메뉴 건너뛰기




Volumn 73, Issue , 2006, Pages 97-124

Natural Triple β-Stranded Fibrous Folds1

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR; VIRUS PROTEIN;

EID: 33845648118     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(06)73004-2     Document Type: Review
Times cited : (33)

References (104)
  • 4
    • 0032848187 scopus 로고    scopus 로고
    • Folding of peptide models of collagen and misfolding in disease
    • Baum J., and Brodsky B. Folding of peptide models of collagen and misfolding in disease. Curr. Opin. Struct. Biol. 9 (1999) 122-128
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 122-128
    • Baum, J.1    Brodsky, B.2
  • 6
    • 0033584785 scopus 로고    scopus 로고
    • Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR
    • Bewley M.C., Springer K., Zhang Y.B., Freimuth P., and Flanagan J.M. Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR. Science 286 (1999) 1579-1583
    • (1999) Science , vol.286 , pp. 1579-1583
    • Bewley, M.C.1    Springer, K.2    Zhang, Y.B.3    Freimuth, P.4    Flanagan, J.M.5
  • 7
    • 0033569814 scopus 로고    scopus 로고
    • Folding of coliphage T4 short tail fiber in vitro. Analysing the role of a bacteriophage-encoded chaperone
    • Burda M.R., and Miller S. Folding of coliphage T4 short tail fiber in vitro. Analysing the role of a bacteriophage-encoded chaperone. Eur. J. Biochem. 265 (1999) 771-778
    • (1999) Eur. J. Biochem. , vol.265 , pp. 771-778
    • Burda, M.R.1    Miller, S.2
  • 8
    • 3142729320 scopus 로고    scopus 로고
    • Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites
    • Burmeister W.P., Guilligay D., Cusack S., Wadell G., and Arnberg N. Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites. J. Virol. 78 (2004) 7727-7736
    • (2004) J. Virol. , vol.78 , pp. 7727-7736
    • Burmeister, W.P.1    Guilligay, D.2    Cusack, S.3    Wadell, G.4    Arnberg, N.5
  • 9
    • 0030564888 scopus 로고    scopus 로고
    • Stoichiometry and domainal organization of the long tail-fiber of bacteriophage T4: A hinged viral adhesin
    • Cerritelli M.E., Wall J.S., Simon M.N., Conway J.F., and Steven A.C. Stoichiometry and domainal organization of the long tail-fiber of bacteriophage T4: A hinged viral adhesin. J. Mol. Biol. 260 (1996) 767-780
    • (1996) J. Mol. Biol. , vol.260 , pp. 767-780
    • Cerritelli, M.E.1    Wall, J.S.2    Simon, M.N.3    Conway, J.F.4    Steven, A.C.5
  • 10
    • 0037080985 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber
    • Chappell J.D., Prota A.E., Dermody T.S., and Stehle T. Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber. EMBO J. 21 (2002) 1-11
    • (2002) EMBO J. , vol.21 , pp. 1-11
    • Chappell, J.D.1    Prota, A.E.2    Dermody, T.S.3    Stehle, T.4
  • 11
    • 0025867101 scopus 로고
    • Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase
    • Chen B.-L., and King J. Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase. Biochemistry 30 (1991) 6260-6269
    • (1991) Biochemistry , vol.30 , pp. 6260-6269
    • Chen, B.-L.1    King, J.2
  • 12
    • 23944519950 scopus 로고    scopus 로고
    • The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats
    • Cherny I., Rockah L., Levy-Nissenbaum O., Gophna U., Ron E.Z., and Gazit E. The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats. J. Mol. Biol. 352 (2005) 245-252
    • (2005) J. Mol. Biol. , vol.352 , pp. 245-252
    • Cherny, I.1    Rockah, L.2    Levy-Nissenbaum, O.3    Gophna, U.4    Ron, E.Z.5    Gazit, E.6
  • 15
    • 0025066414 scopus 로고
    • Structure of adenovirus fibre. I. Analysis of crystals of fibre from adenovirus serotype 2 and 5 by electron microscopy and X-ray crystallography
    • Devaux C., Adrian M., Berthet-Colominas C., Cusack S., and Jacrot B. Structure of adenovirus fibre. I. Analysis of crystals of fibre from adenovirus serotype 2 and 5 by electron microscopy and X-ray crystallography. J. Mol. Biol. 215 (1990) 567-588
