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Volumn 6, Issue 10, 2010, Pages

Evolution of a signaling nexus constrained by protein interfaces and conformational states

Author keywords

[No Author keywords available]

Indexed keywords

INTERFACE STATES; MAMMALS;

EID: 78349234247     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000962     Document Type: Article
Times cited : (21)

References (65)
  • 1
    • 0033572358 scopus 로고    scopus 로고
    • The G protein subunit gene families
    • Downes GB, Gautam N (1999) The G protein subunit gene families. Genomics 62: 544-552.
    • (1999) Genomics , vol.62 , pp. 544-552
    • Downes, G.B.1    Gautam, N.2
  • 2
    • 15644379354 scopus 로고    scopus 로고
    • Promiscuous coupling of receptors to Gq class a subunits and effector proteins in pancreatic and submandibular gland cells
    • Xu X, Croy JT, Zeng W, Zhao L, Davignon I, et al. (1998) Promiscuous coupling of receptors to Gq class a subunits and effector proteins in pancreatic and submandibular gland cells. J Biol Chem 273: 27275-27279.
    • (1998) J Biol Chem , vol.273 , pp. 27275-27279
    • Xu, X.1    Croy, J.T.2    Zeng, W.3    Zhao, L.4    Davignon, I.5
  • 3
    • 33749546642 scopus 로고    scopus 로고
    • Signal transfer from GPCRs to G proteins: Role of the Ga N-terminal region in rhodopsin-transducin coupling
    • Herrmann R, Heck M, Henklein P, Hofmann KP, Ernst OP (2006) Signal transfer from GPCRs to G proteins: role of the Ga N-terminal region in rhodopsin-transducin coupling. J Biol Chem 281: 30234-30241.
    • (2006) J Biol Chem , vol.281 , pp. 30234-30241
    • Herrmann, R.1    Heck, M.2    Henklein, P.3    Hofmann, K.P.4    Ernst, O.P.5
  • 4
    • 33750615086 scopus 로고    scopus 로고
    • Rhodopsintransducin coupling: Role of the Ga C-terminus in nucleotide exchange catalysis
    • Herrmann R, Heck M, Henklein P, Kleuss C, Wray V, et al. (2006) Rhodopsintransducin coupling: role of the Ga C-terminus in nucleotide exchange catalysis. Vision Res 47: 4582-4593.
    • (2006) Vision Res , vol.47 , pp. 4582-4593
    • Herrmann, R.1    Heck, M.2    Henklein, P.3    Kleuss, C.4    Wray, V.5
  • 5
    • 56549119570 scopus 로고    scopus 로고
    • Turning a hobby into a job: How duplicated genes find new functions
    • Conant GC, Wolfe KH (2008) Turning a hobby into a job: how duplicated genes find new functions. Nat Rev Genet 9: 938-950.
    • (2008) Nat Rev Genet , vol.9 , pp. 938-950
    • Conant, G.C.1    Wolfe, K.H.2
  • 6
    • 2942681717 scopus 로고    scopus 로고
    • Plants: The latest model system for G-protein research
    • Jones AM, Assmann SM (2004) Plants: the latest model system for G-protein research. EMBO Rep 5: 572-578.
    • (2004) EMBO Rep , vol.5 , pp. 572-578
    • Jones, A.M.1    Assmann, S.M.2
  • 7
    • 69749120682 scopus 로고    scopus 로고
    • Prediction of protein-protein interfaces on G-protein b subunits reveals a novel phospholipase C b2 binding domain
    • Friedman EJ, Temple BRS, Hicks SN, Sondek J, Jones CD, et al. (2009) Prediction of protein-protein interfaces on G-protein b subunits reveals a novel phospholipase C b2 binding domain. J Mol Biol 392: 1044-1054.
    • (2009) J Mol Biol , vol.392 , pp. 1044-1054
    • Friedman, E.J.1    Temple, B.R.S.2    Hicks, S.N.3    Sondek, J.4    Jones, C.D.5
  • 9
    • 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
  • 10
    • 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
  • 11
    • 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
  • 12
    • 0001388569 scopus 로고
    • On a statistical estimate for the entropy of a sequence of independent random variables
    • Basharin G (1959) On a statistical estimate for the entropy of a sequence of independent random variables. Theory Prob Appl 4: 333-336.
