메뉴 건너뛰기




Volumn 170, Issue 2, 2010, Pages 202-215

A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

Author keywords

Bacterial cytoskeleton; Coiled coil; FilP; Scy; Sequence repeat; Streptomyces

Indexed keywords

BACTERIAL PROTEIN; CYTOSKELETON PROTEIN;

EID: 77951979336     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.02.008     Document Type: Article
Times cited : (28)

References (84)
  • 2
    • 0346020436 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: an intermediate filament-like function in cell shape
    • Ausmees N., Kuhn J.R., Jacobs-Wagner C. The bacterial cytoskeleton: an intermediate filament-like function in cell shape. Cell 2003, 115:705-713.
    • (2003) Cell , vol.115 , pp. 705-713
    • Ausmees, N.1    Kuhn, J.R.2    Jacobs-Wagner, C.3
  • 3
    • 54249099195 scopus 로고    scopus 로고
    • Intermediate filament-like proteins in bacteria and a cytoskeletal function in Streptomyces
    • Bagchi S., Tomenius H., Belova L.M., Ausmees N. Intermediate filament-like proteins in bacteria and a cytoskeletal function in Streptomyces. Mol. Microbiol. 2008, 70:1037-1050.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1037-1050
    • Bagchi, S.1    Tomenius, H.2    Belova, L.M.3    Ausmees, N.4
  • 5
    • 46349105337 scopus 로고    scopus 로고
    • Probing the functional tolerance of the b subunit of Escherichia coli ATP synthase for sequence manipulation through a chimera approach
    • Bi Y., Watts J.C., Bamford P.K., Briere L.K., Dunn S.D. Probing the functional tolerance of the b subunit of Escherichia coli ATP synthase for sequence manipulation through a chimera approach. Biochim. Biophys. Acta 2008, 1777:583-591.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 583-591
    • Bi, Y.1    Watts, J.C.2    Bamford, P.K.3    Briere, L.K.4    Dunn, S.D.5
  • 7
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani D.W., Rogers D.P., Engler J.A., Brouillette C.G. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. USA 1997, 94:12291-12296.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 8
    • 33748256486 scopus 로고    scopus 로고
    • The regulation of myosin II in Dictyostelium
    • Bosgraaf L., van Haastert P.J. The regulation of myosin II in Dictyostelium. Eur. J. Cell Biol. 2006, 85:969-979.
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 969-979
    • Bosgraaf, L.1    van Haastert, P.J.2
  • 9
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in α-helical coiled coils: stutters and stammers
    • Brown J.H., Cohen C., Parry A.D. Heptad breaks in α-helical coiled coils: stutters and stammers. Proteins Struct. Funct. Genet. 1996, 26:134-145.
    • (1996) Proteins Struct. Funct. Genet. , vol.26 , pp. 134-145
    • Brown, J.H.1    Cohen, C.2    Parry, A.D.3
  • 11
    • 35948967558 scopus 로고    scopus 로고
    • Skin and bones: the bacterial cytoskeleton, cell wall, and cell morphogenesis
    • Cabeen M.T., Jacobs-Wagner C. Skin and bones: the bacterial cytoskeleton, cell wall, and cell morphogenesis. J. Cell Biol. 2007, 179:381-387.
    • (2007) J. Cell Biol. , vol.179 , pp. 381-387
    • Cabeen, M.T.1    Jacobs-Wagner, C.2
  • 12
    • 65449137972 scopus 로고    scopus 로고
    • Bacterial intermediate filaments: in vivo assembly, organization, and dynamics of crescentin
    • Charbon G., Cabeen M.T., Jacobs-Wagner C. Bacterial intermediate filaments: in vivo assembly, organization, and dynamics of crescentin. Genes Dev. 2009, 23:1131-1144.
