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Volumn 78, Issue 6, 2010, Pages 1441-1456

UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate

Author keywords

HIV 1; Induced folding; Natively unfolded protein; Protein chemical synthesis; SAXS; Tat; Trifluoroethanol; Vaccine candidate

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; MUTANT PROTEIN; TRANSACTIVATOR PROTEIN; VIRUS PROTEIN;

EID: 77951221951     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22661     Document Type: Article
Times cited : (30)

References (73)
  • 1
    • 0032855497 scopus 로고    scopus 로고
    • Multifaceted activities of the HIV-1 transactivator of transcription
    • Jeang KT, Xiao H, Rich EA. Multifaceted activities of the HIV-1 transactivator of transcription. Tat J Biol Chem 1999;274;28837-28840.
    • (1999) Tat J Biol Chem , vol.274 , pp. 28837-28840
    • Jeang, K.T.1    Xiao, H.2    Rich, E.A.3
  • 3
    • 0025039326 scopus 로고
    • HIV-1 tat protein stimulates transcription by binding to a U-rich bulge in the stem of the TAR RNA structure
    • Dingwall C, Ernberg I, Gait MJ, Green SM, Heaphy S, Kam J, Lowe AD, Singh M, Skinner MA. HIV-1 tat protein stimulates transcription by binding to a U-rich bulge in the stem of the TAR RNA structure. Embo J 1990;9:4145-4153.
    • (1990) Embo J , vol.9 , pp. 4145-4153
    • Dingwall, C.1    Ernberg, I.2    Gait, M.J.3    Green, S.M.4    Heaphy, S.5    Kam, J.6    Lowe, A.D.7    Singh, M.8    Ma, S.9
  • 4
    • 0023876147 scopus 로고
    • HIV-1. tat trans-activation requires the loop sequence within TAR
    • Feng S, Holland EC. HIV-1. tat trans-activation requires the loop sequence within TAR. Nature 1988;334:165-167.
    • (1988) Nature , vol.334 , pp. 165-167
    • Feng, S.1    Holland, E.C.2
  • 5
    • 0028290825 scopus 로고
    • Control of RNA initiation and elongation at the HIV-1 promoter
    • Jones KA, Peterlin BM. Control of RNA initiation and elongation at the HIV-1 promoter. Annu Rev Biochem 1994;63:717-743.
    • (1994) Annu Rev Biochem , vol.63 , pp. 717-743
    • Jones, K.A.1    Peterlin, B.M.2
  • 6
    • 0027191817 scopus 로고
    • Does HIV-1 Tat induce a change in viral initiation rights
    • Cullen BR. Does HIV-1 Tat induce a change in viral initiation rights? Cell 1993;73:417-420.
    • (1993) Cell , vol.73 , pp. 417-420
    • Cullen, B.R.1
  • 7
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyciin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • Wei P, Garber ME, Fang SM, Fischer WH, Jones KA. A novel CDK9-associated C-type cyciin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 1998;92:451-462.
    • (1998) Cell , vol.92 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.M.3    Fischer, W.H.4    Jones, K.A.5
  • 8
    • 0033548533 scopus 로고    scopus 로고
    • Tat-associated kinase (P-TEFb): A component of transcription preinitiation and elongation complexes
    • Ping YH, Rana TM. Tat-associated kinase (P-TEFb): a component of transcription preinitiation and elongation complexes. J Biol Chem 1999;274:7399-7404.
    • (1999) J Biol Chem , vol.274 , pp. 7399-7404
    • Ping, Y.H.1    Rana, T.M.2
  • 9
    • 0032991426 scopus 로고    scopus 로고
    • Human and rodent transcription elongation factor P-TEFb: Interactions with human immunodeficiency vims type 1 tat and carboxyterminal domain substrate
    • Ramanathan Y, Reza SM, Young TM, Mathews MB, .Pe'ery T. Human and rodent transcription elongation factor P-TEFb: interactions with human immunodeficiency vims type 1 tat and carboxyterminal domain substrate. J Virol 1999;73:5448-5458.