    • (1959) Theory Prob Appl , vol.4 , pp. 333-336
    • Basharin, G.1
  • 13
    • 27944458910 scopus 로고    scopus 로고
    • Using information theory to search for co-evolving residues in proteins
    • Martin LC, Gloor GB, Dunn SD, Wahl LM (2005) Using information theory to search for co-evolving residues in proteins. Bioinformatics 21: 4116-4124.
    • (2005) Bioinformatics , vol.21 , pp. 4116-4124
    • Martin, L.C.1    Gloor, G.B.2    Dunn, S.D.3    Wahl, L.M.4
  • 14
    • 0029664921 scopus 로고    scopus 로고
    • Evolutionarily conserved Gabc binding surfaces support a model of the G protein-receptor complex
    • Lichtarge O, Bourne HR, Cohen FE (1996) Evolutionarily conserved Gabc binding surfaces support a model of the G protein-receptor complex. Proc Natl Acad Sci U S A 93: 7507-7511.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7507-7511
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 15
    • 33847238811 scopus 로고    scopus 로고
    • Functional divergence after gene duplication and sequence-structure relationship: A case study of G-protein alpha subunits
    • Zheng Y, Xu D, Gu X (2007) Functional divergence after gene duplication and sequence-structure relationship: a case study of G-protein alpha subunits. Mol Dev Evol 308B: 85-96.
    • (2007) Mol Dev Evol , vol.308 B , pp. 85-96
    • Zheng, Y.1    Xu, D.2    Gu, X.3
  • 16
    • 0029664589 scopus 로고    scopus 로고
    • The 2.0 Å crystal structure of a heterotrimeric G Protein
    • Lambright DG, Sondek J, Bohm A, Skiba NP, Hamm HE, et al. (1996) The 2.0 Å crystal structure of a heterotrimeric G Protein. Nature 379: 311-319.
    • (1996) Nature , vol.379 , pp. 311-319
    • Lambright, D.G.1    Sondek, J.2    Bohm, A.3    Skiba, N.P.4    Hamm, H.E.5
  • 18
    • 0035931919 scopus 로고    scopus 로고
    • Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å
    • Slep KC, Kercher MA, He W, Cowan CW, Wensel TG, et al. (2001) Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å. Nature 409: 1071-1077.
    • (2001) Nature , vol.409 , pp. 1071-1077
    • Slep, K.C.1    Kercher, M.A.2    He, W.3    Cowan, C.W.4    Wensel, T.G.5
  • 19
    • 0030982264 scopus 로고    scopus 로고
    • Structure of RGS4 bound to AlF4 2-activated Gia1: Stabilization of the transition state for GTP hydrolysis
    • Tesmer JJ, Berman DM, Gilman AG, Sprang SR (1997) Structure of RGS4 bound to AlF4 2-activated Gia1: stabilization of the transition state for GTP hydrolysis. Cell 89: 251-261.
    • (1997) Cell , vol.89 , pp. 251-261
    • Tesmer, J.J.1    Berman, D.M.2    Gilman, A.G.3    Sprang, S.R.4
  • 20
    • 15544373780 scopus 로고    scopus 로고
    • Structure of the p115RhoGEF rgRGS domain-Ga13/i1 chimera complex suggests convergent evolution of a GTPase activator
    • Chen Z, Singer WD, Sternweis PC, Sprang SR (2005) Structure of the p115RhoGEF rgRGS domain-Ga13/i1 chimera complex suggests convergent evolution of a GTPase activator. Nat Struct Mol Biol 12: 191-197.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 191-197
    • Chen, Z.1    Singer, W.D.2    Sternweis, P.C.3    Sprang, S.R.4
  • 22
    • 0031051444 scopus 로고    scopus 로고
    • Signalling functions and biochemical properties of pertussis toxin-resistant G-proteins
    • Fields TA, Casey PJ (1997) Signalling functions and biochemical properties of pertussis toxin-resistant G-proteins. Biochem J 321: 561-571.