    • (2009) Genes Dev. , vol.23 , pp. 1131-1144
    • Charbon, G.1    Cabeen, M.T.2    Jacobs-Wagner, C.3
  • 13
    • 0000920828 scopus 로고
    • The packing of α-helices: simple coiled-coils
    • Crick F.H.C. The packing of α-helices: simple coiled-coils. Acta Crystallogr. 1953, 6:689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 15
    • 0037188394 scopus 로고    scopus 로고
    • The second stalk of Escherichia coli ATP synthase: structure of the isolated dimerization domain
    • Del Rizzo P.A., Bi Y., Dunn S.D., Shilton B.H. The second stalk of Escherichia coli ATP synthase: structure of the isolated dimerization domain. Biochemistry 2002, 41:6875-6884.
    • (2002) Biochemistry , vol.41 , pp. 6875-6884
    • Del Rizzo, P.A.1    Bi, Y.2    Dunn, S.D.3    Shilton, B.H.4
  • 16
    • 33750951013 scopus 로고    scopus 로고
    • ATP synthase b subunit dimerization domain: a right-handed coiled coil with offset helices
    • Del Rizzo P.A., Bi Y., Dunn S.D. ATP synthase b subunit dimerization domain: a right-handed coiled coil with offset helices. J. Mol. Biol. 2006, 364:735-746.
    • (2006) J. Mol. Biol. , vol.364 , pp. 735-746
    • Del Rizzo, P.A.1    Bi, Y.2    Dunn, S.D.3
  • 17
    • 0035999986 scopus 로고    scopus 로고
    • An HMM model for coiled-coil domains and a comparison with PSSM-based predictions
    • Delorenzi M., Speed T. An HMM model for coiled-coil domains and a comparison with PSSM-based predictions. Bioinformatics 2002, 18:617-625.
    • (2002) Bioinformatics , vol.18 , pp. 617-625
    • Delorenzi, M.1    Speed, T.2
  • 18
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004, 32:1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 19
    • 0030876575 scopus 로고    scopus 로고
    • The Bacillus subtilis DivIVA protein targets to the division septum and controls the site specificity of cell division
    • Edwards D.H., Errington J. The Bacillus subtilis DivIVA protein targets to the division septum and controls the site specificity of cell division. Mol. Microbiol. 1997, 24:905-915.
    • (1997) Mol. Microbiol. , vol.24 , pp. 905-915
    • Edwards, D.H.1    Errington, J.2
  • 20
    • 0034212381 scopus 로고    scopus 로고
    • Promiscuous targeting of Bacillus subtilis cell division protein DivIVA to division sites in Escherichia coli and fission yeast
    • Edwards D.H., Thomaides H.B., Errington J. Promiscuous targeting of Bacillus subtilis cell division protein DivIVA to division sites in Escherichia coli and fission yeast. EMBO J. 2000, 19:2719-2727.
    • (2000) EMBO J. , vol.19 , pp. 2719-2727
    • Edwards, D.H.1    Thomaides, H.B.2    Errington, J.3
  • 23
    • 0024412074 scopus 로고
    • Streptococcal M protein: molecular design and biological behavior
    • Fischetti V.A. Streptococcal M protein: molecular design and biological behavior. Clin. Microbiol. Rev. 1989, 2:285-314.