    • (1990) J. Mol. Biol. , vol.215 , pp. 567-588
    • Devaux, C.1    Adrian, M.2    Berthet-Colominas, C.3    Cusack, S.4    Jacrot, B.5
  • 17
    • 0024357657 scopus 로고
    • The structure of tumor necrosis factor-alpha at 2.6 A resolution. Implications for receptor binding
    • Eck M.J., and Sprang S.R. The structure of tumor necrosis factor-alpha at 2.6 A resolution. Implications for receptor binding. J. Biol. Chem. 264 (1989) 17595-17605
    • (1989) J. Biol. Chem. , vol.264 , pp. 17595-17605
    • Eck, M.J.1    Sprang, S.R.2
  • 18
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • Emsley P., Charles I.G., Fairweather N.F., and Isaacs N.W. Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature 381 (1996) 90-92
    • (1996) Nature , vol.381 , pp. 90-92
    • Emsley, P.1    Charles, I.G.2    Fairweather, N.F.3    Isaacs, N.W.4
  • 19
    • 0025904728 scopus 로고
    • The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper
    • Engel J., and Prockop D.J. The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper. Annu. Rev. Biophys. Biophys. Chem. 20 (1991) 137-152
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 137-152
    • Engel, J.1    Prockop, D.J.2
  • 23
    • 12744273899 scopus 로고    scopus 로고
    • Self-organization of short peptide fragments: From amyloid fibrils to nanoscale supramolecular assemblies
    • Gilead S., and Gazit E. Self-organization of short peptide fragments: From amyloid fibrils to nanoscale supramolecular assemblies. Supramol. Chem. 17 (2005) 87-92
    • (2005) Supramol. Chem. , vol.17 , pp. 87-92
    • Gilead, S.1    Gazit, E.2
  • 24
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed beta-helices into trimers
    • Govaerts C., Wille H., Prusiner S.B., and Cohen F.E. Evidence for assembly of prions with left-handed beta-helices into trimers. Proc. Natl. Acad. Sci. USA 101 (2004) 8342-8347
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 25
    • 0021092717 scopus 로고
    • Evidence for a repeating cross-beta sheet structure in the adenovirus fiber
    • Green N.M., Wrigley N.G., Russell W.C., Martin S.R., and McLachlan A.D. Evidence for a repeating cross-beta sheet structure in the adenovirus fiber. EMBO J. 2 (1983) 1357-1365
    • (1983) EMBO J. , vol.2 , pp. 1357-1365
    • Green, N.M.1    Wrigley, N.G.2    Russell, W.C.3    Martin, S.R.4    McLachlan, A.D.5
  • 27
    • 0027984799 scopus 로고
    • Determinants of receptor specificity of coliphages of the T4 family. A chaperone alters the host range
    • Hashemolhosseini S., Montag D., Kramer L., and Henning U. Determinants of receptor specificity of coliphages of the T4 family. A chaperone alters the host range. J. Mol. Biol. 241 (1994) 524-533
    • (1994) J. Mol. Biol. , vol.241 , pp. 524-533
    • Hashemolhosseini, S.1    Montag, D.2    Kramer, L.3    Henning, U.4
  • 28
    • 0029957949 scopus 로고    scopus 로고
    • Characterization of the helper proteins for the assembly of tail fibers of coliphages T4 and lambda
    • Hashemolhosseini S., Stierhof Y.D., Hindennach I., and Henning U. Characterization of the helper proteins for the assembly of tail fibers of coliphages T4 and lambda. J. Bacteriol. 178 (1996) 6258-6265
    • (1996) J. Bacteriol. , vol.178 , pp. 6258-6265
    • Hashemolhosseini, S.1    Stierhof, Y.D.2    Hindennach, I.3    Henning, U.4
  • 29
    • 0028567868 scopus 로고
    • De novo design of beta-sheet proteins
    • Hecht M.H. De novo design of beta-sheet proteins. Proc. Natl. Acad. Sci. USA 91 (1994) 8729-8730
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8729-8730
    • Hecht, M.H.1
  • 30
    • 0028283086 scopus 로고
    • Characterization of the knob domain of the adenovirus type 5 fiber protein expressed in Escherichia coli
