 1108-1123
    • Perryman, A.L.1    Lin, J.-H.2    McCammon, J.A.3
  • 46
    • 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
    • G Toth A Borics 2006 Closing of the flaps of HIV-1 protease induced by substrate binding: a model of a flap closing mechanism in retroviral aspartic proteases Biochemistry 45 6606 6614 10.1021/bi060188k 1:CAS:528: DC%2BD28XktVSmu7k%3D (Pubitemid 43825361)
    • (2006) Biochemistry , vol.45 , Issue.21 , pp. 6606-6614
    • Toth, G.1    Borics, A.2
  • 47
    • 0026344399 scopus 로고
    • The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU
    • 10.1016/0300-9084(91)90169-2 1:CAS:528:DyaK38Xht1eqs7s%3D
    • S Spinelli QZ Liu PM Alzari PH Hirel RJ Poljak 1991 The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU Biochimie 73 1391 1396 10.1016/0300-9084(91)90169-2 1:CAS:528:DyaK38Xht1eqs7s%3D
    • (1991) Biochimie , vol.73 , pp. 1391-1396
    • Spinelli, S.1    Liu, Q.Z.2    Alzari, P.M.3    Hirel, P.H.4    Poljak, R.J.5
  • 48
    • 0036147844 scopus 로고    scopus 로고
    • Rapid structural fluctuations of the free HIV protease flaps in solution: Relationship to crystal structures and comparison with predictions of dynamics calculations
    • DOI 10.1110/ps.33202
    • DI Freedberg R Ishima J Jacob YX Wang I Kustanovich JM Louis DA Torchia 2002 Rapid structural fluctuations of the free HIV protease flaps in solution: relationship to crystal structures and comparison with predictions of dynamics calculations Protein Sci 11 221 232 10.1110/ps.33202 1:CAS:528: DC%2BD38XosFylsw%3D%3D (Pubitemid 34075785)
    • (2002) Protein Science , vol.11 , Issue.2 , pp. 221-232
    • Freedberg, D.I.1    Ishima, R.2    Jacob, J.3    Wang, Y.-X.4    Kustanovich, I.5    Louis, J.M.6    Torchia, D.A.7
  • 49
    • 0033200247 scopus 로고    scopus 로고
    • Flap opening and dimer-interface flexibility in the free and inhibitor- bound HIV protease, and their implications for function
    • DOI 10.1016/S0969-2126(99)80172-5
    • R Ishima DI Freedberg YX Wang JM Louis DA Torchia 1999 Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function Structure 7 1047 1055 10.1016/S0969-2126(99) 80172-5 1:CAS:528:DyaK1MXmtlartL8%3D (Pubitemid 29436502)
    • (1999) Structure , vol.7 , Issue.9 , pp. 1047-1055
    • Ishima, R.1    Freedberg, D.I.2    Wang, Y.-X.3    Louis, J.M.4    Torchia, D.A.5
  • 50
    • 62849123601 scopus 로고    scopus 로고
    • Drug pressure selected mutations in HIV-1 protease alter flap conformations
    • 10.1021/ja807531v 1:CAS:528:DC%2BD1cXhsFantbrE
    • L Galiano F Ding AM Veloro ME Blackburn C Simmerling GE Fanucci 2009 Drug pressure selected mutations in HIV-1 protease alter flap conformations J Am Chem Soc 131 430 431 10.1021/ja807531v 1:CAS:528:DC%2BD1cXhsFantbrE
    • (2009) J Am Chem Soc , vol.131 , pp. 430-431
    • Galiano, L.1    Ding, F.2    Veloro, A.M.3    Blackburn, M.E.4    Simmerling, C.5    Fanucci, G.E.6
  • 52
    • 70350052784 scopus 로고    scopus 로고
    • Subtype polymorphisms among HIV-1 protease variants confer altered flap conformations and flexibility
    • 10.1021/ja907088a 1:CAS:528:DC%2BD1MXhtF2lurrP
    • JL Kear ME Blackburn AM Veloro BM Dunn GE Fanucci 2009 Subtype polymorphisms among HIV-1 protease variants confer altered flap conformations and flexibility J Am Chem Soc 131 14650 14651 10.1021/ja907088a 1:CAS:528:DC%2BD1MXhtF2lurrP
    • (2009) J Am Chem Soc , vol.131 , pp. 14650-14651
    • Kear, J.L.1    Blackburn, M.E.2    Veloro, A.M.3    Dunn, B.M.4    Fanucci, G.E.5
  • 53
    • 35448970266 scopus 로고    scopus 로고
    • A molecular dynamics study comparing a wild-type with a multiple drug resistant HIV protease: Differences in flap and aspartate 25 cavity dimensions
    • DOI 10.1002/prot.21535
    • SA Seibold RI Cukier 2007 A molecular dynamics study comparing a wild-type with a multiple drug resistant HIV protease: differences in flap and aspartate 25 cavity dimensions Proteins 69 551 565 10.1002/prot.21535 1:CAS:528:DC%2BD2sXht1aju7%2FK (Pubitemid 47623871)
    • (2007) Proteins: Structure, Function and Genetics , vol.69 , Issue.3 , pp. 551-565