    • (1989) Clin. Microbiol. Rev. , vol.2 , pp. 285-314
    • Fischetti, V.A.1
  • 24
    • 0141789744 scopus 로고    scopus 로고
    • Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3(2)
    • Flardh K. Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3(2). Mol. Microbiol. 2003, 49:1523-1536.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1523-1536
    • Flardh, K.1
  • 26
    • 16944363590 scopus 로고    scopus 로고
    • Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism
    • Gonzalez L., Brown R.A., Richardson D., Alber T. Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism. Nat. Struct. Biol. 1996, 3:1002-1010.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1002-1010
    • Gonzalez, L.1    Brown, R.A.2    Richardson, D.3    Alber, T.4
  • 27
    • 16944366990 scopus 로고    scopus 로고
    • Buried polar residues and structural specificity in the GCN4 leucine zipper
    • Gonzalez L., Woolfson D.N., Alber T. Buried polar residues and structural specificity in the GCN4 leucine zipper. Nat. Struct. Biol. 1996, 3:1011-1018.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1011-1018
    • Gonzalez, L.1    Woolfson, D.N.2    Alber, T.3
  • 28
    • 0029974730 scopus 로고    scopus 로고
    • An engineered allosteric switch in leucine-zipper oligomerization
    • Gonzalez L., Plecs J.J., Alber T. An engineered allosteric switch in leucine-zipper oligomerization. Nat. Struct. Biol. 1996, 3:510-515.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 510-515
    • Gonzalez, L.1    Plecs, J.J.2    Alber, T.3
  • 29
    • 0344628627 scopus 로고    scopus 로고
    • Historical review: another 50th anniversary - new periodicities in coiled coils
    • Gruber M., Lupas A.N. Historical review: another 50th anniversary - new periodicities in coiled coils. Trends Biochem. Sci. 2003, 28:679-685.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 679-685
    • Gruber, M.1    Lupas, A.N.2
  • 31
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P.B., Zhang T., Kim P.S., Alber T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 1993, 262:1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 32
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury P.B., Kim P.S., Alber T. Crystal structure of an isoleucine-zipper trimer. Nature 1994, 371:80-83.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 33
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann H., Aebi U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 2004, 73:749-789.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 34
    • 0030624409 scopus 로고    scopus 로고
    • Coiled-coil assembly by peptides with non-heptad sequence motifs
    • Hicks M.R., Holberton D.V., Kowalczyk C., Woolfson D.N. Coiled-coil assembly by peptides with non-heptad sequence motifs. Fold. Des. 1997, 2:149-158.
    • (1997) Fold. Des. , vol.2 , pp. 149-158
    • Hicks, M.R.1    Holberton, D.V.2    Kowalczyk, C.3    Woolfson, D.N.4
  • 35
    • 0034669051 scopus 로고    scopus 로고
    • Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins
    • Hoiczyk E., Roggenkamp A., Reichenbecher M., Lupas A., Heesemann J. Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. EMBO J. 2000, 19:5989-5999.
    • (2000) EMBO J. , vol.19 , pp. 5989-5999
    • Hoiczyk, E.1    Roggenkamp, A.2    Reichenbecher, M.3    Lupas, A.4    Heesemann, J.5
  • 36
    • 0024279637 scopus 로고
    • Segmented α-helical coiled-coil structure of the protein giardin from the Giardia cytoskeleton
    • Holberton D., Baker D.A., Marshall J. Segmented α-helical coiled-coil structure of the protein giardin from the Giardia cytoskeleton. J. Mol. Biol. 1988, 204:789-795.
    • (1988) J. Mol. Biol. , vol.204 , pp. 789-795
    • Holberton, D.1    Baker, D.A.2    Marshall, J.3
  • 37
    • 45849114753 scopus 로고    scopus 로고
    • Structure of the cytosolic part of the subunit b-dimer of Escherichia coli F0F1-ATP synthase
    • Hornung T., Volkov O.A., Zaida T.M., Delannoy S., Wise J.G., Vogel P.D. Structure of the cytosolic part of the subunit b-dimer of Escherichia coli F0F1-ATP synthase. Biophys. J. 2008, 94:5053-5064.
    • (2008) Biophys. J. , vol.94 , pp. 5053-5064
    • Hornung, T.1    Volkov, O.A.2    Zaida, T.M.3    Delannoy, S.4    Wise, J.G.5    Vogel, P.D.6
  • 38
    • 70249116807 scopus 로고    scopus 로고
    • Actin dynamics at the leading edge: from simple machinery to complex networks
    • Insall R.H., Machesky L.M. Actin dynamics at the leading edge: from simple machinery to complex networks. Dev. Cell 2009, 17:310-322.
    • (2009) Dev. Cell , vol.17 , pp. 310-322
    • Insall, R.H.1    Machesky, L.M.2
  • 39
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova G., Pidoux J., Ullmann A., Ladant D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. USA 1998, 95:5752-5756.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 41
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.2
  • 42
    • 42549130004 scopus 로고    scopus 로고
    • DivIVA is required for polar growth in the MreB-lacking rod-shaped actinomycete Corynebacterium glutamicum
    • Letek M., Ordonez E., Vaquera J., Margolin W., Flardh K., Mateos L.M., Gil J.A. DivIVA is required for polar growth in the MreB-lacking rod-shaped actinomycete Corynebacterium glutamicum. J. Bacteriol. 2008, 190:3283-3292.
