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Volumn 277, Issue 1, 2010, Pages 106-118

Molecular basis of cytokine signalling - Theme and variations: Delivered on 8 July 2009 at the 34th FEBS Congress in Prague

Author keywords

Bone morphogenetic proteins (BMP); Drug development; Interleukins; Molecular recognition; Receptor oligomers

Indexed keywords

ACTIVIN RECEPTOR IIA; ACTIVIN RECEPTOR IIB; AEROVANT; BISPHOSPHONIC ACID DERIVATIVE; BONE MORPHOGENETIC PROTEIN 2; BONE MORPHOGENETIC PROTEIN RECEPTOR; CYTOKINE RECEPTOR; CYTOKINE RECEPTOR ANTAGONIST; HYBRID PROTEIN; INTERLEUKIN 2 RECEPTOR ALPHA; INTERLEUKIN 4; INTERLEUKIN 4 RECEPTOR ALPHA; OSTEOGENIC PROTEIN 1; PEGVISOMANT; RECOMBINANT BONE MORPHOGENETIC PROTEIN 2; RECOMBINANT ERYTHROPOIETIN; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 73649146615     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07480.x     Document Type: Conference Paper
Times cited : (5)

References (67)
  • 1
    • 2442716797 scopus 로고    scopus 로고
    • Mechanistic diversity of cytokine receptor signaling across cell membranes
    • Stroud RM Wells JA (2004) Mechanistic diversity of cytokine receptor signaling across cell membranes. Sci STKE 2004, re7.
    • (2004) Sci STKE , vol.2004 , pp. 7
    • Stroud, R.M.1    Wells, J.A.2
  • 3
    • 0035254335 scopus 로고    scopus 로고
    • Type III TGF-beta receptor-independent signalling of TGF-β2 via TβRII-B, an alternatively spliced TGF-beta type II receptor
    • Rotzer D, Roth M, Lutz M, Lindemann D, Sebald W Knaus P (2001) Type III TGF-beta receptor-independent signalling of TGF-β2 via TβRII-B, an alternatively spliced TGF-beta type II receptor. EMBO J 20, 480 490.
    • (2001) EMBO J , vol.20 , pp. 480-490
    • Rotzer, D.1    Roth, M.2    Lutz, M.3    Lindemann, D.4    Sebald, W.5    Knaus, P.6
  • 4
    • 34247899117 scopus 로고    scopus 로고
    • Three is better than one: Pre-ligand receptor assembly in the regulation of TNF receptor signaling
    • Chan FK (2007) Three is better than one: pre-ligand receptor assembly in the regulation of TNF receptor signaling. Cytokine 37, 101 107.
    • (2007) Cytokine , vol.37 , pp. 101-107
    • Chan, F.K.1
  • 5
    • 65749108703 scopus 로고    scopus 로고
    • Chapter 5. Multiple approaches to the study of chemokine receptor homo- and heterodimerization
    • Rodriguez-Frade J, Munoz LM Mellado M (2009) Chapter 5. Multiple approaches to the study of chemokine receptor homo- and heterodimerization. Methods Enzymol 461, 105 122.
    • (2009) Methods Enzymol , vol.461 , pp. 105-122
    • Rodriguez-Frade, J.1    Munoz, L.M.2    Mellado, M.3
  • 6
    • 0023686033 scopus 로고
    • Signal transduction by allosteric receptor oligomerization
    • Schlessinger J (1988) Signal transduction by allosteric receptor oligomerization. Trends Biochem Sci 13, 443 447. (Pubitemid 18264445)
    • (1988) Trends in Biochemical Sciences , vol.13 , Issue.11 , pp. 443-447
    • Schlessinger, J.1
  • 7
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham BC, Ultsch M, De Vos AM, Mulkerrin MG, Clauser KR Wells JA (1991) Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254, 821 825. (Pubitemid 21917402)
    • (1991) Science , vol.254 , Issue.5033 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    De Vos, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 9
    • 0037064548 scopus 로고    scopus 로고
    • Structure, binding, and antagonists in the IL-4/IL-13 receptor system
    • Mueller TD, Zhang JL, Sebald W Duschl A (2002) Structure, binding, and antagonists in the IL-4/IL-13 receptor system. Biochim Biophys Acta 1592, 237 250.
