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Volumn 7, Issue 6, 2011, Pages

Mechanisms for the evolution of a derived function in the ancestral glucocorticoid receptor

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOCORTICOID RECEPTOR; MINERALOCORTICOID RECEPTOR; GLUCOCORTICOID;

EID: 79959834622     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1002117     Document Type: Article
Times cited : (51)

References (72)
  • 1
    • 0004274563 scopus 로고
    • The molecular basis of evolution
    • New York, Wiley
    • Anfinsen CB, (1959) The molecular basis of evolution. New York Wiley.
    • (1959)
    • Anfinsen, C.B.1
  • 2
    • 0002725360 scopus 로고
    • Chemical paleogenetics: molecular "restoration studies" of extinct forms of life
    • Pauling L, Zuckerkandl E, (1963) Chemical paleogenetics: molecular "restoration studies" of extinct forms of life. Acta Chem Scand 17: S9-S16.
    • (1963) Acta Chem Scand , vol.17 , pp. 9-16
    • Pauling, L.1    Zuckerkandl, E.2
  • 3
    • 0003515251 scopus 로고
    • Evolution by gene duplication
    • BerlinNew York, Springer-Verlag
    • Ohno S, (1970) Evolution by gene duplication. BerlinNew York Springer-Verlag.
    • (1970)
    • Ohno, S.1
  • 4
    • 0016008138 scopus 로고
    • Gene pool of higher organisms as a product of evolution
    • Kimura M, (1974) Gene pool of higher organisms as a product of evolution. Cold Spring Harb Symp Quant Biol 38: 515-524.
    • (1974) Cold Spring Harb Symp Quant Biol , vol.38 , pp. 515-524
    • Kimura, M.1
  • 5
    • 0021004799 scopus 로고
    • Species adaptation in a protein molecule
    • Perutz MF, (1983) Species adaptation in a protein molecule. Mol Biol Evol 1: 1-28.
    • (1983) Mol Biol Evol , vol.1 , pp. 1-28
    • Perutz, M.F.1
  • 6
    • 0031966661 scopus 로고    scopus 로고
    • The structural basis of molecular adaptation
    • Golding GB, Dean AM, (1998) The structural basis of molecular adaptation. Mol Biol Evol 15: 355-369.
    • (1998) Mol Biol Evol , vol.15 , pp. 355-369
    • Golding, G.B.1    Dean, A.M.2
  • 7
    • 0013776758 scopus 로고
    • Molecules as documents of evolutionary history
    • Zuckerkandl E, Pauling L, (1965) Molecules as documents of evolutionary history. J Theor Biol 8: 357-366.
    • (1965) J Theor Biol , vol.8 , pp. 357-366
    • Zuckerkandl, E.1    Pauling, L.2
  • 8
    • 0027441807 scopus 로고
    • Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability
    • Serrano L, Day AG, Fersht AR, (1993) Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. J Mol Biol 233: 305-312.
    • (1993) J Mol Biol , vol.233 , pp. 305-312
    • Serrano, L.1    Day, A.G.2    Fersht, A.R.3
  • 9
    • 46249099576 scopus 로고    scopus 로고
    • Characterization and prediction of residues determining protein functional specificity
    • Capra JA, Singh M, (2008) Characterization and prediction of residues determining protein functional specificity. Bioinformatics 24: 1473-1480.
    • (2008) Bioinformatics , vol.24 , pp. 1473-1480
    • Capra, J.A.1    Singh, M.2
  • 10
    • 58149187903 scopus 로고    scopus 로고
    • SDR: a database of predicted specificity-determining residues in proteins
    • Donald JE, Shakhnovich EI, (2009) SDR: a database of predicted specificity-determining residues in proteins. Nucleic Acids Res 37: D191-4.
    • (2009) Nucleic Acids Res , vol.37 , pp. 191-194
    • Donald, J.E.1    Shakhnovich, E.I.2
  • 11
    • 65249143885 scopus 로고    scopus 로고
    • Enzyme (re)design: lessons from natural evolution and computation
    • Gerlt JA, Babbitt PC, (2009) Enzyme (re)design: lessons from natural evolution and computation. Curr Opin Chem Biol 13: 10-18.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 10-18
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 12
    • 77955584075 scopus 로고    scopus 로고
    • Analyzing protein structure and function using ancestral gene reconstruction
    • Harms MJ, Thornton JW, (2010) Analyzing protein structure and function using ancestral gene reconstruction. Curr Opin Struct Biol 20: 360-366.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 360-366
    • Harms, M.J.1    Thornton, J.W.2
  • 14
    • 33845864966 scopus 로고    scopus 로고
    • Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein
    • Bershtein S, Segal M, Bekerman R, Tokuriki N, Tawfik DS, (2006) Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein. Nature 444: 929-932.
