메뉴 건너뛰기




Volumn 16, Issue 11, 2009, Pages 1297-1322

Non-Globular structures of tandem repeats in proteins

Author keywords

Concerted evolution; Intrinsically unstructured protein; Ligand interaction; Rapid evolution; Structural change; Tandem repeats

Indexed keywords

POLYMER; PROTEIN;

EID: 70349967807     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609789353745     Document Type: Article
Times cited : (6)

References (341)
  • 2
    • 0031864543 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998
    • DOI 10.1093/nar/26.1.38
    • Bairoch, A.; Apweiler, R. The SWISS-PROT protein sequence data bank, and its supplement TrEMBL in 1998. Nucleic Acids Res.,1998, 26(1), 38-42. (Pubitemid 28291509)
    • (1998) Nucleic Acids Research , vol.26 , Issue.1 , pp. 38-42
    • Bairoch, A.1    Apweiler, R.2
  • 3
    • 25444517281 scopus 로고    scopus 로고
    • COPASAAR-a database for proteomic analysis of single amino acid repeats
    • Depledge, D. P.; Dalby, A. R. COPASAAR-a database for proteomic analysis of single amino acid repeats. BMC Bioinformatics, 2005, 6, 196.
    • (2005) BMC Bioinformatics , vol.6 , pp. 196
    • Depledge, D.P.1    Dalby, A.R.2
  • 4
    • 34247495687 scopus 로고    scopus 로고
    • RepSeq-a database of amino acid repeats present in lower eukaryotic pathogens
    • Depledge, D. P.; Lower, R. P.; Smith, D. F. RepSeq-a database of amino acid repeats present in lower eukaryotic pathogens. BMC Bioinformatics, 2007, 8,122.
    • (2007) BMC Bioinformatics , vol.8 , pp. 122
    • Depledge, D.P.1    Lower, R.P.2    Smith, D.F.3
  • 5
    • 65549139776 scopus 로고    scopus 로고
    • Kretsinger, R. H. Flexible Structures and Ligand Interactions of Tandem Repeats Consisting of Proline, Glycine, Asparagine, Serine, and/or Threonine Rich Oligopeptides in. Proteins
    • Matsushima, N.; Yoshida, H.; Kumaki, Y.; Kamiya, M.; Tanaka, T.; Izumi, Y.; Kretsinger, R. H. Flexible Structures and Ligand Interactions of Tandem Repeats Consisting of Proline, Glycine, Asparagine, Serine, and/or Threonine Rich Oligopeptides in. Proteins Curr. Protein Pept. Sci., 2008, 9(6), 591-610.
    • (2008) Curr. Protein Pept. Sci. , vol.9 , Issue.6 , pp. 591-610
    • Matsushima, N.1    Yoshida, H.2    Kumaki, Y.3    Kamiya, M.4    Tanaka, T.5    Izumi, Y.6
  • 6
    • 1542358787 scopus 로고    scopus 로고
    • Jones, D. T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J.; Sodhi, J. S.; McGuffin, L. J.; Buxton, B. F.; Jones, D. T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol, 2004, 337(3), 635-645.
    • (2004) J. Mol. Biol , vol.337 , Issue.3 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4
  • 7
    • 34748854289 scopus 로고    scopus 로고
    • Predicting mostly disordered proteins by using structure-unknown protein data
    • Shimizu, K. M.; Y. Hirose, S.; Tomii, K.; Noguchi, T. Predicting mostly disordered proteins by using structure-unknown protein data. BMC Bioinformatics, 2007, 8, 78.
    • (2007) BMC Bioinformatics , vol.8 , pp. 78
    • Shimizu, K.M.1    Hirose S, Y.2    Tomii, K.3    Noguchi, T.4
  • 8
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: From transcript synthesis to protein degradation
    • Gsponer, J.; Futschik, M. E.; Teichmann, S. A.; Babu, M. M. Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science, 2008, 322(5906), 1365-1368.
    • (2008) Science , vol.322 , Issue.5906 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 9
    • 37849030901 scopus 로고    scopus 로고
    • Polyglutamine diseases: Emerging concepts in pathogenesis and therapy
    • Shao, J.; Diamond, M. I. Polyglutamine diseases: emerging concepts in pathogenesis and therapy. Hum. Mol. Genet., 2007, 16(Spec No. 2), 115-123.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 115-123
    • Shao, J.1    Diamond, M.I.2
  • 10
    • 49349110821 scopus 로고    scopus 로고
    • Huntington's disease: Revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases
    • Truant, R.; Atwal, R. S.; Desmond, C.; Munsie, L.; Tran, T. Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases. FEBS J, 2008, 275(17), 42524262.
    • (2008) FEBS J , vol.275 , Issue.17 , pp. 42524262
    • Truant, R.1    Atwal, R.S.2    Desmond, C.3    Munsie, L.4    Tran, T.5
  • 12
    • 0037181179 scopus 로고    scopus 로고
    • Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins
    • DOI 10.1016/S0014-5793(02)02335-9, PII S0014579302023359
    • Masino, L.; Kelly, G.; Leonard, K.; Trottier, Y.; Pastore, A. Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins. FEBS Lett., 2002, 573(2-3), 267-272. (Pubitemid 34251276)
    • (2002) FEBS Letters , vol.513 , Issue.2-3 , pp. 267-272
    • Masino, L.1    Kelly, G.2    Leonard, K.3    Trottier, Y.4    Pastore, A.5
  • 13
    • 0030739464 scopus 로고    scopus 로고
    • Random coil conformation for extended polyglutamine stretches in aqueous soluble monomeric peptides
    • Altschuler, E. L.; Hud, N. V.; Mazrimas, J. A.; Rupp, B. Random coil conformation for extended polyglutamine stretches in aqueous soluble monomeric peptides. J Pept. Res., 1997, 50(1), 73-75. (Pubitemid 27345451)
    • (1997) Journal of Peptide Research , vol.50 , Issue.1 , pp. 73-75
    • Altschuler, E.L.1    Hud, N.V.2    Mazrimas, J.A.3    Rupp, B.4
  • 14
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • DOI 10.1006/jmbi.2001.4850
    • Chen, S.; Berthelier, V.; Yang, W.; Wetzel, R. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. J. Mol. Biol, 2001, 311(1), 173-182. (Pubitemid 32735322)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.1 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3    Wetzel, R.4
  • 15
    • 0034814752 scopus 로고    scopus 로고
    • Solution studies of chymotrypsin inhibitor-2 glutamine insertion mutants show no interglutamine interactions
    • DOI 10.1006/bbrc.2000.4196
    • Gordon-Smith, D. J.; Carbajo, R. J.; Stott, K.; Neuhaus, D. Solution studies of chymotrypsin inhibitors glutamine insertion mutants show no interglutamine interactions. Biochem. Biophys. Res. Commun., 2001, 250(3), 855-860. (Pubitemid 32924510)
    • (2001) Biochemical and Biophysical Research Communications , vol.280 , Issue.3 , pp. 855-860
    • Gordon-Smith, D.J.1    Carbajo, R.J.2    Stott, K.3    Neuhaus, D.4
  • 16
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in. inherited neurodegenerative diseases
    • Perutz, M. F.; Johnson, T.; Suzuki, M.; Finch, J. T. Glutamine repeats as polar zippers: their possible role in. inherited neurodegenerative diseases. Proc. Natl. Acad. Sci USA, 1994, 91(12), 5355-5358.
    • (1994) Proc. Natl. Acad. Sci USA , vol.91 , Issue.12 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 17
    • 0345832225 scopus 로고    scopus 로고
    • X-ray structure and activity of the yeast Pop2 protein: A nuclease subunit of the mRNA deadenylase complex
    • DOI 10.1038/sj.embor.7400020
    • Thore, S.; Mauxion, F.; Seraphin, B.; Suck, D. X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex. EMBO Rep., 2003, 4(12), 1150-1155. (Pubitemid 38088410)
    • (2003) EMBO Reports , vol.4 , Issue.12 , pp. 1150-1155
    • Thore, S.1    Mauxion, F.2    Seraphin, B.3    Suck, D.4
  • 19
    • 0028222235 scopus 로고
    • Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
    • Chakrabartty, A.; Kortemme, T.; Baldwin, R. L. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci., 1994, 3(5), 843-852.
    • (1994) Protein Sci. , vol.3 , Issue.5 , pp. 843-852
    • Chakrabartty, A.1    Kortemme, T.2    Baldwin, R.L.3
  • 20
    • 0030853453 scopus 로고    scopus 로고
    • Polyalanine-based peptides as models for self-associated β-pleated- Sheet complexes
    • DOI 10.1021/bi963015b
    • Blondelle, S. E.; Forood, B.; Houghten, R. A.; Perez-Paya, E. Polyalanine-based peptides as models for self-associated beta-pleatedsheet complexes. Biochemistry, 1997, 36(27), 8393-8400. (Pubitemid 27297551)
    • (1997) Biochemistry , vol.36 , Issue.27 , pp. 8393-8400
    • Blondelle, S.E.1    Forood, B.2    Houghten, R.A.3    Perez-Paya, E.4
  • 21
    • 0038182556 scopus 로고    scopus 로고
    • Solution structure and function of the "tandem inactivation domain" of the neuronal A-type potassium channel Kv1.4
    • Wissmann, R.; Bildl, W.; Oliver, D.; Beyermann, M.; Kalbitzer, H. R.; Bentrop, D.; Fakler, B. Solution structure and function of the "tandem inactivation domain" of the neuronal A-type potassium channel Kv1.4. J. Biol Chem., 2003, 275(18), 16142-16150.
    • (2003) J. Biol Chem. , vol.275 , Issue.18 , pp. 16142-16150
    • Wissmann, R.1    Bildl, W.2    Oliver, D.3    Beyermann, M.4    Kalbitzer, H.R.5    Bentrop, D.6    Fakler, B.7
  • 22
    • 51649117099 scopus 로고    scopus 로고
    • The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning
    • Wilson, D. N.; Schluenzen, F.; Harms, J. M.; Starosta, A. L.; Connell, S. R.; Fucini, P. The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning. Proc. Natl. Acad. Sci. USA, 2008, 105(36), 13339-13344.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.36 , pp. 13339-13344
    • Wilson, D.N.1    Schluenzen, F.2    Harms, J.M.3    Starosta, A.L.4    Connell, S.R.5    Fucini, P.6
  • 25
    • 34249689094 scopus 로고    scopus 로고
    • Vertebrate yolk complexes and the functional implications of Phosvitins and other subdomains in vitellogenins
    • Finn, R. N. Vertebrate yolk complexes and the functional implications of Phosvitins and other subdomains in vitellogenins. Biol. Reprod, 2007, 76(6), 926-935.
    • (2007) Biol. Reprod , vol.76 , Issue.6 , pp. 926-935
    • Finn, R.N.1
  • 27
    • 0032527992 scopus 로고    scopus 로고
    • The structural basis of Lipid interactions in. lipovitellin, a soluble lipoprotein
    • Anderson, T. A.; Levitt, D. G.; Banaszak, L. J. The structural basis of Lipid interactions in. lipovitellin, a soluble lipoprotein. Structure, 1998, 6(7), 895-909.
    • (1998) Structure , vol.6 , Issue.7 , pp. 895-909
    • Anderson, T.A.1    Levitt, D.G.2    Banaszak, L.J.3
  • 28
    • 0346850625 scopus 로고    scopus 로고
    • Volumetric characterization of homopolymeric amino acids
    • Noudeh, G. D.; Taulier, N.; Chalikian, T. V. Volumetric characterization of homopolymeric amino acids. Biopolymers, 2003, 70(4), 563-574.
    • (2003) Biopolymers , Issue.704 , pp. 563-574
    • Noudeh, G.D.1    Taulier, N.2    Chalikian, T.V.3
  • 29
    • 0346850867 scopus 로고    scopus 로고
    • A novel extremely aspartic acid-rich protein, in fish muscle, promotes iron-mediated demethylation of trimethylamine-N-oxide
    • Takeuchi, K.; Hatanaka, A.; Kimura, M.; Seki, N.; Kimura, I.; Yamada, S.; Yamashita, S. Aspolin, a novel extremely aspartic acid-rich protein, in fish muscle, promotes iron-mediated demethylation of trimethylamine-N-oxide. J. Biol Chem., 2003, 275(48), 47416-47422.
    • (2003) J. Biol Chem. , vol.275 , Issue.48 , pp. 47416-47422
    • Takeuchi, K.1    Hatanaka, A.2    Kimura, M.3    Seki, N.4    Kimura, I.5    Yamada, S.6    Aspolin, Y.S.7
  • 30
    • 24944520857 scopus 로고    scopus 로고
    • The existence of aspolin and its trimethylamine-N-oxide demethylating activity in the muscle of freshwater fish
    • DOI 10.1111/j.1444-2906.2005.01044.x
    • Kimura, M.; Takeuchi, K.; Kimura, I.; Seki, N. The existence of aspolin and its trimethylamine-N-oxide demethylating activity in. the muscle of freshwater fish. Fish Sci, 2005, 71, 904-913. (Pubitemid 41323674)
    • (2005) Fisheries Science , vol.71 , Issue.4 , pp. 904-913
    • Kimura, M.1    Takeuchi, K.2    Kimura, I.3    Seki, N.4
  • 31
    • 0001628555 scopus 로고
    • Polypeptides. VIII, molecular configuration of poly-L-glutamic acid in. water-dioxane solution
    • Doty, P. W. A.; Yang, J. T.; Blout E. R. Polypeptides. VIII, Molecular configuration of poly-L-glutamic acid in. water-dioxane solution. J. Polym. Sci, 1957, 23, 851-861.
    • (1957) J. Polym. Sci , vol.23 , pp. 851-861
    • Doty, P.W.A.1    Yang, J.T.2    Blout, E.R.3
  • 32
    • 0034491563 scopus 로고    scopus 로고
    • Spring mechanics of alpha-helical polypeptide
    • Idiris, A.; Alam, M. T.; Ikai, A. Spring mechanics of alpha-helical polypeptide. Protein Eng., 2000, 13(11), 763-770.
    • (2000) Protein Eng. , vol.13 , Issue.11 , pp. 763-770
    • Idiris, A.1    Alam, M.T.2    Ikai, A.3
  • 33
    • 84985720045 scopus 로고
    • Potentiometrie titration of polyelectrolytes. Having stiff backbones
    • Muroga, Y. S., K.; Kawaguchi, Y.; Nagasawa, M. Potentiometrie Titration of Polyelectrolytes. Having Stiff Backbones. Biopolymers, 1912, 11, 137-144.
    • (1912) Biopolymers , vol.11 , pp. 137-144
    • Muroga, Y.S.K.1    Kawaguchi, Y.2    Nagasawa, M.3
  • 34
    • 33947486526 scopus 로고
    • The helix-coil transition in solutions of polyglutamic acid
    • Nagasawa, M.; Holtzer, A. The helix-coil transition in solutions of polyglutamic acid. J. Am. Chem. Soc., 1964, 56, 538-543.
    • (1964) J. Am. Chem. Soc. , vol.56 , pp. 538-543
    • Nagasawa, M.1    Holtzer, A.2
  • 35
    • 0014413927 scopus 로고
    • Stability of the polyglutamic acid alpha helix
    • Olander, D. S.; Holtzer, A. Stability of the polyglutamic acid alpha helix. J. Am. Chem. Soc., 1968, 90, 4549-4560.
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 4549-4560
    • Olander, D.S.1    Holtzer, A.2
  • 36
    • 34248401680 scopus 로고    scopus 로고
    • Small-angle X-ray scattering study on conformation of poly(sodium L-glutamate) in NaCl and NaF aqueous solutions
    • DOI 10.1107/S0021889807006255, PII S0021889807006255
    • Shimizu, S. M. Y.; Hyono, T.; Kurita, K. Small-angle x-ray scatteting study on conformation of poly(sodium L-glutamate) in NaCl and NaF aqueous solutions. J. Appl Cryst. 2007, 40, s553-s557. (Pubitemid 46732759)
    • (2007) Journal of Applied Crystallography , vol.40 , Issue.SUPPL. 1
    • Shimizu, S.1    Muroga, Y.2    Hyono, T.3    Kurita, K.4
  • 37
    • 0001406264 scopus 로고
    • The Helix-Coil Transition in Charged Macromolecules
    • Zimm, B. H.; Rice, S. A. The Helix-Coil Transition in Charged Macromolecules. Mol. Phys., 1960, 3, 391-407.
    • (1960) Mol. Phys. , vol.3 , pp. 391-407
    • Zimm, B.H.1    Rice, S.A.2
  • 38
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich, M.; Dobson, C. M. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBOJ, 2002, 27(21), 5682-5690.
    • (2002) EMBOJ , vol.27 , Issue.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 39
    • 41249099050 scopus 로고    scopus 로고
    • The formation of a novel supramolecular structure by amyloid of poly-Lglutamic acid
    • Bai, F.; Zeng, C.; Yang, S.; Zhang, Y.; He, Y.; Jin, J. The formation of a novel supramolecular structure by amyloid of poly-Lglutamic acid. Biochem. Biophys. Res. Commun., 2008, 369(3), 830-834.
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , Issue.3 , pp. 830-834
    • Bai, F.1    Zeng, C.2    Yang, S.3    Zhang, Y.4    He, Y.5    Jin, J.6
  • 40
    • 33644860767 scopus 로고    scopus 로고
    • Protamines, in the footsteps of linker histone evolution
    • Eirin-Lopez, J. M.; Frehlick, L. J.; Ausio, J. Protamines, in the footsteps of linker histone evolution. J. Biol Chem., 2006, 257(1), 1-4.
    • (2006) J. Biol Chem. , vol.257 , Issue.1 , pp. 1-4
    • Eirin-Lopez, J.M.1    Frehlick, L.J.2    Ausio, J.3
  • 41
    • 0025224880 scopus 로고
    • Zinc-induced secondary structure transitions in human sperm protamines
    • Gatewood, J. M.; Schroth, G. P.; Schmid, C. W.; Bradbury, E. M. Zinc-induced secondary structure transitions in human sperm protamines. J. Biol. Chem., 1990, 265(33), 20667-20672.
    • (1990) J. Biol. Chem. , vol.265 , Issue.33 , pp. 20667-20672
    • Gatewood, J.M.1    Schroth, G.P.2    Schmid, C.W.3    Bradbury, E.M.4
  • 42
    • 85013801340 scopus 로고
    • Solubilization and conformation, of protamines in reverse micelles
    • Ebert, G.; Zölzer, U.; Nishi, N. Solubilization and conformation, of protamines in reverse micelles. Prog. Coll. Polymer Sci., 1990, 53, 181-187.
    • (1990) Prog. Coll. Polymer Sci. , vol.53 , pp. 181-187
    • Ebert, G.1    Zölzer, U.2    Nishi, N.3
  • 43
    • 0028286473 scopus 로고
    • Evidence of novel secondary structure in DNA-bound protamine is revealed by raman spectroscopy
    • DOI 10.1021/bi00190a005
    • Hud, N. V.; Milanovich, F. P.; Balhorn, R. Evidence of novel secondary structure in DNA-bound protamine is revealed by Raman. spectroscopy. Biochemistry, 1994, 33(24), 7528-7535. (Pubitemid 24230576)
    • (1994) Biochemistry , vol.33 , Issue.24 , pp. 7528-7535
    • Hud, N.V.1    Milanovich, F.P.2    Balhorn, R.3
  • 44
    • 33745237318 scopus 로고    scopus 로고
    • The probable structure of the protamine-DNA complex
    • Biegeleisen, K. The probable structure of the protamine-DNA complex. J. Theor. Biol, 2006, 241(3), 533-540.
