메뉴 건너뛰기




Volumn 2013, Issue 2, 2013, Pages

Structure and function of the Smoothened extracellular domain in vertebrate Hedgehog signaling

Author keywords

[No Author keywords available]

Indexed keywords

FRIZZLED PROTEIN; G PROTEIN COUPLED RECEPTOR; LIGAND; PROTEIN BINDING; RECOMBINANT PROTEIN; SMOH PROTEIN, ZEBRAFISH; SMOOTHENED PROTEIN; SONIC HEDGEHOG PROTEIN; STEROL; ZEBRAFISH PROTEIN;

EID: 84887326705     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.01340.001     Document Type: Article
Times cited : (121)

References (93)
  • 1
    • 67449094358 scopus 로고    scopus 로고
    • The extracellular domain of Smoothened regulates ciliary localization and is required for high-level Hh signaling
    • doi: 10.1016/j.cub.2009.04.053
    • Aanstad P, Santos N, Corbit KC, Scherz PJ, Trinh le A, Salvenmoser W, et al. 2009. The extracellular domain of Smoothened regulates ciliary localization and is required for high-level Hh signaling. Curr Biol 19:1034-9. doi: 10.1016/j.cub.2009.04.053.
    • (2009) Curr Biol , vol.19 , pp. 1034-1039
    • Aanstad, P.1    Santos, N.2    Corbit, K.C.3    Scherz, P.J.4    Trinhle, A.5    Salvenmoser, W.6
  • 3
    • 33745912405 scopus 로고    scopus 로고
    • A time-and cost-efficient system for high-level protein production in mammalian cells
    • doi: 10.1107/S0907444906029799
    • Aricescu AR, Lu W, Jones EY. 2006. A time-and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr D Biol Crystallogr 62:1243-50. doi: 10.1107/S0907444906029799.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 4
    • 0036406843 scopus 로고    scopus 로고
    • Hedgehog signaling and human disease
    • doi: 10.1146/annurev.genom.3.022502.103031
    • Bale AE. 2002. Hedgehog signaling and human disease. Annu Rev Genomics Human Genet 3:47-65. doi: 10.1146/annurev.genom.3.022502.103031.
    • (2002) Annu Rev Genomics Human Genet , vol.3 , pp. 47-65
    • Bale, A.E.1
  • 5
    • 0000357241 scopus 로고
    • Synthese du diethylheptenol
    • Barbier P. 1899. Synthese du diethylheptenol. C R Hebd Seances Acad Sc 128:110.
    • (1899) C R Hebd Seances Acad Sc , vol.128 , pp. 110
    • Barbier, P.1
  • 6
    • 70149100995 scopus 로고    scopus 로고
    • Structural ties between cholesterol transport and morphogen signaling
    • doi: 10.1016/j.cell.2009.09.006
    • Bazan JF, de Sauvage FJ. 2009. Structural ties between cholesterol transport and morphogen signaling. Cell 138:1055-6. doi: 10.1016/j.cell.2009.09.006.
    • (2009) Cell , vol.138 , pp. 1055-1056
    • Bazan, J.F.1    de Sauvage, F.J.2
  • 7
    • 84865073858 scopus 로고    scopus 로고
    • Structural architecture and functional evolution of Wnts
    • doi: 10.1016/j.devcel.2012.07.011
    • Bazan JF, Janda CY, Garcia KC. 2012. Structural architecture and functional evolution of Wnts. Dev Cell 23:227-32. doi: 10.1016/j.devcel.2012.07.011.
    • (2012) Dev Cell , vol.23 , pp. 227-232
    • Bazan, J.F.1    Janda, C.Y.2    Garcia, K.C.3
  • 9
    • 84879414522 scopus 로고    scopus 로고
    • The mechanisms of Hedgehog signalling and its roles in development and disease
    • doi: 10.1038/nrm3598
    • Briscoe J, Therond PP. 2013. The mechanisms of Hedgehog signalling and its roles in development and disease. Nat Rev Mol Cell Biol 14:418-31. doi: 10.1038/nrm3598.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 418-431
    • Briscoe, J.1    Therond, P.P.2
  • 10
    • 0036499988 scopus 로고    scopus 로고
    • Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur
    • doi: 10.1093/emboj/21.5.1054
    • Brown J, Esnouf RM, Jones MA, Linnell J, Harlos K, Hassan AB, et al. 2002. Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur. EMBO J 21:1054-62. doi: 10.1093/emboj/21.5.1054.
    • (2002) EMBO J , vol.21 , pp. 1054-1062
    • Brown, J.1    Esnouf, R.M.2    Jones, M.A.3    Linnell, J.4    Harlos, K.5    Hassan, A.B.6
  • 11
    • 84882818980 scopus 로고    scopus 로고
    • Structural basis for molecular recognition of folic acid by folate receptors
    • doi: 10.1038/nature12327
    • Chen C, Ke J, Zhou XE, Yi W, Brunzelle JS, Li J, et al. 2013. Structural basis for molecular recognition of folic acid by folate receptors. Nature 500:486-9. doi: 10.1038/nature12327.
    • (2013) Nature , vol.500 , pp. 486-489
    • Chen, C.1    Ke, J.2    Zhou, X.E.3    Yi, W.4    Brunzelle, J.S.5    Li, J.6
  • 12
    • 0036829397 scopus 로고    scopus 로고
    • Inhibition of Hedgehog signaling by direct binding of cyclopamine to Smoothened
    • doi: 10.1101/gad.1025302
    • Chen JK, Taipale J, Cooper MK, Beachy PA. 2002a. Inhibition of Hedgehog signaling by direct binding of cyclopamine to Smoothened. Genes Dev 16:2743-8. doi: 10.1101/gad.1025302.