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 237-250
    • Mueller, T.D.1    Zhang, J.L.2    Sebald, W.3    Duschl, A.4
  • 10
    • 0034683059 scopus 로고    scopus 로고
    • The interleukin-4-receptor: From recognition mechanism to pharmacological target structure
    • Reinemer P, Sebald W Duschl A (2000) The interleukin-4-receptor: from recognition mechanism to pharmacological target structure. Angew Chem Int Ed Engl 39, 2834 2846.
    • (2000) Angew Chem Int Ed Engl , vol.39 , pp. 2834-2846
    • Reinemer, P.1    Sebald, W.2    Duschl, A.3
  • 12
    • 33646749327 scopus 로고    scopus 로고
    • Structure of the ternary signaling complex of a TGF-β superfamily member
    • Allendorph GP, Vale WW Choe S (2006) Structure of the ternary signaling complex of a TGF-β superfamily member. Proc Natl Acad Sci USA 103, 7643 7648.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7643-7648
    • Allendorph, G.P.1    Vale, W.W.2    Choe, S.3
  • 13
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos AM, Ultsch M Kossiakoff AA (1992) Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306 312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 16
    • 0033574713 scopus 로고    scopus 로고
    • Crystal structure of the interleukin-4/receptor α chain complex reveals a mosaic binding interface
    • Hage T, Sebald W Reinemer P (1999) Crystal structure of the interleukin-4/receptor α chain complex reveals a mosaic binding interface. Cell 97, 271 281.
    • (1999) Cell , vol.97 , pp. 271-281
    • Hage, T.1    Sebald, W.2    Reinemer, P.3
  • 17
    • 0032188943 scopus 로고    scopus 로고
    • The interleukin-4 site-2 epitope determining binding of the common receptor γ chain
    • Letzelter F, Wang Y Sebald W (1998) The interleukin-4 site-2 epitope determining binding of the common receptor γ chain. Eur J Biochem 257, 11 20. (Pubitemid 28462575)
    • (1998) European Journal of Biochemistry , vol.257 , Issue.1 , pp. 11-20
    • Letzelter, F.1    Wang, Y.2    Sebald, W.3
  • 18
    • 33745227715 scopus 로고    scopus 로고
    • A modular interface of IL-4 allows for scalable affinity without affecting specificity for the IL-4 receptor
    • Kraich M, Klein M, Patino E, Harrer H, Nickel J, Sebald W Mueller TD (2006) A modular interface of IL-4 allows for scalable affinity without affecting specificity for the IL-4 receptor. BMC Biol 4, 13.
    • (2006) BMC Biol , vol.4 , pp. 13
    • Kraich, M.1    Klein, M.2    Patino, E.3    Harrer, H.4    Nickel, J.5    Sebald, W.6    Mueller, T.D.7
  • 19
    • 27944505913 scopus 로고    scopus 로고
    • Structure of the quaternary complex of interleukin-2 with its α, β, and γc receptors
    • Wang X, Rickert M Garcia KC (2005) Structure of the quaternary complex of interleukin-2 with its α, β, and γc receptors. Science 310, 1159 1163.
    • (2005) Science , vol.310 , pp. 1159-1163
    • Wang, X.1    Rickert, M.2    Garcia, K.C.3
  • 20
    • 4544286802 scopus 로고    scopus 로고
    • Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction
    • Sebald W, Nickel J, Zhang JL Mueller TD (2004) Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction. Biol Chem 385, 697 710.