    • (2006) J. Theor. Biol , vol.241 , Issue.3 , pp. 533-540
    • Biegeleisen, K.1
  • 45
    • 0017927903 scopus 로고
    • S.H. alpha-Helix-double helix interaction shown in the structure of a protamine-transfer RNA complex and a nucleoprotamine model
    • Warrant, R. W. K., S.H. alpha-Helix-double helix interaction shown in the structure of a protamine-transfer RNA complex and a nucleoprotamine model. Nature, 1978, 271,13-15.
    • (1978) Nature , vol.271 , pp. 13-15
    • Warrant, R.W.K.1
  • 46
    • 0017594334 scopus 로고
    • Formation and structure of Cu(II) poly (L lysine) complexes in aqueous solution
    • DOI 10.1016/0006-291X(77)91657-6
    • Garnier, A.; Tosi, L. Formation and structure of Cu(II)-poly(Llysine) complexes in aqueous solution. Biochem. Biophys. Res. Commun., 1977, 74(3), 1280-1286. (Pubitemid 8036271)
    • (1977) Biochemical and Biophysical Research Communications , vol.74 , Issue.3 , pp. 1280-1286
    • Garnier, A.1    Tosi, L.2
  • 47
    • 0021224383 scopus 로고
    • Binding sites and endocytosis of heparin and polylysine are changed when the two molecules are given as a complex to Chinese hamster ovary cells
    • Morad, N.; Ryser, H. J.; Shen, W. C. Binding sites and endocytosis of heparin and polylysine are changed when the two molecules are given as a complex to Chinese hamster ovary cells. Biochim. Biophys. Acta, 1984, 801(1), 117-126.
    • (1984) Biochim. Biophys. Acta , vol.801 , Issue.1 , pp. 117-126
    • Morad, N.1    Ryser, H.J.2    Shen, W.C.3
  • 48
    • 0015791256 scopus 로고
    • Conformational studies of nucleoprotein. Circular dichroism of deoxyribonucleic acid base pairs bound by polylysine
    • Chang, C.; Weiskopf, M.; Li, H. J. Conformational studies of nucleoprotein. Circular dichroism of deoxyribonucleic acid base pairs bound by polylysine. Biochemistry, 1973, 12(16), 3028-3032.
    • (1973) Biochemistry , vol.12 , Issue.16 , pp. 3028-3032
    • Chang, C.1    Weiskopf, M.2    Li, H.J.3
  • 49
    • 0015929484 scopus 로고
    • The study of the DNA structure in DNApolylysine and DNA-polyarginine complexes: Induced optical activities of bound dyes
    • Zama, M.; Ichimura, S. The study of the DNA structure in DNApolylysine and DNA-polyarginine complexes: induced optical activities of bound dyes. Biochim. Biophys. Acta, 1973, 294(1), 214-226.
    • (1973) Biochim. Biophys. Acta , vol.294 , Issue.1 , pp. 214-226
    • Zama, M.1    Ichimura, S.2
  • 50
    • 0015289998 scopus 로고
    • Optical properties of deoxyribonucleic acid-polylysine complexes
    • Carroll, D. Optical properties of deoxyribonucleic acid-polylysine complexes. Biochemistry, 1972, 11(3), 421-426.
    • (1972) Biochemistry , vol.11 , Issue.3 , pp. 421-426
    • Carroll, D.1
  • 51
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N.; Fasman, G. D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry, 1969, 5(10), 4108-4116.
    • (1969) Biochemistry , vol.5 , Issue.10 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 52
    • 42449159377 scopus 로고    scopus 로고
    • SR proteins and related factors in alternative splicing
    • Lin, S.; Fu, X. D. SR proteins and related factors in alternative splicing. Adv. Exp. Med. Biol., 2007, 623, 107-122.
    • (2007) Adv. Exp. Med. Biol. , vol.623 , pp. 107-122
    • Lin, S.1    Fu, X.D.2
  • 53
    • 35448961596 scopus 로고    scopus 로고
    • A proposed signaling motif for nuclear import in mRNA processing via the formation of arginine claw
    • Hamelberg, D.; Shen, T.; McCammon, J. A. A proposed signaling motif for nuclear import in mRNA processing via the formation of arginine claw. Proc. Natl. Acad. Sci. USA, 2007, 104(38), 14947-14951.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.38 , pp. 14947-14951
    • Hamelberg, D.1    Shen, T.2    McCammon, J.A.3
  • 55
    • 25844491145 scopus 로고    scopus 로고
    • Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2
    • DOI 10.1016/j.molcel.2005.08.025, PII S1097276505015674
    • go, J. C.; Chakrabarti, S.; Ding, J. H.; Velazquez-Dones, A.; Nolen, B.; Aubol, B. E.; Adams, J. A.; Fu, X. D.; Ghosh, G. Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2. Mol. Cell, 2005, 20(1), 77-89. (Pubitemid 41396564)
    • (2005) Molecular Cell , vol.20 , Issue.1 , pp. 77-89
    • Ngo, J.C.K.1    Chakrabarti, S.2    Ding, J.-H.3    Velazquez-Dones, A.4    Nolen, B.5    Aubol, B.E.6    Adams, J.A.7    Fu, X.-D.8    Ghosh, G.9
  • 56
    • 0035427372 scopus 로고    scopus 로고
    • Silk, fibroin: Structural implications of a remarkable amino acid sequence
    • Zhou, C. Z.; Confalonieri, F.; Jacquet, M.; Perasso, R.; Li, Z. G.; Janin, J. Silk, fibroin: structural implications of a remarkable amino acid sequence. Proteins, 2001, 44(2), 119-122.
    • (2001) Proteins , vol.44 , Issue.2 , pp. 119-122
    • Zhou, C.Z.1    Confalonieri, F.2    Jacquet, M.3    Perasso, R.4    Li, Z.G.5    Janin, J.6
  • 57
    • 0035895432 scopus 로고    scopus 로고
    • A repeated β-turn structure in poly(Ala-Gly) as a model for silk i of Bombyx mori silk fibroin studied with two-dimensional spin-diffusion NMR under off magic angle spinning and rotational echo double resonance
    • DOI 10.1006/jmbi.2000.4394
    • sakura, T.; Ashida, J.; Yamane, T.; Kameda, T.; Nakazawa, Y.; Ohgo, K.; Komatsu, K. A repeated beta-turn structure in poly(AlaGly) as a model for silk I of Bombyx mori silk fibroin studied with two-dimensional, spin-diffusion NMR under off magic angle spinning and rotational echo double resonance. J. Mol. Biol, 2001, 306(2), 291-305. (Pubitemid 33032881)
    • (2001) Journal of Molecular Biology , vol.306 , Issue.2 , pp. 291-305
    • Asakura, T.1    Ashida, J.2    Yamane, T.3    Kameda, T.4    Nakazawa, Y.5    Ohgo, K.6    Komatsu, K.7
  • 58
    • 0035045539 scopus 로고    scopus 로고
    • 13C cross-polarization/ magic angle spinning NMR
    • DOI 10.1002/1097-0282(20010415)58:5<521::AID-BIP1027>3.0.CO;2-T
    • Asakura, T.; Yamane, T.; Nakazawa, Y.; Kameda, T.; Ando, K. Structure of Bombyx mori silk fibroin before spinning in solid state studied with wide angle x-ray scattering and(13)C crosspolarization/magic angle spinning NMR. Biopolymers, 2001, 58(5), 521-525. (Pubitemid 32303817)
    • (2001) Biopolymers , vol.58 , Issue.5 , pp. 521-525
    • Asakura, T.1    Yamane, T.2    Nakazawa, Y.3    Kameda, T.4    Ando, K.5
  • 59
    • 14044250010 scopus 로고    scopus 로고
    • Possible Implications of Serine and Tyrosine Residues and Intermolecular Interactions on the Appearance of Silk i Structure of Bombyx mori Silk Fibroin-Derived Synthetic Peptides: HighResolution 13C Cross-Polarization/Magic- Angle Spinning NMR Study
    • Asakura, T.; Ohgo, K.; Ishida, T.; Taddei, P.; Monti, P.; R., K. Possible Implications of Serine and Tyrosine Residues and Intermolecular Interactions on the Appearance of Silk I Structure of Bombyx mori Silk Fibroin-Derived Synthetic Peptides: HighResolution 13C Cross-Polarization/Magic-Angle Spinning NMR Study. Biomacromolecules, 2005, 6, 468-474.
    • (2005) Biomacromolecules , vol.6 , pp. 468-474
    • Asakura, T.1    Ohgo, K.2    Ishida, T.3    Taddei, P.4    Monti, P.5
  • 60
    • 5044231758 scopus 로고    scopus 로고
    • 13C NMR spectroscopy
    • DOI 10.1021/bm049831d
    • Yao, J.; Ohgo, K.; Sugino, R.; Kishore, R.; Asakura, T. Structural Analysis of Bombyx mori Silk Fibroin Peptides with Formic Acid Treatment Using High-Resolution Solid-State 13C NMR Spectroscopy. Biomacromolecules, 2004, 5, 1763-1769. (Pubitemid 39335212)
    • (2004) Biomacromolecules , vol.5 , Issue.5 , pp. 1763-1769
    • Yao, J.1    Ohgo, K.2    Sugino, R.3    Kishore, R.4    Asakura, T.5
  • 61
    • 31544466491 scopus 로고    scopus 로고
    • Distinctive Influence of Two Hexafluoro Solvents on the Structural Stabilization of Bombyx mori Silk Fibroin Protein, and Its Derived Peptides: 13C NMR and CD Studies
    • Ha, S.-W.; Asakura, T.; R., K. Distinctive Influence of Two Hexafluoro Solvents on the Structural Stabilization of Bombyx mori Silk Fibroin Protein, and Its Derived Peptides: 13C NMR and CD Studies. Biomacromolecules, 2006, 7, 18-23.
    • (2006) Biomacromolecules , vol.7 , pp. 18-23
    • Ha, S.-W.1    Asakura, T.2
  • 62
    • 42449101298 scopus 로고    scopus 로고
    • Serglycin-structure and biology
    • Kolset, S. O.; Tveit, H. Serglycin-structure and biology. Cell. Mol. Life Sci, 2008, 65(7-8), 1073-1085.
    • (2008) Cell. Mol. Life Sci , vol.65 , Issue.7-8 , pp. 1073-1085
    • Kolset, S.O.1    Tveit, H.2
  • 63
    • 0029658570 scopus 로고    scopus 로고
    • Complete 1H NMR assignments of synthetic glycopeptides from, the carbohydrate-protein linkage region of serglycins
    • Curto, E. V.; Sakai, T. T.; Jablonsky, M. J.; Rio-Anneheim, S.; Jacquinet, J. C.; Krishna, N. R. Complete 1H NMR assignments of synthetic glycopeptides from, the carbohydrate-protein linkage region of serglycins. Glycoconj. J., 1996, 13(4), 599-607.
    • (1996) Glycoconj. J. , vol.13 , Issue.4 , pp. 599-607
    • Curto, E.V.1    Sakai, T.T.2    Jablonsky, M.J.3    Rio-Anneheim, S.4    Jacquinet, J.C.5    Krishna, N.R.6
  • 65
    • 0029032138 scopus 로고
    • Polar zippers: Their role in human disease
    • Perutz, M. F. Polar zippers: their role in human disease. Pharm. Ada Helv., 1995, 69(4), 213-224.
    • (1995) Pharm. Ada Helv. , vol.69 , Issue.4 , pp. 213-224
    • Perutz, M.F.1
  • 66
    • 0027995352 scopus 로고
    • Immunoreactivity between a monoclonal lupud autoantibody and the arrginine/aspartic acid repeats conformationally restricted
    • Pelsue, S.; Agris, P. F. Immunoreactivity between a monoclonal lupus autoantibody and the arginine/aspartic acid repeats within the Ul-snRNP 70K autoantigen is conformationally restricted. J. Protein Chem., 1994, 13(4), 401-408. (Pubitemid 2119422)
    • (1994) Journal of Protein Chemistry , vol.13 , Issue.4 , pp. 401-408
    • Pelsue, S.1    Agris, P.F.2
  • 67
    • 0021459721 scopus 로고
    • Solution conformation of poly(L-lysyl-L-glutamic acid) and poly(L-lysyl-Lglutamine)
    • Rao, M. V.; Atreyi, M.; Chauhan, V. S.; Kumar, S. Solution conformation of poly(L-lysyl-L-glutamic acid) and poly(L-lysyl-Lglutamine). Int. J. Pept. Protein Res., 1984, 24(1), 48-54.
    • (1984) Int. J. Pept. Protein Res. , vol.24 , Issue.1 , pp. 48-54
    • Rao, M.V.1    Atreyi, M.2    Chauhan, V.S.3    Kumar, S.4
  • 68
    • 0016715114 scopus 로고
    • Beta structures of alternating polypeptides and their possible prebiotic significance
    • Brack, A.; Orgel, L. E. Beta structures of alternating polypeptides and their possible prebiotic significance. Nature, 1975, 256(5516), 383-387.
    • (1975) Nature , vol.256 , Issue.5516 , pp. 383-387
    • Brack, A.1    Orgel, L.E.2
  • 69
    • 0017863435 scopus 로고
    • Conformational studies of sequential polypeptides containing lysine and tyrosine
    • Pierre, S. S.; Ingwall, R. T.; Verlander, M. S.; Goodman, M. Conformational, studies of sequential polypeptides containing lysine and. tyrosine. Biopolymers, 1978, 17(8), 1837-1848. (Pubitemid 8401319)
    • (1978) Biopolymers , vol.17 , Issue.8 , pp. 1837-1848
    • Pierre, S.S.1    Ingwall, R.T.2    Verlander, M.S.3    Goodman, M.4
  • 70
    • 0015914845 scopus 로고
    • Spectroscopic characterization of poly(Glu-Ala)
    • Rippon, W. B.; Chen, H. H.; Walton, A. G. Spectroscopic characterization of poly(Glu-Ala). J. Mol Biol, 1973, 75(2), 369-375.
    • (1973) J. Mol Biol , vol.75 , Issue.2 , pp. 369-375
    • Rippon, W.B.1    Chen, H.H.2    Walton, A.G.3
  • 71
    • 0344340970 scopus 로고
    • Conformational study of the sequential(Tyr-Glu)n copolymer in a aqueous solution
    • Trudelle, Y. Conformational study of the sequential(Tyr-Glu)n copolymer in a aqueous solution. Polymer, 1975, 16, 9-15.
    • (1975) Polymer , vol.16 , pp. 9-15
    • Trudelle, Y.1
  • 72
    • 0346731295 scopus 로고    scopus 로고
    • Antimicrobial Activity of a Chelatable Poly(Arginyl-Histidine) Produced by the Ergot Fungus Verticillium kibiense
    • DOI 10.1128/AAC.48.1.229-235.2004
    • Nishikawa, M.; Ogawa, K. Antimicrobial activity of a chelatable poly(arginyl-histidine) produced by the ergot fungus Verticillium kibiense. Antimicroh. Agents Chemother., 2004, 45(1), 229-235. (Pubitemid 38040202)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.1 , pp. 229-235
    • Nishikawa, M.1    Ogawa, K.2
  • 73
    • 0344507194 scopus 로고    scopus 로고
    • Zinc-Induced Conformational Transitions of Acidic Peptides: Characterization by Circular Dichroism and Electrospray Mass Spectrometry
    • Henin, O.; Barbier, B.; Boulot, F.; Brack, A. A. Zinc-Induced Conformational Transitions of Acidic Peptides: Characterization by Circular Dichroism and Electrospray Mass Spectrometry. Chem. Eur, J. 1999, 5(1), 218-226.
    • (1999) Chem. Eur, J. , vol.5 , Issue.1 , pp. 218-226
    • Henin, O.1    Barbier, B.2    Boulot, F.3    Brack, A.A.4
  • 74
    • 0031608332 scopus 로고    scopus 로고
    • Dentin matrix proteins
    • Butler, W. T. Dentin matrix proteins. Eur. J. Oral Sci., 1998, 106 (Suppl 1), 204-210.
    • (1998) Eur. J. Oral Sci. , vol.106 , Issue.1 , pp. 204-210
    • Butler, W.T.1
  • 75
    • 0028519204 scopus 로고
    • Phosphophoryn, an "acidic" biomineralization regulatory protein: Conformational folding in the presence of Cd(II)
    • Evans, J. S.; Chiu, T.; Chan, S. I. Phosphophoryn, an "acidic" biomineralization regulatory protein: conformational folding in the presence of Cd(II). Biopolymers, 1994, 34(10), 1359-1375.
    • (1994) Biopolymers , vol.34 , Issue.10 , pp. 1359-1375
    • Evans, J.S.1    Chiu, T.2    Chan, S.I.3
  • 76
    • 22344448659 scopus 로고    scopus 로고
    • Protein dynamics of bovine dentin phosphophoryn
    • Cross, K. J.; Huq, N. L.; Reynolds, E. C. Protein dynamics of bovine dentin phosphophoryn. J. Pept. Res., 2005, 66(2), 59-67.
    • (2005) J. Pept. Res. , vol.66 , Issue.2 , pp. 59-67
    • Cross, K.J.1    Huq, N.L.2    Reynolds, E.C.3
  • 77
    • 0021115826 scopus 로고
    • Bovine dentin phosphophoryn: Composition and molecular weight
    • Stetler-Stevenson, W. G.; Veis, A. Bovine dentin phosphophoryn: composition and molecular weight. Biochemistry, 1983, 22(18), 4326-4335.
    • (1983) Biochemistry , vol.22 , Issue.18 , pp. 4326-4335
    • Stetler-Stevenson, W.G.1    Veis, A.2
  • 79
    • 34548726219 scopus 로고    scopus 로고
    • Interactions of the G quartet forming semaphorin 3F RNA with the RGG box domain of the fragile X protein family
    • Menon, L.; Mihailescu, M. R. Interactions of the G quartet forming semaphorin 3F RNA with the RGG box domain of the fragile X protein family. Nucleic Acids Res., 2007, 35(16), 5379-5392.
    • (2007) Nucleic Acids Res. , vol.35 , Issue.16 , pp. 5379-5392
    • Menon, L.1    Mihailescu, M.R.2
  • 80
    • 38449094080 scopus 로고    scopus 로고
    • Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain
    • Kusakawa, T.; Shimakami, T.; Kaneko, S.; Yoshioka, K.; Murakami, S. Functional interaction of hepatitis C Virus NS5B with Nucleolin GAR domain. J. Biochem., 2007, 141(6), 917-927.
    • (2007) J. Biochem. , vol.141 , Issue.6 , pp. 917-927
    • Kusakawa, T.1    Shimakami, T.2    Kaneko, S.3    Yoshioka, K.4    Murakami, S.5
  • 81
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein arginine methylation
    • Gary, J. D.; Clarke, S. RNA and protein interactions modulated by protein arginine methylation, Prog. Nucleic Acid Res. Mol. Biol, 1998, 61, 65-131.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 82
    • 0026660237 scopus 로고
    • The glycine-rich domain of nucleolin has an unusual supersecondary structure responsible for its RNA-helix-destabilizing properties
    • Ghisolfi, L.; Joseph, G.; Amalric, F.; Erard, M. The glycine-rich domain of nucleolin has an unusual supersecondary structure responsible for its RNA-helix-destabilizing properties. J. Biol. Chem., 1992, 267(5), 2955-2959.