    • (2002) Genes Dev , vol.16 , pp. 2743-2748
    • Chen, J.K.1    Taipale, J.2    Cooper, M.K.3    Beachy, P.A.4
  • 14
    • 0015590528 scopus 로고
    • Synthesis of 3 beta-Acetoxy-24-Norchola-5,20(22)-Dien-23-al-new Intermediate for an Improved synthesis of [24-C-14]-Cholesterol
    • doi: 10.1016/0022-4731(73)90023-X
    • Colonna AO, Gros EG. 1973. Synthesis of 3 beta-Acetoxy-24-Norchola-5,20(22)-Dien-23-al-new Intermediate for an Improved synthesis of [24-C-14]-Cholesterol. J Steroid Biochem 4:171-9. doi: 10.1016/0022-4731(73)90023-X.
    • (1973) J Steroid Biochem , vol.4 , pp. 171-179
    • Colonna, A.O.1    Gros, E.G.2
  • 15
    • 0029791854 scopus 로고    scopus 로고
    • Spatial regulation of a zebrafish patched homologue reflects the roles of sonic hedgehog and protein kinase A in neural tube and somite patterning
    • Concordet JP, Lewis KE, Moore JW, Goodrich LV, Johnson RL, Scott MP, et al. 1996. Spatial regulation of a zebrafish patched homologue reflects the roles of sonic hedgehog and protein kinase A in neural tube and somite patterning. Development 122:2835-46.
    • (1996) Development , vol.122 , pp. 2835-2846
    • Concordet, J.P.1    Lewis, K.E.2    Moore, J.W.3    Goodrich, L.V.4    Johnson, R.L.5    Scott, M.P.6
  • 17
    • 33744788672 scopus 로고    scopus 로고
    • Oxysterols stimulate Sonic hedgehog signal transduction and proliferation of medulloblastoma cells
    • doi: 10.1073/pnas.0602852103
    • Corcoran RB, Scott MP. 2006. Oxysterols stimulate Sonic hedgehog signal transduction and proliferation of medulloblastoma cells. Proc Natl Acad Sci USA 103:8408-13. doi: 10.1073/pnas.0602852103.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8408-8413
    • Corcoran, R.B.1    Scott, M.P.2
  • 18
    • 0035811492 scopus 로고    scopus 로고
    • Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains
    • doi: 10.1038/35083601
    • Dann CE, Hsieh JC, Rattner A, Sharma D, Nathans J, Leahy DJ. 2001. Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains. Nature 412:86-90. doi: 10.1038/35083601.
    • (2001) Nature , vol.412 , pp. 86-90
    • Dann, C.E.1    Hsieh, J.C.2    Rattner, A.3    Sharma, D.4    Nathans, J.5    Leahy, D.J.6
  • 19
    • 0034704244 scopus 로고    scopus 로고
    • Transmembrane molecular pump activity of Niemann-Pick C1 protein
    • doi: 10.1126/science.290.5500.2295
    • Davies JP, Chen FW, Ioannou YA. 2000. Transmembrane molecular pump activity of Niemann-Pick C1 protein. Science 290:2295-8. doi: 10.1126/science.290.5500.2295.
    • (2000) Science , vol.290 , pp. 2295-2298
    • Davies, J.P.1    Chen, F.W.2    Ioannou, Y.A.3
  • 20
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • doi: 10.1093/nar/gkm216
    • Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, et al. 2007. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35:W375-83. doi: 10.1093/nar/gkm216.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5    Wang, X.6
  • 21
    • 13444263350 scopus 로고    scopus 로고
    • Solution structure of the E. coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain
    • doi: 10.1016/j.jmb.2004.12.028
    • Deprez C, Lloubes R, Gavioli M, Marion D, Guerlesquin F, Blanchard L. 2005. Solution structure of the E. coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain. J Mol Biol 346:1047-57. doi: 10.1016/j.jmb.2004.12.028.
    • (2005) J Mol Biol , vol.346 , pp. 1047-1057
    • Deprez, C.1    Lloubes, R.2    Gavioli, M.3    Marion, D.4    Guerlesquin, F.5    Blanchard, L.6
  • 22
    • 33746373174 scopus 로고    scopus 로고
    • Asymmetric synthesis of enantioenriched (+)-elaeokanine A
    • doi: 10.1021/jo060717q
    • Dieter RK, Chen NY. 2006. Asymmetric synthesis of enantioenriched (+)-elaeokanine A. J Org Chem 71:5674-8. doi: 10.1021/jo060717q.
    • (2006) J Org Chem , vol.71 , pp. 5674-5678
    • Dieter, R.K.1    Chen, N.Y.2
  • 23
    • 78751520029 scopus 로고    scopus 로고
    • Small molecule inhibition of GDC-0449 refractory smoothened mutants and downstream mechanisms of drug resistance
    • doi: 10.1158/0008-5472.CAN-10-2876
    • Dijkgraaf GJ, Alicke B, Weinmann L, Januario T, West K, Modrusan Z, et al. 2011. Small molecule inhibition of GDC-0449 refractory smoothened mutants and downstream mechanisms of drug resistance. Cancer Res 71:435-44. doi: 10.1158/0008-5472.CAN-10-2876.
    • (2011) Cancer Res , vol.71 , pp. 435-444
    • Dijkgraaf, G.J.1    Alicke, B.2    Weinmann, L.3    Januario, T.4    West, K.5    Modrusan, Z.6
  • 24
    • 34247844371 scopus 로고    scopus 로고
    • Oxysterols are novel activators of the hedgehog signaling pathway in pluripotent mesenchymal cells
    • doi: 10.1074/jbc.M611741200
    • Dwyer JR, Sever N, Carlson M, Nelson SF, Beachy PA, Parhami F. 2007. Oxysterols are novel activators of the hedgehog signaling pathway in pluripotent mesenchymal cells. J Biol Chem 282:8959-68. doi: 10.1074/jbc.M611741200.
    • (2007) J Biol Chem , vol.282 , pp. 8959-8968
    • Dwyer, J.R.1    Sever, N.2    Carlson, M.3    Nelson, S.F.4    Beachy, P.A.5    Parhami, F.6
  • 25
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • doi: 10.1107/S0907444904019158
    • Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60:2126-32. doi: 10.1107/S0907444904019158.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 26
    • 49649114605 scopus 로고    scopus 로고
    • Protein structure modeling with MODELLER
    • doi: 10.1007/978-1-60327-058-8_8
    • Eswar N, Eramian D, Webb B, Shen M, Sali A. 2008. Protein structure modeling with MODELLER. Methods Mol Biol 426:145-9. doi: 10.1007/978-1-60327-058-8_8.