    • (1999) J Virol , vol.73 , pp. 5448-5458
    • Ramanathan, Y.1    Reza, S.M.2    Young, T.M.3    Mathews, M.B.4    Pe'ery, T.5
  • 10
    • 57349170148 scopus 로고    scopus 로고
    • Role of the cyclin-dependent kinase 9-related pathway in mammalian gene expression and human diseases
    • Romano G, Giordano A. Role of the cyclin-dependent kinase 9-related pathway in mammalian gene expression and human diseases. Cell Cycle 2008;7:3664-3668.
    • (2008) Cell Cycle , vol.7 , pp. 3664-3668
    • Romano, G.1    Giordano, A.2
  • 13
    • 0028223435 scopus 로고
    • Human immunodeficiency virus 1 Tat binds to dipeptidyl aminopeptidase IV (CD26): A possible mechanism for Tat's immunosuppressive activity
    • Gutheil WG, Subramanyam M, Flentke GR, Sanford DG, Munoz E, Huber BT, Bachovchin WW. Human immunodeficiency virus 1 Tat binds to dipeptidyl aminopeptidase IV (CD26): a possible mechanism for Tat's immunosuppressive activity. Proc Natl Acad Sci USA. 1994;91:6594-6598.
    • (1994) Proc Natl Acad Sci USA. , vol.91 , pp. 6594-6598
    • Gutheil, W.G.1    Subramanyam, M.2    Flentke, G.R.3    Sanford, D.G.4    Munoz, E.5    Huber, B.T.6    Bachovchin, W.W.7
  • 14
    • 77951248864 scopus 로고    scopus 로고
    • HIV sequence compendium 2001
    • Kuiken CL, Foley B, Hahn B, Marx PA, McCutchan F, Mellors JW, Wolinksy S, Korber B, editors. Los Alamos National Laboratory
    • Kuiken CL, Foley B, Hahn B, Marx PA, McCutchan F, Mellors JW, Wolinksy S, Korber B, editors. HIV sequence compendium 2001. Los Alamos: Theoretical Biology and Biophysics, Los Alamos National Laboratory; 2001.
    • (2001) Los Alamos: Theoretical Biology and Biophysics
  • 17
    • 0024594466 scopus 로고
    • Mutational analysis of the conserved basic domain of human immunodeficiency virus Tat protein
    • Hauber J, Malim MH, Cullen BR. Mutational analysis of the conserved basic domain of human immunodeficiency virus Tat protein. J Virol 1989;63:1181-1187.
    • (1989) J Virol , vol.63 , pp. 1181-1187
    • Hauber, J.1    Malim, M.H.2    Cullen, B.R.3
  • 18
    • 0030862924 scopus 로고    scopus 로고
    • HIV-1 Tat protein exists from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region
    • Chang HC, Samaniego F, Nair BC, Buonaguro L, Ensoli B. HIV-1 Tat protein exists from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region. AIDS 1997;11:1421-1431.
    • (1997) AIDS , vol.11 , pp. 1421-1431
    • Chang, H.C.1    Samaniego, F.2    Nair, B.C.3    Buonaguro, L.4    Ensoli, B.5
  • 19
    • 0027220944 scopus 로고
    • The Tat protein of human immunodeficiency virus type 1, a growth factor for AIDS Kaposi sarcoma, and cytokine-activated vascular cells, induces adhesion of the same cell types by using integrin receptors recognizing the RGD amino acid sequence
    • Barillari G, Gendelman R, Gallo RC, Ensoli. B. The Tat protein of human immunodeficiency virus type 1, a growth factor for AIDS Kaposi sarcoma, and cytokine-activated vascular cells, induces adhesion of the same cell types by using integrin receptors recognizing the RGD amino acid sequence. Proc Natl Acad Sci USA 1993;90: 7941-7945.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7941-7945
    • Barillari, G.1    Gendelman, R.2    Gallo, R.C.3    Ensoli, B.4
  • 20
    • 33746750048 scopus 로고    scopus 로고
    • Reciprocal transactivation between HIV-1 and other human viruses
    • White MK, Gorrill TS, Khalili K, Reciprocal transactivation between HIV-1 and other human viruses. Virology 2006;352:1-13.