    • (1992) J. Biol. Chem. , vol.267 , Issue.5 , pp. 2955-2959
    • Ghisolfi, L.1    Joseph, G.2    Amalric, F.3    Erard, M.4
  • 83
    • 0017337454 scopus 로고
    • S-adenosylmethionine: Proteinarginine methyltransferase. Purification and mechanism of the enzyme
    • Lee, H. W.; Kim, S.; Paik, W. K. S-adenosylmethionine: proteinarginine methyltransferase. Purification and mechanism of the enzyme. Biochemistry, 1977, 16(1), 78-85.
    • (1977) Biochemistry , vol.16 , Issue.1 , pp. 78-85
    • Lee, H.W.1    Kim, S.2    Paik, W.K.3
  • 84
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides
    • DOI 10.1016/S0969-2126(03)00071-6
    • Zhang, X.; Cheng, X. Structure of the predominant protein arginine methyltransferase PRMTl and analysis of its binding to substrate peptides. Structure, 2003, 11(5), 509-520. (Pubitemid 36579129)
    • (2003) Structure , vol.11 , Issue.5 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 85
    • 0024465335 scopus 로고
    • SPKK, a new nucleic acid-binding unit of protein found in histone
    • Suzuki, M. SPKK, a new nucleic acid-binding unit of protein found in histone. EMBOJ, 1989, 5(3), 797-804.
    • (1989) EMBOJ , vol.5 , Issue.3 , pp. 797-804
    • Suzuki, M.1
  • 86
    • 0028199619 scopus 로고
    • Interaction of two peptide-acridine conjugates containing the SPKK peptide motif with DNA and chromatin
    • Flock, S.; Bailly, F.; Bailly, C. Waring, M. J.; Henichart, J. P.; Colson, P.; Houssier, C Interaction of two peptide-acridine conjugates containing the SPKK peptide motif with DNA and chromatin. J. Biomol Struct. Dyn., 1994, 11(4), 881-900.
    • (1994) J. Biomol Struct. Dyn. , vol.11 , Issue.4 , pp. 881-900
    • Flock, S.1    Bailly, F.2    Bailly, C.3    Waring, M.J.4    Henichart, J.P.5    Colson, P.6    Houssier, C.7
  • 87
    • 0027216094 scopus 로고
    • Phosphorylation weakens DNA binding by peptides containing multiple "SPKK" sequences
    • Green, G. R.; Lee, H. J.; Poccia, D. L. Phosphorylation weakens DNA binding by peptides containing multiple "SPKK" sequences. J. Biol Chem., 1993, 265(15), 11247-11255.
    • (1993) J. Biol Chem. , vol.265 , Issue.15 , pp. 11247-11255
    • Green, G.R.1    Lee, H.J.2    Poccia, D.L.3
  • 88
    • 0027264033 scopus 로고
    • A tandem repeat of the SPKK peptide motif induces Ψ-type DNA structures at alternating at sequences
    • DOI 10.1016/0014-5793(93)81389-H
    • Bailly, F.; Bailly, C.; Colson, P.; Houssier, C.; Henichart, J. P. A tandem repeat of the SPKK peptide motif induces psi-lype DNA structures at alternating AT sequences. FEBS Lett., 1993, 324(2), 181-184. (Pubitemid 23170411)
    • (1993) FEBS Letters , vol.324 , Issue.2 , pp. 181-184
    • Bailly, F.1    Bailly, C.2    Colson, P.3    Houssier, C.4    Henichart, J.-P.5
  • 89
    • 0024841735 scopus 로고
    • 'SPKK' motifs prefer to bind to DNA at A/T-rich sites
    • Churchill, M. E.; Suzuki, M. 'SPKK' motifs prefer to bind to DNA at A/T-rich sites. EMBO J., 1989, 5(13), 4189-4195. (Pubitemid 20066862)
    • (1989) EMBO Journal , vol.8 , Issue.13 , pp. 4189-4195
    • Churchill, M.E.A.1    Suzuki, M.2
  • 90
    • 0028962767 scopus 로고
    • Structural modification of DNA by a DNA-binding motif SPKK: Detection of changes in base-pair hydrogen bonding and base stacking by UV resonance Raman, spectroscopy
    • Takeuchi, H.; Sasamori, J. Structural modification of DNA by a DNA-binding motif SPKK: detection of changes in base-pair hydrogen bonding and base stacking by UV resonance Raman, spectroscopy. Biopolymers, 1995, 35(4), 359-367.
    • (1995) Biopolymers , vol.35 , Issue.4 , pp. 359-367
    • Takeuchi, H.1    Sasamori, J.2
  • 91
    • 0026661397 scopus 로고
    • Packaging and unpackaging the sea urchin sperm genome
    • Poccia, D. L.; Green, G. R. Packaging and unpackaging the sea urchin sperm genome. Trends Biochem. Sci, 1992, 17(6), 223-227.
    • (1992) Trends Biochem. Sci , vol.17 , Issue.6 , pp. 223-227
    • Poccia, D.L.1    Green, G.R.2
  • 92
    • 0027284143 scopus 로고
    • An NMR study on the DNA-binding SPKK motif and a model for its interaction with DNA
    • Suzuki, M.; Gerstein, M.; Johnson, T. An NMR study on the DNAbinding SPKK motif and a model for its interaction with DNA. Protein Eng., 1993, 6(6), 565-574. (Pubitemid 23246507)
    • (1993) Protein Engineering , vol.6 , Issue.6 , pp. 565-574
    • Suzuki, M.1    Gerstein, M.2    Johnson, T.3
  • 93
    • 0025362431 scopus 로고
    • Repeat peptide motifs which contain β-turns and modulate DNA condensation in chromatin
    • DOI 10.1111/j.1432-1033.1990.tb19088.x
    • Erard, M.; Lakhdar-Ghazal, F.; Amalric, F. Repeat peptide motifswhich contain beta-turns and. modulate DNA condensation in chromatin. Eur. J. Biochem., 1990, 191(1), 19-26. (Pubitemid 20219025)
    • (1990) European Journal of Biochemistry , vol.191 , Issue.1 , pp. 19-26
    • Erard, M.1    Lakhdar-Ghazal, F.2    Amalric, F.3
  • 94
    • 0017401125 scopus 로고
    • Studies on the role and mode of operation of the very-lysine-rich histone H1 in. eukaryote chromatin. the three structural regions of the histone H1 molecule
    • Hartman, P. G.; Chapman, G. E.; Moss, T.; Bradbury, E. M. Studies on the role and mode of operation of the very-lysine-rich histone H1 in. eukaryote chromatin. The three structural regions of the histone H1 molecule. Eur. J. Biochem., 1977, 77(1), 45-51.
    • (1977) Eur. J. Biochem. , vol.77 , Issue.1 , pp. 45-51
    • Hartman, P.G.1    Chapman, G.E.2    Moss, T.3    Bradbury, E.M.4
  • 95
    • 0037357480 scopus 로고    scopus 로고
    • Sequence complexity of histone H1 subtypes
    • Ponte, I.; Vila, R.; Suau, P. Sequence complexity of histone H1 subtypes. Mol. Biol Evol, 2003, 20(3), 371-380.
    • (2003) Mol. Biol Evol , vol.20 , Issue.3 , pp. 371-380
    • Ponte, I.1    Vila, R.2    Suau, P.3
  • 96
    • 70349938605 scopus 로고    scopus 로고
    • Structure prediction of tandem repeats within the C-terminus of histone H1 from various species
    • Matsushima, N.; Nitta, J. Structure prediction of tandem repeats within the C-terminus of histone H1 from various species. Repts. Progr. Polym. Phys. Jpn., 1998, 41, 585-588.
    • (1998) Repts. Progr. Polym. Phys. Jpn. , vol.41 , pp. 585-588
    • Matsushima, N.1    Nitta, J.2
  • 97
    • 0028986682 scopus 로고
    • Kretsinger, R. H. Interactions Of(Ala*Ala* Lys*Pro)n and(Lys*Lys*Ser*Pro)n with DNA, Proposed coiled-coil structure of AlgR3 and AlgP from Pseudomonas aeruginosa
    • Medvedkin, V. N.; Permyakov, E. A.; Klimenko, L. V.; Mitin, Y. V.; Matsushima, N.; Nakayama, S.; Kretsinger, R. H. Interactions Of(Ala*Ala* Lys*Pro)n and(Lys*Lys*Ser*Pro)n with DNA, Proposed coiled-coil structure of AlgR3 and AlgP from Pseudomonas aeruginosa. Protein Eng., 1995, 5(1), 63-70.
    • (1995) Protein Eng. , vol.5 , Issue.1 , pp. 63-70
    • Medvedkin, V.N.1    Permyakov, E.A.2    Klimenko, L.V.3    Mitin, Y.V.4    Matsushima, N.5    Nakayama, S.6
  • 98
    • 0023711642 scopus 로고
    • Alpha-helix in the carboxy-terminal domains of histones H1 and H5
    • Clark, D. J.; Hill, C. S.; Martin, S. R.; Thomas, J. O. Alpha-helix in the carboxy-terminal domains of histones H1 and H5. EMBO J., 1988, 7(1), 69-75.
    • (1988) EMBO J. , vol.7 , Issue.1 , pp. 69-75
    • Clark, D.J.1    Hill, C.S.2    Martin, S.R.3    Thomas, J.O.4
  • 99
    • 0024426046 scopus 로고
    • A stable alpha-helical element in the carboxy-terminal domain of free and chromatinbound histone H1 from sea urchin sperm
    • Hill, C. S.; Martin, S. R.; Thomas, J. O. A stable alpha-helical element in the carboxy-terminal domain of free and chromatinbound histone H1 from sea urchin sperm. EMBO J., 1989, 5(9), 2591-2599.
    • (1989) EMBO J. , vol.5 , Issue.9 , pp. 2591-2599
    • Hill, C.S.1    Martin, S.R.2    Thomas, J.O.3
  • 100
    • 0027159331 scopus 로고
    • Helical structure of basic proteins from spermatozoa. Comparison, with, model peptides
    • Verdaguer, N.; Perello, M.; Palau, J.; Subirana, J. A. Helical structure of basic proteins from spermatozoa. Comparison, with, model peptides. Eur. J. Biochem., 1993,214(3), 879-887.
    • (1993) Eur. J. Biochem. , vol.214 , Issue.3 , pp. 879-887
    • Verdaguer, N.1    Perello, M.2    Palau, J.3    Subirana, J.A.4
  • 101
    • 25444523218 scopus 로고    scopus 로고
    • DNA induced secondary structure of the carboxyl-terminal domain of histone H1
    • Roque, A.; lloro, I.; Ponte, I.; Arrondo, J. L; Suau, P. DNA induced secondary structure of the carboxyl-terminal domain of histone H1. J. Biol. Chem., 2005, 250(37), 32141-32147.
    • (2005) J. Biol. Chem. , vol.250 , Issue.37 , pp. 32141-32147
    • Roque, A.1    Lloro, I.2    Ponte, I.3    Arrondo, J.L.4    Suau, P.5
  • 102
    • 34548722169 scopus 로고    scopus 로고
    • Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1
    • DOI 10.1529/biophysj.107.104513
    • Roque, A.; Ponte, I.; Suau, P. Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1. Biophys. J, 2007, 93(6), 2170-2177. (Pubitemid 47437600)
    • (2007) Biophysical Journal , vol.93 , Issue.6 , pp. 2170-2177
    • Roque, A.1    Ponte, I.2    Suau, P.3
  • 103
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci., 2002, 11(4), 739-756.
    • (2002) Protein Sci. , vol.11 , Issue.4 , pp. 739-756
    • Uversky, V.N.1
  • 104
    • 0027238126 scopus 로고
    • Interchangeability of the adsorption proteins of bacteriophages Ff and IKe
    • Endemann, H.; Gailus, V; Rasched, I. Interchangeability of the adsorption proteins of bacteriophages Ff and IKe. J. Virol, 1993, 67(6), 3332-3337.
    • (1993) J. Virol , vol.67 , Issue.6 , pp. 3332-3337
    • Endemann, H.1    Gailus, V.2    Rasched, I.3
  • 105
    • 0000046526 scopus 로고    scopus 로고
    • Filamentous phage infection: Crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA
    • DOI 10.1016/S0969-2126(99)80092-6
    • Lubkowski, J.; Hennecke, F.; Pluckthun, A.; Wlodawer, A. Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal. domain of TolA. Structure, 1999, 7(6), 711-722. (Pubitemid 29277424)
    • (1999) Structure , vol.7 , Issue.6 , pp. 711-722
    • Lubkowski, J.1    Hennecke, F.2    Pluckthun, A.3    Wlodawer, A.4
  • 106
    • 0023088728 scopus 로고
    • Possible eggshell protein gene from Schistosoma mansoni
    • Johnson, K. S.; Taylor, D. W.; Cordingley, J. S. Possible eggshell protein gene from Schistosoma mansoni. Mol. Biochem. Parasitai, 1987, 22(1), 89-100.
    • (1987) Mol. Biochem. Parasitai , vol.22 , Issue.1 , pp. 89-100
    • Johnson, K.S.1    Taylor, D.W.2    Cordingley, J.S.3
  • 108
    • 0030047252 scopus 로고    scopus 로고
    • Domain structure and conformation of histidine-proline-rich glycoprotein
    • DOI 10.1021/bi952061t
    • Borza, D. B.; Tatum, F. M.; Morgan, W. T. Domain structure and conformation of histidine-proline-rich glycoprotein. Biochemistry, 1996, 35(6), 1925-1934. (Pubitemid 26062642)
    • (1996) Biochemistry , vol.35 , Issue.6 , pp. 1925-1934
    • Borza, D.-B.1    Tatum, F.M.2    Morgan, W.T.3
  • 109
    • 0032489379 scopus 로고    scopus 로고
    • Histidine-proline-rich glycoprotein as a plasma pH sensor. Modulation of its interaction with glycosaminoglycans by ph and metals
    • Borza, D. B.; Morgan, W. T. Histidine-proline-rich glycoprotein as a plasma pH sensor. Modulation of its interaction with glycosaminoglycans by ph and metals. J. Biol. Chem., 1998, 273(10), 5493-5499.
    • (1998) J. Biol. Chem. , vol.273 , Issue.10 , pp. 5493-5499
    • Borza, D.B.1    Morgan, W.T.2
  • 110
    • 0023522387 scopus 로고
    • Further characterization of the interaction of histidine-rich glycoprotein with heparin: Evidence for the binding of two molecules of histidine-rich glycoprotein by high molecular weight heparin and for the involvement of histidine residues in heparin binding
    • Burch, M. K.; Blackburn, M. N.; Morgan, W. T. Further characterization of the interaction of histidine-rich glycoprotein with heparin: evidence for the binding of two molecules of histidine-rich glycoprotein by high molecular weight heparin and for the involvement of histidine residues in heparin binding. Biochemistry, 1987, 26(23), 7477-7482.
    • (1987) Biochemistry , vol.26 , Issue.23 , pp. 7477-7482
    • Burch, M.K.1    Blackburn, M.N.2    Morgan, W.T.3
  • 112
    • 0024297499 scopus 로고
    • Paramagnetic probes of the domain structure of histidine-rich glycoprotein
    • Muhoberac, B. B.; Burch, M. K.; Morgan, W. T. Paramagnetic probes of the domain structure of histidine-rich glycoprotein. Biochemistry, 1988, 27(2), 746-752.
    • (1988) Biochemistry , vol.27 , Issue.2 , pp. 746-752
    • Muhoberac, B.B.1    Burch, M.K.2    Morgan, W.T.3
  • 113
    • 0026232321 scopus 로고
    • Metal ion affinity adsorption of a Zn(II)-transport protein present in. maternal plasma during lactation: Structural characterization and identification as histidine-rich glycoprotein
    • Yip, T. T.; Hutchens, T. W. Metal ion affinity adsorption of a Zn(II)-transport protein present in. maternal plasma during lactation: structural characterization and identification as histidine-rich glycoprotein. Protein Expr. Purif, 1991, 2(5-6), 355-362.
    • (1991) Protein Expr. Purif , vol.2 , Issue.5-6 , pp. 355-362
    • Yip, T.T.1    Hutchens, T.W.2
  • 114
    • 0027972369 scopus 로고
    • Study of a salivary proline-rich protein, repeat sequence
    • Murray, N. J.; Williamson, M. P. Conformational, study of a salivary proline-rich protein, repeat sequence. Eur. J. Biochem., 1994, 219(3), 915-921.
    • (1994) Eur. J. Biochem. , vol.219 , Issue.3 , pp. 915-921
    • Murray, N.J.1    Conformational, W.M.P.2
  • 115
    • 0023644946 scopus 로고
    • Histidine-rich glycoprotein modulation of the anticoagulant activity of heparin. Evidence for a mechanism involving competition with both antithrombin and thrombin for heparin binding
    • Peterson, C. B.; Morgan, W. T.; Blackburn, M. N. Histidine-rich glycoprotein modulation of the anticoagulant activity of heparin. Evidence for a mechanism involving competition with both antithrombin and thrombin for heparin binding. J. Biol Chem., 1987, 262(16), 7567-7574.
    • (1987) J. Biol Chem. , vol.262 , Issue.16 , pp. 7567-7574
    • Peterson, C.B.1    Morgan, W.T.2    Blackburn, M.N.3
  • 117
    • 0026093234 scopus 로고
    • Molecular cloning and primary structure of squid(Loligo forbesi) rhodopsin, a phospholipase C-directed G-protein-linked receptor
    • Hall, M. D.; Hoon, M. A.; Ryba, N. J.; Pottinger, J. D.; Keen, J. N.; Saibil, H. R.; Findlay, J. B. Molecular cloning and primary structure of squid(Loligo forbesi) rhodopsin, a phospholipase C-directed G-protein-linked receptor. Biochem. J., 1991, 274(1), 35-40.
    • (1991) Biochem. J. , vol.274 , Issue.1 , pp. 35-40
    • Hall, M.D.1    Hoon, M.A.2    Ryba, N.J.3    Pottinger, J.D.4    Keen, J.N.5    Saibil, H.R.6    Findlay, J.B.7
  • 118
    • 0027406791 scopus 로고
    • Cloning and nucleotide sequence of cDNA for rhodopsin of the squid Todarodes pacificus
    • DOI 10.1016/0014-5793(93)81480-N
    • Hara-Nishimura, I.; Kondo, M.; Nishimura, M.; Hara, R.; Hara, T. Cloning and nucleotide sequence of cDNA for rhodopsin of the squid Todarodes pacificus. FEBSLett., 1993, 317(1-2), 5-11. (Pubitemid 23043928)
    • (1993) FEBS Letters , vol.317 , Issue.1-2 , pp. 5-11
    • Hara-Nishimura, I.1    Kondo, M.2    Nishimura, M.3    Hara, R.4    Hara, T.5
  • 121
    • 0035976714 scopus 로고    scopus 로고
    • Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane
    • Davies, A.; Gowen, B. E.; Krebs, A. M.; Schertler, G. f.; Saibil, H. R. Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane. J. Mol Biol, 2001, 314(3), 455-463.