    • (2008) Methods Mol Biol , vol.426 , pp. 145-149
    • Eswar, N.1    Eramian, D.2    Webb, B.3    Shen, M.4    Sali, A.5
  • 27
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • doi: 10.1107/S0907444905036693
    • Evans P. 2006. Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62:72-82. doi: 10.1107/S0907444905036693.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 28
    • 0000122573 scopus 로고
    • PHYLIP-Phylogeny Inference Package (Version 3.2)
    • Felsenstein J. 1989. PHYLIP-Phylogeny Inference Package (Version 3.2). Cladistics 5:164-6.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 29
    • 18644368453 scopus 로고    scopus 로고
    • Small-molecule modulators of Hedgehog signaling: Identification and characterization of Smoothened agonists and antagonists
    • doi: 10.1186/1475-4924-1-10
    • Frank-Kamenetsky M, Zhang XM, Bottega S, Guicherit O, Wichterle H, Dudek H, et al. 2002. Small-molecule modulators of Hedgehog signaling: identification and characterization of Smoothened agonists and antagonists. J Biol 1:10. doi: 10.1186/1475-4924-1-10.
    • (2002) J Biol , vol.1 , pp. 10
    • Frank-Kamenetsky, M.1    Zhang, X.M.2    Bottega, S.3    Guicherit, O.4    Wichterle, H.5    Dudek, H.6
  • 30
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • doi: 10.1124/mol.63.6.1256
    • Fredriksson R, Lagerstrom MC, Lundin LG, Schioth HB. 2003. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol Pharmacol 63:1256-72. doi: 10.1124/mol.63.6.1256.
    • (2003) Mol Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 31
    • 84863543371 scopus 로고    scopus 로고
    • Structural basis of Wnt recognition by Frizzled
    • doi: 10.1126/science.1222879
    • Janda CY, Waghray D, Levin AM, Thomas C, Garcia KC. 2012. Structural basis of Wnt recognition by Frizzled. Science 337:59-64. doi: 10.1126/science.1222879.
    • (2012) Science , vol.337 , pp. 59-64
    • Janda, C.Y.1    Waghray, D.2    Levin, A.M.3    Thomas, C.4    Garcia, K.C.5
  • 32
    • 79954544086 scopus 로고    scopus 로고
    • Novel oxysterols have pro-osteogenic and anti-adipogenic effects in vitro and induce spinal fusion in vivo
    • doi: 10.1002/jcb.23082
    • Johnson JS, Meliton V, Kim WK, Lee KB, Wang JC, Nguyen K, et al. 2011. Novel oxysterols have pro-osteogenic and anti-adipogenic effects in vitro and induce spinal fusion in vivo. J Cell Biochem 112:1673-84. doi: 10.1002/jcb.23082.
    • (2011) J Cell Biochem , vol.112 , pp. 1673-1684
    • Johnson, J.S.1    Meliton, V.2    Kim, W.K.3    Lee, K.B.4    Wang, J.C.5    Nguyen, K.6
  • 34
    • 3242804594 scopus 로고    scopus 로고
    • Oxysterols regulate differentiation of mesenchymal stem cells: Pro-bone and anti-fat
    • doi: 10.1359/jbmr.040115
    • Kha HT, Basseri B, Shouhed D, Richardson J, Tetradis S, Hahn TJ, et al. 2004. Oxysterols regulate differentiation of mesenchymal stem cells: pro-bone and anti-fat. J Bone Miner Res 19:830-40. doi: 10.1359/jbmr.040115.
    • (2004) J Bone Miner Res , vol.19 , pp. 830-840
    • Kha, H.T.1    Basseri, B.2    Shouhed, D.3    Richardson, J.4    Tetradis, S.5    Hahn, T.J.6
  • 35
    • 77950492233 scopus 로고    scopus 로고
    • Itraconazole, a commonly used antifungal that inhibits Hedgehog pathway activity and cancer growth
    • doi: 10.1016/j.ccr.2010.02.027
    • Kim J, Tang JY, Gong R, Kim J, Lee JJ, Clemons KV, et al. 2010. Itraconazole, a commonly used antifungal that inhibits Hedgehog pathway activity and cancer growth. Cancer Cell 17:388-99. doi: 10.1016/j.ccr.2010.02.027.
    • (2010) Cancer Cell , vol.17 , pp. 388-399
    • Kim, J.1    Tang, J.Y.2    Gong, R.3    Kim, J.4    Lee, J.J.5    Clemons, K.V.6
  • 36
    • 80051991015 scopus 로고    scopus 로고
    • Structure of the protein core of the glypican Dally-like and localization of a region important for hedgehog signaling
    • doi: 10.1073/pnas.1109877108
    • Kim MS, Saunders AM, Hamaoka BY, Beachy PA, Leahy DJ. 2011. Structure of the protein core of the glypican Dally-like and localization of a region important for hedgehog signaling. Proc Natl Acad Sci USA 108:13112-7. doi: 10.1073/pnas.1109877108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 13112-13117
    • Kim, M.S.1    Saunders, A.M.2    Hamaoka, B.Y.3    Beachy, P.A.4    Leahy, D.J.5
  • 37
    • 38449113816 scopus 로고    scopus 로고
    • 20(S)-hydroxycholesterol inhibits PPARgamma expression and adipogenic differentiaion of bone marrow stromal cells through a hedgehog-dependent mechanism
    • doi: 10.1359/jbmr.070710
    • Kim WK, Meliton V, Amantea CM, Hahn TJ, Parhami F. 2007. 20(S)-hydroxycholesterol inhibits PPARgamma expression and adipogenic differentiaion of bone marrow stromal cells through a hedgehog-dependent mechanism. J Bone Miner Res 22:1711-9. doi: 10.1359/jbmr.070710.
