메뉴 건너뛰기




Volumn 86, Issue 5, 2012, Pages

Sequence repeats and protein structure

Author keywords

[No Author keywords available]

Indexed keywords

COARSE GRAINED MODELS; FOLDING PROPERTIES; FUNCTIONAL PROTEINS; PHYSIOLOGICAL TEMPERATURE; PROTEIN SEQUENCES; PROTEIN STRUCTURES; RANDOM SEQUENCE; REPEATED SEQUENCES; SEQUENCE CONSERVATION; SEQUENCE REPETITION; TANDEM REPEATS;

EID: 84870442494     PISSN: 15393755     EISSN: 15502376     Source Type: Journal    
DOI: 10.1103/PhysRevE.86.050901     Document Type: Article
Times cited : (2)

References (33)
  • 4
    • 40749144066 scopus 로고    scopus 로고
    • De novo identification of highly diverged protein repeats by probabilistic consistency
    • DOI 10.1093/bioinformatics/btn039
    • A. Biegert and J. Soeding, Bioinformatics BOINFP 1367-4803 10.1093/bioinformatics/btn039 24, 807 (2008). (Pubitemid 351386919)
    • (2008) Bioinformatics , vol.24 , Issue.6 , pp. 807-814
    • Biegert, A.1    Soding, J.2
  • 6
    • 77956541123 scopus 로고    scopus 로고
    • BOINFP 1367-4803 10.1093/bioinformatics/btq371
    • A. Vo and N. Nguyen, and H. Huang, Bioinformatics BOINFP 1367-4803 10.1093/bioinformatics/btq371 26, I467 (2010).
    • (2010) Bioinformatics , vol.26 , pp. 467
    • Vo, A.1    Nguyen, N.2    Huang, H.3
  • 7
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • DOI 10.1006/jmbi.1999.3110
    • P. E. Wright, and H. J. Dyson, J. Mol. Biol. JMOBAK 0022-2836 10.1006/jmbi.1999.3110 293, 7960 (1999). (Pubitemid 29516173)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.2 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 9
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity - Linking function and disorder
    • DOI 10.1038/nbt0901-805
    • A. K. Dunker, and Z. Obradovic, Nat. Biotechnol. NABIF9 1087-0156 10.1038/nbt0901-805 19, 805 (2001). (Pubitemid 32816745)
    • (2001) Nature Biotechnology , vol.19 , Issue.9 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 10
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • DOI 10.1016/S0959-440X(02)00289-0
    • H. J. Dyson, and P. E. Wright, Curr. Opin. Struct. Biol. COSBEF 0959-440X 10.1016/S0959-440X(02)00289-0 12, 54 (2002). (Pubitemid 34142721)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.1 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 11
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • DOI 10.1016/S0968-0004(02)02169-2, PII S0968000402021692
    • P. Tompa, Trends Biochem. Sci. 0968-0004 10.1016/S0968-0004(02)02169-2 27, 527 (2002). (Pubitemid 35279598)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 527-533
    • Tompa, P.1
  • 12
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • DOI 10.1046/j.0014-2956.2001.02649.x
    • V. N. Uversky, Eur. J. Biochem. EJBCAI 0014-2956 10.1046/j.0014-2956. 2001.02649.x 269, 2 (2002). (Pubitemid 34107333)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.1 , pp. 2-12
    • Uversky, V.N.1
  • 13
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • DOI 10.1016/j.jmb.2004.03.017, PII S0022283604003079
    • M. Fuxreiter, I. Simon, P. Friedrich, and P. Tompa, J. Mol. Biol. JMOBAK 0022-2836 10.1016/j.jmb.2004.03.017 338, 1015 (2004). (Pubitemid 38542830)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.5 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 14