    • (2008) J. Bacteriol. , vol.190 , pp. 3283-3292
    • Letek, M.1    Ordonez, E.2    Vaquera, J.3    Margolin, W.4    Flardh, K.5    Mateos, L.M.6    Gil, J.A.7
  • 43
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: exploring protein sequences for globularity and disorder
    • Linding R., Russell R.B., Neduva V., Gibson T.J. GlobPlot: exploring protein sequences for globularity and disorder. Nucleic Acids Res. 2003, 31:3701-3708.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 44
    • 17444425670 scopus 로고    scopus 로고
    • PM2, a group 3 LEA protein from soybean, and its 22-mer repeating region confer salt tolerance in Escherichia coli
    • Liu Y., Zheng Y. PM2, a group 3 LEA protein from soybean, and its 22-mer repeating region confer salt tolerance in Escherichia coli. Biochem. Biophys. Res. Commun. 2005, 331:325-332.
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 325-332
    • Liu, Y.1    Zheng, Y.2
  • 45
    • 56949093012 scopus 로고    scopus 로고
    • Evolution of cytomotive filaments: the cytoskeleton from prokaryotes to eukaryotes
    • Löwe J., Amos L.A. Evolution of cytomotive filaments: the cytoskeleton from prokaryotes to eukaryotes. Int. J. Biochem. Cell Biol. 2009, 41:323-329.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 323-329
    • Löwe, J.1    Amos, L.A.2
  • 46
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: new structures and new functions
    • Lupas A. Coiled coils: new structures and new functions. Trends Biochem. Sci. 1996, 21:375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 47
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A., Van Dyke M., Stock J. Predicting coiled coils from protein sequences. Science 1991, 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 48
    • 0028987628 scopus 로고
    • Model structure of the Ompα rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacterium Thermotoga maritima
    • Lupas A., Müller S., Goldie K., Engel M., Engel A., Baumeister W. Model structure of the Ompα rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacterium Thermotoga maritima. J. Mol. Biol. 1995, 248:180-189.
    • (1995) J. Mol. Biol. , vol.248 , pp. 180-189
    • Lupas, A.1    Müller, S.2    Goldie, K.3    Engel, M.4    Engel, A.5    Baumeister, W.6
  • 49
    • 0027157011 scopus 로고
    • Sequence and structure of a new coiled coil protein from a microtubule bundle in Giardia
    • Marshall J., Holberton D.V. Sequence and structure of a new coiled coil protein from a microtubule bundle in Giardia. J. Mol. Biol. 1993, 231:521-530.
    • (1993) J. Mol. Biol. , vol.231 , pp. 521-530
    • Marshall, J.1    Holberton, D.V.2
  • 50
    • 0029099085 scopus 로고
    • Giardia gene predicts a 183 kDa nucleotide-binding head-stalk protein
    • Marshall J., Holberton D.V. Giardia gene predicts a 183 kDa nucleotide-binding head-stalk protein. J. Cell Sci. 1995, 108:2683-2692.
    • (1995) J. Cell Sci. , vol.108 , pp. 2683-2692
    • Marshall, J.1    Holberton, D.V.2
  • 51
    • 30744443287 scopus 로고    scopus 로고
    • The scc spirochetal coiled-coil protein forms helix-like filaments and binds to nucleic acids generating nucleoprotein structures
    • Mazouni K., Pehau-Arnaudet G., England P., Bourhy P., Saint Girons I., Picardeau M. The scc spirochetal coiled-coil protein forms helix-like filaments and binds to nucleic acids generating nucleoprotein structures. J. Bacteriol. 2006, 188:469-476.
    • (2006) J. Bacteriol. , vol.188 , pp. 469-476
    • Mazouni, K.1    Pehau-Arnaudet, G.2    England, P.3    Bourhy, P.4    Saint Girons, I.5    Picardeau, M.6
  • 52
    • 32144456009 scopus 로고    scopus 로고
    • Paircoil2: improved prediction of coiled coils from sequence
    • McDonnell A.V., Jiang T., Keating A.E., Berger B. Paircoil2: improved prediction of coiled coils from sequence. Bioinformatics 2006, 22:356-358.