    • Henry L.J., Xia D., Wilke M.E., Deisenhofer J., and Gerard R.D. Characterization of the knob domain of the adenovirus type 5 fiber protein expressed in Escherichia coli. J. Virol. 68 (1994) 5239-5246
    • (1994) J. Virol. , vol.68 , pp. 5239-5246
    • Henry, L.J.1    Xia, D.2    Wilke, M.E.3    Deisenhofer, J.4    Gerard, R.D.5
  • 32
    • 0029792292 scopus 로고    scopus 로고
    • Domains required for assembly of adenovirus type 2 fiber trimers
    • Hong J.S., and Engler J.A. Domains required for assembly of adenovirus type 2 fiber trimers. J. Virol. 70 (1996) 7071-7078
    • (1996) J. Virol. , vol.70 , pp. 7071-7078
    • Hong, J.S.1    Engler, J.A.2
  • 33
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson G., and Thornton J.M. A revised set of potentials for beta-turn formation in proteins. Prot. Sci. 3 (1994) 2207-2216
    • (1994) Prot. Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, G.1    Thornton, J.M.2
  • 34
    • 0036708477 scopus 로고    scopus 로고
    • Molecular organization of amyloid protofilament-like assembly of betabellin 15D: Helical array of beta-sandwiches
    • Inouye H., Bond J.E., Deverin S.P., Lim A., Costello C.E., and Kirschner D.A. Molecular organization of amyloid protofilament-like assembly of betabellin 15D: Helical array of beta-sandwiches. Biophys. J. 83 (2002) 1716-1727
    • (2002) Biophys. J. , vol.83 , pp. 1716-1727
    • Inouye, H.1    Bond, J.E.2    Deverin, S.P.3    Lim, A.4    Costello, C.E.5    Kirschner, D.A.6
  • 35
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez J.L., Guijarro J.I., Orlova E., Zurdo J., Dobson C.M., Sunde M., and Saibil H.R. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18 (1999) 815-821
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 36
    • 2542542833 scopus 로고    scopus 로고
    • A model for Ure2p prion filaments and other amyloids: The parallel superpleated beta-structure
    • Kajava A.V., Baxa U., Wickner R.B., and Steven A.C. A model for Ure2p prion filaments and other amyloids: The parallel superpleated beta-structure. Proc. Natl. Acad. Sci. USA 101 (2004) 7885-7890
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7885-7890
    • Kajava, A.V.1    Baxa, U.2    Wickner, R.B.3    Steven, A.C.4
  • 38
    • 0016599239 scopus 로고
    • Genetic control of bacteriophage T4 baseplate morphogenesis. III. Formation of the central plug and overall assembly pathway
    • Kikuchi Y., and King J. Genetic control of bacteriophage T4 baseplate morphogenesis. III. Formation of the central plug and overall assembly pathway. J. Mol. Biol. 99 (1975) 695-716
    • (1975) J. Mol. Biol. , vol.99 , pp. 695-716
    • Kikuchi, Y.1    King, J.2
  • 39
    • 0015243885 scopus 로고
    • Polypeptides of the tail fibres of bacteriophage T4
    • King J., and Laemmli U.K. Polypeptides of the tail fibres of bacteriophage T4. J. Mol. Biol. 62 (1971) 465-477
    • (1971) J. Mol. Biol. , vol.62 , pp. 465-477
    • King, J.1    Laemmli, U.K.2
  • 42
    • 0035043341 scopus 로고    scopus 로고
    • Genetic targeting of an adenovirus vector via replacement of the fiber protein with the phage T4 fibritin
    • Krasnykh V., Belousova N., Korokhov N., Mikheeva G., and Curiel D.T. Genetic targeting of an adenovirus vector via replacement of the fiber protein with the phage T4 fibritin. J. Virol. 75 (2001) 4176-4183
    • (2001) J. Virol. , vol.75 , pp. 4176-4183
    • Krasnykh, V.1    Belousova, N.2    Korokhov, N.3    Mikheeva, G.4    Curiel, D.T.5
  • 44
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from beta-helical protofibrils
    • Lazo N.D., and Downing D.T. Amyloid fibrils may be assembled from beta-helical protofibrils. Biochemistry 37 (1998) 1731-1735
    • (1998) Biochemistry , vol.37 , pp. 1731-1735
    • Lazo, N.D.1    Downing, D.T.2
  • 45