    • (2006) Virology , vol.352 , pp. 1-13
    • White, M.K.1    Gorrill, T.S.2    Khalili, K.3
  • 21
    • 0026442836 scopus 로고
    • Effects of the human immunodeficiency virus type 1 Tat protein on the expression of inflammatory cytokines
    • Buonaguro L, Barillari. G, Chang HK, Bohan CA, Kao V, Morgan R, Gallo RC, Ensoli B. Effects of the human immunodeficiency virus type 1 Tat protein on the expression of inflammatory cytokines. J Virol 1992;66:7159-7167.
    • (1992) J Virol , vol.66 , pp. 7159-7167
    • Buonaguro, L.1    Barillari, G.2    Chang, H.K.3    Bohan, C.A.4    Kao, V.5    Morgan, R.6    Gallo, R.C.7    Ensoli, B.8
  • 22
    • 0028274136 scopus 로고
    • The human immunodeficiency virus type 1 Tat protein transactivates tumor necrosis factor beta gene expression, through a TAR-like structure
    • Buonaguro L, Buonaguro FM, Giraldo G, Ensoli B. The human immunodeficiency virus type 1 Tat protein transactivates tumor necrosis factor beta gene expression, through a TAR-like structure. J Virol 1994;68:2677-2682.
    • (1994) J Virol , vol.68 , pp. 2677-2682
    • Buonaguro, L.1    Buonaguro, F.M.2    Giraldo, G.3    Ensoli, B.4
  • 23
    • 0030914237 scopus 로고    scopus 로고
    • HIV-1 Tat induces the expression of the interleukin-6 (IL6) gene by binding to the IL6 leader RNA and by interacting with CAAT enhancer-binding protein beta (NF-IL6) transcription factors
    • Ambrosino C, Ruocco MR, Chen X, Mallardo M, Baudi F, Trematerra S, Quinto I, Venuta S, Scala G. HIV-1 Tat induces the expression of the interleukin-6 (IL6) gene by binding to the IL6 leader RNA and by interacting with CAAT enhancer-binding protein beta (NF-IL6) transcription factors. J Biol Chem 1997;272:14883-14892.
    • (1997) J Biol Chem , vol.272 , pp. 14883-14892
    • Ambrosino, C.1    Ruocco, M.R.2    Chen, X.3    Mallardo, M.4    Baudi, F.5    Trematerra, S.6    Quinto, I.7    Venuta, S.8    Scala, G.9
  • 24
    • 0038303112 scopus 로고    scopus 로고
    • Distinct transcriptional pathways regulate basal and activated major histocompatibility complex class i expression
    • Howcroft TK, Ravai A, Weissman JD, Gegonne A, Singer DS. Distinct transcriptional pathways regulate basal and activated major histocompatibility complex class I expression. Mol Cell Biol 2003; 23:3377-3391.
    • (2003) Mol Cell Biol , vol.23 , pp. 3377-3391
    • Howcroft, T.K.1    Ravai, A.2    Weissman, J.D.3    Gegonne, A.4    Singer, D.S.5
  • 25
    • 0035313077 scopus 로고    scopus 로고
    • HIV-1 Tat inhibits IL-2 gene transcription through qualitative and quantitative alterations of the cooperative Rel/API complex, bound to the C.D28RE/ API composite element of the IL-2 promoter
    • Gonzalez E, Punzon C, Gonzalez M, Fresno M. HIV-1 Tat inhibits IL-2 gene transcription through qualitative and quantitative alterations of the cooperative Rel/API complex, bound to the C.D28RE/ API composite element of the IL-2 promoter, J Immunol 2001;166; 4560-4569.