    • Seibold, S.A.1    Cukier, R.I.2
  • 54
    • 84857801177 scopus 로고    scopus 로고
    • HIVDB Team (1998-2008) Stanford HIV Database
    • HIVDB Team (1998-2008) Stanford HIV Database. http://hivdb.stanford.edu/
  • 56
    • 68149173312 scopus 로고    scopus 로고
    • Molecular dynamics and free energy studies on the wild-type and mutated HIV-1 protease complexed with four approved drugs: Mechanism of binding and drug resistance
    • 10.1021/ci900012k 1:CAS:528:DC%2BD1MXnsVeit7g%3D
    • S Alcaro A Artese F Ceccherini-Silberstein F Ortuso CF Perno T Sing V Svicher 2009 Molecular dynamics and free energy studies on the wild-type and mutated HIV-1 protease complexed with four approved drugs: mechanism of binding and drug resistance J Chem Inf Model 49 1751 1761 10.1021/ci900012k 1:CAS:528:DC%2BD1MXnsVeit7g%3D
    • (2009) J Chem Inf Model , vol.49 , pp. 1751-1761
    • Alcaro, S.1    Artese, A.2    Ceccherini-Silberstein, F.3    Ortuso, F.4    Perno, C.F.5    Sing, T.6    Svicher, V.7
  • 59
    • 0033001019 scopus 로고    scopus 로고
    • Molecular mechanics analysis of drug-resistant mutants of HIV protease
    • IT Weber RW Harrison 1999 Molecular mechanics analysis of drug-resistant mutants of HIV protease Protein Eng 12 469 474 10.1093/protein/12.6.469 1:CAS:528:DyaK1MXkslGhsb0%3D (Pubitemid 29322444)
    • (1999) Protein Engineering , vol.12 , Issue.6 , pp. 469-474
    • Weber, I.T.1    Harrison, R.W.2
  • 60
    • 35748950982 scopus 로고    scopus 로고
    • Molecular Analysis of the HIV-1 Resistance Development: Enzymatic Activities, Crystal Structures, and Thermodynamics of Nelfinavir-resistant HIV Protease Mutants
    • DOI 10.1016/j.jmb.2007.09.083, PII S0022283607012958
    • M Kozisek J Bray P Rezacova K Saskova J Brynda J Pokorna F Mammano L Rulisek J Konvalinka 2007 Molecular analysis of the HIV-1 resistance development: enzymatic activities, crystal structures, and thermodynamics of nelfinavir-resistant HIV protease mutants J Mol Biol 374 1005 1016 10.1016/j.jmb.2007.09.083 1:CAS:528:DC%2BD2sXht1ykurjK (Pubitemid 350052096)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.4 , pp. 1005-1016
    • Kozisek, M.1    Bray, J.2    Rezacova, P.3    Saskova, K.4    Brynda, J.5    Pokorna, J.6    Mammano, F.7    Rulisek, L.8    Konvalinka, J.9
  • 61
    • 33745407153 scopus 로고    scopus 로고
    • Computational simulations of HIV-1 proteases-multi-drug resistance due to nonactive site mutation L90M
    • DOI 10.1021/ja060682b
    • H Ode S Neya M Hata W Sugiura T Hoshino 2006 Computational simulations of HIV-1 proteases-multi-drug resistance due to nonactive site mutation L90M J Am Chem Soc 128 7887 7895 10.1021/ja060682b 1:CAS:528:DC%2BD28XkvVehtbg%3D (Pubitemid 43945729)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.24 , pp. 7887-7895
    • Ode, H.1    Neya, S.2    Hata, M.3    Sugiura, W.4    Hoshino, T.5
  • 62
    • 42049099944 scopus 로고    scopus 로고
    • Novel method for probing the specificity binding profile of ligands: Applications to HIV protease
    • DOI 10.1111/j.1747-0285.2008.00659.x
    • W Sherman B Tidor 2008 Novel method for probing the specificity binding profile of ligands: applications to HIV protease Chem Biol Drug Des 71 387 407 10.1111/j.1747-0285.2008.00659.x 1:CAS:528:DC%2BD1cXlsVSrt78%3D (Pubitemid 351519509)
    • (2008) Chemical Biology and Drug Design , vol.71 , Issue.5 , pp. 387-407
    • Sherman, W.1    Tidor, B.2
  • 63
    • 33846798356 scopus 로고    scopus 로고
    • Hydrophobic Sliding: A Possible Mechanism for Drug Resistance in Human Immunodeficiency Virus Type 1 Protease
    • DOI 10.1016/j.str.2007.01.006, PII S0969212607000354
    • JE Foulkes-Murzycki WR Scott CA Schiffer 2007 Hydrophobic sliding: a possible mechanism for drug resistance in human immunodeficiency virus type 1 protease Structure 15 225 233 10.1016/j.str.2007.01.006 1:CAS:528: DC%2BD2sXhs1Smsrg%3D (Pubitemid 46209819)
    • (2007) Structure , vol.15 , Issue.2 , pp. 225-233
    • Foulkes-Murzycki, J.E.1    Scott, W.R.P.2    Schiffer, C.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.