    • (2007) J Bone Miner Res , vol.22 , pp. 1711-1719
    • Kim, W.K.1    Meliton, V.2    Amantea, C.M.3    Hahn, T.J.4    Parhami, F.5
  • 38
    • 67549105629 scopus 로고    scopus 로고
    • Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol
    • doi: 10.1016/j.cell.2009.03.049
    • Kwon HJ, Abi-Mosleh L, Wang ML, Deisenhofer J, Goldstein JL, Brown MS, et al. 2009. Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol. Cell 137:1213-24. doi: 10.1016/j.cell.2009.03.049.
    • (2009) Cell , vol.137 , pp. 1213-1224
    • Kwon, H.J.1    Abi-Mosleh, L.2    Wang, M.L.3    Deisenhofer, J.4    Goldstein, J.L.5    Brown, M.S.6
  • 40
    • 0034663722 scopus 로고    scopus 로고
    • The penultimate rotamer library
    • doi: 10.1002/1097-0134(20000815)40:3<389::AID-PROT50>3.0.CO;2-2
    • Lovell SC, Word JM, Richardson JS, Richardson DC. 2000. The penultimate rotamer library. Proteins 40:389-408. doi: 10.1002/1097-0134(20000815)40:3<389::AID-PROT50>3.0.CO;2-2.
    • (2000) Proteins , vol.40 , pp. 389-408
    • Lovell, S.C.1    Word, J.M.2    Richardson, J.S.3    Richardson, D.C.4
  • 41
    • 10744230965 scopus 로고    scopus 로고
    • Sonic hedgehog is required for progenitor cell maintenance in telencephalic stem cell niches
    • doi: 10.1016/S0896-6273(03)00561-0
    • Machold R, Hayashi S, Rutlin M, Muzumdar MD, Nery S, Corbin JG, et al. 2003. Sonic hedgehog is required for progenitor cell maintenance in telencephalic stem cell niches. Neuron 39:937-50. doi: 10.1016/S0896-6273(03)00561-0.
    • (2003) Neuron , vol.39 , pp. 937-950
    • McHold, R.1    Hayashi, S.2    Rutlin, M.3    Muzumdar, M.D.4    Nery, S.5    Corbin, J.G.6
  • 42
    • 0029948270 scopus 로고    scopus 로고
    • Biochemical evidence that patched is the Hedgehog receptor
    • doi: 10.1038/384176a0
    • Marigo V, Davey RA, Zuo Y, Cunningham JM, Tabin CJ. 1996. Biochemical evidence that patched is the Hedgehog receptor. Nature 384:176-9. doi: 10.1038/384176a0.
    • (1996) Nature , vol.384 , pp. 176-179
    • Marigo, V.1    Davey, R.A.2    Zuo, Y.3    Cunningham, J.M.4    Tabin, C.J.5
  • 43
    • 79951542472 scopus 로고    scopus 로고
    • Integration of Hedgehog and BMP signalling by the engrailed2a gene in the zebrafish myotome
    • doi: 10.1242/dev.062521
    • Maurya AK, Tan H, Souren M, Wang X, Wittbrodt J, Ingham PW. 2011. Integration of Hedgehog and BMP signalling by the engrailed2a gene in the zebrafish myotome. Development 138:755-65. doi: 10.1242/dev.062521.
    • (2011) Development , vol.138 , pp. 755-765
    • Maurya, A.K.1    Tan, H.2    Souren, M.3    Wang, X.4    Wittbrodt, J.5    Ingham, P.W.6
  • 44
    • 13844266400 scopus 로고    scopus 로고
    • Benefits of automated crystallization plate tracking, imaging, and analysis
    • doi: 10.1016/j.str.2004.12.010
    • Mayo CJ, Diprose JM, Walter TS, Berry IM, Wilson J, Owens RJ, et al. 2005. Benefits of automated crystallization plate tracking, imaging, and analysis. Structure 13:175-82. doi: 10.1016/j.str.2004.12.010.
    • (2005) Structure , vol.13 , pp. 175-182
    • Mayo, C.J.1    Diprose, J.M.2    Walter, T.S.3    Berry, I.M.4    Wilson, J.5    Owens, R.J.6
  • 46
    • 0002452569 scopus 로고    scopus 로고
    • Developmental roles and clinical significance of hedgehog signaling
    • doi: 10.1016/S0070-2153(03)53002-2
    • McMahon AP, Ingham PW, Tabin CJ. 2003. Developmental roles and clinical significance of hedgehog signaling. Curr Top Dev Biol 53:1-114. doi: 10.1016/S0070-2153(03)53002-2.
    • (2003) Curr Top Dev Biol , vol.53 , pp. 1-114
    • McMahon, A.P.1    Ingham, P.W.2    Tabin, C.J.3
  • 47
    • 0014066613 scopus 로고
    • Studies on C-20 epimers of 20-Hydroxycholesterol
    • doi: 10.1021/jo01278a066
    • Mijares A, Cargill DI, Glasel JA, Lieberman S. 1967. Studies on C-20 epimers of 20-Hydroxycholesterol. J Org Chem 32:810-2. doi: 10.1021/jo01278a066.
    • (1967) J Org Chem , vol.32 , pp. 810-812
    • Mijares, A.1    Cargill, D.I.2    Glasel, J.A.3    Lieberman, S.4
  • 48
    • 0020713543 scopus 로고
    • Monoclonal antibodies to rhodopsin: Characterization, cross-reactivity, and application as structural probes
    • doi: 10.1021/bi00272a020
    • Molday RS, MacKenzie D. 1983. Monoclonal antibodies to rhodopsin: characterization, cross-reactivity, and application as structural probes. Biochemistry 22:653-60. doi: 10.1021/bi00272a020.