    • (2001) J Immunol , vol.166 , pp. 4560-4569
    • Gonzalez, E.1    Punzon, C.2    Gonzalez, M.3    Fresno, M.4
  • 26
    • 34447521820 scopus 로고    scopus 로고
    • Design and characterization of an HIV-I Tat mutant: Inactivation of viral and cellular functions but not antigenicity
    • Mayol K, Munier S, Beck A, Verrier B, Guillon C. Design and characterization of an HIV-I Tat mutant: inactivation of viral and cellular functions but not antigenicity. Vaccine 2007;25:6047-6060.
    • (2007) Vaccine , vol.25 , pp. 6047-6060
    • Mayol, K.1    Munier, S.2    Beck, A.3    Verrier, B.4    Guillon, C.5
  • 27
    • 0025344596 scopus 로고
    • Tat protein of HIV-I stimulates growth of cells derived from Kaposi's sarcoma lesions of AIDS patients
    • Ensoli B, Barillari G, Salahuddin SZ, Gallo RC, Wong-Staal F. Tat protein of HIV-I stimulates growth of cells derived from Kaposi's sarcoma lesions of AIDS patients. Nature 1990;345:84-86.
    • (1990) Nature , vol.345 , pp. 84-86
    • Ensoli, B.1    Barillari, G.2    Salahuddin, S.Z.3    Gallo, R.C.4    Wong-Staal, F.5
  • 30
    • 0032978963 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Tat induces apoptosis and increases sensitivity to apoptotic signals by up-regulating FLICE/Caspase-8
    • Bartz SR, Emerman M. Human immunodeficiency virus type 1 Tat induces apoptosis and increases sensitivity to apoptotic signals by up-regulating FLICE/Caspase-8. J Virol 1999;73:1956-1963.
    • (1999) J Virol , vol.73 , pp. 1956-1963
    • Bartz, S.R.1    Emerman, M.2
  • 31
    • 0039129153 scopus 로고    scopus 로고
    • Expression of human immunodeficiency virus type i tat results in down-regulation of bcl-2 and induction of apoptosis in hematopoietic cells
    • Sastry KJ, Marin MC, Nehete PN, McConnell K, el-Naggar AK, McDonnell TJ. Expression of human immunodeficiency virus type I tat results in down-regulation of bcl-2 and induction of apoptosis in hematopoietic cells. Oncogene 1996;13:487-493.
    • (1996) Oncogene , vol.13 , pp. 487-493
    • Sastry, K.J.1    Marin, M.C.2    Nehete, P.N.3    McConnell, K.4    El-Naggar, A.K.5    McDonnell, T.J.6
  • 32
    • 0347319110 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Tat regulates endothelial, ceil actin cytoskeletal dynamics through PAKl activation and oxidant production
    • Wu RF, Gu Y, Xu YC, Mitoia S, Bussolino F, Terada LS. Human immunodeficiency virus type 1 Tat regulates endothelial, ceil actin cytoskeletal dynamics through PAKl activation and oxidant production. J Virol 2004;78:779-789.
    • (2004) J Virol , vol.78 , pp. 779-789
    • Wu, R.F.1    Gu, Y.2    Xu, Y.C.3    Mitoia, S.4    Bussolino, F.5    Terada, L.S.6
  • 33
    • 0033401493 scopus 로고    scopus 로고
    • Extracellular HIV-I Tat protein differentially activates the JNK and ERK/MAPK pathways in CD4 T cells
    • Mischiati C, Pironi F, Milani D, Giacca M, Mirándola P, Capitani S, Zauii G. Extracellular HIV-I Tat protein differentially activates the JNK and ERK/MAPK pathways in CD4 T cells. Aids 1999;13:1637-1645.
    • (1999) Aids , vol.13 , pp. 1637-1645
    • Mischiati, C.1    Pironi, F.2    Milani, D.3    Giacca, M.4    Mirándola, P.5    Capitani, S.6    Zauii, G.7
  • 37
    • 53349173299 scopus 로고    scopus 로고
    • Homonuclear 1H NMR and circular dichroism study of the HIV-1 Tat Eli variant
    • Watkins JD, Campbell GR, Halimi H, Loret EP. Homonuclear 1H NMR and circular dichroism study of the HIV-1 Tat Eli variant. Retrovirology 2008;5:83.