    • (2006) Nature , vol.444 , pp. 929-932
    • Bershtein, S.1    Segal, M.2    Bekerman, R.3    Tokuriki, N.4    Tawfik, D.S.5
  • 15
    • 34548040966 scopus 로고    scopus 로고
    • Crystal structure of an ancient protein: Evolution by conformational epistasis
    • Ortlund EA, Bridgham JT, Redinbo MR, Thornton JW, (2007) Crystal structure of an ancient protein: Evolution by conformational epistasis. Science 317: 1544-1548.
    • (2007) Science , vol.317 , pp. 1544-1548
    • Ortlund, E.A.1    Bridgham, J.T.2    Redinbo, M.R.3    Thornton, J.W.4
  • 16
    • 70349464621 scopus 로고    scopus 로고
    • An epistatic ratchet constrains the direction of glucocorticoid receptor evolution
    • Bridgham JT, Ortlund EA, Thornton JW, (2009) An epistatic ratchet constrains the direction of glucocorticoid receptor evolution. Nature 461: 515-519.
    • (2009) Nature , vol.461 , pp. 515-519
    • Bridgham, J.T.1    Ortlund, E.A.2    Thornton, J.W.3
  • 17
    • 58549106768 scopus 로고    scopus 로고
    • Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility
    • Tomatis PE, Fabiane SM, Simona F, Carloni P, Sutton BJ, et al. (2008) Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility. Proc Natl Acad Sci U S A 105: 20605-20610.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 20605-20610
    • Tomatis, P.E.1    Fabiane, S.M.2    Simona, F.3    Carloni, P.4    Sutton, B.J.5
  • 18
    • 1942531303 scopus 로고    scopus 로고
    • Resurrecting ancient genes: experimental analysis of extinct molecules
    • Thornton JW, (2004) Resurrecting ancient genes: experimental analysis of extinct molecules. Nat Rev Genet 5: 366-375.
    • (2004) Nat Rev Genet , vol.5 , pp. 366-375
    • Thornton, J.W.1
  • 19
    • 33645691679 scopus 로고    scopus 로고
    • Evolution of hormone-receptor complexity by molecular exploitation
    • Bridgham JT, Carroll SM, Thornton JW, (2006) Evolution of hormone-receptor complexity by molecular exploitation. Science 312: 97-101.
    • (2006) Science , vol.312 , pp. 97-101
    • Bridgham, J.T.1    Carroll, S.M.2    Thornton, J.W.3
  • 20
    • 0024545638 scopus 로고
    • Gene regulation by steroid hormones
    • Beato M, (1989) Gene regulation by steroid hormones. Cell 56: 335-344.
    • (1989) Cell , vol.56 , pp. 335-344
    • Beato, M.1
  • 21
    • 0003937447 scopus 로고    scopus 로고
    • Comparative vertebrate endocrinology
    • New York, Cambridge University Press
    • Bentley PJ, (1998) Comparative vertebrate endocrinology. New York Cambridge University Press.
    • (1998)
    • Bentley, P.J.1
  • 22
    • 0023221667 scopus 로고
    • Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor
    • Arriza JL, Weinberger C, Cerelli G, Glaser TM, Handelin BL, et al. (1987) Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor. Science 237: 268-275.
    • (1987) Science , vol.237 , pp. 268-275
    • Arriza, J.L.1    Weinberger, C.2    Cerelli, G.3    Glaser, T.M.4    Handelin, B.L.5
  • 23
    • 56449119335 scopus 로고    scopus 로고
    • Evolution of hormone signaling in elasmobranchs by exploitation of promiscuous receptors
    • Carroll SM, Bridgham JT, Thornton JW, (2008) Evolution of hormone signaling in elasmobranchs by exploitation of promiscuous receptors. Mol Biol Evol 25: 2643-2652.