    • (1983) Biochemistry , vol.22 , pp. 653-660
    • Molday, R.S.1    McKenzie, D.2
  • 49
    • 0030952249 scopus 로고    scopus 로고
    • Crystal Structure of the chicken riboflavin-binding protein
    • doi: 10.1093/emboj/16.7.1475
    • Monaco HL. 1997. Crystal Structure of the chicken riboflavin-binding protein. EMBO J 16:1475-83. doi: 10.1093/emboj/16.7.1475.
    • (1997) EMBO J , vol.16 , pp. 1475-1483
    • Monaco, H.L.1
  • 50
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with Selective receptor flexibility
    • doi: 10.1002/jcc.21256
    • Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, Goodsell DS, et al. 2009. AutoDock4 and AutoDockTools4: automated docking with Selective receptor flexibility. J Comput Chem 30:2785-91. doi: 10.1002/jcc.21256.
    • (2009) J Comput Chem , vol.30 , pp. 2785-2791
    • Morris, G.M.1    Huey, R.2    Lindstrom, W.3    Sanner, M.F.4    Belew, R.K.5    Goodsell, D.S.6
  • 51
    • 0009603803 scopus 로고    scopus 로고
    • Sonic hedgehog signaling by the patched-smoothened receptor complex
    • doi: 10.1016/S0960-9822(99)80018-9
    • Murone M, Rosenthal A, de Sauvage FJ. 1999. Sonic hedgehog signaling by the patched-smoothened receptor complex. Curr Biol 9:76-84. doi: 10.1016/S0960-9822(99)80018-9.
    • (1999) Curr Biol , vol.9 , pp. 76-84
    • Murone, M.1    Rosenthal, A.2    de Sauvage, F.J.3
  • 52
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • doi: 10.1107/S0907444996012255
    • Murshudov GN, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53:240-55. doi: 10.1107/S0907444996012255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 54
    • 1142289021 scopus 로고    scopus 로고
    • Functional domains and sub-cellular distribution of the Hedgehog transducing protein Smoothened in Drosophila
    • doi: 10.1016/j.mod.2004.04.015
    • Nakano Y, Nystedt S, Shivdasani AA, Strutt H, Thomas C, Ingham PW. 2004. Functional domains and sub-cellular distribution of the Hedgehog transducing protein Smoothened in Drosophila. Mech of Dev 121:507-18. doi: 10.1016/j.mod.2004.04.015.
    • (2004) Mech of Dev , vol.121 , pp. 507-518
    • Nakano, Y.1    Nystedt, S.2    Shivdasani, A.A.3    Strutt, H.4    Thomas, C.5    Ingham, P.W.6
  • 55
    • 84883185477 scopus 로고    scopus 로고
    • Oxysterol binding to the extracellular domain of Smoothened in Hedgehog signaling
    • doi: 10.1038/nchembio.1290
    • Nedelcu D, Liu J, Xu Y, Jao C, Salic A. 2013. Oxysterol binding to the extracellular domain of Smoothened in Hedgehog signaling. Nat Chem Biol 9:557-64. doi: 10.1038/nchembio.1290.
    • (2013) Nat Chem Biol , vol.9 , pp. 557-564
    • Nedelcu, D.1    Liu, J.2    Xu, Y.3    Jao, C.4    Salic, A.5
  • 56
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in Oscillation Mode
    • doi: 10.1016/s0076-6879(97)76066-x
    • Otwinowski Z, Minor W. 1997. Processing of x-ray diffraction data collected in Oscillation Mode. Methods Enzymol 276:307-26. doi: 10.1016/s0076-6879(97)76066-x.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 57
    • 0027172623 scopus 로고
    • Cloning of the zebrafish krox-20 gene (krx-20) and its expression during hindbrain development
    • doi: 10.1093/nar/21.5.1087
    • Oxtoby E, Jowett T. 1993. Cloning of the zebrafish krox-20 gene (krx-20) and its expression during hindbrain development. Nucleic Acids Res 21:1087-95. doi: 10.1093/nar/21.5.1087.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1087-1095
    • Oxtoby, E.1    Jowett, T.2
  • 58
    • 84863793247 scopus 로고    scopus 로고
    • Cysteine-rich domains related to Frizzled receptors and Hedgehog-interacting proteins
    • doi: 10.1002/pro.2105
    • Pei J, Grishin NV. 2012. Cysteine-rich domains related to Frizzled receptors and Hedgehog-interacting proteins. Protein Sci 21:1172-84. doi: 10.1002/pro.2105.
    • (2012) Protein Sci , vol.21 , pp. 1172-1184
    • Pei, J.1    Grishin, N.V.2
  • 59
    • 0028926048 scopus 로고
    • Protein-protein interactions: Methods for detection and analysis
    • Phizicky EM, Fields S. 1995. Protein-protein interactions: methods for detection and analysis. Microbiol Rev 59:94-123.
    • (1995) Microbiol Rev , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 60
    • 33749986728 scopus 로고    scopus 로고
    • Design and synthesis of fluconazole/bile acid conjugate using click reaction
    • doi: 10.1016/j.tet.2006.09.021
    • Pore VS, Aher NG, Kumar M, Shukla PK. 2006. Design and synthesis of fluconazole/bile acid conjugate using click reaction. Tetrahedron 62:11178-86. doi: 10.1016/j.tet.2006.09.021.
    • (2006) Tetrahedron , vol.62 , pp. 11178-11186
    • Pore, V.S.1    Aher, N.G.2    Kumar, M.3    Shukla, P.K.4
  • 61
    • 79251502034 scopus 로고    scopus 로고
    • Ligand-based receptor tyrosine kinase partial agonists: New paradigm for cancer drug discovery?
    • doi: 10.1517/17460441.2011.547468
    • Riese DJ II. 2011. Ligand-based receptor tyrosine kinase partial agonists: new paradigm for cancer drug discovery? Expert Opin Drug Discov 6:185-93. doi: 10.1517/17460441.2011.547468.
    • (2011) Expert Opin Drug Discov , vol.6 , pp. 185-193
    • Riese II, D.J.1
  • 62
    • 1842859044 scopus 로고    scopus 로고
    • Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins
    • doi: 10.1016/S0969-2126(02)00896-1
    • Riffel N, Harlos K, Iourin O, Rao ZH, Kingsman A, Stuart D, et al. 2002. Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins. Structure 10:1627-36. doi: 10.1016/S0969-2126(02)00896-1.
