메뉴 건너뛰기




Volumn 4, Issue JULY 2015, 2015, Pages 1-27

Structure and functional properties of norrin mimic wnt for signalling with Frizzled4, Lrp5/6, and proteoglycan

Author keywords

[No Author keywords available]

Indexed keywords

FRIZZLED 4 PROTEIN; GLYCOSAMINOGLYCAN; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN 5; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN 6; NORRIE DISEASE PROTEIN; PROTEIN; PROTEOGLYCAN; TETRASPANIN; UNCLASSIFIED DRUG; WNT PROTEIN; EYE PROTEIN; FRIZZLED PROTEIN; FZD4 PROTEIN, HUMAN; LRP5 PROTEIN, MOUSE; LRP6 PROTEIN, MOUSE; MUTANT PROTEIN; NDP PROTEIN, HUMAN; NERVE PROTEIN;

EID: 85016043869     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.06554     Document Type: Article
Times cited : (102)

References (94)
  • 3
    • 80755186529 scopus 로고    scopus 로고
    • Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6
    • Ahn VE, Chu ML, Choi HJ, Tran D, Abo A, Weis WI. 2011. Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6. Developmental Cell 21:862-873. doi: 10.1016/j.devcel.2011.09.003.
    • (2011) Developmental Cell , vol.21 , pp. 862-873
    • Ahn, V.E.1    Chu, M.L.2    Choi, H.J.3    Tran, D.4    Abo, A.5    Weis, W.I.6
  • 4
    • 0041671071 scopus 로고    scopus 로고
    • QSulf1 remodels the 6-O sulfation states of cell surface heparan sulfate proteoglycans to promote Wnt signaling
    • Ai X, Do AT, Lozynska O, Kusche-Gullberg M, Lindahl U, Emerson CP Jr. 2003. QSulf1 remodels the 6-O sulfation states of cell surface heparan sulfate proteoglycans to promote Wnt signaling. The Journal of Cell Biology 162: 341-351. doi: 10.1083/jcb.200212083.
    • (2003) The Journal of Cell Biology , vol.162 , pp. 341-351
    • Ai, X.1    Do, A.T.2    Lozynska, O.3    Kusche-Gullberg, M.4    Lindahl, U.5    Emerson, C.P.6
  • 5
    • 84871846692 scopus 로고    scopus 로고
    • WNT signalling pathways as therapeutic targets in cancer. Nature Reviews
    • Anastas JN, Moon RT. 2013. WNT signalling pathways as therapeutic targets in cancer. Nature Reviews. Cancer 13:11-26. doi: 10.1038/nrc3419.
    • (2013) Cancer , vol.13 , pp. 11-26
    • Anastas, J.N.1    Moon, R.T.2
  • 7
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N. 2010. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Research 38:W529-W533. doi: 10.1093/nar/gkq399.
    • (2010) Nucleic Acids Research , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 8
    • 50049130165 scopus 로고    scopus 로고
    • Valproic acid: A viable alternative to sodium butyrate for enhancing protein expression in mammalian cell cultures
    • Backliwal G, Hildinger M, Kuettel I, Delegrange F, Hacker DL, Wurm FM. 2008. Valproic acid: a viable alternative to sodium butyrate for enhancing protein expression in mammalian cell cultures. Biotechnology and Bioengineering 101:182-189. doi: 10.1002/bit.21882.
    • (2008) Biotechnology and Bioengineering , vol.101 , pp. 182-189
    • Backliwal, G.1    Hildinger, M.2    Kuettel, I.3    Delegrange, F.4    Hacker, D.L.5    Wurm, F.M.6
  • 9
    • 0035152025 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are critical for the organization of the extracellular distribution of Wingless
    • Baeg GH, Lin X, Khare N, Baumgartner S, Perrimon N. 2001. Heparan sulfate proteoglycans are critical for the organization of the extracellular distribution of Wingless. Development 128:87-94.
    • (2001) Development , vol.128 , pp. 87-94
    • Baeg, G.H.1    Lin, X.2    Khare, N.3    Baumgartner, S.4    Perrimon, N.5
  • 10
    • 7544229806 scopus 로고    scopus 로고
    • The Wingless morphogen gradient is established by the cooperative action of Frizzled and Heparan Sulfate Proteoglycan receptors
    • Baeg GH, Selva EM, Goodman RM, Dasgupta R, Perrimon N. 2004. The Wingless morphogen gradient is established by the cooperative action of Frizzled and Heparan Sulfate Proteoglycan receptors. Developmental Biology 276:89-100. doi: 10.1016/j.ydbio.2004.08.023.