    • (2008) Mol Biol Evol , vol.25 , pp. 2643-2652
    • Carroll, S.M.1    Bridgham, J.T.2    Thornton, J.W.3
  • 24
    • 0035826690 scopus 로고    scopus 로고
    • Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions
    • Thornton JW, (2001) Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions. Proc Natl Acad Sci U S A 98: 5671-5676.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 5671-5676
    • Thornton, J.W.1
  • 25
    • 0033214639 scopus 로고    scopus 로고
    • Effects of insulin-like growth factor-I, corticosterone, and 3,3′, 5-tri-iodo-L-thyronine on glycosaminoglycan synthesis in vertebral cartilage of the clearnose skate, Raja eglanteria
    • Gelsleichter J, Musick JA, (1999) Effects of insulin-like growth factor-I, corticosterone, and 3,3′, 5-tri-iodo-L-thyronine on glycosaminoglycan synthesis in vertebral cartilage of the clearnose skate, Raja eglanteria. J Exp Zool 284: 549-556.
    • (1999) J Exp Zool , vol.284 , pp. 549-556
    • Gelsleichter, J.1    Musick, J.A.2
  • 26
    • 33845188433 scopus 로고    scopus 로고
    • Characterization of cDNAs encoding cholesterol side chain cleavage and 3beta-hydroxysteroid dehydrogenase in the freshwater stingray Potamotrygon motoro
    • Nunez BS, Evans AN, Simpson MA, Wong WP, Ip YK, (2006) Characterization of cDNAs encoding cholesterol side chain cleavage and 3beta-hydroxysteroid dehydrogenase in the freshwater stingray Potamotrygon motoro. Comp Biochem Physiol B Biochem Mol Biol 145: 306-317.
    • (2006) Comp Biochem Physiol B Biochem Mol Biol , vol.145 , pp. 306-317
    • Nunez, B.S.1    Evans, A.N.2    Simpson, M.A.3    Wong, W.P.4    Ip, Y.K.5
  • 27
    • 0033215001 scopus 로고    scopus 로고
    • Regulation of interrenal gland steroidogenesis in the Atlantic stingray (Dasyatis sabina)
    • Nunez S, Trant JM, (1999) Regulation of interrenal gland steroidogenesis in the Atlantic stingray (Dasyatis sabina). J Exp Zool 284: 517-525.
    • (1999) J Exp Zool , vol.284 , pp. 517-525
    • Nunez, S.1    Trant, J.M.2
  • 28
    • 36048980045 scopus 로고    scopus 로고
    • Sex, seasonal, and stress-related variations in elasmobranch corticosterone concentrations
    • Manire CA, Rasmussen LEL, Maruska KP, Tricas TC, (2007) Sex, seasonal, and stress-related variations in elasmobranch corticosterone concentrations. Comp Biochem Phys A 148: 926-935.
    • (2007) Comp Biochem Phys A , vol.148 , pp. 926-935
    • Manire, C.A.1    Rasmussen, L.E.L.2    Maruska, K.P.3    Tricas, T.C.4
  • 29
    • 0021180536 scopus 로고
    • Secretory dynamics of 1 alpha-hydroxycorticosterone in the elasmobranch fish, Scyliorhinus canicula
    • Hazon N, Henderson IW, (1984) Secretory dynamics of 1 alpha-hydroxycorticosterone in the elasmobranch fish, Scyliorhinus canicula. J Endocrinol 103: 205-211.
    • (1984) J Endocrinol , vol.103 , pp. 205-211
    • Hazon, N.1    Henderson, I.W.2
  • 30
    • 0027521719 scopus 로고
    • The effect of dietary protein restriction on the secretory dynamics of 1 alpha-hydroxycorticosterone and urea in the dogfish, Scyliorhinus canicula: a possible role for 1 alpha-hydroxycorticosterone in sodium retention
    • Armour KJ, O'Toole LB, Hazon N, (1993) The effect of dietary protein restriction on the secretory dynamics of 1 alpha-hydroxycorticosterone and urea in the dogfish, Scyliorhinus canicula: a possible role for 1 alpha-hydroxycorticosterone in sodium retention. J Endocrinol 138: 275-282.
    • (1993) J Endocrinol , vol.138 , pp. 275-282
    • Armour, K.J.1    O'Toole, L.B.2    Hazon, N.3
  • 31
    • 0032023889 scopus 로고    scopus 로고
    • Taxonomic sampling, phylogenetic accuracy, and investigator bias
    • Hillis DM, (1998) Taxonomic sampling, phylogenetic accuracy, and investigator bias. Syst Biol 47: 3-8.
    • (1998) Syst Biol , vol.47 , pp. 3-8
    • Hillis, D.M.1
  • 32
    • 47749095118 scopus 로고    scopus 로고
    • Taxon sampling affects inferences of macroevolutionary processes from phylogenetic trees
    • Heath TA, Zwickl DJ, Kim J, Hillis DM, (2008) Taxon sampling affects inferences of macroevolutionary processes from phylogenetic trees. Syst Biol 57: 160-166.