    • (2002) Structure , vol.10 , pp. 1627-1636
    • Riffel, N.1    Harlos, K.2    Iourin, O.3    Rao, Z.H.4    Kingsman, A.5    Stuart, D.6
  • 64
    • 62549159642 scopus 로고    scopus 로고
    • Hedgehog signal transduction by Smoothened: Pharmacologic evidence for a 2-step activation process
    • doi: 10.1073/pnas.0813373106
    • Rohatgi R, Milenkovic L, Corcoran RB, Scott MP. 2009. Hedgehog signal transduction by Smoothened: pharmacologic evidence for a 2-step activation process. Proc Natl Acad Sci USA 106:3196-201. doi: 10.1073/pnas.0813373106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3196-3201
    • Rohatgi, R.1    Milenkovic, L.2    Corcoran, R.B.3    Scott, M.P.4
  • 65
    • 34547110771 scopus 로고    scopus 로고
    • Patched1 regulates hedgehog signaling at the primary cilium
    • doi: 10.1126/science.1139740
    • Rohatgi R, Milenkovic L, Scott MP. 2007. Patched1 regulates hedgehog signaling at the primary cilium. Science 317:372-6. doi: 10.1126/science.1139740.
    • (2007) Science , vol.317 , pp. 372-376
    • Rohatgi, R.1    Milenkovic, L.2    Scott, M.P.3
  • 66
    • 66749119621 scopus 로고    scopus 로고
    • Evidence for allosteric interactions of antagonist binding to the smoothened receptor
    • doi: 10.1124/jpet.109.152090
    • Rominger CM, Bee WL, Copeland RA, Davenport EA, Gilmartin A, Gontarek R, et al. 2009. Evidence for allosteric interactions of antagonist binding to the smoothened receptor. J Pharmacol Exp Ther 329:995-1005. doi: 10.1124/jpet.109.152090.
    • (2009) J Pharmacol Exp Ther , vol.329 , pp. 995-1005
    • Rominger, C.M.1    Bee, W.L.2    Copeland, R.A.3    Davenport, E.A.4    Gilmartin, A.5    Gontarek, R.6
  • 67
    • 33748993139 scopus 로고    scopus 로고
    • Solvent-induced amphiphilic molecular baskets: Unimolecular reversed micelles with different size, shape, and flexibility
    • doi: 10.1021/jo0607663
    • Ryu EH, Yan J, Zhong Z, Zhao Y. 2006. Solvent-induced amphiphilic molecular baskets: Unimolecular reversed micelles with different size, shape, and flexibility. J Org Chem 71:7205-13. doi: 10.1021/jo0607663.
    • (2006) J Org Chem , vol.71 , pp. 7205-7213
    • Ryu, E.H.1    Yan, J.2    Zhong, Z.3    Zhao, Y.4
  • 68
    • 0030891148 scopus 로고    scopus 로고
    • A binding site for Gli proteins is essential for HNF-3beta floor plate enhancer activity in transgenics and can respond to Shh in vitro
    • Sasaki H, Hui C, Nakafuku M, Kondoh H. 1997. A binding site for Gli proteins is essential for HNF-3beta floor plate enhancer activity in transgenics and can respond to Shh in vitro. Development 124:1313-22.
    • (1997) Development , vol.124 , pp. 1313-1322
    • Sasaki, H.1    Hui, C.2    Nakafuku, M.3    Kondoh, H.4
  • 69
    • 67650289584 scopus 로고    scopus 로고
    • Mechanisms of Hedgehog pathway activation in cancer and implications for therapy
    • doi: 10.1016/j.tips.2009.03.007
    • Scales SJ, de Sauvage FJ. 2009. Mechanisms of Hedgehog pathway activation in cancer and implications for therapy. Trends Pharmacol Sci 30:303-12. doi: 10.1016/j.tips.2009.03.007.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 303-312
    • Scales, S.J.1    de Sauvage, F.J.2
  • 71
    • 84856089402 scopus 로고    scopus 로고
    • Signaling: An oxysterol ligand for Smoothened
    • doi: 10.1038/nchembio.774
    • Sharpe HJ, de Sauvage FJ. 2012. Signaling: an oxysterol ligand for Smoothened. Nat Chem Biol 8:139-40. doi: 10.1038/nchembio.774.
    • (2012) Nat Chem Biol , vol.8 , pp. 139-140
    • Sharpe, H.J.1    de Sauvage, F.J.2
  • 72
    • 33947335055 scopus 로고
    • 17beta Alkylation of a 17-Keto steroid by Alkylmagnesium Halides
    • doi: 10.1021/jo01345a016
    • Shaw PE. 1966. 17beta Alkylation of a 17-Keto steroid by Alkylmagnesium Halides. J Org Chem 31:2119-24. doi: 10.1021/jo01345a016.
    • (1966) J Org Chem , vol.31 , pp. 2119-2124
    • Shaw, P.E.1
  • 73
    • 79953746223 scopus 로고    scopus 로고
    • Hedgehog/Wnt feedback supports regenerative proliferation of epithelial stem cells in bladder
    • doi: 10.1038/nature09851
    • Shin K, Lee J, Guo N, Kim J, Lim A, Qu L, et al. 2011. Hedgehog/Wnt feedback supports regenerative proliferation of epithelial stem cells in bladder. Nature 472:110-4. doi: 10.1038/nature09851.
    • (2011) Nature , vol.472 , pp. 110-114
    • Shin, K.1    Lee, J.2    Guo, N.3    Kim, J.4    Lim, A.5    Qu, L.6
  • 74
    • 70349244639 scopus 로고    scopus 로고
    • Crystal structure of the frizzled-like cysteine-rich domain of the receptor tyrosine kinase MuSK
    • doi: 10.1016/j.jmb.2009.07.091
    • Stiegler AL, Burden SJ, Hubbard SR. 2009. Crystal structure of the frizzled-like cysteine-rich domain of the receptor tyrosine kinase MuSK. J Mol Biol 393:1-9. doi: 10.1016/j.jmb.2009.07.091.