    • (2008) Retrovirology , vol.5 , pp. 83
    • Watkins, J.D.1    Campbell, G.R.2    Halimi, H.3    Loret, E.P.4
  • 38
    • 33646835410 scopus 로고    scopus 로고
    • HIV-1 Tat is a natively unfolded protein: The solution conformation and dynamics of reduced HIV-1. Tat-(l-72) by NMR spectroscopy
    • Shojania S, O'Neil JD. HIV-1 Tat is a natively unfolded protein: the solution conformation and dynamics of reduced HIV-1. Tat-(l-72) by NMR spectroscopy. J Biol Chem 2006;281:8347-8356.
    • (2006) J Biol Chem , vol.281 , pp. 8347-8356
    • Shojania, S.1    O'Neil, J.D.2
  • 39
    • 0027264496 scopus 로고
    • Repression of MHC class i gene promoter activity by two-exon Tat of HIV
    • Howcroft TK, Strebel K, Martin MA, Sinder DS. Repression of MHC class I gene promoter activity by two-exon Tat of HIV. Science 1993;260:1320-1322.
    • (1993) Science , vol.260 , pp. 1320-1322
    • Howcroft, T.K.1    Strebel, K.2    Martin, M.A.3    Sinder, D.S.4
  • 40
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet P, Robert X, Courcelle E. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res 2003;31:3320-3323.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 41
    • 0023860379 scopus 로고
    • A. quantitative bioassay for HIV-1 based on trans-activation
    • Felber BK, Pavlakis GN. A. quantitative bioassay for HIV-1 based on trans-activation. Science 1988;239:184-187.
    • (1988) Science , vol.239 , pp. 184-187
    • Felber, B.K.1    Pavlakis, G.N.2
  • 42
    • 0036188466 scopus 로고    scopus 로고
    • Antibody-mediated enhancement of HIV-1 infectivity is determined by the structure of gpl20 and depends on the modulation of gpl20/CCR5 interaction
    • Guilion C, Schutten M, Boers PHM, Gruters RA, Osterhaus ADME. Antibody-mediated enhancement of HIV-1 infectivity is determined by the structure of gpl20 and depends on the modulation of gpl20/CCR5 interaction. J Virol 2002;76:2827-2834.
    • (2002) J Virol , vol.76 , pp. 2827-2834
    • Guilion, C.1    Schutten, M.2    Boers, P.H.M.3    Gruters, R.A.4    Adme, O.5
  • 43
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade MA, Chacon P, Merelo JJ, Moran F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng 1993;6:383-390.
    • (1993) Protein Eng , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 44
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution, by circular dichroism
    • Chen YH, Yang JT, Chau KH. Determination of the helix and beta form of proteins in aqueous solution, by circular dichroism. Biochemistry 1974;13:3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 45
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky VN. Natively unfolded proteins: a point where biology waits for physics. Protein Sci 2002;11:739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 46
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins DK, Grimshaw SB, Receveur V, Dobson CM, Jones JA, Smith LJ. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 1999;38:16424-16431.
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 47
    • 0023709016 scopus 로고
    • Study of the translationsl diffusion of macromolecules in beads of gel chromatography by the FRAP method
    • Poitevin. E, Wahl P. Study of the translationsl diffusion of macromolecules in beads of gel chromatography by the FRAP method. Biophys Chem 1988;31:247-258.
    • (1988) Biophys Chem , vol.31 , pp. 247-258
    • Poitevin, E.1    Wahl, P.2
  • 49
    • 0026910457 scopus 로고
    • Determination of the reguiarization parameter in indirect-transform methods using perceptual criteria
    • Svergun D. Determination of the reguiarization parameter in indirect-transform methods using perceptual criteria. J Appl Cryst 1992;25:495-503.