    • (2001) J. Mol Biol , vol.314 , Issue.3 , pp. 455-463
    • Davies, A.1    Gowen, B.E.2    Krebs, A.M.3    Saibil, H.R.4
  • 122
    • 70349960575 scopus 로고
    • Structure of the repetitive carboxy-terminal domain of octopus rhodopsin: 1H-NMR studies of the synthetic repeat pentapeptides
    • Matsushima, N.; Imafuku, T.; Tsuda, S.; Aimoto, S.; Hojo, H.; Yoshimura, S.; K., H. Structure of the repetitive carboxy-terminal domain of octopus rhodopsin: 1H-NMR studies of the synthetic repeat pentapeptides. Repts. Progr. Polym. Phys. Jpn., 1990, 33, 595-596.
    • (1990) Repts. Progr. Polym. Phys. Jpn. , vol.33 , pp. 595-596
    • Matsushima, N.1    Imafuku, T.2    Tsuda, S.3    Aimoto, S.4    Hojo, H.5    Yoshimura, S.6
  • 123
    • 70349951201 scopus 로고
    • Two-dimensional NMR studies of the synthetic repeat pentapeptide at the carboxy-terminal domain of octopus rhodopsin
    • Kumaki, K.; Sakae, T.; Hikichi, K.; Hojo, H.; Aimoto, S.; Matsushima, N. Two-dimensional NMR studies of the synthetic repeat pentapeptide at the carboxy-terminal domain of octopus rhodopsin, Repts. Progr. Polym. Phys. Jpn., 1991, 34, 475-478.
    • (1991) Repts. Progr. Polym. Phys. Jpn. , vol.34 , pp. 475-478
    • Kumaki, K.1    Sakae, T.2    Hikichi, K.3    Hojo, H.4    Aimoto, S.5    Matsushima, N.6
  • 124
    • 70349949613 scopus 로고
    • Structure of tandem reapeats at the c-terminal of octopus/squid rhodopsin as studied by twodimensional NMR and molecular modeling
    • Kumaki, K.; Hikichi, H.; Hojo, H.; Aimoto, S.; Nakayama, S.; Kretsinger, R. H.; Matsushima, N. Structure of tandem reapeats at the c-terminal of octopus/squid rhodopsin as studied by twodimensional NMR and molecular modeling. Repts. Progr. Polym. Phys. Jpn., 1992, 36,551-554.
    • (1992) Repts. Progr. Polym. Phys. Jpn. , vol.36 , pp. 551-554
    • Kumaki, K.1    Hikichi, H.2    Hojo, H.3    Aimoto, S.4    Nakayama, S.5    Kretsinger, R.H.6    Matsushima, N.7
  • 125
    • 8844241421 scopus 로고    scopus 로고
    • Type i secretion in gram-negative bacteria
    • Delepelaire, P. Type I secretion in gram-negative bacteria. Biochim Biophys. Acta, 2004, 1694(1-3), 149-161.
    • (2004) Biochim Biophys. Acta , vol.1694 , Issue.1-3 , pp. 149-161
    • Delepelaire, P.1
  • 126
    • 18844428872 scopus 로고    scopus 로고
    • Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway
    • DOI 10.1080/09687860500042013
    • Holland, I. B.; Schmitt, L.; Young, J. Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway(review). Mol. Membr. Biol., 2005, 22(1-2), 29-39. (Pubitemid 40692152)
    • (2005) Molecular Membrane Biology , vol.22 , Issue.1-2 , pp. 29-39
    • Holland, I.B.1    Schmitt, L.2    Young, J.3
  • 127
    • 0034467679 scopus 로고    scopus 로고
    • RTX toxin structure and function: A story of numerous anomalies and few analogies in toxin, biology
    • Welch, R. A. RTX toxin structure and function: a story of numerous anomalies and few analogies in toxin, biology. Curr. Top. Microbiol. Immunol, 2001, 257, 85-111.
    • (2001) Curr. Top. Microbiol. Immunol , vol.257 , pp. 85-111
    • Welch, R.A.1
  • 128
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
    • Baumann, U.; Wu, S.; Flaherty, K. M.; McKay, D. B. Threedimensional, structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with, a calcium binding parallel, beta roll motif. EMBO J, 1993, 12(9), 3357-3364. (Pubitemid 23256422)
    • (1993) EMBO Journal , vol.12 , Issue.9 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 129
    • 35748968219 scopus 로고    scopus 로고
    • A calcium-gated lid and a large β-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens
    • DOI 10.1074/jbc.M704942200
    • Meier, R.; Drepper, T.; Svensson, V.; Jaeger, K. E.; Baumann, U. A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens. J. Biol Chem, 2007, 252(43), 31477-31483. (Pubitemid 350044856)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.43 , pp. 31477-31483
    • Meier, R.1    Drepper, T.2    Svensson, V.3    Jaeger, K.-E.4    Baumann, U.5
  • 130
    • 59449107337 scopus 로고    scopus 로고
    • RTX calcium, binding motifs are intrinsically disordered in the absence of calcium.: Implication for protein secretion
    • Chenal, A.; Guijarro, J. I.; Raynal, B.; Delepierre, M.; Ladant, D. RTX calcium, binding motifs are intrinsically disordered in the absence of calcium.: implication for protein secretion, J. Biol. Chem., 2009, 254(3), 1781-1789.
    • (2009) J. Biol. Chem. , vol.254 , Issue.3 , pp. 1781-1789
    • Chenal, A.1    Guijarro, J.I.2    Raynal, B.3    Delepierre, M.4    Ladant, D.5
  • 131
    • 0001952505 scopus 로고
    • Homologous genes encode two distinct histidine-rich proteins in a cloned isolate of Plasmodium falciparum
    • Wellems, T. E.; Howard, R. J. Homologous genes encode two distinct histidine-rich proteins in a cloned isolate of Plasmodium falciparum. Proc. Natl Acad. Sci. USA, 1986, 53(16), 6065-6069.
    • (1986) Proc. Natl Acad. Sci. USA , vol.53 , Issue.16 , pp. 6065-6069
    • Wellems, T.E.1    Howard, R.J.2
  • 132
    • 35348895635 scopus 로고    scopus 로고
    • Interaction of iron(II)-heme and artemisinin with a peptide mimic of Plasmodium falciparum HRP-II
    • DOI 10.1016/j.jinorgbio.2007.04.016, PII S0162013407000876
    • ccardo, A.; Laurent, S. A.; Mazarguil, H.; Meyer, M.; Robert, A.; Meunier, B. Interaction of iron(II)-heme and artemisinin with a peptide mimic of Plasmodium falciparum HRP-II. J. Inorg. Biochem., 2007, 101(11-12), 1739-1747. (Pubitemid 47576188)
    • (2007) Journal of Inorganic Biochemistry , vol.101 , Issue.11-12 , pp. 1739-1747
    • Accardo, A.1    Laurent, S.A.2    Mazarguil, H.3    Meyer, M.4    Robert, A.5    Meunier, B.6
  • 133
    • 0032829561 scopus 로고    scopus 로고
    • Heme binding and polymerization by Plasmodium falciparum histidine rich protein II: Influence of pH on activity and. conformation
    • Lynn, A.; Chandra, S.; Malhotra, P.; Chauhan, V. S. Heme binding and polymerization by Plasmodium falciparum histidine rich protein II: influence of pH on activity and. conformation. FEBS Lett., 1999, 459(2), 267-271.
    • (1999) FEBS Lett. , vol.459 , Issue.2 , pp. 267-271
    • Lynn, A.1    Chandra, S.2    Malhotra, P.3    Chauhan, V.S.4
  • 134
    • 0031469955 scopus 로고    scopus 로고
    • Synthetic peptides corresponding to a repetitive sequence of ma-larial histidine rich protein bind haem and inhibit haemozoin formation in vitro
    • Pandey, A. V.; Joshi, R.; Tekwani, B. L.; Singh, R. L.; Chauhan, V. S. Synthetic peptides corresponding to a repetitive sequence of ma-larial histidine rich protein bind haem and inhibit haemozoin formation in vitro. Mol. Biochem. Parasitol., 1997, 90(1), 281-287.
    • (1997) Mol. Biochem. Parasitol. , vol.90 , Issue.1 , pp. 281-287
    • Pandey, A.V.1    Joshi, R.2    Tekwani, B.L.3    Singh, R.L.4    Chauhan, V.S.5
  • 135
    • 12344295392 scopus 로고    scopus 로고
    • Heme binding to the histidine-rich protein II from Plasmodium falciparum
    • DOI 10.1021/bi048570p
    • Schneider, E. L.; Marietta, M. A. Heme binding to the histidinerich protein II from Plasmodium falciparum. Biochemistry, 2005, 44(3), 979-986. (Pubitemid 40129658)
    • (2005) Biochemistry , vol.44 , Issue.3 , pp. 979-986
    • Schneider, E.L.1    Marletta, M.A.2
  • 136
    • 0037651040 scopus 로고    scopus 로고
    • Plasmodium falciparum histidine-rich protein II binds to actin, phosphatidylinositol 4,5-bisphosphate and erythrocyte ghosts in a pH-dependent manner and undergoes coil-to-helix transitions in anionic micelles
    • DOI 10.1016/S0166-6851(03)00057-4
    • Benedetti, C. E.; Kobarg, J.; Pertinhez, T. A.; Gatti, R. M.; de Souza, O. N.; Spisni, A.; Meneghini, R. Plasmodium falciparum histidine-rich protein II binds to actin, phosphatidylinositol 4,5-bisphosphate and erythrocyte ghosts in a pH-dependent manner and undergoes coil-to-helix transitions in anionic micelles. Mol. Biochem. Parasitol., 2003, 128(2), 157-166. (Pubitemid 36549245)
    • (2003) Molecular and Biochemical Parasitology , vol.128 , Issue.2 , pp. 157-166
    • Benedetti, C.E.1    Kobarg, J.2    Pertinhez, T.A.3    Gatti, R.M.4    De Souza, O.N.5    Spisni, A.6    Meneghini, R.7
  • 137
    • 0024355175 scopus 로고
    • Purification and partial characterization of an unusual protein of Plasmodium falciparum: Histidine-rich protein II
    • Panton, L. J.; McPhie, P.; Maloy, W. L.; Wellems, T. E.; Taylor, D. W.; Howard, R. J. Purification and partial characterization of an unusual protein of Plasmodium falciparum: histidine-rich protein II. Mol. Biochem. Parasitol., 1989, 35(2), 149-160.
    • (1989) Mol. Biochem. Parasitol. , vol.35 , Issue.2 , pp. 149-160
    • Panton, L.J.1    McPhie, P.2    Maloy, W.L.3    Wellems, T.E.4    Taylor, D.W.5    Howard, R.J.6
  • 139
    • 33745006606 scopus 로고    scopus 로고
    • Flogel, M. Galectin-3: An open-ended story
    • Dumic, J.; Dabelic, S.; Flogel, M. Galectin-3: an open-ended story. Biochim. Biophys. Acta, 2006, 1760(4), 616-635.
    • (2006) Biochim. Biophys. Acta , vol.1760 , Issue.4 , pp. 616-635
    • Dumic, J.1    Dabelic, S.2
  • 140
    • 0028225890 scopus 로고
    • Structure of baby hamster kidney carbohydrate-binding protein CBP30, an S-type animal lectin
    • ehul, B.; Bawumia, S.; Martin, S. R.; Hughes, R. C. Structure of baby hamster kidney carbohydrate-binding protein CBP30, an Stype animal lectin. J. Biol. Chem., 1994, 269(27), 18250-18258. (Pubitemid 24982661)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.27 , pp. 18250-18258
    • Mehul, B.1    Bawumia, S.2    Martin, S.R.3    Hughes, R.C.4
  • 141
    • 0035901521 scopus 로고    scopus 로고
    • NMR solution studies of hamster galectin-3 and electron microscopic visualization of surface-adsorbed complexes: Evidence for interactions between the N- And C-terminal domains
    • Birdsall, B.; Feeney, J.; Burdett, I. D.; Bawumia, S.; Barboni, E. A.; Hughes, R. C. NMR solution studies of hamster galectin-3 and electron microscopic visualization of surface-adsorbed complexes: evidence for interactions between the N- and C-terminal domains. Biochemistry, 2001, 40(15), 4859-4866.
    • (2001) Biochemistry , vol.40 , Issue.15 , pp. 4859-4866
    • Birdsall, B.1    Feeney, J.2    Burdett, I.D.3    Bawumia, S.4    Barboni, E.A.5    Hughes, R.C.6
  • 142
    • 0027165161 scopus 로고
    • Carbohydrate-binding protein 35. I. Properties of the recombinant polypeptide and the individuality of the domains
    • grwal, N.; Sun, Q.; Wang, S. Y.; Wang, J. L. Carbohydratebinding protein. 35. I. Properties of the recombinant polypeptide and the individuality of the domains. J. Biol. Chem., 1993, 265(20), 14932-14939. (Pubitemid 23206641)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.20 , pp. 14932-14939
    • Agrwal, N.1    Sun, Q.2    Wang, S.-Y.3    Wang, J.L.4
  • 145
    • 0034705390 scopus 로고    scopus 로고
    • A protein containing a serine-rich domain with vesicle fusing properties mediates cell cycle-dependent cytosolic pH regulation
    • Brazill, D. T.; Caprette, D. R.; Myler, H. A.; Hatton, R. D.; Ammann, R. R.; Lindsey, D. F.; Brock, D. A.; Gomer, R. H. A protein containing a serine-rich domain with vesicle fusing properties mediates cell cycle-dependent cytosolic pH regulation, J. Biol. Chem., 2000, 275(25), 19231-19240.
    • (2000) J. Biol. Chem. , vol.275 , Issue.25 , pp. 19231-19240
    • Brazill, D.T.1    Caprette, D.R.2    Myler, H.A.3    Hatton, R.D.4    Ammann, R.R.5    Lindsey, D.F.6    Brock, D.A.7    Gomer, R.H.8
  • 146
    • 0029855247 scopus 로고    scopus 로고
    • RtoA links initial cell type choice to the cell cycle in Diclyostelium
    • Wood, S. A.; Ammann, R. R.; Brock, D. A.; Li, L.; Spann, T.; Gomer, R. H. RtoA links initial cell type choice to the cell cycle in Diclyostelium. Development, 1996, 122(11), 3677-3685.
    • (1996) Development , vol.122 , Issue.11 , pp. 3677-3685
    • Wood, S.A.1    Ammann, R.R.2    Brock, D.A.3    Li, L.4    Spann, T.5    Gomer, R.H.6
  • 147
    • 0027564435 scopus 로고
    • 3rd A repeating 11-mer amino acid motif and plant desiccation
    • Dure, L., 3rd A repeating 11-mer amino acid motif and plant desiccation. Plant J., 1993, 3(3), 363-369.
    • (1993) Plant J. , vol.3 , Issue.3 , pp. 363-369
    • Dure, L.1
  • 148
    • 0742323272 scopus 로고    scopus 로고
    • POPP the question: What do LEA proteins do?
    • DOI 10.1016/j.tplants.2003.10.012
    • ise, M. J.; Tunnacliffe, A. POPP the question: what do LEA proteins do? Trends Plant Sci., 2004, 9(1), 13-17. (Pubitemid 38157641)
    • (2004) Trends in Plant Science , vol.9 , Issue.1 , pp. 13-17
    • Wise, M.J.1    Tunnacliffe, A.2
  • 149
    • 34548460796 scopus 로고    scopus 로고
    • The continuing conundrum of the LEA. proteins
    • Tunnacliffe, A.; Wise, M. J. The continuing conundrum of the LEA. proteins. Naturwissenschaften, 2007, 94(10), 791-812.
    • (2007) Naturwissenschaften , vol.94 , Issue.10 , pp. 791-812
    • Tunnacliffe, A.1    Wise, M.J.2
  • 150
    • 55949092886 scopus 로고    scopus 로고
    • Alpha-synuclein misfolding and neurodegenerative diseases
    • Uversky, V. N. Alpha-synuclein misfolding and neurodegenerative diseases. Curr. Protein Pept. Sci, 2008, 9(5), 507-540.
    • (2008) Curr. Protein Pept. Sci , vol.9 , Issue.5 , pp. 507-540
    • Uversky, V.N.1
  • 151
    • 0027564363 scopus 로고
    • Unusual sequence of group 3 LEA(II) mRNA inducible by dehydration stress in wheat
    • Curry, J.; Walker-Simmons, M. K. Unusual sequence of group 3 LEA(II) mRNA inducible by dehydration stress in wheat. Plant Mol. Biol., 1993, 27(5), 907-912.
    • (1993) Plant Mol. Biol. , vol.27 , Issue.5 , pp. 907-912
    • Curry, J.1    Walker-Simmons, M.K.2
  • 152
    • 0037034885 scopus 로고    scopus 로고
    • Anhydrobiosis: Plant desiccation gene found in a nematode
    • Browne, J.; Tunnacliffe, A.; Burnell, A. Anhydrobiosis: plant desiccation gene found in a nematode. Nature, 2002, 416(6876), 38.
    • (2002) Nature , vol.416 , Issue.6876 , pp. 38
    • Browne, J.1    Tunnacliffe, A.2    Burnell, A.3
  • 153
    • 0038305931 scopus 로고    scopus 로고
    • Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein
    • DOI 10.1074/jbc.M212007200
    • Goyal, K.; Tisi, L.; Basran, A.; Browne, J.; Burnell, A.; Zurdo, J.; Tunnacliffe, A. Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J. Biol. Chem., 2003, 275(15), 12977-12984. (Pubitemid 36800064)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 12977-12984
    • Goyal, K.1    Tisi, L.2    Basran, A.3    Browne, J.4    Burnell, A.5    Zurdo, J.6    Tunnacliffe, A.7
  • 154
    • 0035847037 scopus 로고    scopus 로고
    • Isolation and characterization of a D-7 LEA protein from, pollen that stabilizes glasses in vitro
    • Wolkers, W. F.; McCready, S.; Brandt, W. F.; Lindsey, G. G.; Hoekstra, F. A. Isolation and characterization of a D-7 LEA protein from, pollen that stabilizes glasses in vitro. Biochim. Biophys. Acta, 2001, 1544(1-2), 196-206.
    • (2001) Biochim. Biophys. Acta , vol.1544 , Issue.1-2 , pp. 196-206
    • Wolkers, W.F.1    McCready, S.2    Brandt, W.F.3    Lindsey, G.G.4    Hoekstra, F.A.5
  • 155
    • 44849083256 scopus 로고    scopus 로고
    • What determines the molecular composition of abnormal protein aggregates in neurodegenerative disease?
    • Armstrong, R. A.; Lantos, P. L.; Cairns, N. J. What determines the molecular composition of abnormal protein aggregates in neurodegenerative disease? Neuropathology, 2008, 28(4), 351-365.
    • (2008) Neuropathology , vol.28 , Issue.4 , pp. 351-365
    • Armstrong, R.A.1    Lantos, P.L.2    Cairns, N.J.3
  • 157
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of α-synuclein in its free and lipid-associated states
    • DOI 10.1006/jmbi.2001.4538
    • Eliezer, D.; Kutluay, E.; Bussell, R., Jr.; Browne, G. Conformational properties of alpha-synuclein in its free and lipid-associated states. J. Mol. Biol., 2001, 307(4), 1061-1073. (Pubitemid 33029953)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.4 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell Jr., R.3    Browne, G.4
  • 158
    • 0141677840 scopus 로고    scopus 로고
    • A protein-chameleon: Conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders
    • Uversky, V. N. A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders. J. Biomol Struct. Dyn., 2003, 27(2), 211-234.