    • (2004) Developmental Biology , vol.276 , pp. 89-100
    • Baeg, G.H.1    Selva, E.M.2    Goodman, R.M.3    Dasgupta, R.4    Perrimon, N.5
  • 12
    • 84865073858 scopus 로고    scopus 로고
    • Structural architecture and functional evolution of Wnts
    • Bazan JF, Janda CY, Garcia KC. 2012. Structural architecture and functional evolution of Wnts. Developmental Cell 23:227-232. doi: 10.1016/j.devcel.2012.07.011.
    • (2012) Developmental Cell , vol.23 , pp. 227-232
    • Bazan, J.F.1    Janda, C.Y.2    Garcia, K.C.3
  • 14
    • 34250827150 scopus 로고    scopus 로고
    • Wnt induces LRP6 signalosomes and promotes dishevelled-dependent LRP6 phosphorylation
    • Bilic J, Huang YL, Davidson G, Zimmermann T, Cruciat CM, Bienz M, Niehrs C. 2007. Wnt induces LRP6 signalosomes and promotes dishevelled-dependent LRP6 phosphorylation. Science 316:1619-1622. doi: 10.1126/science.1137065.
    • (2007) Science , vol.316 , pp. 1619-1622
    • Bilic, J.1    Huang, Y.L.2    Davidson, G.3    Zimmermann, T.4    Cruciat, C.M.5    Bienz, M.6    Niehrs, C.7
  • 16
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value. Methods and applications. Acta Crystallographica. Section D
    • Brunger AT. 1993. Assessment of phase accuracy by cross validation: the free R value. Methods and applications. Acta Crystallographica. Section D, Biological Crystallography 49:24-36. doi: 10.1107/S0907444992007352.
    • (1993) Biological Crystallography , vol.49 , pp. 24-36
    • Brunger, A.T.1
  • 17
    • 84897462045 scopus 로고    scopus 로고
    • Glypican-3 binds to Frizzled and plays a direct role in the stimulation of canonical Wnt signaling
    • Capurro M, Martin T, Shi W, Filmus J. 2014. Glypican-3 binds to Frizzled and plays a direct role in the stimulation of canonical Wnt signaling. Journal of Cell Science 127:1565-1575. doi: 10.1242/jcs.140871.
    • (2014) Journal of Cell Science , vol.127 , pp. 1565-1575
    • Capurro, M.1    Martin, T.2    Shi, W.3    Filmus, J.4
  • 23
    • 84907487414 scopus 로고    scopus 로고
    • Stem cell signaling. An integral program for tissue renewal and regeneration: Wnt signaling and stem cell control
    • Clevers H, Loh KM, Nusse R. 2014. Stem cell signaling. An integral program for tissue renewal and regeneration: Wnt signaling and stem cell control. Science 346:1248012. doi: 10.1126/science.1248012.
    • (2014) Science , vol.346
    • Clevers, H.1    Loh, K.M.2    Nusse, R.3
  • 24
    • 84861986053 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling and disease
    • Clevers H, Nusse R. 2012. Wnt/beta-catenin signaling and disease. Cell 149:1192-1205. doi: 10.1016/j.cell.2012.05.012.
    • (2012) Cell , vol.149 , pp. 1192-1205
    • Clevers, H.1    Nusse, R.2
  • 25
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan K. 2006. The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallographica. Section D, Biological Crystallography 62:1002-1011. doi: 10.1107/S0907444906022116.
    • (2006) Acta Crystallographica. Section D, Biological Crystallography , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 27
    • 0035811492 scopus 로고    scopus 로고
    • Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains
    • 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
  • 30
    • 84879367781 scopus 로고    scopus 로고
    • How good are my data and what is the resolution? Acta Crystallographica. Section D
    • Evans PR, Murshudov GN. 2013. How good are my data and what is the resolution? Acta Crystallographica. Section D, Biological Crystallography 69:1204-1214. doi: 10.1107/S0907444913000061.
    • (2013) Biological Crystallography , vol.69 , pp. 1204-1214
    • Evans, P.R.1    Murshudov, G.N.2
  • 31
    • 73949092833 scopus 로고    scopus 로고
    • A study on the interactions between heparan sulfate proteoglycans and Wnt proteins
    • Fuerer C, Habib SJ, Nusse R. 2010. A study on the interactions between heparan sulfate proteoglycans and Wnt proteins. Developmental Dynamics 239:184-190. doi: 10.1002/dvdy.22067.