    • (2008) Syst Biol , vol.57 , pp. 160-166
    • Heath, T.A.1    Zwickl, D.J.2    Kim, J.3    Hillis, D.M.4
  • 33
    • 0036699885 scopus 로고    scopus 로고
    • Increased taxon sampling is advantageous for phylogenetic inference
    • Pollock DD, Zwickl DJ, McGuire JA, Hillis DM, (2002) Increased taxon sampling is advantageous for phylogenetic inference. Syst Biol 51: 664-671.
    • (2002) Syst Biol , vol.51 , pp. 664-671
    • Pollock, D.D.1    Zwickl, D.J.2    McGuire, J.A.3    Hillis, D.M.4
  • 34
    • 0001162654 scopus 로고
    • 1-alpha-hydroxycorticosterone from cartilaginous fish: a new adrenal steroid in blood
    • Idler DR, Truscott B, (1966) 1-alpha-hydroxycorticosterone from cartilaginous fish: a new adrenal steroid in blood. Journal of the Fisheries Research Board of Canada 23: 615-619.
    • (1966) Journal of the Fisheries Research Board of Canada , vol.23 , pp. 615-619
    • Idler, D.R.1    Truscott, B.2
  • 35
    • 0015344371 scopus 로고
    • Corticosteroids in plasma of elasmobranchs
    • Truscott B, Idler DR, (1972) Corticosteroids in plasma of elasmobranchs. Comp Biochem Physiol A 42: 41-50.
    • (1972) Comp Biochem Physiol A , vol.42 , pp. 41-50
    • Truscott, B.1    Idler, D.R.2
  • 36
    • 77955975654 scopus 로고    scopus 로고
    • Robustness of ancestral sequence reconstruction to phylogenetic uncertainty
    • Hanson-Smith V, Kolaczkowski B, Thornton JW, (2010) Robustness of ancestral sequence reconstruction to phylogenetic uncertainty. Mol Biol Evol 27: 1988-1999.
    • (2010) Mol Biol Evol , vol.27 , pp. 1988-1999
    • Hanson-Smith, V.1    Kolaczkowski, B.2    Thornton, J.W.3
  • 37
    • 18444405534 scopus 로고    scopus 로고
    • Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition
    • Bledsoe RK, Montana VG, Stanley TB, Delves CJ, Apolito CJ, et al. (2002) Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell 110: 93-105.
    • (2002) Cell , vol.110 , pp. 93-105
    • Bledsoe, R.K.1    Montana, V.G.2    Stanley, T.B.3    Delves, C.J.4    Apolito, C.J.5
  • 38
    • 3242784885 scopus 로고    scopus 로고
    • Mechanism of the nuclear receptor molecular switch
    • Nagy L, Schwabe JW, (2004) Mechanism of the nuclear receptor molecular switch. Trends Biochem Sci 29: 317-324.
    • (2004) Trends Biochem Sci , vol.29 , pp. 317-324
    • Nagy, L.1    Schwabe, J.W.2
  • 39
    • 0032511086 scopus 로고    scopus 로고
    • Hormone-dependent coactivator binding to a hydrophobic cleft on nuclear receptors
    • Feng W, Ribeiro RC, Wagner RL, Nguyen H, Apriletti JW, et al. (1998) Hormone-dependent coactivator binding to a hydrophobic cleft on nuclear receptors. Science 280: 1747-1749.
    • (1998) Science , vol.280 , pp. 1747-1749
    • Feng, W.1    Ribeiro, R.C.2    Wagner, R.L.3    Nguyen, H.4    Apriletti, J.W.5
  • 40
    • 0038265311 scopus 로고    scopus 로고
    • The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism
    • Kauppi B, Jakob C, Farnegardh M, Yang J, Ahola H, et al. (2003) The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism. J Biol Chem 278: 22748-22754.
    • (2003) J Biol Chem , vol.278 , pp. 22748-22754
    • Kauppi, B.1    Jakob, C.2    Farnegardh, M.3    Yang, J.4    Ahola, H.5
  • 41
    • 24744451821 scopus 로고    scopus 로고
    • A ligand-mediated hydrogen bond network required for the activation of the mineralocorticoid receptor
    • Bledsoe RK, Madauss KP, Holt JA, Apolito CJ, Lambert MH, et al. (2005) A ligand-mediated hydrogen bond network required for the activation of the mineralocorticoid receptor. J Biol Chem 280: 31283-31293.