    • (1997) Biochem J , vol.321 , pp. 561-571
    • Fields, T.A.1    Casey, P.J.2
  • 24
    • 0028085776 scopus 로고
    • Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates Gbc-mediated signaling
    • Koch WJ, Hawes BE, Inglese J, Luttrell LM, Lefkowitz RJ (1994) Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates Gbc-mediated signaling. J Biol Chem 269: 6193.
    • (1994) J Biol Chem , vol.269 , pp. 6193
    • Koch, W.J.1    Hawes, B.E.2    Inglese, J.3    Luttrell, L.M.4    Lefkowitz, R.J.5
  • 26
  • 27
    • 15744364175 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor p63RhoGEF, a specific link between Gq/11-coupled receptor signaling and RhoA
    • Lutz S, Freichel-Blomquist A, Yang Y, Rumenapp U, Jakobs KH, et al. (2005) The guanine nucleotide exchange factor p63RhoGEF, a specific link between Gq/11-coupled receptor signaling and RhoA. J Biol Chem 280: 11134-11139.
    • (2005) J Biol Chem , vol.280 , pp. 11134-11139
    • Lutz, S.1    Freichel-Blomquist, A.2    Yang, Y.3    Rumenapp, U.4    Jakobs, K.H.5
  • 28
    • 35748983198 scopus 로고    scopus 로고
    • Gaq directly activates p63RhoGEF and trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain
    • Rojas RJ, Yohe ME, Gershburg S, Kawano T, Kozasa T, et al. (2007) Gaq directly activates p63RhoGEF and trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain. J Biol Chem 282: 29201-29210.
    • (2007) J Biol Chem , vol.282 , pp. 29201-29210
    • Rojas, R.J.1    Yohe, M.E.2    Gershburg, S.3    Kawano, T.4    Kozasa, T.5
  • 29
    • 18244363129 scopus 로고    scopus 로고
    • Human p63RhoGEF, a novel RhoA-specific guanine nucleotide exchange factor, is localized in cardiac sarcomere
    • Souchet M, Portales-Casamar E, Mazurais D, Schmidt S, Leger I, et al. (2002) Human p63RhoGEF, a novel RhoA-specific guanine nucleotide exchange factor, is localized in cardiac sarcomere. J Cell Sci 115: 629-640.
    • (2002) J Cell Sci , vol.115 , pp. 629-640
    • Souchet, M.1    Portales-Casamar, E.2    Mazurais, D.3    Schmidt, S.4    Leger, I.5
  • 30
    • 35948968634 scopus 로고    scopus 로고
    • Structure of Gaq-p63RhoGEF-RhoA complex reveals a pathway for the activation of RhoA by GPCRs
    • Lutz S, Shankaranarayanan A, Coco C, Ridilla M, Nance MR, et al. (2007) Structure of Gaq-p63RhoGEF-RhoA complex reveals a pathway for the activation of RhoA by GPCRs. Science 318: 1923-1927.
    • (2007) Science , vol.318 , pp. 1923-1927
    • Lutz, S.1    Shankaranarayanan, A.2    Coco, C.3    Ridilla, M.4    Nance, M.R.5
  • 31
    • 0032568868 scopus 로고    scopus 로고
    • Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Ga13
    • Hart M, Jiang J, X., Kozasa T, Roscoe W, Singer WD, et al. (1998) Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Ga13. Science 280: 2112-2114.
    • (1998) Science , vol.280 , pp. 2112-2114
    • Hart, M.1    Jiang, J.X.2    Kozasa, T.3    Roscoe, W.4    Singer, W.D.5
  • 32
  • 33
    • 0032573086 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factor GEF115 specifically mediates activation of Rho and serum response factor by the G protein a subunit Ga13
    • Mao J, Yuan H, Xie W, Wu D (1998) Guanine nucleotide exchange factor GEF115 specifically mediates activation of Rho and serum response factor by the G protein a subunit Ga13. Proc Natl Acad Sci U S A 95: 12973-12976.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12973-12976
    • Mao, J.1    Yuan, H.2    Xie, W.3    Wu, D.4
  • 34
    • 16444368009 scopus 로고    scopus 로고
    • Functional consequences of Ga13 mutations that disrupt interaction with p115RhoGEF
    • Grabocka E, Wedegaertner PB (2005) Functional consequences of Ga13 mutations that disrupt interaction with p115RhoGEF. Oncogene 24: 2155-2165.