    • (2010) Developmental Dynamics , vol.239 , pp. 184-190
    • Fuerer, C.1    Habib, S.J.2    Nusse, R.3
  • 33
    • 84874855471 scopus 로고    scopus 로고
    • All-atom ensemble modeling to analyze small-angle x-ray scattering of glycosylated proteins
    • Guttman M, Weinkam P, Sali A, Lee KK. 2013. All-atom ensemble modeling to analyze small-angle x-ray scattering of glycosylated proteins. Structure 21:321-331. doi: 10.1016/j.str.2013.02.004.
    • (2013) Structure , vol.21 , pp. 321-331
    • Guttman, M.1    Weinkam, P.2    Sali, A.3    Lee, K.K.4
  • 34
    • 0033616573 scopus 로고    scopus 로고
    • Biochemical characterization of Wnt-frizzled interactions using a soluble, biologically active vertebrate Wnt protein
    • Hsieh JC, Rattner A, Smallwood PM, Nathans J. 1999. Biochemical characterization of Wnt-frizzled interactions using a soluble, biologically active vertebrate Wnt protein. Proceedings of the National Academy of Sciences of USA 96:3546-3551. doi: 10.1073/pnas.96.7.3546.
    • (1999) Proceedings of the National Academy of Sciences of USA , vol.96 , pp. 3546-3551
    • Hsieh, J.C.1    Rattner, A.2    Smallwood, P.M.3    Nathans, J.4
  • 35
    • 84863543371 scopus 로고    scopus 로고
    • Structural basis of Wnt recognition by Frizzled
    • 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
  • 36
    • 84925002888 scopus 로고    scopus 로고
    • The heparan sulfate mimetic PG545 interferes with Wnt/beta-catenin signaling and significantly suppresses pancreatic tumorigenesis alone and in combination with gemcitabine
    • Jung DB, Yun M, Kim EO, Kim J, Kim B, Jung JH, Wang E, Mukhopadhyay D, Hammond E, Dredge K, Shridhar V, Kim SH. 2015. The heparan sulfate mimetic PG545 interferes with Wnt/beta-catenin signaling and significantly suppresses pancreatic tumorigenesis alone and in combination with gemcitabine. Oncotarget 6:4992-5004.
    • (2015) Oncotarget , vol.6 , pp. 4992-5004
    • Jung, D.B.1    Yun, M.2    Kim, E.O.3    Kim, J.4    Kim, B.5    Jung, J.H.6    Wang, E.7    Mukhopadhyay, D.8    Hammond, E.9    Dredge, K.10    Shridhar, V.11    Kim, S.H.12
  • 37
    • 70349838225 scopus 로고    scopus 로고
    • TSPAN12 regulates retinal vascular development by promoting Norrin-but not Wnt-induced FZD4/beta-catenin signaling
    • Junge HJ, Yang S, Burton JB, Paes K, Shu X, French DM, Costa M, Rice DS, Ye W. 2009. TSPAN12 regulates retinal vascular development by promoting Norrin-but not Wnt-induced FZD4/beta-catenin signaling. Cell 139: 299-311. doi: 10.1016/j.cell.2009.07.048.
    • (2009) Cell , vol.139 , pp. 299-311
    • Junge, H.J.1    Yang, S.2    Burton, J.B.3    Paes, K.4    Shu, X.5    French, D.M.6    Costa, M.7    Rice, D.S.8    Ye, W.9
  • 38
    • 84903767326 scopus 로고    scopus 로고
    • Can we safely target the WNT pathway? Nature Reviews
    • Kahn M. 2014. Can we safely target the WNT pathway? Nature Reviews. Drug Discovery 13:513-532. doi: 10.1038/nrd4233.
    • (2014) Drug Discovery , vol.13 , pp. 513-532
    • Kahn, M.1
  • 41
    • 1342332090 scopus 로고    scopus 로고
    • Mutant Frizzled 4 associated with vitreoretinopathy traps wild-type Frizzled in the endoplasmic reticulum by oligomerization
    • Kaykas A, Yang-Snyder J, Heroux M, Shah KV, Bouvier M, Moon RT. 2004. Mutant Frizzled 4 associated with vitreoretinopathy traps wild-type Frizzled in the endoplasmic reticulum by oligomerization. Nature Cell Biology 6: 52-58. doi: 10.1038/ncb1081.