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti and C. M. Dobson, Annu. Rev. Biochem. ARBOAW 0066-4154 10.1146/annurev.biochem.75.101304.123901 75, 333 (2006). (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 16
    • 77953211283 scopus 로고    scopus 로고
    • 1742-464X 10.1111/j.1742-4658.2010.07684.x
    • J. Jorda, B. Xue, V. N. Uversky, and A. V. Kajava, FEBS J. 1742-464X 10.1111/j.1742-4658.2010.07684.x 277, 2673 (2010).
    • (2010) FEBS J. , vol.277 , pp. 2673
    • Jorda, J.1    Xue, B.2    Uversky, V.N.3    Kajava, A.V.4
  • 17
    • 23044475553 scopus 로고    scopus 로고
    • A recurring theme in protein engineering: The design, stability and folding of repeat proteins
    • DOI 10.1016/j.sbi.2005.07.003, PII S0959440X05001259, Membranes/Engineering and Desing
    • E. R. G. Main, A. R. Lowe, S. G. J. Mochrie, S. E. Jackson, and L. Regan, Curr. Opin. Struct. Biol. COSBEF 0959-440X 10.1016/j.sbi.2005.07.003 15, 464 (2005). (Pubitemid 41073839)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.4 , pp. 464-471
    • Main, E.R.G.1    Lowe, A.R.2    Mochrie, S.G.J.3    Jackson, S.E.4    Regan, L.5
  • 18
    • 0034691565 scopus 로고    scopus 로고
    • Optimal shapes of compact strings
    • DOI 10.1038/35018538
    • A. Maritan, C. Micheletti, A. Trovato, and J. R. Banavar, Nature (London) NATUAS 0028-0836 10.1038/35018538 406, 287 (2000). (Pubitemid 30604402)
    • (2000) Nature , vol.406 , Issue.6793 , pp. 287-290
    • Maritan, A.1    Micheletti, C.2    Trovato, A.3    Banavar, J.R.4
  • 24
    • 0027122748 scopus 로고
    • NATUAS 0028-0836 10.1038/357543a0
    • C. Chothia, Nature (London) NATUAS 0028-0836 10.1038/357543a0 357, 543 (1992).
    • (1992) Nature (London) , vol.357 , pp. 543
    • Chothia, C.1
  • 28
    • 35949020425 scopus 로고
    • PRLTAO 0031-9007 10.1103/PhysRevLett.57.2607
    • R. H. Swendsen and J. S. Wang, Phys. Rev. Lett. PRLTAO 0031-9007 10.1103/PhysRevLett.57.2607 57, 2607 (1986).
    • (1986) Phys. Rev. Lett. , vol.57 , pp. 2607
    • Swendsen, R.H.1    Wang, J.S.2
  • 29
    • 33646987405 scopus 로고
    • PRLTAO 0031-9007 10.1103/PhysRevLett.63.1195
    • A. M. Ferrenberg and R. H. Swendsen, Phys. Rev. Lett. PRLTAO 0031-9007 10.1103/PhysRevLett.63.1195 63, 1195 (1989).
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 30
    • 0035783062 scopus 로고    scopus 로고
    • JSBIEM 1047-8477 10.1006/jsbi.2000.4328
    • A. V. Kajava, J. Struct. Biol. JSBIEM 1047-8477 10.1006/jsbi.2000.4328 134, 132 (2001).
    • (2001) J. Struct. Biol. , vol.134 , pp. 132
    • Kajava, A.V.1
  • 31
    • 0034310589 scopus 로고    scopus 로고
    • Energetic components of cooperative protein folding
    • DOI 10.1103/PhysRevLett.85.4823
    • H. Kaya and H. S. Chan, Phys. Rev. Lett. PRLTAO 0031-9007 10.1103/PhysRevLett.85.4823 85, 4823 (2000). (Pubitemid 32070431)
    • (2000) Physical Review Letters , vol.85 , Issue.22 , pp. 4823-4826
    • Kaya, H.1    Chan, H.S.2
  • 33
    • 0035188314 scopus 로고    scopus 로고
    • Sequence complexity of disordered protein
    • DOI 10.1002/1097-0134(20010101)42:1<38::AID-PROT50>3.0.CO;2-3
    • P. Romero, Z. Obradovic, X. Li, E. C. Garner, C. J. Brown, and A. K. Dunker, Proteins 18PLAF 0887-3585 10.1002/1097-0134(20010101)42:1<38::AID- PROT50>3.0.CO;2-3 42, 38 (2001). (Pubitemid 32015215)
    • (2001) Proteins: Structure, Function and Genetics , vol.42 , Issue.1 , pp. 38-48
    • Xue, Y.1    Liu, J.-N.2    Sun, Z.3    Ma, Z.4    Wu, C.5    Zhu, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.