    • (2003) J. Biomol Struct. Dyn. , vol.27 , Issue.2 , pp. 211-234
    • Uversky, V.N.1
  • 159
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • Uversky, V. N.; Li, J.; Fink, A. L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem., 2001, 276(14), 10737-10744.
    • (2001) J. Biol. Chem. , vol.276 , Issue.14 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 160
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb, P. H.; Zhen, W.; Poon, A. W.; Conway, K. A.; Lansbury, P. T., Jr. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded, Biochemistry, 1996, 35(43), 13709-13715.
    • (1996) Biochemistry , vol.35 , Issue.43 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury Jr., P.T.5
  • 161
    • 0036157963 scopus 로고    scopus 로고
    • A Raman optical activity study of rheomorphism in. caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins
    • Syme, C. D.; Blanch, E. W.; Holt, C.; Jakes, R.; Goedert, M.; Hecht, L.; Barron, L. D. A Raman optical activity study of rheomorphism in. caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins. Eur. J. Biochem., 2002, 269(1), 148-156.
    • (2002) Eur. J. Biochem. , vol.269 , Issue.1 , pp. 148-156
    • Syme, C.D.1    Blanch, E.W.2    Holt, C.3    Jakes, R.4    Goedert, M.5    Hecht, L.6    Barron, L.D.7
  • 162
    • 0038341134 scopus 로고    scopus 로고
    • A broken alpha -helix in folded alpha -Synuclein
    • Chandra, S.; Chen, X.; Rizo, J.; Jahn, R.; Sudhof, T. C. A broken alpha -helix in folded alpha -Synuclein. J. Biol Chem., 2003, 275(17), 15313-15318.
    • (2003) J. Biol Chem. , vol.275 , Issue.17 , pp. 15313-15318
    • Chandra, S.1    Chen, X.2    Rizo, J.3    Jahn, R.4    Sudhof, T.C.5
  • 163
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human α-synuclein
    • DOI 10.1074/jbc.M411805200
    • Ulmer, T. S.; Bax, A.; Cole, N. B.; Nussbaum, R. L. Structure and dynamics of micelle-bound human alpha-synuclein. J. Biol. Chem., 2005, 250(10), 9595-9603. (Pubitemid 40409655)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 165
    • 0037432332 scopus 로고    scopus 로고
    • Conformational behavior and aggregation of alpha-synuclein in organic solvents: Modeling the effects of membranes
    • Munishkina, L. A.; Phelan, C.; Uversky, V. N.; Fink, A. L. Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes. Biochemistry, 2003, 42(9), 2720-2730.
    • (2003) Biochemistry , vol.42 , Issue.9 , pp. 2720-2730
    • Munishkina, L.A.1    Phelan, C.2    Uversky, V.N.3    Fink, A.L.4
  • 167
    • 0037469147 scopus 로고    scopus 로고
    • The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation
    • Kessler, J. C.; Rochet, J. C.; Lansbury, P. T., Jr. The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation, Biochemistry, 2003, 42(3), 672-678.
    • (2003) Biochemistry , vol.42 , Issue.3 , pp. 672-678
    • Kessler, J.C.1    Rochet, J.C.2    Lansbury Jr., P.T.3
  • 168
    • 0024698889 scopus 로고
    • A cDNA-based comparison of dehydration-induced proteins(dehydrins) in barley and corn
    • Close, T. J.; Kortt, A. A.; Chandler, P. M. A cDNA-based comparison of dehydration-induced proteins(dehydrins) in barley and corn, Plant Mol. Biol., 1989, 13(1), 95-108.
    • (1989) Plant Mol. Biol. , vol.13 , Issue.1 , pp. 95-108
    • Close, T.J.1    Kortt, A.A.2    Chandler, P.M.3
  • 169
    • 33847140438 scopus 로고    scopus 로고
    • Plant dehydrins - Tissue location, structure and function
    • DOI 10.2478/s11658-006-0044-0
    • Rorat, T. Plant dehydrins-tissue location, structure and function. Cell Mol. Biol. Lett., 2006, 11(4), 536-556. (Pubitemid 46708880)
    • (2006) Cellular and Molecular Biology Letters , vol.11 , Issue.4 , pp. 536-556
    • Rorat, T.1
  • 170
    • 0031007034 scopus 로고    scopus 로고
    • Dehydrins: A commonalty in the response of plants to dehydration and low temperature
    • Close, T. J. Dehydrins: A commonalty in the response of plants to dehydration and low temperature. Physiol. Plant, 1997, 100, 196-206.
    • (1997) Physiol. Plant , vol.100 , pp. 196-206
    • Close, T.J.1
  • 172
    • 0034781789 scopus 로고    scopus 로고
    • Characterization and cryoprotective activity of cold-responsive dehydrin from. Citrus unshiu
    • Hara, M.; Terashima, S.; Kuboi, T. Characterization and cryoprotective activity of cold-responsive dehydrin. from. Citrus unshiu. J. Plant Physiol, 2001, 158(10), 1333-1339.
    • (2001) J. Plant Physiol , vol.158 , Issue.10 , pp. 1333-1339
    • Hara, M.1    Terashima, S.2    Kuboi, T.3
  • 173
    • 0033134023 scopus 로고    scopus 로고
    • Purification and partial characterization of a dehydrin involved in chilling tolerance during seedling emergence of cowpea
    • Ismail, A. M.; Hall, A. E.; Close, T. J. Purification and partial characterization of a dehydrin involved in chilling tolerance during seedling emergence of cowpea. Plant Physiol, 1999, 120(1), 237-244.
    • (1999) Plant Physiol , vol.120 , Issue.1 , pp. 237-244
    • Ismail, A.M.1    Hall, A.E.2    Close, T.J.3
  • 174
    • 0029805280 scopus 로고    scopus 로고
    • The recombinant dehydrin-like desiccation stress protein from the resurrection plant Craterostigma plantagineum displays no defined three-dimensional structure in its native state
    • Lisse, T.; Bartels, D.; Kalbitzer, H. R.; Jaenicke, R. The recombinant dehydrin-like desiccation stress protein from the resurrection, plant Craterostigma plantagineum displays no defined threedimensional structure in its native state. Biol Chem., 1996, 377(9), 555-561. (Pubitemid 26383818)
    • (1996) Biological Chemistry , vol.377 , Issue.9 , pp. 555-561
    • Lisse, T.1    Bartels, D.2    Kalbitzer, H.R.3    Jaenicke, R.4
  • 175
    • 33745655415 scopus 로고    scopus 로고
    • Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments
    • DOI 10.1104/pp.106.079848
    • Mouillon, J. M. G. P.; Harryson, P. Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments. Plant Physiol, 2006, 141(2), 638-650. (Pubitemid 43974557)
    • (2006) Plant Physiology , vol.141 , Issue.2 , pp. 638-650
    • Mouillon, J.-M.1    Gustafsson, P.2    Harryson, P.3
  • 176
    • 0346034535 scopus 로고    scopus 로고
    • Conformation of a group 2 late embryogenesis abundant protein from soybean, Evidence of poly(L-proline)-type II structure
    • Soulages, J. L.; Kim, K.; Arrese, E. L.; Walters, C.; Cushman, J. C. Conformation of a group 2 late embryogenesis abundant protein from soybean, Evidence of poly(L-proline)-type II structure. Plant Physiol, 2003, 137(3), 963-975.
    • (2003) Plant Physiol , vol.137 , Issue.3 , pp. 963-975
    • Soulages, J.L.1    Kim, K.2    Arrese, E.L.3    Walters, C.4    Cushman, J.C.5
  • 177
    • 0028078078 scopus 로고
    • Nuclear and cytoplasmic localization of maize embryo and aleurone dehydrin
    • Asghar, R.; Fenton, R. D.; DeMason, D. A.; Close, T. J. Nuclear and cytoplasmic localization of maize embryo and aleurone dehydrin. Protoplasma, 1994, 177, 87-94.
    • (1994) Protoplasma , vol.177 , pp. 87-94
    • Asghar, R.1    Fenton, R.D.2    Demason, D.A.3    Close, T.J.4
  • 178
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions: Sparc, tenascin, and thrombospondin
    • Sage, E. H.; Bornstein, P. Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin, J. Biol. Chem., 1991, 266(23), 14831-14834. (Pubitemid 21907577)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.23 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 179
    • 0029952406 scopus 로고    scopus 로고
    • Natural history study of pseudoachondroplasia
    • McKeand, J.; Rotta, J.; Hecht, J. T. Natural history study of pseudoachondroplasia. Am. J. Med. Genet, 1996, 63(2), 406-410.
    • (1996) Am. J. Med. Genet , vol.63 , Issue.2 , pp. 406-410
    • McKeand, J.1    Rotta, J.2    Hecht, J.T.3
  • 182
    • 0032454584 scopus 로고    scopus 로고
    • Classification, and evolution of EF-hand proteins
    • Kawasaki, H.; Nakayama, S.; Kretsinger, R. H. Classification, and evolution of EF-hand proteins. Biometals, 1998, 11(4), 277-295.
    • (1998) Biometals , vol.11 , Issue.4 , pp. 277-295
    • Kawasaki, H.1    Nakayama, S.2    Kretsinger, R.H.3
  • 183
    • 34447130835 scopus 로고    scopus 로고
    • Structures and metal-ionbinding properties of the Ca2+-binding helix-loop-helix EF-hand motifs
    • Giffbrd, J. L.; Walsh, M. P.; Vogel, H. J. Structures and metal-ionbinding properties of the Ca2+-binding helix-loop-helix EF-hand motifs. Biochem. J, 2007, 405(2), 199-221.
    • (2007) Biochem. J , vol.405 , Issue.2 , pp. 199-221
    • Giffbrd, J.L.1    Walsh, M.P.2    Vogel, H.J.3
  • 184
    • 0037155820 scopus 로고    scopus 로고
    • Disease-causing mutations in. cartilage oligomeric matrix protein cause an unstructured Ca2+ binding domain
    • Kleerekoper, Q.; Hecht, J. T.; Putkey, J. A. Disease-causing mutations in. cartilage oligomeric matrix protein cause an unstructured Ca2+ binding domain. J Biol Chem., 2002, 277(12), 10581-10589.
    • (2002) J Biol Chem. , vol.277 , Issue.12 , pp. 10581-10589
    • Kleerekoper, Q.1    Hecht, J.T.2    Putkey, J.A.3
  • 185
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loophelix calcium-binding proteins
    • Strynadka, N. C.; James, M. N. Crystal structures of the helix-loophelix calcium-binding proteins. Annu. Rev. Biochem., 1989, 55, 951-958.
    • (1989) Annu. Rev. Biochem. , vol.55 , pp. 951-958
    • Strynadka, N.C.1    James, M.N.2
  • 186
    • 34548158023 scopus 로고    scopus 로고
    • Thrombospondins, their polymorphisms, and cardiovascular disease
    • Stenina, O. I.; Topol, E. J.; Plow, E. F. Thrombospondins, their polymorphisms, and cardiovascular disease. Arterioscler. Thromb. Vase. Biol., 2001, 27(9), 1886-1894.
    • (2001) Arterioscler. Thromb. Vase. Biol. , vol.27 , Issue.9 , pp. 1886-1894
    • Stenina, O.I.1    Topol, E.J.2    Plow, E.F.3
  • 189
    • 1942535754 scopus 로고    scopus 로고
    • Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats
    • DOI 10.1038/sj.emboj.7600166
    • Kvansakul, M.; Adams, J. C.; Hohenester, E. Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats. EMBO J., 2004, 23(6), 1223-1233. (Pubitemid 38524995)
    • (2004) EMBO Journal , vol.23 , Issue.6 , pp. 1223-1233
    • Kvansakul, M.1    Adams, J.C.2    Hohenester, E.3
  • 190
    • 53349144370 scopus 로고    scopus 로고
    • The natively unfolded character of tau and its aggregation, to Alzheimer-Like paired helical filaments
    • Jeganathan, S.; von Bergen, M.; Mandelkow, E. M.; Mandelkow, E. The natively unfolded character of tau and its aggregation, to Alzheimer-Like paired helical filaments. Biochemistry, 2008, 47(40), 10526-10539.
    • (2008) Biochemistry , vol.47 , Issue.40 , pp. 10526-10539
    • Jeganathan, S.1    Von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 191
  • 192
    • 33750185145 scopus 로고    scopus 로고
    • Spectroscopic approaches to the conformation of tau protein in solution and in paired helical filaments
    • DOI 10.1159/000095257
    • von Bergen, M.; Barghorn, S.; Jeganathan, S.; Mandelkow, E. M.; Mandelkow, E. Spectroscopic approaches to the conformation of tau protein in solution, and in paired helical filaments. Neurodegener Dis., 2006, 3(4-5), 197-206. (Pubitemid 44600305)
    • (2006) Neurodegenerative Diseases , vol.3 , Issue.4-5 , pp. 197-206
    • Von Bergen, M.1    Barghorn, S.2    Jeganathan, S.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 193
    • 19744382953 scopus 로고    scopus 로고
    • The MAP2/Tau family of microtubuleassociated proteins
    • Dehmelt, L.; Halpain, S. The MAP2/Tau family of microtubuleassociated proteins. Genome Biol, 2005, 6(1), 204.
    • (2005) Genome Biol , vol.6 , Issue.1 , pp. 204
    • Dehmelt, L.1    Halpain, S.2
  • 194
    • 0028153172 scopus 로고
    • Localization of specific epitopes on human microtubule-associated protein 2
    • Kalcheva, N.; Albala, J. S.; Binder, L. I.; Shafit-Zagardo, B. Localization of specific epitopes on human, microtubule-associated protein 2. J. Neurochem., 1994, 63(6), 2336-2341. (Pubitemid 24370012)
    • (1994) Journal of Neurochemistry , vol.63 , Issue.6 , pp. 2336-2341
    • Kalcheva, N.1    Albala, J.S.2    Binder, L.I.3    Shafit-Zagardo, B.4
  • 195
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • Cleveland, D. W.; Hwo, S. Y.; Kirschner, M. W. Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. J. Mol Biol. 1977, 116(2), 227-247.
    • (1977) J. Mol Biol. , vol.116 , Issue.2 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 196
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from, microtubule-associated protein tau
    • Wille, H.; Drewes, G.; Biernat, J.; Mandelkow, E. M.; Mandelkow, E. Alzheimer-like paired helical filaments and antiparallel dimers formed from, microtubule-associated protein tau in vitro. J. Cell Biol, 1992, 115(3), 573-584.
    • (1992) In Vitro. J. Cell Biol , vol.115 , Issue.3 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 197
    • 0028170411 scopus 로고
    • Structural studies of Tau protein and Alzheimer paired helical filaments show no evidence for beta-structure
    • Schweers, O.; Schonbrunn-Hanebeck, E.; Marx, A.; Mandelkow, E. Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure, J. Biol Chem., 1994, 269(39), 24290-24297. (Pubitemid 2145765)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.39 , pp. 24290-24297
    • Schweers, O.1    Schonbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4
  • 199
    • 33646365908 scopus 로고    scopus 로고
    • Hyperphosphorylation of tau induces local polyproline II helix
    • Bielska, A. A.; Zondlo, N. J. Hyperphosphorylation of tau induces local polyproline II helix. Biochemistry, 2006, 45(17), 5527-5537.
    • (2006) Biochemistry , vol.45 , Issue.17 , pp. 5527-5537
    • Bielska, A.A.1    Zondlo, N.J.2
  • 200
    • 21644446496 scopus 로고    scopus 로고
    • Sites of tau important for aggregation populate β-structure and bind to microtubules and polyanions
    • DOI 10.1074/jbc.M501565200
    • Mukrasch, M. D.; Biernat, J.; von Bergen, M.; Griesinger, C.; Mandelkow, E.; Zweckstetter, M. Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions. J. Biol. Chem., 2005, 250(26), 24978-24986. (Pubitemid 40934590)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24978-24986
    • Mukrasch, M.D.1    Biernat, J.2    Von Bergen, M.3    Griesinger, C.4    Mandelkow, E.5    Zweckstetter, M.6
  • 201
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local β-Structure
    • von Bergen, M.; Barghorn, S.; Li, L.; Marx, A.; Biernat, J.; Mandelkow, E. M.; Mandelkow, E. Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure. J. Biol Chem., 2001, 276(51),48165-48174. (Pubitemid 37370720)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.51 , pp. 48165-48174
    • Von Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.-M.6    Mandelkow, E.7
  • 203
    • 1042288284 scopus 로고    scopus 로고
    • Tau Paired helical filaments from alzheimer's disease brain and assembled in vitro are based on β-Structure in the core domain
    • DOI 10.1021/bi0357006
    • Barghorn, S.; Davies, P.; Mandelkow, E. Tau paired helical, filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain. Biochemistry, 2004, 43(6), 1694-1703. (Pubitemid 38200576)
    • (2004) Biochemistry , vol.43 , Issue.6 , pp. 1694-1703
    • Barghorn, S.1    Davies, P.2    Mandelkow, E.3
  • 204
    • 12344328360 scopus 로고    scopus 로고
    • Residual, structure in the repeat domain of tau: Echoes of microtubule binding and. paired helical filament formation
    • Eliezer, D.; Barre, P.; Kobaslija, M.; Chan, D.; Li, X.; Heend, L. Residual, structure in the repeat domain of tau: echoes of microtubule binding and. paired helical filament formation. Biochemistry, 2005,44(3), 1026-1036.