    • (2004) Nature Cell Biology , vol.6 , pp. 52-58
    • Kaykas, A.1    Yang-Snyder, J.2    Heroux, M.3    Shah, K.V.4    Bouvier, M.5    Moon, R.T.6
  • 43
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallographica. Section D
    • Krissinel E, Henrick K. 2004. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallographica. Section D, Biological Crystallography 60:2256-2268. doi: 10.1107/S0907444904026460.
    • (2004) Biological Crystallography , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 44
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K. 2007. Inference of macromolecular assemblies from crystalline state. Journal of Molecular Biology 372:774-797. doi: 10.1016/j.jmb.2007.05.022.
    • (2007) Journal of Molecular Biology , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 45
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence MC, Colman PM. 1993. Shape complementarity at protein/protein interfaces. Journal of Molecular Biology 234:946-950. doi: 10.1006/jmbi.1993.1648.
    • (1993) Journal of Molecular Biology , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 46
    • 0033566126 scopus 로고    scopus 로고
    • Dally cooperates with Drosophila Frizzled 2 to transduce Wingless signalling
    • Lin X, Perrimon N. 1999. Dally cooperates with Drosophila Frizzled 2 to transduce Wingless signalling. Nature 400: 281-284. doi: 10.1038/22343.
    • (1999) Nature , vol.400 , pp. 281-284
    • Lin, X.1    Perrimon, N.2
  • 49
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallographica. Section D
    • McCoy AJ. 2007. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallographica. Section D, Biological Crystallography 63:32-41. doi: 10.1107/S0907444906045975.
    • (2007) Biological Crystallography , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 50
    • 0020713543 scopus 로고
    • Monoclonal antibodies to rhodopsin: Characterization, cross-reactivity, and application as structural probes
    • Molday RS, MacKenzie D. 1983. Monoclonal antibodies to rhodopsin: characterization, cross-reactivity, and application as structural probes. Biochemistry 22:653-660. doi: 10.1021/bi00272a020.
    • (1983) Biochemistry , vol.22 , pp. 653-660
    • Molday, R.S.1    Mackenzie, D.2
  • 51
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallographica. Section D
    • Murshudov GN, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallographica. Section D, Biological Crystallography 53:240-255. doi: 10.1107/S0907444996012255.
    • (1997) Biological Crystallography , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 53
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai T, Ibata K, Park ES, Kubota M, Mikoshiba K, Miyawaki A. 2002. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nature Biotechnology 20:87-90. doi: 10.1038/nbt0102-87.
    • (2002) Nature Biotechnology , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 57
    • 74849101559 scopus 로고    scopus 로고
    • Norrin promotes vascular regrowth after oxygen-induced retinal vessel loss and suppresses retinopathy in mice
    • Ohlmann A, Seitz R, Braunger B, Seitz D, Bosl MR, Tamm ER. 2010. Norrin promotes vascular regrowth after oxygen-induced retinal vessel loss and suppresses retinopathy in mice. The Journal of Neuroscience 30:183-193. doi: 10.1523/JNEUROSCI.3210-09.2010.
    • (2010) The Journal of Neuroscience , vol.30 , pp. 183-193
    • Ohlmann, A.1    Seitz, R.2    Braunger, B.3    Seitz, D.4    Bosl, M.R.5    Tamm, E.R.6
  • 58
    • 84859938636 scopus 로고    scopus 로고
    • Norrin: Molecular and functional properties of an angiogenic and neuroprotective growth factor
    • Ohlmann A, Tamm ER. 2012. Norrin: molecular and functional properties of an angiogenic and neuroprotective growth factor. Progress in Retinal and Eye Research 31:243-257. doi: 10.1016/j.preteyeres.2012.02.002.
    • (2012) Progress in Retinal and Eye Research , vol.31 , pp. 243-257
    • Ohlmann, A.1    Tamm, E.R.2
  • 59
    • 6344228386 scopus 로고    scopus 로고
    • Biotinylated tags for recovery and characterization of ribonucleoprotein complexes
    • Penalva LO, Keene JD. 2004. Biotinylated tags for recovery and characterization of ribonucleoprotein complexes. Biotechniques 37:608-610.