    • (2004) Biol Chem , vol.385 , pp. 697-710
    • Sebald, W.1    Nickel, J.2    Zhang, J.L.3    Mueller, T.D.4
  • 21
    • 34547124340 scopus 로고    scopus 로고
    • Repulsive guidance molecule RGMa alters utilization of bone morphogenetic protein (BMP) type II receptors by BMP2 and BMP4
    • Xia Y, Yu PB, Sidis Y, Beppu H, Bloch KD, Schneyer AL Lin HY (2007) Repulsive guidance molecule RGMa alters utilization of bone morphogenetic protein (BMP) type II receptors by BMP2 and BMP4. J Biol Chem 282, 18129 18140.
    • (2007) J Biol Chem , vol.282 , pp. 18129-18140
    • Xia, Y.1    Yu, P.B.2    Sidis, Y.3    Beppu, H.4    Bloch, K.D.5    Schneyer, A.L.6    Lin, H.Y.7
  • 22
    • 0037424231 scopus 로고    scopus 로고
    • Inhibin is an antagonist of bone morphogenetic protein signaling
    • Wiater E Vale W (2003) Inhibin is an antagonist of bone morphogenetic protein signaling. J Biol Chem 278, 7934 7941.
    • (2003) J Biol Chem , vol.278 , pp. 7934-7941
    • Wiater, E.1    Vale, W.2
  • 23
    • 33745195026 scopus 로고    scopus 로고
    • Identification of distinct inhibin and transforming growth factor β-binding sites on betaglycan: Functional separation of betaglycan co-receptor actions
    • Wiater E, Harrison CA, Lewis KA, Gray PC Vale WW (2006) Identification of distinct inhibin and transforming growth factor β-binding sites on betaglycan: functional separation of betaglycan co-receptor actions. J Biol Chem 281, 17011 17022.
    • (2006) J Biol Chem , vol.281 , pp. 17011-17022
    • Wiater, E.1    Harrison, C.A.2    Lewis, K.A.3    Gray, P.C.4    Vale, W.W.5
  • 24
    • 0034021776 scopus 로고    scopus 로고
    • Bone morphogenetic protein receptor complexes on the surface of live cells: A new oligomerization mode for serine/threonine kinase receptors
    • Gilboa L, Nohe A, Geissendorfer T, Sebald W, Henis YI Knaus P (2000) Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors. Mol Biol Cell 11, 1023 1035.
    • (2000) Mol Biol Cell , vol.11 , pp. 1023-1035
    • Gilboa, L.1    Nohe, A.2    Geissendorfer, T.3    Sebald, W.4    Henis, Y.I.5    Knaus, P.6
  • 25
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Conte LL, Chothia C Janin J (1999) The atomic structure of protein-protein recognition sites. J Mol Biol 285, 2177 2198.
    • (1999) J Mol Biol , vol.285 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 26
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T Wells JA (1995) A hot spot of binding energy in a hormone-receptor interface. Science 267, 383 386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 27
    • 0027132013 scopus 로고
    • Comparison of a structural and a functional epitope
    • Cunningham BC Wells JA (1993) Comparison of a structural and a functional epitope. J Mol Biol 234, 554 563.
    • (1993) J Mol Biol , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 28
    • 0036300916 scopus 로고    scopus 로고
    • The high-affinity interaction of human IL-4 and the receptor α chain is constituted by two independent binding clusters
    • Zhang JL, Simeonowa I, Wang Y Sebald W (2002) The high-affinity interaction of human IL-4 and the receptor α chain is constituted by two independent binding clusters. J Mol Biol 315, 399 407.