    • (2009) J Mol Biol , vol.393 , pp. 1-9
    • Stiegler, A.L.1    Burden, S.J.2    Hubbard, S.R.3
  • 75
    • 0011102935 scopus 로고    scopus 로고
    • The tumour-suppressor gene patched encodes a candidate receptor for Sonic hedgehog
    • doi: 10.1038/384129a0
    • Stone DM, Hynes M, Armanini M, Swanson TA, Gu Q, Johnson RL, et al. 1996. The tumour-suppressor gene patched encodes a candidate receptor for Sonic hedgehog. Nature 384:129-34. doi: 10.1038/384129a0.
    • (1996) Nature , vol.384 , pp. 129-134
    • Stone, D.M.1    Hynes, M.2    Armanini, M.3    Swanson, T.A.4    Gu, Q.5    Johnson, R.L.6
  • 76
    • 0018792428 scopus 로고
    • Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å
    • doi: 10.1016/0022-2836(79)90416-9
    • Stuart DI, Levine M, Muirhead H, Stammers DK. 1979. Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å. J Mol Biol 134:109-42. doi: 10.1016/0022-2836(79)90416-9.
    • (1979) J Mol Biol , vol.134 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4
  • 77
    • 84859986516 scopus 로고    scopus 로고
    • Crystal structure of N-glycosylated human glypican-1 core protein: Structure of two loops evolutionarily conserved in vertebrate glypican-1
    • doi: 10.1074/jbc.M111.322487
    • Svensson G, Awad W, Håkansson M, Mani K, Logan DT. 2012. Crystal structure of N-glycosylated human glypican-1 core protein: structure of two loops evolutionarily conserved in vertebrate glypican-1. J Biol Chem 287:14040-51. doi: 10.1074/jbc.M111.322487.
    • (2012) J Biol Chem , vol.287 , pp. 14040-14051
    • Svensson, G.1    Awad, W.2    Håkansson, M.3    Mani, K.4    Logan, D.T.5
  • 78
    • 0034738979 scopus 로고    scopus 로고
    • Effects of oncogenic mutations in Smoothened and Patched can be reversed by cyclopamine
    • doi: 10.1038/35023008
    • Taipale J, Chen JK, Cooper MK, Wang B, Mann RK, Milenkovic L, et al. 2000. Effects of oncogenic mutations in Smoothened and Patched can be reversed by cyclopamine. Nature 406:1005-9. doi: 10.1038/35023008.
    • (2000) Nature , vol.406 , pp. 1005-1009
    • Taipale, J.1    Chen, J.K.2    Cooper, M.K.3    Wang, B.4    Mann, R.K.5    Milenkovic, L.6
  • 79
    • 0037158748 scopus 로고    scopus 로고
    • Patched acts catalytically to suppress the activity of Smoothened
    • doi: 10.1038/nature00989
    • Taipale J, Cooper MK, Maiti T, Beachy PA. 2002. Patched acts catalytically to suppress the activity of Smoothened. Nature 418:892-7. doi: 10.1038/nature00989.
    • (2002) Nature , vol.418 , pp. 892-897
    • Taipale, J.1    Cooper, M.K.2    Maiti, T.3    Beachy, P.A.4
  • 80
    • 84861876867 scopus 로고    scopus 로고
    • Inhibiting the hedgehog pathway in patients with the basal-cell nevus syndrome
    • doi: 10.1056/NEJMoa1113538
    • Tang JY, Mackay-Wiggan JM, Aszterbaum M, Yauch RL, Lindgren J, Chang K, et al. 2012. Inhibiting the hedgehog pathway in patients with the basal-cell nevus syndrome. N Engl J Med 366:2180-8. doi: 10.1056/NEJMoa1113538.
    • (2012) N Engl J Med , vol.366 , pp. 2180-2188
    • Tang, J.Y.1    McKay-Wiggan, J.M.2    Aszterbaum, M.3    Yauch, R.L.4    Lindgren, J.5    Chang, K.6
  • 81
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution and density modification
    • doi: 10.1016/S0076-6879(03)74002-6
    • Terwilliger TC. 2003. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol 374:22-37. doi: 10.1016/S0076-6879(03)74002-6.
    • (2003) Methods Enzymol , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 82
    • 31744436876 scopus 로고    scopus 로고
    • Divergence of hedgehog signal transduction mechanism between Drosophila and mammals
    • doi: 10.1016/j.devcel.2005.12.014
    • Varjosalo M, Li SP, Taipale J. 2006. Divergence of hedgehog signal transduction mechanism between Drosophila and mammals. Dev Cell 10:177-86. doi: 10.1016/j.devcel.2005.12.014.
    • (2006) Dev Cell , vol.10 , pp. 177-186
    • Varjosalo, M.1    Li, S.P.2    Taipale, J.3
  • 83
    • 70349238733 scopus 로고    scopus 로고
    • Inhibition of the hedgehog pathway in advanced basal-cell carcinoma
    • doi: 10.1056/NEJMoa0905360
    • Von Hoff DD, LoRusso PM, Rudin CM, Reddy JC, Yauch RL, Tibes R, et al. 2009. Inhibition of the hedgehog pathway in advanced basal-cell carcinoma. N Engl J Med 361:1164-72. doi: 10.1056/NEJMoa0905360.
    • (2009) N Engl J Med , vol.361 , pp. 1164-1172
    • Von Hoff, D.D.1    LoRusso, P.M.2    Rudin, C.M.3    Reddy, J.C.4    Yauch, R.L.5    Tibes, R.6
  • 84
    • 23844515485 scopus 로고    scopus 로고
    • A procedure for setting up high-throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization
    • doi: 10.1107/S0907444905007808
    • Walter TS, Diprose JM, Mayo CJ, Siebold C, Pickford MG, Carter L, et al. 2005. A procedure for setting up high-throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization. Acta Crystallogr D Biol Crystallogr 61:651-7. doi: 10.1107/S0907444905007808.