    • (2004) Biotechniques , vol.37 , pp. 608-610
    • Penalva, L.O.1    Keene, J.D.2
  • 60
    • 0031469913 scopus 로고    scopus 로고
    • Norrie disease protein (Norrin) forms disulfide-linked oligomers associated with the extracellular matrix
    • Perez-Vilar J, Hill RL. 1997. Norrie disease protein (norrin) forms disulfide-linked oligomers associated with the extracellular matrix. The Journal of Biological Chemistry 272:33410-33415. doi: 10.1074/jbc.272.52.33410.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 33410-33415
    • Perez-Vilar, J.1    Hill, R.L.2
  • 62
    • 50049088245 scopus 로고    scopus 로고
    • Enhanced protein expression in mammalian cells using engineered SUMO fusions: Secreted phospholipase A2
    • Peroutka RJ, Elshourbagy N, Piech T, Butt TR. 2008. Enhanced protein expression in mammalian cells using engineered SUMO fusions: secreted phospholipase A2. Protein Science 17:1586-1595. doi: 10.1110/ps.035576.108.
    • (2008) Protein Science , vol.17 , pp. 1586-1595
    • Peroutka, R.J.1    Elshourbagy, N.2    Piech, T.3    Butt, T.R.4
  • 64
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law
    • Rambo RP, Tainer JA. 2011. Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law. Biopolymers 95:559-571. doi: 10.1002/bip.21638.
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 66
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible Nacetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, khorana HG. 2002. Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible Nacetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proceedings of the National Academy of Sciences of USA 99:13419-13424. doi: 10.1073/pnas.212519299.
    • (2002) Proceedings of the National Academy of Sciences of USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 68
    • 0029844909 scopus 로고    scopus 로고
    • Glycosaminoglycans can modulate extracellular localization of the wingless protein and promote signal transduction
    • Reichsman F, Smith L, Cumberledge S. 1996. Glycosaminoglycans can modulate extracellular localization of the wingless protein and promote signal transduction. The Journal of Cell Biology 135:819-827. doi: 10.1083/jcb.135.3.819.
    • (1996) The Journal of Cell Biology , vol.135 , pp. 819-827
    • Reichsman, F.1    Smith, L.2    Cumberledge, S.3
  • 70
    • 0035726693 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: Modulation of receptor function
    • Rios CD, Jordan BA, Gomes I, Devi LA. 2001. G-protein-coupled receptor dimerization: modulation of receptor function. Pharmacology & Therapeutics 92:71-87. doi: 10.1016/S0163-7258(01)00160-7.
    • (2001) Pharmacology &Amp; Therapeutics , vol.92 , pp. 71-87
    • Rios, C.D.1    Jordan, B.A.2    Gomes, I.3    Devi, L.A.4
  • 72
    • 77954280480 scopus 로고    scopus 로고
    • FoXS: A web server for rapid computation and fitting of SAXS profiles
    • Schneidman-Duhovny D, Hammel M, Sali A. 2010. FoXS: a web server for rapid computation and fitting of SAXS profiles. Nucleic Acids Research 38:W540-W544. doi: 10.1093/nar/gkq461.
    • (2010) Nucleic Acids Research , vol.38
    • Schneidman-Duhovny, D.1    Hammel, M.2    Sali, A.3
  • 74
    • 77951658627 scopus 로고    scopus 로고
    • Norrin mediates neuroprotective effects on retinal ganglion cells via activation of the Wnt/beta-catenin signaling pathway and the induction of neuroprotective growth factors in Muller cells
    • Seitz R, Hackl S, Seibuchner T, Tamm ER, Ohlmann A. 2010. Norrin mediates neuroprotective effects on retinal ganglion cells via activation of the Wnt/beta-catenin signaling pathway and the induction of neuroprotective growth factors in Muller cells. The Journal of Neuroscience 30:5998-6010. doi: 10.1523/JNEUROSCI.0730-10.2010.
    • (2010) The Journal of Neuroscience , vol.30 , pp. 5998-6010
    • Seitz, R.1    Hackl, S.2    Seibuchner, T.3    Tamm, E.R.4    Ohlmann, A.5
  • 75
    • 0344826634 scopus 로고    scopus 로고
    • Overproduction and partial purification of the Norrie disease gene product, norrin, from a recombinant baculovirus
    • Shastry BS, Trese MT. 2003. Overproduction and partial purification of the Norrie disease gene product, norrin, from a recombinant baculovirus. Biochemical and Biophysical Research Communications 312:229-234. doi: 10.1016/j.bbrc.2003.09.223.