    • (2002) J Mol Biol , vol.315 , pp. 399-407
    • Zhang, J.L.1    Simeonowa, I.2    Wang, Y.3    Sebald, W.4
  • 29
    • 0031048778 scopus 로고    scopus 로고
    • A mixed-charge pair in human interleukin 4 dominates high-affinity interaction with the receptor α chain
    • Wang Y, Shen BJ Sebald W (1997) A mixed-charge pair in human interleukin 4 dominates high-affinity interaction with the receptor α chain. Proc Natl Acad Sci USA 94, 1657 1662.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1657-1662
    • Wang, Y.1    Shen, B.J.2    Sebald, W.3
  • 30
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan AA Thorn KS (1998) Anatomy of hot spots in protein interfaces. J Mol Biol 280, 1 9.
    • (1998) J Mol Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 31
    • 0028291136 scopus 로고
    • Receptor binding properties of four-helix-bundle growth factors deduced from electrostatic analysis
    • Demchuk E, Mueller T, Oschkinat H, Sebald W Wade RC (1994) Receptor binding properties of four-helix-bundle growth factors deduced from electrostatic analysis. Protein Sci 3, 920 935.
    • (1994) Protein Sci , vol.3 , pp. 920-935
    • Demchuk, E.1    Mueller, T.2    Oschkinat, H.3    Sebald, W.4    Wade, R.C.5
  • 32
    • 17744386517 scopus 로고    scopus 로고
    • Structure of the complete extracellular domain of the common β subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration
    • Carr PD, Gustin SE, Church AP, Murphy JM, Ford SC, Mann DA, Woltring DM, Walker I, Ollis DL Young IG (2001) Structure of the complete extracellular domain of the common β subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration. Cell 104, 291 300.
    • (2001) Cell , vol.104 , pp. 291-300
    • Carr, P.D.1    Gustin, S.E.2    Church, A.P.3    Murphy, J.M.4    Ford, S.C.5    Mann, D.A.6    Woltring, D.M.7    Walker, I.8    Ollis, D.L.9    Young, I.G.10
  • 33
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling from cell membrane to the nucleus
    • Shi Y Massague J (2003) Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 113, 685 700.
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 34
    • 20344385511 scopus 로고    scopus 로고
    • A single residue of GDF-5 defines binding specificity to BMP receptor IB
    • Nickel J, Kotzsch A, Sebald W Mueller TD (2005) A single residue of GDF-5 defines binding specificity to BMP receptor IB. J Mol Biol 349, 933 947.
    • (2005) J Mol Biol , vol.349 , pp. 933-947
    • Nickel, J.1    Kotzsch, A.2    Sebald, W.3    Mueller, T.D.4
  • 36
    • 65449189690 scopus 로고    scopus 로고
    • Crystal structure analysis reveals a spring-loaded latch as molecular mechanism for GDF-5-type i receptor specificity
    • Kotzsch A, Nickel J, Seher A, Sebald W Muller TD (2009) Crystal structure analysis reveals a spring-loaded latch as molecular mechanism for GDF-5-type I receptor specificity. EMBO J 28, 937 947.
    • (2009) EMBO J , vol.28 , pp. 937-947
    • Kotzsch, A.1    Nickel, J.2    Seher, A.3    Sebald, W.4    Muller, T.D.5
  • 37
    • 0242668869 scopus 로고    scopus 로고
    • Bone morphogenetic proteins, their antagonists, and the skeleton
    • Canalis E, Economides AN Gazzerro E (2003) Bone morphogenetic proteins, their antagonists, and the skeleton. Endocr Rev 24, 218 235.
    • (2003) Endocr Rev , vol.24 , pp. 218-235
    • Canalis, E.1    Economides, A.N.2    Gazzerro, E.3
  • 38
    • 0036399170 scopus 로고    scopus 로고
    • Extracellular regulation of BMP signaling in vertebrates: A cocktail of modulators
    • Balemans W Van Hul W (2002) Extracellular regulation of BMP signaling in vertebrates: a cocktail of modulators. Dev Biol 250, 231 250.