    • (2005) Oncogene , vol.24 , pp. 2155-2165
    • Grabocka, E.1    Wedegaertner, P.B.2
  • 35
    • 4844222939 scopus 로고    scopus 로고
    • Critical role of lysine 204 in switch I region of Ga13 for regulation of p115RhoGEF and leukemia-associated RhoGEF
    • Nakamura S, Kreutz B, Tanabe S, Suzuki N, Kozasa T (2004) Critical role of lysine 204 in switch I region of Ga13 for regulation of p115RhoGEF and leukemia-associated RhoGEF. Mol Pharmacol 66: 1029-1034.
    • (2004) Mol Pharmacol , vol.66 , pp. 1029-1034
    • Nakamura, S.1    Kreutz, B.2    Tanabe, S.3    Suzuki, N.4    Kozasa, T.5
  • 36
    • 30144445198 scopus 로고    scopus 로고
    • A new approach to producing functional Ga subunits yields the activated and deactivated structures of Ga12/13 proteins
    • Kreutz B, Yau DM, Nance MR, Tanabe S, Tesmer JJ, et al. (2006) A new approach to producing functional Ga subunits yields the activated and deactivated structures of Ga12/13 proteins. Biochemistry 45: 167-174.
    • (2006) Biochemistry , vol.45 , pp. 167-174
    • Kreutz, B.1    Yau, D.M.2    Nance, M.R.3    Tanabe, S.4    Tesmer, J.J.5
  • 37
    • 0027965652 scopus 로고
    • Structures of active conformations of Gia1 and the mechanism of GTP hydrolysis
    • Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, et al. (1994) Structures of active conformations of Gia1 and the mechanism of GTP hydrolysis. Science 265: 1405-1412.
    • (1994) Science , vol.265 , pp. 1405-1412
    • Coleman, D.E.1    Berghuis, A.M.2    Lee, E.3    Linder, M.E.4    Gilman, A.G.5
  • 38
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducina complexed with GTPcS
    • Noel JP, Hamm HE, Sigler PB (1993) The 2.2 Å crystal structure of transducina complexed with GTPcS. Nature 366: 654-663.
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 39
  • 40
    • 2642689663 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domains of adenylyl cyclase in a complex with GsaNGTPcS
    • Tesmer JJG, Sunahara RK, Gilman AG, Sprang SR (1997) Crystal structure of the catalytic domains of adenylyl cyclase in a complex with GsaNGTPcS. Science 278: 1907-1916.
    • (1997) Science , vol.278 , pp. 1907-1916
    • Tesmer, J.J.G.1    Sunahara, R.K.2    Gilman, A.G.3    Sprang, S.R.4
  • 41
    • 0026552077 scopus 로고
    • Identification of effector-activating residues of Gsa
    • Berlot CH, Bourne HR (1992) Identification of effector-activating residues of Gsa. Cell 68: 911-922.
    • (1992) Cell , vol.68 , pp. 911-922
    • Berlot, C.H.1    Bourne, H.R.2
  • 42
    • 0037171778 scopus 로고    scopus 로고
    • Structural determinants for GoLoco-induced inhibition of nucleotide release by Ga subunits
    • Kimple RJ, Kimple ME, Betts L, Sondek J, Siderovski DP (2002) Structural determinants for GoLoco-induced inhibition of nucleotide release by Ga subunits. Nature 416: 878-881.
    • (2002) Nature , vol.416 , pp. 878-881
    • Kimple, R.J.1    Kimple, M.E.2    Betts, L.3    Sondek, J.4    Siderovski, D.P.5
  • 43
    • 0023716027 scopus 로고    scopus 로고
    • Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit
    • Hamm HE, Deretic D, Arendt A, Hargrave PA, Koenig B, et al. (1998) Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit. Science 241: 832-835.
    • (1998) Science , vol.241 , pp. 832-835
    • Hamm, H.E.1    Deretic, D.2    Arendt, A.3    Hargrave, P.A.4    Koenig, B.5
  • 44
    • 52949153619 scopus 로고    scopus 로고
    • Receptormediated changes at the myristoylated amino terminus of Gai1 proteins
    • Preininger AM, Parello J, Meier SM, Liao G, Hamm HE (2008) Receptormediated changes at the myristoylated amino terminus of Gai1 proteins. Biochemistry 47: 10281-10293.