    • (2005) Biochemistry , vol.44 , Issue.3 , pp. 1026-1036
    • Eliezer, D.1    Barre, P.2    Kobaslija, M.3    Chan, D.4    Li, X.5    Heend, L.6
  • 206
    • 22944466125 scopus 로고    scopus 로고
    • High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments
    • DOI 10.1021/ja0516211
    • Sillen, A.; Wieruszeski, J. M.; Leroy, A.; Younes, A. B.; Landrieu, I.; Lippens, G. High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments. J. Am. Chem. Soc., 2005, 127(29), 10138-10139. (Pubitemid 41045458)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.29 , pp. 10138-10139
    • Sillen, A.1    Wieruszeski, J.-M.2    Leroy, A.3    Younes, A.B.4    Landrieu, I.5    Lippens, G.6
  • 207
    • 0042307302 scopus 로고    scopus 로고
    • Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure
    • Berriman, J.; Serpell, L. C.; Oberg, K. A.; Fink, A. L.; Goedert, M.; Crowther, R. A. Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure. Proc. Natl. Acad. Sci. USA, 2003, 100(15), 9034-9038.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.15 , pp. 9034-9038
    • Berriman, J.1    Serpell, L.C.2    Oberg, K.A.3    Fink, A.L.4    Goedert, M.5    Crowther, R.A.6
  • 208
    • 42949135930 scopus 로고    scopus 로고
    • Characterization of Alzheimer's-like paired helical filaments from the core domain of tau protein using solid-state NMR spectroscopy
    • DOI 10.1021/ja7100517
    • Andronesi, O. C.; von Bergen, M.; Biernat, J.; Seidel, K.; Griesinger, C.; Mandelkow, E.; Baldus, M. Characterization of Alzheimer's-like paired helical filaments from the core domain of tau protein using solid-state NMR spectroscopy. J. Am. Chem. Soc., 2008, 130(18), 5922-5928. (Pubitemid 351620838)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.18 , pp. 5922-5928
    • Andronesi, O.C.1    Von Bergen, M.2    Biernat, J.3    Seidel, K.4    Griesinger, C.5    Mandelkow, E.6    Baldus, M.7
  • 209
    • 0037137228 scopus 로고    scopus 로고
    • The conformations of filamentous and soluble tau associated with Alzheimer paired helical filaments
    • DOI 10.1021/bi016079h
    • Goux, W. J. The conformations of filamentous and soluble tau associated with. Alzheimer paired helical filaments. Biochemistry, 2002, 41(46), 13798-13806. (Pubitemid 35332718)
    • (2002) Biochemistry , vol.41 , Issue.46 , pp. 13798-13806
    • Goux, W.J.1
  • 210
    • 33646857025 scopus 로고    scopus 로고
    • The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis
    • DOI 10.1021/bi052530j
    • von Bergen, M.; Barghorn, S.; Muller, S. A.; Pickhardt, M.; Biernat, J.; Mandelkow, E. M.; Davies, P.; Aebi, U.; Mandelkow, E. The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis. Biochemistry, 2006,45(20), 6446-6457. (Pubitemid 43787810)
    • (2006) Biochemistry , vol.45 , Issue.20 , pp. 6446-6457
    • Von Bergen, M.1    Barghorn, S.2    Muller, S.A.3    Pickhardt, M.4    Biernat, J.5    Mandelkow, E.-M.6    Davies, P.7    Aebi, U.8    Mandelkow, E.9
  • 212
    • 33846002029 scopus 로고    scopus 로고
    • Side chain-dependent stacking modulates tau filament structure
    • DOI 10.1074/jbc.M605336200
    • Margittai, M.; Langen, R. Side chain-dependent stacking modulates tau filament structure. J. Biol. Chem., 2006, 281(49), 37820-37827. (Pubitemid 46042084)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.49 , pp. 37820-37827
    • Margittai, M.1    Langen, R.2
  • 213
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn, S.; Zheng-Fischhofer, Q.; Ackmann, M.; Biernat, J.; von Bergen, M.; Mandelkow, E. M.; Mandelkow, E. Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias. Biochemistry, 2000, 39(38), 11714-11721,
    • (2000) Biochemistry , vol.39 , Issue.38 , pp. 11714-11721
    • Barghorn, S.1    Zheng-Fischhofer, Q.2    Ackmann, M.3    Biernat, J.4    Von Bergen, M.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 215
    • 0037465453 scopus 로고    scopus 로고
    • Structure and Behavior of Regenerated Spider Silk
    • Shao, Z.; Vollrath, F.; Yang, Y.; Thogersen, H. C. Structure and Behavior of Regenerated Spider Silk. Macromolecules, 2003, 36(4), 1157-1161.
    • (2003) Macromolecules , vol.36 , Issue.4 , pp. 1157-1161
    • Shao, Z.1    Vollrath, F.2    Yang, Y.3    Thogersen, H.C.4
  • 216
    • 9744257710 scopus 로고    scopus 로고
    • Secondary structures and conformational changes in flagelliform, cylindrical, major, and minor ampullate silk proteins. Temperature and concentration effects
    • DOI 10.1021/bm034486y
    • Dicko, C.; Knight, D.; Kenney, J. M.; Vollrath, F. Secondary structures and conformational changes in flagelliform, cylindrical, major, and minor ampullate silk proteins. Temperature and concentration effects. Biomacromolecules, 2004, 5(6), 2105-2115. (Pubitemid 39585261)
    • (2004) Biomacromolecules , vol.5 , Issue.6 , pp. 2105-2115
    • Dicko, C.1    Knight, D.2    Kenney, J.M.3    Vollrath, F.4
  • 218
    • 0025182945 scopus 로고
    • Conformational preferences of synthetic peptides derived from the immunodominant site of the circumsporozoite protein of Plasmodium falciparum by 1H NMR
    • Dyson, H. J.; Satterthwait, A. C.; Lerner, R. A.; Wright, P. E. Conformational preferences of synthetic peptides derived from the immunodominant site of the circumsporozoite protein of Plasmodium falciparum by 1H NMR. Biochemistry, 1990, 29(34), 7828-7837.
    • (1990) Biochemistry , vol.29 , Issue.34 , pp. 7828-7837
    • Dyson, H.J.1    Satterthwait, A.C.2    Lerner, R.A.3    Wright, P.E.4
  • 219
    • 0028116406 scopus 로고
    • Allelic variation in the circumsporozoite protein of Plasmodium falciparum, from Thai field isolates
    • Jongwutiwes, S.; Tanabe, K.; Hughes, M. K.; Kanbara, H.; Hughes, A. L. Allelic variation in the circumsporozoite protein of Plasmodium falciparum, from Thai field isolates. Am. J. Trop. Med. Hyg., 1994, 51(5), 6596-6668
    • (1994) Am. J. Trop. Med. Hyg. , vol.51 , Issue.5 , pp. 6596-6668
    • Jongwutiwes, S.1    Tanabe, K.2    Hughes, M.K.3    Kanbara, H.4    Hughes, A.L.5
  • 220
    • 0026286121 scopus 로고
    • Conservation and divergence of repeatedstructures in Plasmodium genomes: The molecular drift
    • Frontali, C.; Pizzi, E. Conservation and divergence of repeatedstructures in Plasmodium genomes: the molecular drift. Acta Letden, 1991, 60(1), 69-81.
    • (1991) Acta Letden , vol.60 , Issue.1 , pp. 69-81
    • Frontali, C.1    Pizzi, E.2
  • 221
    • 0034736527 scopus 로고    scopus 로고
    • Genetic variation and the recent worldwide expansion of Plasmodium falciparum
    • Ayala, F. J.; Rich, S. M. Genetic variation and the recent worldwide expansion of Plasmodium falciparum, Gene, 2000, 261(1), 161-170.
    • (2000) Gene , vol.261 , Issue.1 , pp. 161-170
    • Ayala, F.J.1    Rich, S.M.2
  • 222
    • 4644308502 scopus 로고    scopus 로고
    • The evolution of amino acid repeat arrays in Plasmodium and other organisms
    • Hughes, A. L. The evolution of amino acid repeat arrays in Plasmodium and other organisms. J. Mol. Evol., 2004, 59(4), 528-535.
    • (2004) J. Mol. Evol. , vol.59 , Issue.4 , pp. 528-535
    • Hughes, A.L.1
  • 224
    • 0033863775 scopus 로고    scopus 로고
    • NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: A loop conformation with histidine and tryptophan in close proximity
    • Yoshida, H.; Matsushima, N.; Kumaki, Y.; Nakata, M.; Hikichi, K. NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: a loop conformation with histidine and tryptophan in close proximity. J. Biochem., 2000, 128(2), 271-281. (Pubitemid 30671064)
    • (2000) Journal of Biochemistry , vol.128 , Issue.2 , pp. 271-281
    • Yoshida, H.1    Matsushima, N.2    Kumaki, Y.3    Nakata, M.4    Hikichi, K.5
  • 225
    • 0242662244 scopus 로고    scopus 로고
    • The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site
    • DOI 10.1016/j.jmb.2003.09.048
    • Zahn, R. The octapeptide repeats in mammalian prion protein, constitute a pH-dependent folding and aggregation site. J. Mol. Biol., 2003, 334(3), 477-488. (Pubitemid 37386348)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.3 , pp. 477-488
    • Zahn, R.1
  • 227
    • 0032492651 scopus 로고    scopus 로고
    • Site-specific phosphorylation of Lys-Ser-Pro repeat peptides from neurofilament H by cyclin-dependent kinase 5: Structural basis for substrate recognition
    • Sharma, P.; Barchi, J. J., Jr.; Huang, X.; Amin, N. D.; Jaffe, H.; Pant, H. C. Site-specific phosphorylation of Lys-Ser-Pro repeat peptides from neurofilament H by cyclin-dependent kinase 5: structural basis for substrate recognition. Biochemistry, 1998, 37(14), 4759-4766.
    • (1998) Biochemistry , vol.37 , Issue.14 , pp. 4759-4766
    • Sharma, P.1    Barchi Jr, J.J.2    Huang, X.3    Amin, N.D.4    Jaffe, H.5    Pant, H.C.6
  • 228
    • 0026787142 scopus 로고
    • Evidence for unequal crossing over in the evolution of the neurofilament polypeptide H
    • Soppet, D. R.; Beasley, L. L.; Willard, M. B. Evidence for unequal crossing over in the evolution of the neurofilament polypeptide H. J. Biol. Chem., 1992, 267(24), 17354-17361.
    • (1992) J. Biol. Chem. , vol.267 , Issue.24 , pp. 17354-17361
    • Soppet, D.R.1    Beasley, L.L.2    Willard, M.B.3
  • 229
    • 33644620356 scopus 로고    scopus 로고
    • Respiratory tract mucin genes and mucin glycoproteins in health, and disease
    • Rose, M. C.; Voynow, J. A. Respiratory tract mucin genes and mucin glycoproteins in health, and disease. Physiol. Rev., 2006, 56(1), 245-278.
    • (2006) Physiol. Rev. , vol.56 , Issue.1 , pp. 245-278
    • Rose, M.C.1    Voynow, J.A.2
  • 231
    • 42049099903 scopus 로고    scopus 로고
    • Structure, evolution, and biology of the MUC4 mucin
    • Chaturvedi, P.; Singh, A. P.; Batra, S. K. Structure, evolution, and biology of the MUC4 mucin, FASEBJ, 2008, 22(4), 966-981.
    • (2008) FASEBJ , vol.22 , Issue.4 , pp. 966-981
    • Chaturvedi, P.1    Singh, A.P.2    Batra, S.K.3
  • 233
    • 0027168975 scopus 로고
    • Macaque salivary proline-rich protein: Structure, evolution, and expression
    • Ann, D. K.; Lin, H. H. Macaque salivary proline-rich protein: structure, evolution, and expression. Crit. Rev. Oral Biol. Med., 1993, 4(3-4), 545-551.
    • (1993) Crit. Rev. Oral Biol. Med. , vol.4 , Issue.3-4 , pp. 545-551
    • Ann, D.K.1    Lin, H.H.2
  • 234
    • 2642515362 scopus 로고    scopus 로고
    • Salivary proteins: Protective and diagnostic value in cariology?
    • Van Nieuw Amerongen, A.; Bolscher, J. G.; Veerman, E. C. Salivary proteins: protective and diagnostic value in cariology? Caries Res., 2004, 35(3), 247-253.
    • (2004) Caries Res. , vol.35 , Issue.3 , pp. 247-253
    • Van Nieuw Amerongen, A.1    Bolscher, J.G.2    Veerman, E.C.3
  • 236
    • 0024389081 scopus 로고
    • Isolation and characterization of six proteins from rabbit parotid saliva belonging to a unique family of proline-rich proteins
    • Spielman, A. I.; Bennick, A. Isolation and characterization of six proteins from rabbit parotid saliva belonging to a unique family of proline-rich proteins. Arch. Oral Biol, 1989, 34(2), 117-130.
    • (1989) Arch. Oral Biol , vol.34 , Issue.2 , pp. 117-130
    • Spielman, A.I.1    Bennick, A.2
  • 237
    • 0019332620 scopus 로고
    • The primary structure of a salivary calcium-binding proline-rich phosphoprotein(protein C), a possible precursor of a related salivary protein A
    • Wong, R. S.; Bennick, A. The primary structure of a salivary calcium-binding proline-rich phosphoprotein(protein C), a possible precursor of a related salivary protein A. J. Biol. Chem., 1980, 255(12), 5943-5948.
    • (1980) J. Biol. Chem. , vol.255 , Issue.12 , pp. 5943-5948
    • Wong, R.S.1    Bennick, A.2
  • 239
    • 0021349171 scopus 로고
    • Conformational study of the basic proline-rich polypeptides from human parotid saliva
    • Shibata, S.; Asakura, J.; Isemura, T.; Isemura, S.; Saitoh, E.; Sanada, K. Conformational study of the basic proline-rich polypeptides from, human, parotid saliva. Int. J. Pept. Protein Res., 1984, 23(2), 158-165. (Pubitemid 14187105)
    • (1984) International Journal of Peptide and Protein Research , vol.23 , Issue.2 , pp. 158-165
    • Shibata, S.1    Asakura, J.2    Isemura, T.3
  • 240
    • 0037325713 scopus 로고    scopus 로고
    • Synthesis and circular dichroism. study of the human, salivary proline-rich protein IB7
    • Simon, C.; Pianet, I.; Dufourc, E. J. Synthesis and circular dichroism. study of the human, salivary proline-rich protein IB7. J. Pept. Sci., 2003, 9(2), 125-131.
    • (2003) J. Pept. Sci. , vol.9 , Issue.2 , pp. 125-131
    • Simon, C.1    Pianet, I.2    Dufourc, E.J.3
  • 242
    • 0027178365 scopus 로고
    • Solution and solid-state circular dichroism analyses of a human salivary proline-rich glycoprotein repeating domain and its subfragments
    • DOI 10.1016/0141-8130(93)90018-H
    • Gonzalez, M.; Loomis, P. M.; Loomis, R. E. Solution and solidstate circular dichroism analyses of a human, salivary proline-rich. glycoprotein repeating domain and its subfragments. Int. J. Biol. Macromol, 1993, 15(3), 153-167. (Pubitemid 23202628)
    • (1993) International Journal of Biological Macromolecules , vol.15 , Issue.3 , pp. 153-167
    • Gonzalez, M.1    Loomis, P.M.2    Koomis, R.E.3
  • 243
    • 0025366593 scopus 로고
    • A physical map of the human salivary proline-rich protein gene cluster covers over 700 kbp of DNA
    • DOI 10.1016/0888-7543(90)90565-C
    • Kim, H. S.; Smithies, O.; Maeda, N. A physical map of the human salivary proline-rich protein gene cluster covers over 700 kbp of DNA. Genomics, 1990, 6(2), 260-267. (Pubitemid 20164194)
    • (1990) Genomics , vol.6 , Issue.2 , pp. 260-267
    • Kim, H.-S.1    Smithies, O.2    Maeda, N.3
  • 244
    • 0022339828 scopus 로고
    • Localization of the human salivary protein complex (SPC) to chromosome band 12p13.2
    • Mamula, P. W.; Heerema, N. A.; Palmer, C. G.; Lyons, K. M.; Karn, R. C. Localization of the human salivary protein complex(SPC) to chromosome band 12pl.3.2. Cytogenet. Cell Genet., 1985, 39(4), 279-284. (Pubitemid 16208787)
    • (1985) Cytogenetics and Cell Genetics , vol.39 , Issue.4 , pp. 279-284
    • Mamula, P.W.1    Heerema, N.A.2    Palmer, C.G.3
  • 245
    • 0023708209 scopus 로고
    • Many protein products from a few Loci: Assignment of human salivary proline-rich proteins to specific loci
    • Lyons, K. M.; Azen, E. A.; Goodman, P. A.; Smithies, O. Many protein products from a few Loci: assignment of human salivary proline-rich proteins to specific loci. Genetics, 1988, 120(1), 255-265.
    • (1988) Genetics , vol.120 , Issue.1 , pp. 255-265
    • Lyons, K.M.1    Azen, E.A.2    Goodman, P.A.3    Smithies, O.4
  • 246
    • 0022186995 scopus 로고
    • Differential RNA splicing and post-translational cleavages in the human salivary proline-rich protein gene system
    • Maeda, N.; Kim, H. S.; Azen, E. A.; Smithies, O. Differential RNA splicing and post-translational. cleavages in the human salivary proline-rich protein gene system. J. Biol Chem., 1985, 260(20), 11123-11130. (Pubitemid 16253274)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.20 , pp. 11123-11130
    • Maeda, N.1    Kim, H.S.2    Azen, E.A.3    Smithies, O.4
  • 247
    • 0023723097 scopus 로고
    • Length polymorphisms in human proline-rich protein genes generated by intragenic unequal crossing over
    • Lyons, K. M.; Stein, J. H.; Smithies, O. Length polymorphisms in human proline-rich protein genes generated by intragenic unequal crossing over. Genetics, 1988, 120(1), 267-278. (Pubitemid 18222294)
    • (1988) Genetics , vol.120 , Issue.1 , pp. 267-278
    • Lyons, K.M.1    Stein, J.H.2    Smithies, O.3
  • 248
    • 0025847316 scopus 로고
    • Molecular characterization of rat multigene family encoding proline-rich proteins
    • Lin, H. H.; Ann, D. K. Molecular characterization of rat multigene family encoding proline-rich proteins. Genomics, 1991, 10(1), 102-113.
    • (1991) Genomics , vol.10 , Issue.1 , pp. 102-113
    • Lin, H.H.1    Ann, D.K.2
  • 249
    • 0027357053 scopus 로고
    • The structure and evolution of the human salivary proline-rich protein gene family
    • Kim, H. S.; Lyons, K. M.; Saitoh, E.; Azen, E. A.; Smithies, O.; Maeda, N. The structure and evolution of the human salivary proline-rich protein gene family. Mamm. Genome, 1993,4(1), 3-14.
    • (1993) Mamm. Genome , vol.4 , Issue.1 , pp. 3-14
    • Kim, H.S.1    Lyons, K.M.2    Saitoh, E.3    Azen, E.A.4    Smithies, O.5    Maeda, N.6
  • 251
    • 0034788422 scopus 로고    scopus 로고
    • Arabinogalactan-proteins: Structure, expression and function
    • Showalter, A. M. Arabinogalactan-proteins: structure, expression and function. Cell. Mol. Life Sci., 2001, 55(10), 1399-1417. (Pubitemid 32964411)
    • (2001) Cellular and Molecular Life Sciences , vol.58 , Issue.10 , pp. 1399-1417
    • Showalter, A.M.1
  • 252
    • 35848945494 scopus 로고    scopus 로고
    • Reconsidering the mechanism of polyglutamine peptide aggregation
    • Lee, C. C.; Walters, R. H.; Murphy, R. M. Reconsidering the mechanism of polyglutamine peptide aggregation. Biochemistry, 2007, 46(44), 12810-12820.
    • (2007) Biochemistry , vol.46 , Issue.44 , pp. 12810-12820
    • Lee, C.C.1    Walters, R.H.2    Murphy, R.M.3
  • 253
    • 0344305773 scopus 로고    scopus 로고
    • The structure of tri-proline in water probed by polarized Raman, Fourier transform infrared, vibrational circular dichroism, and electric ultraviolet circular dichroism spectroscopy
    • Schweitzer-Stenner, R.; Eker, R.; Perez, A.; Griebenow, K.; Cao, X.; Ñafie, L. A. The structure of tri-proline in water probed by polarized Raman, Fourier transform infrared, vibrational circular dichroism, and electric ultraviolet circular dichroism spectroscopy. Biopolymers, 2003, 71(5), 558-568.
    • (2003) Biopolymers , vol.71 , Issue.5 , pp. 558-568
    • Schweitzer-Stenner, R.1    Eker, R.2    Perez, A.3    Griebenow, K.4    Cao, X.5    Ñafie, L.A.6
  • 254
    • 0000724838 scopus 로고
    • Reinforced Polyproline II Conformation in a Hydroxyproline-Rich Cell. Wall Glycoprotein from Carrot Root
    • van Hoist, G. J.; Varner, J. E. Reinforced Polyproline II Conformation in a Hydroxyproline-Rich Cell. Wall Glycoprotein from Carrot Root. Plant Physiol, 1984, 74(2), 247-251,
    • (1984) Plant Physiol , vol.74 , Issue.2 , pp. 247-251
    • Van Hoist, G.J.1    Varner, J.E.2
  • 255
    • 17144375526 scopus 로고    scopus 로고
    • Elicitation of primary and secondary metabolism during defense in the potato
    • Nakane, E.; Kawakita, K.; Doke, N.; Yoshioka, H. Elicitation of primary and secondary metabolism during defense in the potato. J. General Plant Pathol, 2003, 69(6), 378-384.