    • (2005) J Biol Chem , vol.280 , pp. 31283-31293
    • Bledsoe, R.K.1    Madauss, K.P.2    Holt, J.A.3    Apolito, C.J.4    Lambert, M.H.5
  • 42
    • 23044510503 scopus 로고    scopus 로고
    • Structural and biochemical mechanisms for the specificity of hormone binding and coactivator assembly by mineralocorticoid receptor
    • Li Y, Suino K, Daugherty J, Xu HE, (2005) Structural and biochemical mechanisms for the specificity of hormone binding and coactivator assembly by mineralocorticoid receptor. Mol Cell 19: 367-380.
    • (2005) Mol Cell , vol.19 , pp. 367-380
    • Li, Y.1    Suino, K.2    Daugherty, J.3    Xu, H.E.4
  • 44
    • 0023643422 scopus 로고
    • Genetic and structural analysis of the protein stability problem
    • Matthews BW, (1987) Genetic and structural analysis of the protein stability problem. Biochemistry 26: 6885-6888.
    • (1987) Biochemistry , vol.26 , pp. 6885-6888
    • Matthews, B.W.1
  • 45
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews BW, (1993) Structural and genetic analysis of protein stability. Annu Rev Biochem 62: 139-160.
    • (1993) Annu Rev Biochem , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 47
    • 33846704424 scopus 로고    scopus 로고
    • Breaking proteins with mutations: threads and thresholds in evolution
    • Bloom JD, Arnold FH, Wilke C, (2007) Breaking proteins with mutations: threads and thresholds in evolution. Mol Syst Biol 3: 1-2.
    • (2007) Mol Syst Biol , vol.3 , pp. 1-2
    • Bloom, J.D.1    Arnold, F.H.2    Wilke, C.3
  • 48
    • 67650287695 scopus 로고    scopus 로고
    • In the Light of Evolution III: Two Centuries of Darwin Sackler Colloquium: In the light of directed evolution: Pathways of adaptive protein evolution
    • Bloom JD, Arnold F, (2009) In the Light of Evolution III: Two Centuries of Darwin Sackler Colloquium: In the light of directed evolution: Pathways of adaptive protein evolution. Proc Natl Acad Sci U S A 106: 9995-10000.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 9995-10000
    • Bloom, J.D.1    Arnold, F.2
  • 50
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • Tokuriki N, Tawfik DS, (2009) Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature 459: 668-673.
    • (2009) Nature , vol.459 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 52
    • 0025850262 scopus 로고
    • Global suppression of protein folding defects and inclusion body formation
    • Mitraki A, Fane B, Haase-Pettingell C, Sturtevant J, King J, (1991) Global suppression of protein folding defects and inclusion body formation. Science 253: 54-58.
    • (1991) Science , vol.253 , pp. 54-58
    • Mitraki, A.1    Fane, B.2    Haase-Pettingell, C.3    Sturtevant, J.4    King, J.5
  • 53
    • 0021968408 scopus 로고
    • Genetic analysis of staphylococcal nuclease: identification of three intragenic "global" suppressors of nuclease-minus mutations
    • Shortle D, Lin B, (1985) Genetic analysis of staphylococcal nuclease: identification of three intragenic "global" suppressors of nuclease-minus mutations. Genetics 110: 539-555.
    • (1985) Genetics , vol.110 , pp. 539-555
    • Shortle, D.1    Lin, B.2
  • 54
    • 44349161622 scopus 로고    scopus 로고
    • Intense neutral drifts yield robust and evolvable consensus proteins
    • Bershtein S, Goldin K, Tawfik DS, (2008) Intense neutral drifts yield robust and evolvable consensus proteins. Journal of Molecular Biology 379: 1029-1044.
    • (2008) Journal of Molecular Biology , vol.379 , pp. 1029-1044
    • Bershtein, S.1    Goldin, K.2    Tawfik, D.S.3
  • 55
    • 40149099484 scopus 로고    scopus 로고
    • How protein stability and new functions trade off
    • doi:10.1371/journal.pcbi.1000002
    • Tokuriki N, Stricher F, Serrano L, Tawfik DS, (2008) How protein stability and new functions trade off. PLoS Comput Biol 4: e1000002 doi:10.1371/journal.pcbi.1000002.
    • (2008) PLoS Comput Biol , vol.4
    • Tokuriki, N.1    Stricher, F.2    Serrano, L.3    Tawfik, D.S.4
  • 56
    • 74549160887 scopus 로고    scopus 로고
    • Retracing evolution of red fluorescence in GFP-like proteins from Faviina corals
    • Field SF, Matz MV, (2010) Retracing evolution of red fluorescence in GFP-like proteins from Faviina corals. Mol Biol Evol 27: 225-233.