    • (2008) Biochemistry , vol.47 , pp. 10281-10293
    • Preininger, A.M.1    Parello, J.2    Meier, S.M.3    Liao, G.4    Hamm, H.E.5
  • 45
    • 0035793567 scopus 로고    scopus 로고
    • A novel site on the Ga-protein that recognizes heptahelical receptors
    • Blahos J, Fischer T, Brabet I, Stauffer D, Rovelli G, et al. (2001) A novel site on the Ga-protein that recognizes heptahelical receptors. J Biol Chem 276: 3262-3269.
    • (2001) J Biol Chem , vol.276 , pp. 3262-3269
    • Blahos, J.1    Fischer, T.2    Brabet, I.3    Stauffer, D.4    Rovelli, G.5
  • 46
    • 0035942229 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: Use of a chemically preactivated reagent
    • Itoh Y, Cai K, Khorana HG (2001) Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: Use of a chemically preactivated reagent. Proc Natl Acad Sci U S A 98: 4883-4887.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4883-4887
    • Itoh, Y.1    Cai, K.2    Khorana, H.G.3
  • 47
    • 0348010316 scopus 로고    scopus 로고
    • Closely related G-protein-coupled receptors use multiple and distinct domains on G-protein asubunits for selective coupling
    • Slessareva JE, Ma H, Depree KM, Flood LA, Bae H, et al. (2003) Closely related G-protein-coupled receptors use multiple and distinct domains on G-protein asubunits for selective coupling. J Biol Chem 278: 50530-50536.
    • (2003) J Biol Chem , vol.278 , pp. 50530-50536
    • Slessareva, J.E.1    Ma, H.2    Depree, K.M.3    Flood, L.A.4    Bae, H.5
  • 48
    • 0035942238 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: Use of a photoactivatable reagent
    • Cai K, Itoh Y, Khorana HG (2001) Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: Use of a photoactivatable reagent. Proc Natl Acad Sci U S A 98: 4877-4882.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4877-4882
    • Cai, K.1    Itoh, Y.2    Khorana, H.G.3
  • 49
    • 0029113832 scopus 로고
    • Transducin-a C-terminal mutations prevent activation by rhodopsin: A new assay using recombinant proteins expressed in cultured cells
    • Garcia PD, Onrust R, Bell SM, Sakmar TP, Bourne HR (1995) Transducin-a C-terminal mutations prevent activation by rhodopsin: a new assay using recombinant proteins expressed in cultured cells. EMBO J 14: 4460-4469.
    • (1995) EMBO J , vol.14 , pp. 4460-4469
    • Garcia, P.D.1    Onrust, R.2    Bell, S.M.3    Sakmar, T.P.4    Bourne, H.R.5
  • 50
    • 0033583051 scopus 로고    scopus 로고
    • Roles of the transducin a-subunit a4-helix/a4-b6 loop in the receptor and effector interactions
    • Natochin M, Granovsky AE, Muradov KG, Artemyev NO (1999) Roles of the transducin a-subunit a4-helix/a4-b6 loop in the receptor and effector interactions. J Biol Chem 274: 7865-7869.
    • (1999) J Biol Chem , vol.274 , pp. 7865-7869
    • Natochin, M.1    Granovsky, A.E.2    Muradov, K.G.3    Artemyev, N.O.4
  • 51
    • 0030614427 scopus 로고    scopus 로고
    • Receptor and bc binding sites in the a subunit of the retinal G protein transducin
    • Onrust R, Herzmark P, Chi P, Garcia PD, Lichtarge O, et al. (1997) Receptor and bc binding sites in the a subunit of the retinal G protein transducin. Science 275: 381-384.
    • (1997) Science , vol.275 , pp. 381-384
    • Onrust, R.1    Herzmark, P.2    Chi, P.3    Garcia, P.D.4    Lichtarge, O.5
  • 52
    • 0029569117 scopus 로고
    • The effect of carboxyl-terminal mutagenesis of Gta on rhodopsin and guanine nucleotide binding
    • Osawa S, Weiss ER (1995) The effect of carboxyl-terminal mutagenesis of Gta on rhodopsin and guanine nucleotide binding. J Biol Chem 270: 31052-31058.