    • (2006) Bioinformatics , vol.22 , pp. 356-358
    • McDonnell, A.V.1    Jiang, T.2    Keating, A.E.3    Berger, B.4
  • 53
    • 0017136639 scopus 로고
    • The 14-fold periodicity in α-tropomyosin and the interaction with actin
    • McLachlan A.D., Stewart M. The 14-fold periodicity in α-tropomyosin and the interaction with actin. J. Mol. Biol. 1976, 103:271-298.
    • (1976) J. Mol. Biol. , vol.103 , pp. 271-298
    • McLachlan, A.D.1    Stewart, M.2
  • 54
    • 38549099683 scopus 로고    scopus 로고
    • Membrane-bound structure and energetics of α-synuclein
    • Mihajlovic M., Lazaridis T. Membrane-bound structure and energetics of α-synuclein. Proteins 2008, 70:761-778.
    • (2008) Proteins , vol.70 , pp. 761-778
    • Mihajlovic, M.1    Lazaridis, T.2
  • 55
    • 0030029835 scopus 로고    scopus 로고
    • Formation of parallel and antiparallel coiled-coils controlled by the relative positions of alanine residues in the hydrophobic core
    • Monera O.D., Zhou N.E., Lavigne P., Kay C.M., Hodges R.S. Formation of parallel and antiparallel coiled-coils controlled by the relative positions of alanine residues in the hydrophobic core. J. Biol. Chem. 1996, 271:3995-4001.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3995-4001
    • Monera, O.D.1    Zhou, N.E.2    Lavigne, P.3    Kay, C.M.4    Hodges, R.S.5
  • 56
    • 0026701930 scopus 로고
    • Primary structure of tektin A1: comparison with intermediate-filament proteins and a model for its association with tubulin
    • Norrander J.M., Amos L.A., Linck R.W. Primary structure of tektin A1: comparison with intermediate-filament proteins and a model for its association with tubulin. Proc. Natl. Acad. Sci. USA 1992, 89:8567-8571.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8567-8571
    • Norrander, J.M.1    Amos, L.A.2    Linck, R.W.3
  • 57
    • 36849043686 scopus 로고    scopus 로고
    • Structure of phage P22 cell envelope-penetrating needle
    • Olia A.S., Casjens S., Cingolani G. Structure of phage P22 cell envelope-penetrating needle. Nat. Struct. Mol. Biol. 2007, 14:1221-1226.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1221-1226
    • Olia, A.S.1    Casjens, S.2    Cingolani, G.3
  • 59
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea E.K., Klemm J.D., Kim P.S., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 1991, 254:539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 60
    • 33747768593 scopus 로고    scopus 로고
    • Hendecad repeat in segment 2A and linker L2 of intermediate filament chains implies the possibility of a right-handed coiled-coil structure
    • Parry D.A. Hendecad repeat in segment 2A and linker L2 of intermediate filament chains implies the possibility of a right-handed coiled-coil structure. J. Struct. Biol. 2006, 155:370-374.
    • (2006) J. Struct. Biol. , vol.155 , pp. 370-374
    • Parry, D.A.1
  • 61
    • 0002732819 scopus 로고
    • Compound helical configurations of polypeptide chains: structure of proteins of the α-keratin type
    • Pauling L., Corey R.B. Compound helical configurations of polypeptide chains: structure of proteins of the α-keratin type. Nature 1953, 171:59-61.
    • (1953) Nature , vol.171 , pp. 59-61
    • Pauling, L.1    Corey, R.B.2
  • 62
    • 0029942482 scopus 로고    scopus 로고
    • Hyperthermostable surface layer protein tetrabrachion from the archaebacterium Staphylothermus marinus: evidence for the presence of a right-handed coiled coil derived from the primary structure
    • Peters J., Baumeister W., Lupas A. Hyperthermostable surface layer protein tetrabrachion from the archaebacterium Staphylothermus marinus: evidence for the presence of a right-handed coiled coil derived from the primary structure. J. Mol. Biol. 1996, 257:1031-1041.