    • (2002) Dev Biol , vol.250 , pp. 231-250
    • Balemans, W.1    Van Hul, W.2
  • 39
    • 0037012541 scopus 로고    scopus 로고
    • Chordin-like CR domains and the regulation of evolutionarily conserved extracellular signaling systems
    • Garcia Abreu J, Coffinier C, Larrain J, Oelgeschlager M De Robertis EM (2002) Chordin-like CR domains and the regulation of evolutionarily conserved extracellular signaling systems. Gene 287, 39 47.
    • (2002) Gene , vol.287 , pp. 39-47
    • Garcia Abreu, J.1    Coffinier, C.2    Larrain, J.3    Oelgeschlager, M.4    De Robertis, E.M.5
  • 40
    • 8444237836 scopus 로고    scopus 로고
    • Dorsal-ventral patterning and neural induction in Xenopus embryos
    • De Robertis EM Kuroda H (2004) Dorsal-ventral patterning and neural induction in Xenopus embryos. Annu Rev Cell Dev Biol 20, 285 308.
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 285-308
    • De Robertis, E.M.1    Kuroda, H.2
  • 41
    • 34547117636 scopus 로고    scopus 로고
    • Von Willebrand factor type C domain-containing proteins regulate bone morphogenetic protein signaling through different recognition mechanisms
    • Zhang JL, Huang Y, Qiu LY, Nickel J Sebald W (2007) von Willebrand factor type C domain-containing proteins regulate bone morphogenetic protein signaling through different recognition mechanisms. J Biol Chem 282, 20002 20014.
    • (2007) J Biol Chem , vol.282 , pp. 20002-20014
    • Zhang, J.L.1    Huang, Y.2    Qiu, L.Y.3    Nickel, J.4    Sebald, W.5
  • 42
    • 33645542833 scopus 로고    scopus 로고
    • Crossveinless 2 is an essential positive feedback regulator of Bmp signaling during zebrafish gastrulation
    • Rentzsch F, Zhang J, Kramer C, Sebald W Hammerschmidt M (2006) Crossveinless 2 is an essential positive feedback regulator of Bmp signaling during zebrafish gastrulation. Development 133, 801 811.
    • (2006) Development , vol.133 , pp. 801-811
    • Rentzsch, F.1    Zhang, J.2    Kramer, C.3    Sebald, W.4    Hammerschmidt, M.5
  • 45
    • 38749115086 scopus 로고    scopus 로고
    • Novel erythropoiesis-stimulating agents: A new era in anemia management
    • Macdougall IC (2008) Novel erythropoiesis-stimulating agents: a new era in anemia management. Clin J Am Soc Nephrol 3, 200 207.
    • (2008) Clin J Am Soc Nephrol , vol.3 , pp. 200-207
    • MacDougall, I.C.1
  • 52
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member
    • McPherron AC, Lawler AM Lee SJ (1997) Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member. Nature 387, 83 90.
    • (1997) Nature , vol.387 , pp. 83-90
    • McPherron, A.C.1    Lawler, A.M.2    Lee, S.J.3
  • 53
    • 0035979253 scopus 로고    scopus 로고
    • Regulation of myostatin activity and muscle growth
    • Lee SJ McPherron AC (2001) Regulation of myostatin activity and muscle growth. Proc Natl Acad Sci USA 98, 9306 9311.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9306-9311
    • Lee, S.J.1    McPherron, A.C.2
  • 55
    • 35348909044 scopus 로고    scopus 로고
    • Effect of an interleukin-4 variant on late phase asthmatic response to allergen challenge in asthmatic patients: Results of two phase 2a studies
    • Wenzel S, Wilbraham D, Fuller R, Getz EB Longphre M (2007) Effect of an interleukin-4 variant on late phase asthmatic response to allergen challenge in asthmatic patients: results of two phase 2a studies. Lancet 370, 1422 1431.