    • (1995) J Biol Chem , vol.270 , pp. 31052-31058
    • Osawa, S.1    Weiss, E.R.2
  • 53
    • 70349810683 scopus 로고    scopus 로고
    • Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins
    • Kapoor N, Menon ST, Chauhan R, Sachdev P, Sakmar TP (2009) Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins. J Mol Biol 393: 882-897.
    • (2009) J Mol Biol , vol.393 , pp. 882-897
    • Kapoor, N.1    Menon, S.T.2    Chauhan, R.3    Sachdev, P.4    Sakmar, T.P.5
  • 55
    • 0033035138 scopus 로고    scopus 로고
    • Extensive gene duplication in the early evolution of animals before the parazoaneumetazoan split demonstrated by G proteins and protein tyrosine kinases from sponges and Hydra
    • Suga H, Koyanagi M, Hoshiyama D, Ono K, Iwabe N, et al. (1999) Extensive gene duplication in the early evolution of animals before the parazoaneumetazoan split demonstrated by G proteins and protein tyrosine kinases from sponges and Hydra. J Mol Evol 48: 646-653.
    • (1999) J Mol Evol , vol.48 , pp. 646-653
    • Suga, H.1    Koyanagi, M.2    Hoshiyama, D.3    Ono, K.4    Iwabe, N.5
  • 56
    • 0032472385 scopus 로고    scopus 로고
    • Evolutionary analysis of G-proteins in early metazoans: Cloning of a-and b- subunits from the sponge, Geodia cydonium
    • Seack J, Kruse M, Muller WE (1998) Evolutionary analysis of G-proteins in early metazoans: cloning of a-and b- subunits from the sponge, Geodia cydonium. Biochem Biophys Acta 14: 93-103.
    • (1998) Biochem Biophys Acta , vol.14 , pp. 93-103
    • Seack, J.1    Kruse, M.2    Muller, W.E.3
  • 57
    • 56549119570 scopus 로고    scopus 로고
    • Turning a hobby into a job: How duplicated genes find new functions
    • Conant GC, Wolfe KH (2008) Turning a hobby into a job: How duplicated genes find new functions. Nat Rev Genet 9: 938-950.
    • (2008) Nat Rev Genet , vol.9 , pp. 938-950
    • Conant, G.C.1    Wolfe, K.H.2
  • 59
    • 0043122944 scopus 로고    scopus 로고
    • ExPASy: The proteomics server for in-depth protein knowledge and analysis
    • Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD, et al. (2003) ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucl Acids Res 31: 3784-3788.
    • (2003) Nucl Acids Res , vol.31 , pp. 3784-3788
    • Gasteiger, E.1    Gattiker, A.2    Hoogland, C.3    Ivanyi, I.4    Appel, R.D.5
  • 62
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nuc Acids Res 24: 4876-4882.
    • (1997) Nuc Acids Res , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 63
    • 0034623005 scopus 로고    scopus 로고
    • T-coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J (2000) T-coffee: a novel method for fast and accurate multiple sequence alignment. J Mol Biol 302: 205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 64
    • 0037447059 scopus 로고    scopus 로고
    • Amino acids determining enzymesubstrate specificity in prokaryotic and eukaryotic protein kinases
    • Li L, Shakhnovich EI, Mirny LA (2003) Amino acids determining enzymesubstrate specificity in prokaryotic and eukaryotic protein kinases. Proc Natl Acad Sci U S A 100: 4463-4468.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4463-4468
    • Li, L.1    Shakhnovich, E.I.2    Mirny, L.A.3
  • 65
    • 0034459679 scopus 로고    scopus 로고
    • Evolutionary trace analysis of TGF-b and related growth factors: Implications for site-directed mutagenesis
    • Innis CA, Shi J, Blundell TL (2000) Evolutionary trace analysis of TGF-b and related growth factors: implications for site-directed mutagenesis. Protein Eng 13: 839-847.
    • (2000) Protein Eng , vol.13 , pp. 839-847
    • Innis, C.A.1    Shi, J.2    Blundell, T.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.