    • (1996) J. Mol. Biol. , vol.257 , pp. 1031-1041
    • Peters, J.1    Baumeister, W.2    Lupas, A.3
  • 64
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European Molecular Biology Open Software Suite
    • Rice P., Longden I., Bleasby A. EMBOSS: The European Molecular Biology Open Software Suite. Trends Genet. 2000, 16:276-277.
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 65
    • 0023478698 scopus 로고
    • Fine (2-5-nm) filaments: new types of cytoskeletal structures
    • Roberts T.M. Fine (2-5-nm) filaments: new types of cytoskeletal structures. Cell Motil. Cytoskelet. 1987, 8:130-142.
    • (1987) Cell Motil. Cytoskelet. , vol.8 , pp. 130-142
    • Roberts, T.M.1
  • 66
    • 0025829910 scopus 로고
    • The intermediate filament-related system of higher plant cells shares an epitope with cytokeratin 8
    • Ross J.H.E., Hutchings A., Butcher G.W., Lane E.B., Lloyd C.W. The intermediate filament-related system of higher plant cells shares an epitope with cytokeratin 8. J. Cell Sci. 1991, 99:91-98.
    • (1991) J. Cell Sci. , vol.99 , pp. 91-98
    • Ross, J.H.E.1    Hutchings, A.2    Butcher, G.W.3    Lane, E.B.4    Lloyd, C.W.5
  • 67
    • 0027532105 scopus 로고
    • Pitch diversity in α-helical coiled coils
    • Seo J., Cohen C. Pitch diversity in α-helical coiled coils. Proteins Struct. Funct. Genet. 1993, 15:223-234.
    • (1993) Proteins Struct. Funct. Genet. , vol.15 , pp. 223-234
    • Seo, J.1    Cohen, C.2
  • 68
    • 33645505710 scopus 로고    scopus 로고
    • Crystal structure of the DUF16 domain of MPN010 from Mycoplasma pneumoniae
    • Shin D.H., Kim J.-S., Yokota H., Kim R., Kim S.-H. Crystal structure of the DUF16 domain of MPN010 from Mycoplasma pneumoniae. Protein Sci. 2006, 15:921-928.
    • (2006) Protein Sci. , vol.15 , pp. 921-928
    • Shin, D.H.1    Kim, J.-S.2    Yokota, H.3    Kim, R.4    Kim, S.-H.5
  • 69
    • 18744388274 scopus 로고    scopus 로고
    • Sequence comparisons of intermediate filament chains: evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1
    • Smith T.A., Strelkov S.V., Burkhard P., Aebi U., Parry D.A. Sequence comparisons of intermediate filament chains: evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1. J. Struct. Biol. 2002, 137:128-145.
    • (2002) J. Struct. Biol. , vol.137 , pp. 128-145
    • Smith, T.A.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4    Parry, D.A.5
  • 70
    • 33750843407 scopus 로고    scopus 로고
    • Monitoring intermediate filament assembly by small-angle X-ray scattering reveals the molecular architecture of assembly intermediates
    • Sokolova A.V., Kreplak L., Wedig T., Muëcke N., Svergun D.I., Herrmann H., Aebi U., Strelkov S.V. Monitoring intermediate filament assembly by small-angle X-ray scattering reveals the molecular architecture of assembly intermediates. Proc. Natl. Acad. Sci. USA 2006, 103:16206-16211.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16206-16211
    • Sokolova, A.V.1    Kreplak, L.2    Wedig, T.3    Muëcke, N.4    Svergun, D.I.5    Herrmann, H.6    Aebi, U.7    Strelkov, S.V.8
  • 73
    • 77951974828 scopus 로고    scopus 로고
    • personal communication.
    • S.V. Strelkov, personal communication.
    • Strelkov, S.V.1
  • 74
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    • Strelkov S.V., Burkhard P. Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation. J. Struct. Biol. 2002, 137:54-64.
    • (2002) J. Struct. Biol. , vol.137 , pp. 54-64
    • Strelkov, S.V.1    Burkhard, P.2
  • 76
    • 0021112868 scopus 로고
    • Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure
    • Sweet R.M., Eisenberg D. Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure. J. Mol. Biol. 1983, 171:479-488.