    • (2005) Acta Crystallogr D Biol Crystallogr , vol.61 , pp. 651-657
    • Walter, T.S.1    Diprose, J.M.2    Mayo, C.J.3    Siebold, C.4    Pickford, M.G.5    Carter, L.6
  • 85
    • 84878112106 scopus 로고    scopus 로고
    • Structure of the human smoothened receptor bound to an antitumour agent
    • doi: 10.1038/nature12167
    • Wang C, Wu H, Katritch V, Han GW, Huang XP, Liu W, et al. 2013. Structure of the human smoothened receptor bound to an antitumour agent. Nature 497:338-43. doi: 10.1038/nature12167.
    • (2013) Nature , vol.497 , pp. 338-343
    • Wang, C.1    Wu, H.2    Katritch, V.3    Han, G.W.4    Huang, X.P.5    Liu, W.6
  • 86
    • 78649916808 scopus 로고    scopus 로고
    • Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes
    • doi: 10.1016/j.cmet.2010.05.016
    • Wang ML, Motamed M, Infante RE, Abi-Mosleh L, Kwon HJ, Brown MS, et al. 2010. Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes. Cell Metab 12:166-73. doi: 10.1016/j.cmet.2010.05.016.
    • (2010) Cell Metab , vol.12 , pp. 166-173
    • Wang, M.L.1    Motamed, M.2    Infante, R.E.3    Abi-Mosleh, L.4    Kwon, H.J.5    Brown, M.S.6
  • 87
    • 84865528807 scopus 로고    scopus 로고
    • Glucocorticoid compounds modify smoothened localization and hedgehog pathway activity
    • doi: 10.1016/j.chembiol.2012.06.012
    • Wang Y, Davidow L, Arvanites AC, Blanchard J, Lam K, Xu K, et al. 2012. Glucocorticoid compounds modify smoothened localization and hedgehog pathway activity. Chem Biol 9:972-82. doi: 10.1016/j.chembiol.2012.06.012.
    • (2012) Chem Biol , vol.9 , pp. 972-982
    • Wang, Y.1    Davidow, L.2    Arvanites, A.C.3    Blanchard, J.4    Lam, K.5    Xu, K.6
  • 88
    • 67849104638 scopus 로고    scopus 로고
    • PubChem: A public information system for analyzing bioactivities of small molecules
    • doi: 10.1093/nar/gkp456
    • Wang YL, Xiao JW, Suzek TO, Zhang J, Wang JY, Bryant SH. 2009. PubChem: a public information system for analyzing bioactivities of small molecules. Nucleic Acids Res 37:W623-33. doi: 10.1093/nar/gkp456.
    • (2009) Nucleic Acids Res , vol.37
    • Wang, Y.L.1    Xiao, J.W.2    Suzek, T.O.3    Zhang, J.4    Wang, J.Y.5    Bryant, S.H.6
  • 89
    • 75649151032 scopus 로고    scopus 로고
    • XIA2: An expert system for macromolecular crystallography data reduction
    • doi: 10.1107/S0021889809045701
    • Winter G. 2010. XIA2: an expert system for macromolecular crystallography data reduction. J Appl Crystallogr 43:186-90. doi: 10.1107/S0021889809045701.
    • (2010) J Appl Crystallogr , vol.43 , pp. 186-190
    • Winter, G.1
  • 90
    • 0038376480 scopus 로고    scopus 로고
    • Multiple muscle cell identities induced by distinct levels and timing of Hedgehog activity in the zebrafish embryo
    • doi: 10.1016/S0960-9822(03)00461-5
    • Wolff C, Roy S, Ingham PW. 2003. Multiple muscle cell identities induced by distinct levels and timing of Hedgehog activity in the zebrafish embryo. Curr Biol 13:1169-81. doi: 10.1016/S0960-9822(03)00461-5.
    • (2003) Curr Biol , vol.13 , pp. 1169-1181
    • Wolff, C.1    Roy, S.2    Ingham, P.W.3
  • 91
    • 70350496540 scopus 로고    scopus 로고
    • Smoothened mutation confers resistance to a Hedgehog pathway inhibitor in medulloblastoma
    • doi: 10.1126/science.1179386
    • Yauch RL, Dijkgraaf GJ, Alicke B, Januario T, Ahn CP, Holcomb T, et al. 2009. Smoothened mutation confers resistance to a Hedgehog pathway inhibitor in medulloblastoma. Science 326:572-4. doi: 10.1126/science.1179386.
    • (2009) Science , vol.326 , pp. 572-574
    • Yauch, R.L.1    Dijkgraaf, G.J.2    Alicke, B.3    Januario, T.4    Ahn, C.P.5    Holcomb, T.6
  • 92
    • 79959935033 scopus 로고    scopus 로고
    • Automation of large scale transient protein expression in mammalian cells
    • doi: 10.1016/j.jsb.2011.04.017
    • Zhao Y, Bishop B, Clay JE, Lu W, Jones M, Daenke S, et al. 2011. Automation of large scale transient protein expression in mammalian cells. J Struct Biol 175:209-15. doi: 10.1016/j.jsb.2011.04.017.
    • (2011) J Struct Biol , vol.175 , pp. 209-215
    • Zhao, Y.1    Bishop, B.2    Clay, J.E.3    Lu, W.4    Jones, M.5    Daenke, S.6
  • 93
    • 29344464587 scopus 로고    scopus 로고
    • Oligomeric cholates: Amphiphilic foldamers with nanometer-sized hydrophilic cavities
    • doi: 10.1021/ja056151p
    • Zhao Y, Zhong ZQ. 2005. Oligomeric cholates: amphiphilic foldamers with nanometer-sized hydrophilic cavities. J Am Chem Soc 127:17894-901. doi: 10.1021/ja056151p.
    • (2005) J Am Chem Soc , vol.127 , pp. 17894-17901
    • Zhao, Y.1    Zhong, Z.Q.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.