    • (2003) J. General Plant Pathol , vol.69 , Issue.6 , pp. 378-384
    • Nakane, E.1    Kawakita, K.2    Doke, N.3    Yoshioka, H.4
  • 256
    • 0031005424 scopus 로고    scopus 로고
    • Extensin from suspension-cultured potato cells: A hydroxyproline-rich glycoprotein, devoid of agglutinin activity
    • DOI 10.1007/s004250050117
    • Dey, P. M.; Brownleader, M. D.; Pantelides, A. T.; Trevan, M.; Smith, J. J.; Saddler, G. Extensin from, suspension-cultured potato cells: a hydroxyproline-rich glycoprotein, devoid of agglutinin activity. Planta, 1997, 202(2), 179-187. (Pubitemid 27243119)
    • (1997) Planta , vol.202 , Issue.2 , pp. 179-187
    • Dey, P.M.1    Brownleader, M.D.2    Pantelides, A.T.3    Trevan, M.4    Smith, J.J.5    Saddler, G.6
  • 257
    • 0035814919 scopus 로고    scopus 로고
    • Glycosylated polyproline II rods with kinks as a structural motif in plant hydroxyproline-rich glycoproteins
    • Ferris, P. J.; Woessner, J. P.; Wafifenschmidt, S.; Kilz, S.; Drees, J.; Goodenough, U. W. Glycosylated polyproline II rods with kinks as a structural motif in plant hydroxyproline-rich glycoproteins. Biochemistry, 2001, 40(9), 2978-2987.
    • (2001) Biochemistry , vol.40 , Issue.9 , pp. 2978-2987
    • Ferris, P.J.1    Woessner, J.P.2    Wafifenschmidt, S.3    Kilz, S.4    Drees, J.5    Goodenough, U.W.6
  • 258
    • 0024656034 scopus 로고
    • Trypsin cleaves lysylproline in. a hydroxyproline-rich glycoprotein from. Zea mays
    • Kieliszewski, M. J.; Leykam, J. F.; Lamport, D. T. Trypsin cleaves lysylproline in. a hydroxyproline-rich glycoprotein from. Zea mays. Pept. Res., 1989, 2(3), 246-248.
    • (1989) Pept. Res. , vol.2 , Issue.3 , pp. 246-248
    • Kieliszewski, M.J.1    Leykam, J.F.2    Lamport, D.T.3
  • 259
    • 34547925245 scopus 로고    scopus 로고
    • Between-species analysis of short-repeat modules in cell wall and sex-related hydroxyproline-rich glycoproteins of Chlamydomonas
    • DOI 10.1104/pp.107.100891
    • Lee, J. H.; Waffenschmidt, S.; Small, L.; Goodenough, U. Between-species analysis of short-repeat modules in cell wall and sexrelated hydroxyproline-rich glycoproteins of Chlamydomonas. Plant Physiol, 2007, 144(4), 1813-1826. (Pubitemid 47258105)
    • (2007) Plant Physiology , vol.144 , Issue.4 , pp. 1813-1826
    • Lee, J.-H.1    Waffenschmidt, S.2    Small, L.3    Goodenough, U.4
  • 260
    • 38649097544 scopus 로고    scopus 로고
    • Analysis of the hybrid proline-rich protein families from seven plant species suggests rapid diversification of their sequences and expression patterns
    • DOI 10.1186/1471-2164-8-412
    • Dvorakova, L.; Cvrčkova, F.; Fischer, L. Analysis of the hybrid proline-rich protein families from, seven plant species suggests rapid diversification of their sequences and expression patterns. BMC Genomics, 2007, 8, 412. (Pubitemid 351168209)
    • (2007) BMC Genomics , vol.8 , pp. 412
    • Dvorakova, L.1    Cvrckova, F.2    Fischer, L.3
  • 261
    • 0023072191 scopus 로고
    • The sp-I genes in the Balbiani rings of Chironomus salivary glands
    • Grond, C.; Saiga, H.; Edstrom, J. E. The sp-I genes in the Balbiani rings of Chironomus salivary glands. Results Probl Cell Differ., 1987, 14, 69-80.
    • (1987) Results Probl Cell Differ. , vol.14 , pp. 69-80
    • Grond, C.1    Saiga, H.2    Edstrom, J.E.3
  • 262
    • 0026675708 scopus 로고
    • Conserved and variable repeat structures in the Balbiani ring gene family in Chironomus tentans
    • Paulsson, G.; Bernholm, K.; Wieslander, L. Conserved and variable repeat structures in the Balbiani ring gene family in Chironomus tentans. J. Mol. Evol, 1992, 35(3), 205-216.
    • (1992) J. Mol. Evol , vol.35 , Issue.3 , pp. 205-216
    • Paulsson, G.1    Bernholm, K.2    Wieslander, L.3
  • 263
    • 0026703412 scopus 로고
    • Balbiani ring 1 gene in Chironomus tentans. Sequence organization and dynamics of a coding minisatellite
    • Paulsson, G.; Hoog, C.; Bernholm, K.; Wieslander, L. Balbiani ring 1 gene in Chironomus tentans. Sequence organization and dynamics of a coding minisatellite. J. Mol. Biol, 1992, 225(2), 349-361.
    • (1992) J. Mol. Biol , vol.225 , Issue.2 , pp. 349-361
    • Paulsson, G.1    Hoog, C.2    Bernholm, K.3    Wieslander, L.4
  • 264
    • 0026607695 scopus 로고
    • Sequence organization of the Balbiani ring 2.1 gene in Chironomus tentans
    • Wieslander, L.; Paulsson, G. Sequence organization of the Balbiani ring 2.1 gene in Chironomus tentans. Proc. Natl. Acad. Sci. USA, 1992, 59(10), 4578-4582.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.59 , Issue.10 , pp. 4578-4582
    • Wieslander, L.1    Paulsson, G.2
  • 265
    • 0026704217 scopus 로고
    • Secondary structure of synthetic peptides derived from the repeating unit of a giant secretory protein from Chironomus tentans
    • Wellman, S. E.; Hamodrakas, S. J.; Kamitsos, E. I.; Case, S. T. Secondary structure of synthetic peptides derived from the repeating unit of a giant secretory protein from Chironomus tentans. Biochim. Biophys. Acta, 1992, 1121(3), 279-285.
    • (1992) Biochim. Biophys. Acta , vol.1121 , Issue.3 , pp. 279-285
    • Wellman, S.E.1    Hamodrakas, S.J.2    Kamitsos, E.I.3    Case, S.T.4
  • 266
    • 0021691185 scopus 로고
    • Balbiani ring DNA: Sequence comparisons and evolutionary history of a family of hierarchically repetitive protein-coding genes
    • DOI 10.1007/BF02104734
    • Pustell, J.; Kafatos, F. C.; Wobus, U.; Baumlein, H. Balbiani ring DNA: sequence comparisons and. evolutionary history of a family of hierarchically repetitive protein-coding genes. J. Mol. Evol., 1984, 20(3-4), 281-295. (Pubitemid 15206420)
    • (1984) Journal of Molecular Evolution , vol.20 , Issue.3-4 , pp. 281-295
    • Pustell, J.1    Kafatos, F.C.2    Wobus, U.3    Baumlein, H.4
  • 267
    • 70349936963 scopus 로고
    • Rapid and Concerted Evolution of Repeat Units in a Balbiani Ring Gene
    • Lendahl, U.; Saiga, H.; Hoog, C.; Edstrom, J. E.; Wieslander, L. Rapid and Concerted Evolution of Repeat Units in a Balbiani Ring Gene. Genetics, 1987, 117(1), 43-49.
    • (1987) Genetics , vol.117 , Issue.1 , pp. 43-49
    • Lendahl, U.1    Saiga, H.2    Hoog, C.3    Edstrom, J.E.4    Wieslander, L.5
  • 268
    • 0036715005 scopus 로고    scopus 로고
    • Epithelial barrier function: Assembly and structural features of the cornified cell envelope
    • Kalinin, A. E.; Kajava, A. V.; Steinert, P. M. Epithelial barrier function: assembly and structural features of the cornified cell envelope. Bioessays, 2002, 24(9), 789-800.
    • (2002) Bioessays , vol.24 , Issue.9 , pp. 789-800
    • Kalinin, A.E.1    Kajava, A.V.2    Steinert, P.M.3
  • 271
    • 0025319321 scopus 로고
    • The involucrin gene of the galago. Existence of a correction process acting on its segment of repeats
    • Phillips, M.; Djian, P.; Green, H. The involucrin gene of the galago. Existence of a correction process acting on its segment of repeats. J. Biol. Chem., 1990, 265(14), 7804-7807. (Pubitemid 20158943)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.14 , pp. 7804-7807
    • Phillips, M.1    Djian, P.2    Green, H.3
  • 272
    • 0025767985 scopus 로고
    • The involucrin genes of the white-fronted capuchin and cottontop tamarin: The platyrrhine middle region
    • Phillips, M.; Rice, R. H.; Djian, P.; Green, H. The involucrin genes of the white-fronted capuchin and cottontop tamarin: the platyrrhine middle region. Mol Biol Evol, 1991, 8(5), 579-591. (Pubitemid 21895914)
    • (1991) Molecular Biology and Evolution , vol.8 , Issue.5 , pp. 579-591
    • Phillips, M.1    Rice, R.H.2    Djian, P.3    Green, H.4
  • 273
    • 0031050966 scopus 로고    scopus 로고
    • The involucrin gene of the tree shrew: Recent repeat additions and the relocation of cysteine codons
    • DOI 10.1016/S0378-1119(96)00654-3, PII S0378111996006543
    • Phillips, M.; Rice, R. H.; Djian, P.; Green, H. The involucrin gene of the tree shrew: recent repeat additions and the relocation of cysteine codons. Gene, 1997, 187(1), 29-34. (Pubitemid 27110431)
    • (1997) Gene , vol.187 , Issue.1 , pp. 29-34
    • Phillips, M.1    Rice, R.H.2    Djian, P.3    Green, H.4
  • 274
    • 0023792758 scopus 로고
    • Remodeling of the involucrin gene during primate evolution
    • DOI 10.1016/0092-8674(88)90070-0
    • Tseng, H.; Green, H. Remodeling of the involucrin gene during primate evolution, Cell, 1988, 54(4), 491-496. (Pubitemid 18203404)
    • (1988) Cell , vol.54 , Issue.4 , pp. 491-496
    • Tseng, H.1    Green, H.2
  • 275
    • 0025290421 scopus 로고
    • The involucrin genes of pig and dog: Comparison of their segments of repeats with those of prosimians and higher primates
    • Tseng, H.; Green, H. The involucrin genes of pig and dog: comparison of their segments of repeats with, those of prosimians and higher primates. Mol. Biol. Evol, 1990, 7(4), 293-302. (Pubitemid 20205074)
    • (1990) Molecular Biology and Evolution , vol.7 , Issue.4 , pp. 293-302
    • Tseng, H.1    Green, H.2
  • 276
    • 0026636580 scopus 로고
    • Biophysical characterization of involucrin reveals a molecule ideally suited to function as an intermolecular cross-bridge of the keratinocyte cornified envelope
    • Yaffe, M. B.; Beegen, H.; Eckert, R. L. Biophysical characterization of involucrin reveals a molecule ideally suited to function as an intermolecular cross-bridge of the keratinocyte cornified envelope. J. Biol. Chem., 1992, 267(17), 12233-12238.
    • (1992) J. Biol. Chem. , vol.267 , Issue.17 , pp. 12233-12238
    • Yaffe, M.B.1    Beegen, H.2    Eckert, R.L.3
  • 277
    • 0018721266 scopus 로고
    • Presence in human epidermal cells of a soluble protein precursor of the cross-linked envelope: Activation of the cross-linking by calcium ions
    • Rice, R. H; Green, H. Presence in human epidermal cells of a soluble protein precursor of the cross-linked envelope: activation of the cross-linking by calcium ions. Cell, 1979, 18(3), 681-694. (Pubitemid 10216994)
    • (1979) Cell , vol.18 , Issue.3 , pp. 681-694
    • Rice, R.H.1    Green, H.2
  • 279
    • 0026475591 scopus 로고
    • Consecutive actions of different gene-altering mechanisms in the evolution of involucrin
    • Green, H.; Djian, P. Consecutive actions of different gene-altering mechanisms in the evolution of involucrin. Mol. Biol. Evol, 1992, 9(6), 977-1017.
    • (1992) Mol. Biol. Evol , vol.9 , Issue.6 , pp. 977-1017
    • Green, H.1    Djian, P.2
  • 281
    • 0034636705 scopus 로고    scopus 로고
    • Expansion of mouse involucrin by intra-allelic repeat addition
    • DOI 10.1016/S0378-1119(00)00237-7, PII S0378111900002377
    • Delhomme, B.; Djian, P. Expansion of mouse involucrin by intraallelic repeat addition. Gene, 2000, 252(1-2), 195-207. (Pubitemid 30618826)
    • (2000) Gene , vol.252 , Issue.1-2 , pp. 195-207
    • Delhomme, B.1    Djian, P.2
  • 282
    • 18844399896 scopus 로고    scopus 로고
    • Systematic repeat addition at a precise location in the coding region of the involucrin gene of wild mice reveals their phylogeny
    • DOI 10.1534/genetics.104.036400
    • Djian, P.; Delhomme, B. Systematic repeat addition at a precise location in. the coding region of the involucrin gene of wild mice reveals their phytogeny. Genetics, 2005, 169(4), 2199-2208. (Pubitemid 40695630)
    • (2005) Genetics , vol.169 , Issue.4 , pp. 2199-2208
    • Djian, P.1    Delhomme, B.2
  • 283
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • DOI 10.1038/nrm2114, PII NRM2114
    • Stewart, M. Molecular mechanism of the nuclear protein import cycle. Nat. Rev. Mol. Cell Biol, 2007, 8(3), 195-208. (Pubitemid 46310545)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.3 , pp. 195-208
    • Stewart, M.1
  • 284
    • 0034616910 scopus 로고    scopus 로고
    • Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking
    • Bayliss, R.; Littlewood, T.; Stewart, M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Cell, 2000, 102(1), 99-108.
    • (2000) Cell , vol.102 , Issue.1 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 285
    • 0033763895 scopus 로고    scopus 로고
    • Crystallization and initial X-ray diffraction characterization of complexes of FxFG nucleoporin repeats with nuclear transport factors
    • Bayliss, R.; Kent, H. M.; Corbett, A. H.; Stewart, M. Crystallization and initial X-ray diffraction characterization of complexes of FxFG nucleoporin repeats with nuclear transport factors. J. Struct. Biol, 2000, 131(3), 240-247.
    • (2000) J. Struct. Biol , vol.131 , Issue.3 , pp. 240-247
    • Bayliss, R.1    Kent, H.M.2    Corbett, A.H.3    Stewart, M.4
  • 287
    • 0037031842 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
    • DOI 10.1074/jbc.M203499200
    • Denning, D. P.; Uversky, V.; Patel, S. S.; Fink, A. L.; Rexach, M. The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J. Biol Chem., 2002, 277(36), 33447-33455. (Pubitemid 34984868)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 33447-33455
    • Denning, D.P.1    Uversky, V.2    Patel, S.S.3    Fink, A.L.4    Rexach, M.5
  • 288
    • 33847674551 scopus 로고    scopus 로고
    • Rapid evolution exposes the boundaries of domain structure and function in natively unfolded FG nucleoporins
    • DOI 10.1074/mcp.M600309-MCP200
    • Denning, D. P.; Rexach, M. R Rapid evolution exposes the boundaries of domain structure and function in. natively unfolded FG nucleoporins. Mol. Cell. Proteomics, 2007, 6(2), 272-282. (Pubitemid 46359515)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.2 , pp. 272-282
    • Denning, D.P.1    Rexach, M.F.2
  • 289
    • 0029910536 scopus 로고    scopus 로고
    • Can a polyproline II helical motif be used in the context of sequence- Selectivemajor groove recognition of B-DNA? A molecular modelling investigation
    • Gresh, N. Can a polyproline II helical motif be used in the context of sequence-selective major groove recognition of B-DNA? A molecular modelling investigation. J. Biomol. Struct. Dyn., 1996, 14(2), 255-273. (Pubitemid 26365872)
    • (1996) Journal of Biomolecular Structure and Dynamics , vol.14 , Issue.2 , pp. 255-273
    • Gresh, N.1
  • 292
    • 34547588389 scopus 로고    scopus 로고
    • PrDOS: Prediction of disordered protein regions from amino acid, sequence
    • (Web Server issue)
    • Ishida, T.; Kinoshita, K. PrDOS: prediction of disordered protein regions from amino acid, sequence. Nucleic Acids Res., 2007, 35(Web Server issue), W460-W464.
    • (2007) Nucleic Acids Res. , vol.35
    • Ishida, T.1    Kinoshita, K.2
  • 294
    • 31544433157 scopus 로고    scopus 로고
    • Lakoucheva, L. M. Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins
    • Haynes, C.; lakoucheva, L. M. Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins. Nucleic Acids Res., 2006, 34(1), 305-312.
    • (2006) Nucleic Acids Res. , vol.34 , Issue.1 , pp. 305-312
    • Haynes, C.1
  • 295
    • 0033568338 scopus 로고    scopus 로고
    • 'antifreeze' proteins. Structure-activity studies and mechanisms of ice growth inhibition
    • Harding, M. M.; Ward, L. G.; Haymet, A. D. Type I 'antifreeze' proteins. Structure-activity studies and mechanisms of ice growth inhibition, Eur. J. Biochem., 1999, 264(3), 653-665.
    • (1999) Eur. J. Biochem. , vol.264 , Issue.3 , pp. 653-665
    • Harding, M.M.1    Ward, L.G.2    Type I, H.A.D.3
  • 296
    • 0032529199 scopus 로고    scopus 로고
    • Bactericidal activity and poly-L-proline II conformation of the tandem repeat sequence of human salivary mucin glycoprotein(MG2)
    • Antonyraj, K. J.; Karunakaran, T.; Raj, P. A. Bactericidal activity and poly-L-proline II conformation of the tandem repeat sequence of human salivary mucin glycoprotein(MG2). Arch. Biochem. Biophys., 1998, 356(2), 197-206.
    • (1998) Arch. Biochem. Biophys. , vol.356 , Issue.2 , pp. 197-206
    • Antonyraj, K.J.1    Karunakaran, T.2    Raj, P.A.3
  • 297
    • 0031552605 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal tetrad repeat from synexin (Annexin VII) of Dictyostelium discoideum
    • DOI 10.1006/jmbi.1997.1091
    • Liemann, S.; Bringemeier, I.; Benz, J.; Gottig, P.; Hofmann, A.; Huber, R.; Noegel, A. A.; Jacob, U. Crystal structure of the Cterminal tetrad, repeat from. synexin(annexin VII) of Dictyostelium discoideum. J. Mol. Biol, 1997, 270(1), 79-88. (Pubitemid 27292449)
    • (1997) Journal of Molecular Biology , vol.270 , Issue.1 , pp. 79-88
    • Liemann, S.1    Bringemeier, I.2    Benz, J.3    Gottig, P.4    Hofmann, A.5    Huber, R.6    Noegel, A.A.7    Jacob, U.8
  • 298
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid
    • Balbirnie, M.; Grothe, R.; Eisenberg, D. S. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc. Natl. Acad. Sci USA, 2001, 95(5), 2375-2380.