    • (2007) Lancet , vol.370 , pp. 1422-1431
    • Wenzel, S.1    Wilbraham, D.2    Fuller, R.3    Getz, E.B.4    Longphre, M.5
  • 56
    • 53949088064 scopus 로고    scopus 로고
    • Growth hormone excess and the development of growth hormone receptor antagonists
    • Higham CE Trainer PJ (2008) Growth hormone excess and the development of growth hormone receptor antagonists. Exp Physiol 93, 1157 1169.
    • (2008) Exp Physiol , vol.93 , pp. 1157-1169
    • Higham, C.E.1    Trainer, P.J.2
  • 57
    • 0026731478 scopus 로고
    • Conversion of human interleukin-4 into a high affinity antagonist by a single amino acid replacement
    • Kruse N, Tony HP Sebald W (1992) Conversion of human interleukin-4 into a high affinity antagonist by a single amino acid replacement. EMBO J 11, 3237 3244.
    • (1992) EMBO J , vol.11 , pp. 3237-3244
    • Kruse, N.1    Tony, H.P.2    Sebald, W.3
  • 58
    • 0028126979 scopus 로고
    • Design of human interleukin-4 antagonists inhibiting interleukin-4- dependent and interleukin-13-dependent responses in T-cells and B-cells with high efficiency
    • Tony HP, Shen BJ, Reusch P Sebald W (1994) Design of human interleukin-4 antagonists inhibiting interleukin-4-dependent and interleukin-13-dependent responses in T-cells and B-cells with high efficiency. Eur J Biochem 225, 659 665.
    • (1994) Eur J Biochem , vol.225 , pp. 659-665
    • Tony, H.P.1    Shen, B.J.2    Reusch, P.3    Sebald, W.4
  • 59
    • 0032522641 scopus 로고    scopus 로고
    • An antagonistic IL-4 mutant prevents type i allergy in the mouse: Inhibition of the IL-4/IL-13 receptor system completely abrogates humoral immune response to allergen and development of allergic symptoms in vivo
    • Grunewald SM, Werthmann A, Schnarr B, Klein CE, Brocker EB, Mohrs M, Brombacher F, Sebald W Duschl A (1998) An antagonistic IL-4 mutant prevents type I allergy in the mouse: inhibition of the IL-4/IL-13 receptor system completely abrogates humoral immune response to allergen and development of allergic symptoms in vivo. J Immunol 160, 4004 4009.
    • (1998) J Immunol , vol.160 , pp. 4004-4009
    • Grunewald, S.M.1    Werthmann, A.2    Schnarr, B.3    Klein, C.E.4    Brocker, E.B.5    Mohrs, M.6    Brombacher, F.7    Sebald, W.8    Duschl, A.9
  • 62
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin MR Wells JA (2004) Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 3, 301 317.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 64
    • 33748658250 scopus 로고    scopus 로고
    • Interstrand interactions between side chains in a double-helical foldamer
    • Haldar D, Jiang H, Leger JM Huc I (2006) Interstrand interactions between side chains in a double-helical foldamer. Angew Chem Int Ed Engl 45, 5483 5486.
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 5483-5486
    • Haldar, D.1    Jiang, H.2    Leger, J.M.3    Huc, I.4
  • 65
    • 4143087237 scopus 로고    scopus 로고
    • Beyond de novo protein design -de novo design of non-natural folded oligomers
    • Cheng RP (2004) Beyond de novo protein design -de novo design of non-natural folded oligomers. Curr Opin Struct Biol 14, 512 520.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 512-520
    • Cheng, R.P.1
  • 66
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells JA McClendon CL (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450, 1001 1009.
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 67
    • 0028524625 scopus 로고
    • Antagonist design through forced electrostatic mismatch
    • Muller T, Sebald W Oschkinat H (1994) Antagonist design through forced electrostatic mismatch. Nat Struct Biol 1, 674 676.
    • (1994) Nat Struct Biol , vol.1 , pp. 674-676
    • Muller, T.1    Sebald, W.2    Oschkinat, H.3


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