    • 0028191528 scopus 로고
    • The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi
    • Lietzke S.E., Yoder M.D., Keen N.T., and Jurnak F. The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi. Plant Physiol. 106 (1994) 849-862
    • (1994) Plant Physiol. , vol.106 , pp. 849-862
    • Lietzke, S.E.1    Yoder, M.D.2    Keen, N.T.3    Jurnak, F.4
  • 49
    • 0035937833 scopus 로고    scopus 로고
    • Kinetic analysis of adenovirus fiber binding to its receptor reveals an avidity mechanism for trimeric receptor-ligand interactions
    • Lortat-Jacob H., Chouin E., Cusack S., and van Raaij M.J. Kinetic analysis of adenovirus fiber binding to its receptor reveals an avidity mechanism for trimeric receptor-ligand interactions. J. Biol. Chem. 276 (2001) 9009-9015
    • (2001) J. Biol. Chem. , vol.276 , pp. 9009-9015
    • Lortat-Jacob, H.1    Chouin, E.2    Cusack, S.3    van Raaij, M.J.4
  • 50
  • 52
    • 0030936037 scopus 로고    scopus 로고
    • Isolation and characterization of a molecular chaperone, gp57A, of bacteriophage T4
    • Matsui T., Griniuviene B., Goldberg E., Tsugita A., Tanaka N., and Arisaka F. Isolation and characterization of a molecular chaperone, gp57A, of bacteriophage T4. J. Bacteriol. 179 (1997) 1846-1851
    • (1997) J. Bacteriol. , vol.179 , pp. 1846-1851
    • Matsui, T.1    Griniuviene, B.2    Goldberg, E.3    Tsugita, A.4    Tanaka, N.5    Arisaka, F.6
  • 53
    • 1942437436 scopus 로고    scopus 로고
    • A chimeric adenovirus vector encoding reovirus attachment protein sigma1 targets cells expressing junctional adhesion molecule 1
    • Mercier G.T., Campbell J.A., Chappell J.D., Stehle T., Dermody T.S., and Barry M.A. A chimeric adenovirus vector encoding reovirus attachment protein sigma1 targets cells expressing junctional adhesion molecule 1. Proc. Natl. Acad. Sci. USA 101 (2004) 6188-6193
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6188-6193
    • Mercier, G.T.1    Campbell, J.A.2    Chappell, J.D.3    Stehle, T.4    Dermody, T.S.5    Barry, M.A.6
  • 54
    • 17044438215 scopus 로고    scopus 로고
    • The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture
    • Merckel M.C., Huiskonen J.T., Bamford D.H., Goldman A., and Tuma R. The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture. Mol. Cell 18 (2005) 161-170
    • (2005) Mol. Cell , vol.18 , pp. 161-170
    • Merckel, M.C.1    Huiskonen, J.T.2    Bamford, D.H.3    Goldman, A.4    Tuma, R.5
  • 56
  • 57
    • 0001923913 scopus 로고
    • Virus taxonomy
    • Fields B.N., Knipe D.M., and Howley P.M. (Eds), Lippincott Williams & Wilkins, Philadelphia, PA
    • Murphy F.A. Virus taxonomy. In: Fields B.N., Knipe D.M., and Howley P.M. (Eds). "Fields Virology" (1995), Lippincott Williams & Wilkins, Philadelphia, PA 15-57
    • (1995) "Fields Virology" , pp. 15-57
    • Murphy, F.A.1
  • 58
    • 0024039077 scopus 로고
    • Nature's rules and chemist's tools: A way for creating novel proteins
    • Mutter M. Nature's rules and chemist's tools: A way for creating novel proteins. Trends Biochem. Sci. 13 (1988) 260-265
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 260-265
    • Mutter, M.1
  • 60
    • 0000432516 scopus 로고
    • Reoviruses and their replication
    • Fields B.N., Knipe D.M., and Howley P.M. (Eds), Lippincott Williams & Wilkins, Philadelphia, PA
    • Nibert M.L., Schiff L.A., and Fields B.N. Reoviruses and their replication. In: Fields B.N., Knipe D.M., and Howley P.M. (Eds). "Fields Virology" (1995), Lippincott Williams & Wilkins, Philadelphia, PA 1557-1596
    • (1995) "Fields Virology" , pp. 1557-1596
    • Nibert, M.L.1    Schiff, L.A.2    Fields, B.N.3
  • 61
    • 0026077319 scopus 로고
    • Deletion analysis of functional domains in baculovirus-expressed adenovirus type 2 fiber