    • (2010) Mol Biol Evol , vol.27 , pp. 225-233
    • Field, S.F.1    Matz, M.V.2
  • 58
    • 77953262416 scopus 로고    scopus 로고
    • Permissive secondary mutations enable the evolution of influenza oseltamivir resistance
    • Bloom JD, Gong LI, Baltimore D, (2010) Permissive secondary mutations enable the evolution of influenza oseltamivir resistance. Science 328: 1272-1275.
    • (2010) Science , vol.328 , pp. 1272-1275
    • Bloom, J.D.1    Gong, L.I.2    Baltimore, D.3
  • 59
    • 0027073107 scopus 로고
    • Genetic dissection of the signaling domain of a mammalian steroid receptor in yeast
    • Garabedian MJ, Yamamoto KR, (1992) Genetic dissection of the signaling domain of a mammalian steroid receptor in yeast. Mol Biol Cell 3: 1245-1257.
    • (1992) Mol Biol Cell , vol.3 , pp. 1245-1257
    • Garabedian, M.J.1    Yamamoto, K.R.2
  • 60
    • 34047167881 scopus 로고    scopus 로고
    • A conformational switch in the ligand-binding domain regulates the dependence of the glucocorticoid receptor on Hsp90
    • Ricketson D, Hostick U, Fang L, Yamamoto KR, Darimont BD, (2007) A conformational switch in the ligand-binding domain regulates the dependence of the glucocorticoid receptor on Hsp90. J Mol Biol 368: 729-741.
    • (2007) J Mol Biol , vol.368 , pp. 729-741
    • Ricketson, D.1    Hostick, U.2    Fang, L.3    Yamamoto, K.R.4    Darimont, B.D.5
  • 61
    • 52949135190 scopus 로고    scopus 로고
    • Evolution of a new function by degenerative mutation in cephalochordate steroid receptors
    • doi:10.1371/journal.pgen.1000191
    • Bridgham JT, Brown JE, RodrÌguez-MarÌ A, Catchen JM, Thornton JW, (2008) Evolution of a new function by degenerative mutation in cephalochordate steroid receptors. PLoS Genet 4: e1000191 doi:10.1371/journal.pgen.1000191.
    • (2008) PLoS Genet , vol.4
    • Bridgham, J.T.1    Brown, J.E.2    Rodrìguez-Marì, A.3    Catchen, J.M.4    Thornton, J.W.5
  • 62
    • 33646153793 scopus 로고    scopus 로고
    • How much is enough? Modulation of dose-response curve for steroid receptor-regulated gene expression by changing concentrations of transcription factor
    • Simons SSJ, (2006) How much is enough? Modulation of dose-response curve for steroid receptor-regulated gene expression by changing concentrations of transcription factor. Curr Top Med Chem 6: 271-285.
    • (2006) Curr Top Med Chem , vol.6 , pp. 271-285
    • Simons, S.S.J.1
  • 64
    • 33745256005 scopus 로고    scopus 로고
    • Approximate likelihood-ratio test for branches: A fast, accurate, and powerful alternative
    • Anisimova M, Gascuel O, (2006) Approximate likelihood-ratio test for branches: A fast, accurate, and powerful alternative. Syst Biol 55: 539-552.
    • (2006) Syst Biol , vol.55 , pp. 539-552
    • Anisimova, M.1    Gascuel, O.2
  • 65
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM, (1992) The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 8: 275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 66
    • 0030683599 scopus 로고    scopus 로고
    • PAML: a program package for phylogenetic analysis by maximum likelihood
    • Yang Z, (1997) PAML: a program package for phylogenetic analysis by maximum likelihood. Comput Appl Biosci 13: 555-556.
    • (1997) Comput Appl Biosci , vol.13 , pp. 555-556
    • Yang, Z.1
  • 67
    • 15844406550 scopus 로고    scopus 로고
    • HyPhy: hypothesis testing using phylogenies
    • Pond SL, Frost SD, Muse SV, (2005) HyPhy: hypothesis testing using phylogenies. Bioinformatics 21: 676-679.
    • (2005) Bioinformatics , vol.21 , pp. 676-679
    • Pond, S.L.1    Frost, S.D.2    Muse, S.V.3
  • 68
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods in enzymology 276: 307-326.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 69
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 72


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