    • (1992) J Appl Cryst , vol.25 , pp. 495-503
    • Svergun, D.1
  • 50
    • 33846232281 scopus 로고    scopus 로고
    • Evidence for CTL-mediated selection of Tat and Rev mutants after the onset of the asymptomatic period during HIV-I infection
    • Guilion C, Stankovic K, Ataman-Önal Y, Biron F, Verrier B. Evidence for CTL-mediated selection of Tat and Rev mutants after the onset of the asymptomatic period during HIV-I infection. AIDS Res Hum Retroviruses 2006;22:1283-1292.
    • (2006) AIDS Res Hum Retroviruses , vol.22 , pp. 1283-1292
    • Guilion, C.1    Stankovic, K.2    Ataman-Önal, Y.3    Biron, F.4    Verrier, B.5
  • 52
    • 0037495845 scopus 로고    scopus 로고
    • Synthesis, refolding and protective immune responses of a potential antigen for human respiratory syncytial virus vaccine
    • Klinguer-Hamour C, Bussat MC, Plotnicky H, Velin D, Corvaia N, Nguyen T, Beck A. Synthesis, refolding and protective immune responses of a potential antigen for human respiratory syncytial virus vaccine. J Pept Res 2003;62:27-36.
    • (2003) J Pept Res , vol.62 , pp. 27-36
    • Klinguer-Hamour, C.1    Bussat, M.C.2    Plotnicky, H.3    Velin, D.4    Corvaia, N.5    Nguyen, T.6    Beck, A.7
  • 53
  • 55
    • 0037705413 scopus 로고    scopus 로고
    • The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein
    • Longhi S, Receveur-Brechot V, Karlin D, Johansson K, Darbon H, Bheila D, Yeo R, Finet S, Canard B. The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. J Biol Chem 2003;278:18638-18648.
    • (2003) J Biol Chem , vol.278 , pp. 18638-18648
    • Longhi, S.1    Receveur-Brechot, V.2    Karlin, D.3    Johansson, K.4    Darbon, H.5    Bheila, D.6    Yeo, R.7    Finet, S.8    Canard, B.9
  • 56
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D, Barberato C, Koch M. CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Cryst 1995;28:768-773.
    • (1995) J Appl Cryst , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.3
  • 57
    • 0028061408 scopus 로고
    • Compactness of protein molten globules: Temperature-induced structural changes of the apomyoglobin folding intermediate
    • Gast K, Damaschun H, Misselwitz R, Muller-Frohne M, Zirwer D, Damaschun G. Compactness of protein molten globules: temperature-induced structural changes of the apomyoglobin folding intermediate. Eur Biophys J 1994;23:297-305.
    • (1994) Eur Biophys J , vol.23 , pp. 297-305
    • Gast, K.1    Damaschun, H.2    Misselwitz, R.3    Muller-Frohne, M.4    Zirwer, D.5    Damaschun, G.6
  • 58
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson HJ, Wright PE. Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 2002;12:54-60.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 59
    • 0030070502 scopus 로고    scopus 로고
    • Structural studies of mutant glucocorticoid receptor transactivation domains establish a link between transactivation activity in vivo and alpha-helix-forming potential in vitro
    • Dahlman-Wright K, McEwan IJ. Structural studies of mutant glucocorticoid receptor transactivation domains establish a link between transactivation activity in vivo and alpha-helix-forming potential in vitro. Biochemistry 1996;35:1323-1327.
    • (1996) Biochemistry , vol.35 , pp. 1323-1327
    • Dahlman-Wright, K.1    McEwan, I.J.2
  • 60
    • 0028097046 scopus 로고
    • Trifluoroethanol stabilizes a helix-turn-helix motif in equine infectious-anemia-virus frans-activator protein
    • Sticht H, Willbold D, Ejchart A, Rosin-Arbesfeld R, Yaniv A, Gazit A, Rösch P. Trifluoroethanol stabilizes a helix-turn-helix motif in equine infectious-anemia-virus frans-activator protein. Eur J Biochem 1994;225:855-861.