    • Novelli A., and Boulanger P.A. Deletion analysis of functional domains in baculovirus-expressed adenovirus type 2 fiber. Virology 185 (1991) 365-376
    • (1991) Virology , vol.185 , pp. 365-376
    • Novelli, A.1    Boulanger, P.A.2
  • 62
    • 0042856841 scopus 로고    scopus 로고
    • Assembly of stable human type I and III collagen molecules from hydroxylated recombinant chains in the yeast Pichia pastoris. Effect of an engineered C-terminal oligomerization domain foldon
    • Pakkanen O., Hamalainen E.R., Kivirikko K.I., and Myllyharju J. Assembly of stable human type I and III collagen molecules from hydroxylated recombinant chains in the yeast Pichia pastoris. Effect of an engineered C-terminal oligomerization domain foldon. J. Biol. Chem. 278 (2003) 32478-32483
    • (2003) J. Biol. Chem. , vol.278 , pp. 32478-32483
    • Pakkanen, O.1    Hamalainen, E.R.2    Kivirikko, K.I.3    Myllyharju, J.4
  • 63
    • 1542275365 scopus 로고    scopus 로고
    • Formation of highly stable chimeric trimers by fusion of an adenovirus fiber shaft fragment with the foldon domain of bacteriophage t4 fibritin
    • Papanikolopoulou K., Forge V., Goeltz P., and Mitraki A. Formation of highly stable chimeric trimers by fusion of an adenovirus fiber shaft fragment with the foldon domain of bacteriophage t4 fibritin. J. Biol. Chem. 279 (2004) 8991-8998
    • (2004) J. Biol. Chem. , vol.279 , pp. 8991-8998
    • Papanikolopoulou, K.1    Forge, V.2    Goeltz, P.3    Mitraki, A.4
  • 64
    • 4143062581 scopus 로고    scopus 로고
    • Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif
    • Papanikolopoulou K., Teixeira S., Belrhali H., Forsyth V.T., Mitraki A., and van Raaij M.J. Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif. J. Mol. Biol. 342 (2004) 219-227
    • (2004) J. Mol. Biol. , vol.342 , pp. 219-227
    • Papanikolopoulou, K.1    Teixeira, S.2    Belrhali, H.3    Forsyth, V.T.4    Mitraki, A.5    van Raaij, M.J.6
  • 66
    • 76549238253 scopus 로고
    • The pleated sheet, a new layer configuration of polypeptide chains
    • Pauling L., and Corey R.B. The pleated sheet, a new layer configuration of polypeptide chains. Proc. Natl. Acad. Sci. USA 37 (1951) 251-256
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 251-256
    • Pauling, L.1    Corey, R.B.2
  • 68
    • 0031569829 scopus 로고    scopus 로고
    • The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: A right-handed parallel beta helix
    • Petersen T.N., Kauppinen S., and Larsen S. The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: A right-handed parallel beta helix. Structure 5 (1997) 533-544
    • (1997) Structure , vol.5 , pp. 533-544
    • Petersen, T.N.1    Kauppinen, S.2    Larsen, S.3
  • 69
    • 0027345601 scopus 로고
    • Assembly of bacteriophage P22: A model for ds-DNA virus assembly
    • Prevelige Jr. P.E., and King J. Assembly of bacteriophage P22: A model for ds-DNA virus assembly. Prog. Med. Virol. 40 (1993) 206-221
    • (1993) Prog. Med. Virol. , vol.40 , pp. 206-221
    • Prevelige Jr., P.E.1    King, J.2
  • 70
    • 10044264443 scopus 로고    scopus 로고
    • In vivo bypass of chaperone by extended coiled-coil motif in T4 tail fiber
    • Qu Y., Hyman P., Harrah T., and Goldberg E. In vivo bypass of chaperone by extended coiled-coil motif in T4 tail fiber. J. Bacteriol. 186 (2004) 8363-8369
    • (2004) J. Bacteriol. , vol.186 , pp. 8363-8369
    • Qu, Y.1    Hyman, P.2    Harrah, T.3    Goldberg, E.4
  • 71
    • 4143141192 scopus 로고    scopus 로고
    • Self-assembling peptides and proteins for nanotechnological applications
    • Rajagopal K., and Schneider J.P. Self-assembling peptides and proteins for nanotechnological applications. Curr. Opin. Struct. Biol. 14 (2004) 480-486
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 480-486
    • Rajagopal, K.1    Schneider, J.P.2
  • 72