    • (2001) Proc. Natl. Acad. Sci USA , vol.95 , Issue.5 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 299
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-β spine of amyloid-like fibrils
    • DOI 10.1038/nature03680
    • Nelson, R.; Sawaya, M. R.; Balbirnie, M.; Madsen, A. O.; Riekel, C; Grothe, R.; Eisenberg, D. Structure of the cross-beta spine of amyloid-like fibrils. Nature, 2005, 435(7043), 773-778. (Pubitemid 40839722)
    • (2005) Nature , vol.435 , Issue.7043 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3    Madsen, A.O.4    Riekel, C.5    Grothe, R.6    Eisenberg, D.7
  • 300
    • 58149339635 scopus 로고    scopus 로고
    • Amyloid-beta peptide(Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity
    • Hung, L. W.; Ciccotosto, G. D.; Giannakis, E.; Tew, D. J.; Perez, K.; Masters, C. L.; Cappai, R.; Wade, J. D.; Barnham, K. J. Amyloid-beta peptide(Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity. J. Neurosci., 2008, 25(46), 11950-11958.
    • (2008) J. Neurosci. , vol.25 , Issue.46 , pp. 11950-11958
    • Hung, L.W.1    Ciccotosto, G.D.2    Giannakis, E.3    Tew, D.J.4    Perez, K.5    Masters, C.L.6    Cappai, R.7    Wade, J.D.8    Barnham, K.J.9
  • 302
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. Protein misfolding, evolution and disease. Trends Biochem. Sci, 1999, 24(9), 329-332.
    • (1999) Trends Biochem. Sci , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 303
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson, C. M. The structural basis of protein folding and its links with human disease. Philos. Trans. R. Soc. Lond. B Biol. Sci, 2001, 356(1406), 133-145.
    • (2001) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.356 , Issue.1406 , pp. 133-145
    • Dobson, C.M.1
  • 304
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich, M.; Fletcher, M. A.; Dobson, C M. Amyloid fibrils from muscle myoglobin. Nature, 2001, 470(6825), 165-166.
    • (2001) Nature , vol.470 , Issue.6825 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 305
    • 0028325481 scopus 로고
    • Codon reiteration and the evolution of proteins
    • Green, H.; Wang, N. Codon reiteration and the evolution of proteins. Proc. Natl. Acad. Sci. USA, 1994, 97(10), 4298-4302
    • (1994) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.10 , pp. 4298-4302
    • Green, H.1    Wang, N.2
  • 306
    • 13444292317 scopus 로고    scopus 로고
    • Simple sequence repeats in proteins and their significance for network evolution
    • DOI 10.1016/j.gene.2004.11.023, PII S0378111904006961
    • Hancock, J. M.; Simon, M. Simple sequence repeats in proteins and their significance for network evolution. Gene, 2005, 345(1), 113-118. (Pubitemid 40208507)
    • (2005) Gene , vol.345 , Issue.1 SPEC. ISS , pp. 113-118
    • Hancock, J.M.1    Simon, M.2
  • 307
    • 2442701496 scopus 로고    scopus 로고
    • Microsatellites within genes: Structure, function, and evolution
    • DOI 10.1093/molbev/msh073
    • Li, Y. C.; Korol, A. B.; Fahima, T.; Nevo, E. Microsatellites within genes: structure, function, and evolution. Mol. Biol. Evol, 2004, 27(6), 991-1007. (Pubitemid 38658207)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.6 , pp. 991-1007
    • Li, Y.-C.1    Korol, A.B.2    Fahima, T.3    Nevo, E.4
  • 308
    • 58149182901 scopus 로고    scopus 로고
    • Amino Acid repeats and the structure and evolution of proteins
    • Alba, M. M.; Tompa, P.; Veitia, R. A. Amino Acid repeats and the structure and evolution of proteins. Genome Dyn., 2007, 3, 119-130.
    • (2007) Genome Dyn. , vol.3 , pp. 119-130
    • Alba, M.M.1    Tompa, P.2    Veitia, R.A.3
  • 309
    • 33749543416 scopus 로고    scopus 로고
    • Selection and slippage creating serine homopolymers
    • Huntley, M. A.; Golding, G. B. Selection and slippage creating serine homopolymers. Mol.. Biol. Evol, 2006, 23(11), 2017-2025.
    • (2006) Mol.. Biol. Evol , vol.23 , Issue.11 , pp. 2017-2025
    • Huntley, M.A.1    Golding, G.B.2
  • 310
    • 0028364366 scopus 로고
    • Drive-selection equilibrium: Homopolymer evolution in the Drosophila gene mastermind
    • Newfeld, S. J.; Tachida, H.; Yedvobnick, B. Drive-selection equilibrium: homopolymer evolution in the Drosophila gene master- mind. J. Mol. Evol, 1994, 35(6), 637-641. (Pubitemid 24177297)
    • (1994) Journal of Molecular Evolution , vol.38 , Issue.6 , pp. 637-641
    • Newfeld, S.J.1    Tachida, H.2    Yedvobnick, B.3
  • 311
    • 0033985147 scopus 로고    scopus 로고
    • Evolution of N-terminal sequences of the vertebrate HOXA13 protein
    • DOI 10.1007/s003350010029
    • Mortlock, D. P.; Sateesh, P.; Innis, J. W. Evolution of N-terminal sequences of the vertebrate HOXA13 protein. Mamm. Genome, 2000, 11(2), 151-158. (Pubitemid 30054419)
    • (2000) Mammalian Genome , vol.11 , Issue.2 , pp. 151-158
    • Mortlock, D.P.1    Sateesh, P.2    Innis, J.W.3
  • 313
    • 25844438495 scopus 로고    scopus 로고
    • Repeat instability: Mechanisms of dynamic mutations
    • Pearson, C E.; Nichol Edamura, K.; Cleary, J. D. Repeat instability: mechanisms of dynamic mutations. Nat. Rev. Genet., 2005, 6(10), 729-742.
    • (2005) Nat. Rev. Genet. , vol.6 , Issue.10 , pp. 729-742
    • Pearson, C.E.1    Nichol Edamura, K.2    Cleary, J.D.3
  • 314
    • 0023256559 scopus 로고
    • Slipped-strand mispairing: A major mechanism for DNA sequence evolution
    • Levinson, G.; Gutman, G. A. Slipped-strand mispairing: a major mechanism for DNA sequence evolution. Mol. Biol Evol, 1987, 4(3), 203-221.
    • (1987) Mol. Biol Evol , vol.4 , Issue.3 , pp. 203-221
    • Levinson, G.1    Gutman, G.A.2
  • 315
    • 17644375808 scopus 로고    scopus 로고
    • Replication fork dynamics and dynamic mutations: The fork-shift model of repeat instability
    • cleary, J. D.; Pearson, C E. Replication fork dynamics and dynamic mutations: the fork-shift model of repeat instability. Trends Genet., 2005, 21(5), 272-280.
    • (2005) Trends Genet. , vol.21 , Issue.5 , pp. 272-280
    • Cleary, J.D.1    Pearson, C.E.2
  • 316
    • 0032102835 scopus 로고    scopus 로고
    • Trinucleotide repeat DNA structures: Dynamic mutations from dynamic DNA
    • DOI 10.1016/S0959-440X(98)80065-1
    • Pearson, C. E.; Sinden, R. R. Trinucleotide repeat DNA structures: dynamic mutations from dynamic DNA. Curr. Opin. Struct. Biol., 1998, 5(3), 321-330. (Pubitemid 28321359)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.3 , pp. 321-330
    • Pearson, C.E.1    Sinden, R.R.2
  • 317
    • 0033070196 scopus 로고    scopus 로고
    • Biological implications of the DNA structures associated with disease-causing triplet repeats
    • Sinden, R. R. Biological implications of the DNA structures associated with disease-causing triplet repeats. Am. J. Hum. Genet., 1999, 64(2), 346-353.
    • (1999) Am. J. Hum. Genet. , vol.64 , Issue.2 , pp. 346-353
    • Sinden, R.R.1
  • 318
    • 22244446185 scopus 로고    scopus 로고
    • Advances in mechanisms of genetic instability related to hereditary neurological diseases
    • Wells, R. D.; Dere, R.; Hebert, M. L.; Napierala, M.; Son, L. S. Advances in mechanisms of genetic instability related to hereditary neurological diseases. Nucleic Acids Res., 2005, 33(12), 37853798.
    • (2005) Nucleic Acids Res. , vol.33 , Issue.12 , pp. 37853798
    • Wells, R.D.1    Dere, R.2    Hebert, M.L.3    Napierala, M.4    Son, L.S.5
  • 319
    • 0033845697 scopus 로고    scopus 로고
    • Evolution of simple sequence in. proteins
    • Huntley, M.; Golding, G. B. Evolution of simple sequence in. proteins. J Mol. Evol, 2000, 51(2), 131-140.
    • (2000) J Mol. Evol , vol.51 , Issue.2 , pp. 131-140
    • Huntley, M.1    Golding, G.B.2
  • 320
    • 33745586741 scopus 로고    scopus 로고
    • Genomic and evolutionary insights into genes encoding proteins with single amino acid repeats
    • Siwach, P.; Pophaly, S. D.; Ganesh, S. Genomic and evolutionary insights into genes encoding proteins with single amino acid repeats. Mol.. Biol Evol, 2006, 23(7), 1357-1369.
    • (2006) Mol.. Biol Evol , vol.23 , Issue.7 , pp. 1357-1369
    • Siwach, P.1    Pophaly, S.D.2    Ganesh, S.3
  • 321
    • 33846844726 scopus 로고    scopus 로고
    • Highly constrained proteins contain an unexpectedly large number of amino acid, tandem repeats
    • Mularoni, L.; Veitia, R. A.; Alba, M. M. Highly constrained proteins contain an unexpectedly large number of amino acid, tandem repeats. Genomics, 2007, 59(3), 316-325.
    • (2007) Genomics , vol.59 , Issue.3 , pp. 316-325
    • Mularoni, L.1    Veitia, R.A.2    Alba, M.M.3
  • 322
    • 0029360612 scopus 로고
    • Concerted evolution of repetitive DNA sequences in eukaryotes
    • Elder, J. F., Jr.; Turner, B. J. Concerted evolution of repetitive DNA sequences in eukaryotes. Q. Rev. Biol, 1995, 70(3), 297-320.
    • (1995) Q. Rev. Biol , vol.70 , Issue.3 , pp. 297-320
    • Elder Jr., J.F.1    Turner, B.J.2
  • 323
    • 0033360956 scopus 로고    scopus 로고
    • Concerted evolution: Molecular mechanism and biological implications
    • DOI 10.1086/302221
    • Liao, D. Concerted evolution: molecular mechanism and biological implications. Am. J. Hum. Genet., 1999, 64(1), 24-30. (Pubitemid 30428953)
    • (1999) American Journal of Human Genetics , vol.64 , Issue.1 , pp. 24-30
    • Liao, D.1
  • 324
    • 27944477670 scopus 로고    scopus 로고
    • Concerted and birth-and-death evolution of multigene families
    • DOI 10.1146/annurev.genet.39.073003.112240
    • Nei, M.; Rooney, A. P. Concerted and birth-and-death evolution of multigene families.Annu. Rev. Genet, 2005, 39, 121-152. (Pubitemid 43011110)
    • (2005) Annual Review of Genetics , vol.39 , pp. 121-152
    • Nei, M.1    Rooney, A.P.2
  • 325
    • 0032030236 scopus 로고    scopus 로고
    • Evolution of repetitive proteins: Spider silks from nephila clavipes (Tetragnathidae) and araneus bicentenarius (Araneidae)
    • DOI 10.1016/S0965-1748(97)00083-0, PII S0965174897000830
    • Beckwitt, R.; Arcidiacono, S.; Stote, R. Evolution of repetitive proteins: spider silks from Nephila clavipes(Tetragnathidae) and Araneus bicentenarius(Araneidae). Insect Biochem. Mol. Biol, 1998, 25(3), 121-130. (Pubitemid 28287743)
    • (1998) Insect Biochemistry and Molecular Biology , vol.28 , Issue.3 , pp. 121-130
    • Beckwitt, R.1    Arcidiacono, S.2    Stote, R.3
  • 326
    • 35848932526 scopus 로고    scopus 로고
    • Expansion and intragenic homogenization of spider silk genes since the Triassic: Evidence from Mygalomorphae(tarantulas and. their kin) spidroins
    • Garb, J. E.; DiMauro, T.; Lewis, R. V.; Hayashi, C. Y. Expansion and intragenic homogenization of spider silk genes since the Triassic: evidence from Mygalomorphae(tarantulas and. their kin) spidroins. Mol. Biol. Evol, 2007, 24(11), 2454-2464.
    • (2007) Mol. Biol. Evol , vol.24 , Issue.11 , pp. 2454-2464
    • Garb, J.E.1    Dimauro, T.2    Lewis, R.V.3    Hayashi, C.Y.4
  • 327
    • 38949105514 scopus 로고    scopus 로고
    • Multiple recombining loci encode MaSp1, the primary constituent of dragline silk, in widow spiders(Latrodectus: Theridiidae)
    • Ayoub, N. A.; Hayashi, C. Y. Multiple recombining loci encode MaSp1, the primary constituent of dragline silk, in widow spiders(Latrodectus: Theridiidae). Mol. Biol Evol, 2008, 25(2), 277-286.
    • (2008) Mol. Biol Evol , vol.25 , Issue.2 , pp. 277-286
    • Ayoub, N.A.1    Hayashi, C.Y.2
  • 328
    • 23844471234 scopus 로고    scopus 로고
    • Modular evolution of egg case silk genes across orb-weaving spider superfamilies
    • Garb, J. E.; Hayashi, C. Y. Modular evolution of egg case silk genes across orb-weaving spider superfamilies. Proc. Natl. Acad. Sci. USA, 2005, 102(32), 11379-11384.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.32 , pp. 11379-11384
    • Garb, J.E.1    Hayashi, C.Y.2
  • 329
    • 20144362683 scopus 로고    scopus 로고
    • Molecular characterization and evolutionary study of spider tubuliform (eggcase) silk protein
    • DOI 10.1021/bi050366u
    • Tian, M.; Lewis, R. V. Molecular characterization and evolutionary study of spider rubuliform(eggcase) silk protein. Biochemistry, 2005, 44(22), 8006-8012. (Pubitemid 40776661)
    • (2005) Biochemistry , vol.44 , Issue.22 , pp. 8006-8012
    • Tian, M.1    Lewis, R.V.2
  • 332
    • 0023898752 scopus 로고
    • Concerted gene duplications in the two keratin gene families
    • DOI 10.1007/BF02100075
    • Blumenberg, M. Concerted gene duplications in the two keratin gene families. J MoI Evol, 1988, 27(3), 203-211. (Pubitemid 18161648)
    • (1988) Journal of Molecular Evolution , vol.27 , Issue.3 , pp. 203-211
    • Blumenberg, M.1
  • 333
    • 0021769956 scopus 로고
    • A. new family of tandem repetitive early histone genes in the sea urchin Lytechinus pictus: Evidence for concerted evolution within tandem arrays
    • Holt, C. A.; Childs, G. A. new family of tandem repetitive early histone genes in the sea urchin Lytechinus pictus: evidence for concerted evolution within tandem arrays. Nucleic Acids Res., 1984, 72(16), 6455-6471.
    • (1984) Nucleic Acids Res. , vol.72 , Issue.16 , pp. 6455-6471
    • Holt, C.A.1    Childs, G.2
  • 334
    • 0025056740 scopus 로고
    • Duplication and divergence of the amino-terminal coding region of the complement receptor 1 (CR1) gene. An example of concerted (horizontal) evolution within a gene
    • Hourcade, D.; Miesner, D. R.; Bee, C.; Zeldes, W.; Atkinson, J. P. Duplication and divergence of the amino-terminal coding region of the complement receptor 1 (CRl) gene. An example of concerted(horizontal) evolution within a gene. J. Biol. Chem., 1990, 265(2), 974-980. (Pubitemid 20048886)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.2 , pp. 974-980
    • Hourcade, D.1    Miesner, D.R.2    Bee, C.3    Zeldes, W.4    Atkinson, J.P.5
  • 335
    • 0032415864 scopus 로고    scopus 로고
    • Clusters of resistance genes in plants evolve by divergent selection and
    • Michelmore, R. W.; Meyers, B. C. Clusters of resistance genes in plants evolve by divergent selection and a birth-and-death process. Genome Res., 1998, 8(11), 1113-1130.
    • (1998) Genome Res. , vol.8 , Issue.11 , pp. 1113-1130
    • Michelmore, R.W.1    Meyers, B.C.2
  • 336
    • 33144478758 scopus 로고    scopus 로고
    • Pervasive purifying selection characterizes the evolution of 12 homologs
    • DOI 10.1094/MPMI-19-0288
    • Couch, B. C.; Spangler, R.; Ramos, C.; May, G. Pervasive purifying selection characterizes the evolution of 12 homologa. MoI Plant Microbe. Interact, 2006, 19(3), 288-303. (Pubitemid 43271606)
    • (2006) Molecular Plant-Microbe Interactions , vol.19 , Issue.3 , pp. 288-303
    • Couch, B.C.1    Spangler, R.2    Ramos, C.3    May, G.4
  • 337
    • 34250747504 scopus 로고    scopus 로고
    • Genes encoding pentatricopeptide repeat(PPR) proteins are not conserved in location in plant genomes and may be subject to diversifying selection
    • Geddy, R.; Brown, G. G. Genes encoding pentatricopeptide repeat(PPR) proteins are not conserved in location in plant genomes and may be subject to diversifying selection. BMC Genomics, 2007, 8,130.
    • (2007) BMC Genomics , vol.8 , pp. 130
    • Geddy, R.1    Brown, G.G.2
  • 338
    • 4944233486 scopus 로고    scopus 로고
    • Birth-and-death evolution with strong purifying selection in the histone H1 multigene family and the origin of orphon H2 genes
    • DOI 10.1093/molbev/msh213
    • Eirin-Lopez, J. M.; Gonzalez-Tizon, A. M.; Martinez, A.; Mendez, J. Birth-and-death evolution with strong purifying selection in the histone Hl multigene family and the origin of Orphon H1 genes. Mol. Biol Evol, 2004, 27(10), 1992-2003. (Pubitemid 39331645)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.10 , pp. 1992-2003
    • Eirin-Lopez, J.M.1    Gonzalez-Tizon, A.M.2    Martinez, A.3    Mendez, J.4
  • 340
    • 54049145051 scopus 로고    scopus 로고
    • Selecting the right protein-scoring matrix
    • Chapter 3, Unit 3 5.
    • Wheeler, D. Selecting the right protein-scoring matrix. Curr. Protoe Bioinformatics, 2002, Chapter 3, Unit 3 5.
    • (2002) Curr. Protoe Bioinformatics
    • Wheeler, D.1
  • 341
    • 0035479653 scopus 로고    scopus 로고
    • Distribution of Indel lengths
    • Qian, B.; Goldstein, R. A. Distribution of Indel lengths. Proteins, 2001, 45(1), 102-104.
    • (2001) Proteins , vol.45 , Issue.1 , pp. 102-104
    • Qian, B.1    Goldstein, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.