    • (2003) Biochemical and Biophysical Research Communications , vol.312 , pp. 229-234
    • Shastry, B.S.1    Trese, M.T.2
  • 76
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification. Acta Crystallographica. Section D
    • Sheldrick GM. 2010. Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallographica. Section D, Biological Crystallography 66:479-485. doi: 10.1107/S0907444909038360.
    • (2010) Biological Crystallography , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 78
    • 70349244639 scopus 로고    scopus 로고
    • Crystal structure of the frizzled-like cysteine-rich domain of the receptor tyrosine kinase MuSK
    • Stiegler AL, Burden SJ, Hubbard SR. 2009. Crystal structure of the frizzled-like cysteine-rich domain of the receptor tyrosine kinase MuSK. Journal of Molecular Biology 393:1-9. doi: 10.1016/j.jmb.2009.07.091.
    • (2009) Journal of Molecular Biology , vol.393 , pp. 1-9
    • Stiegler, A.L.1    Burden, S.J.2    Hubbard, S.R.3
  • 79
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D. 1992. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. Journal of Applied Crystallography 25:495-503. doi: 10.1107/S0021889892001663.
    • (1992) Journal of Applied Crystallography , vol.25 , pp. 495-503
    • Svergun, D.1
  • 80
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution and density modification
    • 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
  • 81
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Research 22:4673-4680. doi: 10.1093/nar/22.22.4673.
    • (1994) Nucleic Acids Research , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 82
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta ES, Parodi AJ. 2003. Quality control and protein folding in the secretory pathway. Annual Review of Cell and Developmental Biology 19:649-676. doi: 10.1146/annurev.cellbio.19.110701.153949.
    • (2003) Annual Review of Cell and Developmental Biology , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 86
    • 84870897220 scopus 로고    scopus 로고
    • Norrin/Frizzled4 signaling in retinal vascular development and blood brain barrier plasticity
    • Wang Y, Rattner A, Zhou Y, Williams J, Smallwood PM, Nathans J. 2012. Norrin/Frizzled4 signaling in retinal vascular development and blood brain barrier plasticity. Cell 151:1332-1344. doi: 10.1016/j.cell.2012.10.042.
    • (2012) Cell , vol.151 , pp. 1332-1344
    • Wang, Y.1    Rattner, A.2    Zhou, Y.3    Williams, J.4    Smallwood, P.M.5    Nathans, J.6
  • 88
    • 75649151032 scopus 로고    scopus 로고
    • Xia2: An expert system for macromolecular crystallography data reduction
    • Winter G. 2010. xia2: an expert system for macromolecular crystallography data reduction. Journal of Applied Crystallography 43:186-190. doi: 10.1107/S0021889809045701.
    • (2010) Journal of Applied Crystallography , vol.43 , pp. 186-190
    • Winter, G.1
  • 89
  • 90
    • 79951677187 scopus 로고    scopus 로고
    • Expression of the Norrie disease gene (Ndp) in developing and adult mouse eye, ear, and brain
    • Ye X, Smallwood P, Nathans J. 2011. Expression of the Norrie disease gene (Ndp) in developing and adult mouse eye, ear, and brain. Gene Expression Patterns 11:151-155. doi: 10.1016/j.gep.2010.10.007.
    • (2011) Gene Expression Patterns , vol.11 , pp. 151-155
    • Ye, X.1    Smallwood, P.2    Nathans, J.3
  • 91
    • 77956267435 scopus 로고    scopus 로고
    • The Norrin/Frizzled4 signaling pathway in retinal vascular development and disease
    • Ye X, Wang Y, Nathans J. 2010. The Norrin/Frizzled4 signaling pathway in retinal vascular development and disease. Trends in Molecular Medicine 16:417-425. doi: 10.1016/j.molmed.2010.07.003.
    • (2010) Trends in Molecular Medicine , vol.16 , pp. 417-425
    • Ye, X.1    Wang, Y.2    Nathans, J.3
  • 94
    • 84904469837 scopus 로고    scopus 로고
    • Lysosome sorting of beta-glucocerebrosidase by LIMP-2 is targeted by the mannose 6-phosphate receptor
    • Zhao Y, Ren J, Padilla-Parra S, Fry EE, Stuart DI. 2014. Lysosome sorting of beta-glucocerebrosidase by LIMP-2 is targeted by the mannose 6-phosphate receptor. Nature Communications 5:4321. doi: 10.1038/ncomms5321.
    • (2014) Nature Communications , vol.5
    • Zhao, Y.1    Ren, J.2    Padilla-Parra, S.3    Fry, E.E.4    Stuart, D.I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.