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide nanotubes
    • Reches M., and Gazit E. Casting metal nanowires within discrete self-assembled peptide nanotubes. Science 300 (2003) 625-627
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 73
    • 0037022563 scopus 로고    scopus 로고
    • Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson J.S., and Richardson D.C. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. USA 99 (2002) 2754-2759
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 75
    • 0031666742 scopus 로고    scopus 로고
    • The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F
    • Roelvink P.W., Lizonova A., Lee J.G., Li Y., Bergelson J.M., Finberg R.W., Brough D.E., Kovesdi I., and Wickham T.J. The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F. J. Virol. 72 (1998) 7909-7915
    • (1998) J. Virol. , vol.72 , pp. 7909-7915
    • Roelvink, P.W.1    Lizonova, A.2    Lee, J.G.3    Li, Y.4    Bergelson, J.M.5    Finberg, R.W.6    Brough, D.E.7    Kovesdi, I.8    Wickham, T.J.9
  • 76
    • 0025028874 scopus 로고
    • Structure of adenovirus fibre. II. Morphology of single fibres
    • Ruigrok R.W., Barge A., Albiges-Rizo C., and Dayan S. Structure of adenovirus fibre. II. Morphology of single fibres. J. Mol. Biol. 215 (1990) 589-596
    • (1990) J. Mol. Biol. , vol.215 , pp. 589-596
    • Ruigrok, R.W.1    Barge, A.2    Albiges-Rizo, C.3    Dayan, S.4
  • 77
    • 0033603336 scopus 로고    scopus 로고
    • Formation of fibrous aggregates from a non-native intermediate: The isolated P22 tailspike beta-helix domain
    • Schuler B., Rachel R., and Seckler R. Formation of fibrous aggregates from a non-native intermediate: The isolated P22 tailspike beta-helix domain. J. Biol. Chem. 274 (1999) 18589-18596
    • (1999) J. Biol. Chem. , vol.274 , pp. 18589-18596
    • Schuler, B.1    Rachel, R.2    Seckler, R.3
  • 79
    • 30044442097 scopus 로고    scopus 로고
    • Lactococcal bacteriophage P2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses
    • Spinelli S., Desmyter A., Verrips C.T., de Haard H.J., Moineau S., and Cambillau C. Lactococcal bacteriophage P2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses. Nat. Struct. Mol. Biol. 13 (2006) 85-89
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 85-89
    • Spinelli, S.1    Desmyter, A.2    Verrips, C.T.3    de Haard, H.J.4    Moineau, S.5    Cambillau, C.6
  • 80
    • 0028095571 scopus 로고
    • Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer
    • Steinbacher S., Seckler R., Miller S., Steipe B., Huber R., and Reinemer P. Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer. Science 265 (1994) 383-386
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 81
    • 0029764093 scopus 로고    scopus 로고
    • Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors
    • Steinbacher S., Baxa U., Miller S., Weintraub A., Seckler R., and Huber R. Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. Proc. Natl. Acad. Sci. USA 93 (1996) 10584-10588
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10584-10588
    • Steinbacher, S.1    Baxa, U.2    Miller, S.3    Weintraub, A.4    Seckler, R.5    Huber, R.6
  • 82
    • 0031564610 scopus 로고    scopus 로고
    • Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage
    • Steinbacher S., Miller S., Baxa U., Budisa N., Weintraub A., Seckler R., and Huber R. Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage. J. Mol. Biol. 267 (1997) 865-880
    • (1997) J. Mol. Biol. , vol.267 , pp. 865-880
    • Steinbacher, S.1    Miller, S.2    Baxa, U.3    Budisa, N.4    Weintraub, A.5    Seckler, R.6    Huber, R.7
  • 83
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M., and Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50 (1997) 123-159
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 84