    • (1983) J. Mol. Biol. , vol.171 , pp. 479-488
    • Sweet, R.M.1    Eisenberg, D.2
  • 77
    • 58149191270 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt)
    • The UniProt Consortium
    • The UniProt Consortium The Universal Protein Resource (UniProt). Nucleic Acids Res. 2009, 37:D169-D174.
    • (2009) Nucleic Acids Res. , vol.37
  • 78
    • 70350571135 scopus 로고    scopus 로고
    • On and around microtubules: an overview
    • Wade R.H. On and around microtubules: an overview. Mol. Biotechnol. 2009, 43:177-191.
    • (2009) Mol. Biotechnol. , vol.43 , pp. 177-191
    • Wade, R.H.1
  • 79
    • 0038035971 scopus 로고    scopus 로고
    • Oligomerization, membrane anchoring, and cellulose-binding characteristics of AbpS, a receptor-like Streptomyces protein
    • Walter S., Schrempf H. Oligomerization, membrane anchoring, and cellulose-binding characteristics of AbpS, a receptor-like Streptomyces protein. J. Biol. Chem. 2003, 278:26639-26647.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26639-26647
    • Walter, S.1    Schrempf, H.2
  • 80
    • 0027167511 scopus 로고
    • SF-assemblin, the structural protein of the 2-nm filaments from striated microtubule associated fibers of algal flagellar roots, forms a segmented coiled coil
    • Weber K., Geisler N., Plessmann U., Bremerich A., Lechtreck K.-F., Melkonian M. SF-assemblin, the structural protein of the 2-nm filaments from striated microtubule associated fibers of algal flagellar roots, forms a segmented coiled coil. J. Cell Biol. 1993, 121:837-845.
    • (1993) J. Cell Biol. , vol.121 , pp. 837-845
    • Weber, K.1    Geisler, N.2    Plessmann, U.3    Bremerich, A.4    Lechtreck, K.-F.5    Melkonian, M.6
  • 81
    • 0025860481 scopus 로고
    • Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E
    • Wilson C., Wardell M.R., Weisgraber K.H., Mahley R.W., Agard D.A. Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science 1991, 252:1817-1822.
    • (1991) Science , vol.252 , pp. 1817-1822
    • Wilson, C.1    Wardell, M.R.2    Weisgraber, K.H.3    Mahley, R.W.4    Agard, D.A.5
  • 82
    • 45849087668 scopus 로고    scopus 로고
    • Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils
    • Wise J.G., Vogel P.D. Subunit b-dimer of the Escherichia coli ATP synthase can form left-handed coiled-coils. Biophys. J. 2008, 94:5040-5052.
    • (2008) Biophys. J. , vol.94 , pp. 5040-5052
    • Wise, J.G.1    Vogel, P.D.2
  • 83
    • 0029941239 scopus 로고    scopus 로고
    • Characterization of the cytoplasmic filament protein gene (cfpA) of Treponema pallidum subsp. pallidum
    • You Y., Elmore S., Colton L.L., Mackenzie C., Stoops J.K., Weinstock G.M., Norris S.J. Characterization of the cytoplasmic filament protein gene (cfpA) of Treponema pallidum subsp. pallidum. J. Bacteriol. 1996, 178:3177-3187.
    • (1996) J. Bacteriol. , vol.178 , pp. 3177-3187
    • You, Y.1    Elmore, S.2    Colton, L.L.3    Mackenzie, C.4    Stoops, J.K.5    Weinstock, G.M.6    Norris, S.J.7
  • 84
    • 0344631628 scopus 로고    scopus 로고
    • The plant nucleoskeleton: ultrastructural organization and identification of NuMA homologues in the nuclear matrix and mitotic spindle of plant cells
    • Yu W., Moreno Díaz de la Espina S. The plant nucleoskeleton: ultrastructural organization and identification of NuMA homologues in the nuclear matrix and mitotic spindle of plant cells. Exp. Cell Res. 1999, 246:516-526.
    • (1999) Exp. Cell Res. , vol.246 , pp. 516-526
    • Yu, W.1    Moreno Díaz de la Espina, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.