    • (1994) Eur J Biochem , vol.225 , pp. 855-861
    • Sticht, H.1    Willbold, D.2    Ejchart, A.3    Rosin-Arbesfeld, R.4    Yaniv, A.5    Gazit, A.6    Rösch, P.7
  • 61
    • 67649804607 scopus 로고    scopus 로고
    • Tropoelastin as a thermodynamically unfolded premolten globule protein: The effect of trimethylamlne N-oxide on structure and coacervation
    • Dyksterhuis LB, Carter EA, Mithieux SM, Weiss AS. Tropoelastin as a thermodynamically unfolded premolten globule protein: the effect of trimethylamlne N-oxide on structure and coacervation. Arch Biochem Biophys 2009;487:79-84.
    • (2009) Arch Biochem Biophys , vol.487 , pp. 79-84
    • Dyksterhuis, L.B.1    Carter, E.A.2    Mithieux, S.M.3    Weiss, A.S.4
  • 62
    • 0015997959 scopus 로고
    • Aromatic contributions to circular dichroism spectra of proteins
    • Strickland EH. Aromatic contributions to circular dichroism spectra of proteins. CRC Crit Rev Biochem. .1974;2:113-175.
    • (1974) CRC Crit Rev Biochem. , vol.2 , pp. 113-175
    • Strickland, E.H.1
  • 64
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded
    • Uversky VN. What does it mean to be natively unfolded? Eur J Biochem 2002;269:2-12.
    • (2002) Eur J Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 65
    • 0037666814 scopus 로고    scopus 로고
    • Organic solvents order the dynamic switch II in Ras crystals
    • Buhrman G, de Serrano V, Mattos C. Organic solvents order the dynamic switch II in Ras crystals. Structure 2003;11:747-751.
    • (2003) Structure , vol.11 , pp. 747-751
    • Buhrman, G.1    De Serrano, V.2    Mattos, C.3
  • 66
    • 0036299393 scopus 로고    scopus 로고
    • The N-terminal domain of the phosphoprotein of morbilliviruses belongs to the natively unfolded class of proteins
    • Karlin D, Longhi S, Receveur V, Canard B. The N-terminal domain of the phosphoprotein of morbilliviruses belongs to the natively unfolded class of proteins. Virology 2002;296:251-262.
    • (2002) Virology , vol.296 , pp. 251-262
    • Karlin, D.1    Longhi, S.2    Receveur, V.3    Canard, B.4
  • 67
    • 0027522642 scopus 로고
    • The acidic activation domains of the GCN4 and GAL4 proteins are not alpha helical but form beta sheets
    • van Hoy M, Leuther KK, Kodadek T, Johnston SA. The acidic activation domains of the GCN4 and GAL4 proteins are not alpha helical but form beta sheets. Cell 1993;72:587-594.
    • (1993) Cell , vol.72 , pp. 587-594
    • Van Hoy, M.1    Leuther, K.K.2    Kodadek, T.3    Johnston, S.A.4
  • 68
    • 57149121459 scopus 로고    scopus 로고
    • Structural insights into the cyclin Tl-Tat-TAR RNA transcription activation complex from EIAV
    • Anand K, Schulte A, Vogel-Bachmayr K, Scheffzek K, Geyer M. Structural insights into the cyclin Tl-Tat-TAR RNA transcription activation complex from EIAV. Nat Struct. MoI Biol 2008; 15:1287-1292.
    • (2008) Nat Struct. MoI Biol , vol.15 , pp. 1287-1292
    • Anand, K.1    Schulte, A.2    Vogel-Bachmayr, K.3    Scheffzek, K.4    Geyer, M.5
  • 69
    • 0027956167 scopus 로고
    • NMR structure of a biologically active peptide containing the RNAbinding domain of human immunodeficiency virus type 1 Tat
    • Mujeeb A, Bishop K, Peterlin BM, Turck C, Parsiow TG, James TL. NMR structure of a biologically active peptide containing the RNAbinding domain of human immunodeficiency virus type 1 Tat. Proc Natl Acad Sci USA 1994;91:8248-8252.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8248-8252
    • Mujeeb, A.1    Bishop, K.2    Peterlin, B.M.3    Turck, C.4    Parsiow, T.G.5    James, T.L.6
  • 73
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright PE, Dyson HJ. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 1999;293: 321-331.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.