    • 0031570687 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain
    • Tao Y., Strelkov S.V., Mesyanzhinov V.V., and Rossmann M.G. Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain. Structure 5 (1997) 789-798
    • (1997) Structure , vol.5 , pp. 789-798
    • Tao, Y.1    Strelkov, S.V.2    Mesyanzhinov, V.V.3    Rossmann, M.G.4
  • 85
    • 0042463705 scopus 로고    scopus 로고
    • The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold
    • Thomassen E., Gielen G., Schutz M., Schoehn G., Abrahams J.P., Miller S., and van Raaij M.J. The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold. J. Mol. Biol. 331 (2003) 361-373
    • (2003) J. Mol. Biol. , vol.331 , pp. 361-373
    • Thomassen, E.1    Gielen, G.2    Schutz, M.3    Schoehn, G.4    Abrahams, J.P.5    Miller, S.6    van Raaij, M.J.7
  • 86
    • 4143137098 scopus 로고    scopus 로고
    • Beta-structured viral fibres: Assembly, structure and implications for materials design
    • van Raaij M.J., and Mitraki A. Beta-structured viral fibres: Assembly, structure and implications for materials design. Curr. Opin. Solid. State Mater Sci. 8 (2004) 151-156
    • (2004) Curr. Opin. Solid. State Mater Sci. , vol.8 , pp. 151-156
    • van Raaij, M.J.1    Mitraki, A.2
  • 87
    • 0033619203 scopus 로고    scopus 로고
    • Structure of the human adenovirus serotype 2 fiber head domain at 1.5 A resolution
    • van Raaij M.J., Louis N., Chroboczek J., and Cusack S. Structure of the human adenovirus serotype 2 fiber head domain at 1.5 A resolution. Virology 262 (1999) 333-343
    • (1999) Virology , vol.262 , pp. 333-343
    • van Raaij, M.J.1    Louis, N.2    Chroboczek, J.3    Cusack, S.4
  • 88
    • 0033613385 scopus 로고    scopus 로고
    • A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein
    • van Raaij M.J., Mitraki A., Lavigne G., and Cusack S. A triple beta-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein. Nature 401 (1999) 935-938
    • (1999) Nature , vol.401 , pp. 935-938
    • van Raaij, M.J.1    Mitraki, A.2    Lavigne, G.3    Cusack, S.4
  • 89
    • 0035861998 scopus 로고    scopus 로고
    • Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre
    • van Raaij M.J., Schoehn G., Burda M.R., and Miller S. Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre. J. Mol. Biol. 314 (2001) 1137-1146
    • (2001) J. Mol. Biol. , vol.314 , pp. 1137-1146
    • van Raaij, M.J.1    Schoehn, G.2    Burda, M.R.3    Miller, S.4
  • 90
    • 0034873491 scopus 로고    scopus 로고
    • Identification and crystallisation of a heat- and protease-stable fragment of the bacteriophage T4 short tail fibre
    • van Raaij M.J., Schoehn G., Jaquinod M., Ashman K., Burda M.R., and Miller S. Identification and crystallisation of a heat- and protease-stable fragment of the bacteriophage T4 short tail fibre. Biol. Chem. 382 (2001) 1049-1055
    • (2001) Biol. Chem. , vol.382 , pp. 1049-1055
    • van Raaij, M.J.1    Schoehn, G.2    Jaquinod, M.3    Ashman, K.4    Burda, M.R.5    Miller, S.6
  • 91
    • 0033985920 scopus 로고    scopus 로고
    • The C-terminal portion of the tail fiber protein of bacteriophage lambda is responsible for binding to LamB, its receptor at the surface of Escherichia coli K-12
    • Wang J., Hofnung M., and Charbit A. The C-terminal portion of the tail fiber protein of bacteriophage lambda is responsible for binding to LamB, its receptor at the surface of Escherichia coli K-12. J. Bacteriol. 182 (2000) 508-512
    • (2000) J. Bacteriol. , vol.182 , pp. 508-512
    • Wang, J.1    Hofnung, M.2    Charbit, A.3
  • 92
    • 0037022661 scopus 로고    scopus 로고
    • Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins
    • Wang W., and Hecht M.H. Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins. Proc. Natl. Acad. Sci. USA 99 (2002) 2760-2765
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2760-2765
    • Wang, W.1    Hecht, M.H.2
  • 93
    • 0015243884 scopus 로고
    • Assembly of bacteriophage T4 tail fibers. 3. Genetic control of the major tail fiber polypeptides
    • Ward S., and Dickson R.C. Assembly of bacteriophage T4 tail fibers. 3. Genetic control of the major tail fiber polypeptides. J. Mol. Biol. 62 (1971) 479-492
    • (1971) J. Mol. Biol. , vol.62 , pp. 479-492
    • Ward, S.1    Dickson, R.C.2
  • 94
    • 0030987357 scopus 로고    scopus 로고
    • Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 gp41 ectodomain expressed in Escherichia coli
    • Weissenhorn W., Calder L.J., Dessen A., Laue T., Skehel J.J., and Wiley D.C. Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 gp41 ectodomain expressed in Escherichia coli. Proc. Natl. Acad. Sci. USA 94 (1997) 6065-6069
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6065-6069
    • Weissenhorn, W.1    Calder, L.J.2    Dessen, A.3    Laue, T.4    Skehel, J.J.5    Wiley, D.C.6
  • 96
    • 0036052739 scopus 로고    scopus 로고
    • Ideas of order for amyloid fibril structure
    • Wetzel R. Ideas of order for amyloid fibril structure. Structure 10 (2002) 1031
    • (2002) Structure , vol.10 , pp. 1031
    • Wetzel, R.1
  • 97
    • 0028774724 scopus 로고
    • Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 Å resolution
    • Xia D., Henry L.J., Gerard R.D., and Deisenhofer J. Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 Å resolution. Structure 2 (1994) 1259-1270
    • (1994) Structure , vol.2 , pp. 1259-1270
    • Xia, D.1    Henry, L.J.2    Gerard, R.D.3    Deisenhofer, J.4
  • 98
    • 0037334514 scopus 로고    scopus 로고
    • The receptor binding protein P2 of PRD1, a virus targeting santibiotic-resistant bacteria, has a novel fold suggesting multiple functions
    • Xu L., Benson S.D., Butcher S.J., Bamford D.H., and Burnett R.M. The receptor binding protein P2 of PRD1, a virus targeting santibiotic-resistant bacteria, has a novel fold suggesting multiple functions. Structure 11 (2003) 309-322
    • (2003) Structure , vol.11 , pp. 309-322
    • Xu, L.1    Benson, S.D.2    Butcher, S.J.3    Bamford, D.H.4    Burnett, R.M.5
  • 99
    • 0036231093 scopus 로고    scopus 로고
    • Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin
    • Yang X., Lee J., Mahony E.M., Kwong P.D., Wyatt R., and Sodroski J. Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin. J. Virol. 76 (2002) 4634-4642
    • (2002) J. Virol. , vol.76 , pp. 4634-4642
    • Yang, X.1    Lee, J.2    Mahony, E.M.3    Kwong, P.D.4    Wyatt, R.5    Sodroski, J.6
  • 100
    • 12844264701 scopus 로고    scopus 로고
    • Novel electrochemical biosensing platform using self-assembled peptide nanotubes
    • Yemini M., Reches M., Rishpon J., and Gazit E. Novel electrochemical biosensing platform using self-assembled peptide nanotubes. Nano Lett. 5 (2005) 183-186
    • (2005) Nano Lett. , vol.5 , pp. 183-186
    • Yemini, M.1    Reches, M.2    Rishpon, J.3    Gazit, E.4
  • 101
    • 0029257535 scopus 로고
    • Protein motifs. 3. The parallel beta helix and other coiled folds
    • Yoder M.D., and Jurnak F. Protein motifs. 3. The parallel beta helix and other coiled folds. FASEB J. 9 (1995) 335-342
    • (1995) FASEB J. , vol.9 , pp. 335-342
    • Yoder, M.D.1    Jurnak, F.2
  • 102
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder M.D., Keen N.T., and Jurnak F. New domain motif: The structure of pectate lyase C, a secreted plant virulence factor. Science 260 (1993) 1503-1507
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 103
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • Zhang S. Fabrication of novel biomaterials through molecular self-assembly. Nat. Biotechnol. 21 (2003) 1171-1178
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 104


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.