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Volumn 112, Issue 7, 2011, Pages 1949-1952

Protein folding and the order/disorder paradox

Author keywords

Cancer; Cancer testis antigens; Order disorder paradox; Proteasome; Protein folding

Indexed keywords

GLOBULAR PROTEIN; PROTEOME;

EID: 80051482698     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.23115     Document Type: Article
Times cited : (11)

References (24)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. 1973. Principles that govern the folding of protein chains. Science 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 66749163093 scopus 로고    scopus 로고
    • Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data
    • Edwards YJ, Lobley AE, Pentony MM, Jones DT. 2009. Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data. Genome Biol 10:R50.
    • (2009) Genome Biol , vol.10
    • Edwards, Y.J.1    Lobley, A.E.2    Pentony, M.M.3    Jones, D.T.4
  • 4
    • 42449151176 scopus 로고    scopus 로고
    • Protein folding and misfolding: Mechanism and principles
    • DOI 10.1017/S0033583508004654, PII S0033583508004654
    • Englander SW, Mayne L, Krishna MM. 2007. Protein folding and misfolding: Mechanism and principles. Q Rev Biophys 40:287-326. (Pubitemid 351569384)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.4 , pp. 287-326
    • Englander, S.W.1    Mayne, L.2    Krishna, M.M.G.3
  • 5
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink AL. 1995. Compact intermediate states in protein folding. Annu Rev Biophys Biomol Struct 24:495-522.
    • (1995) Annu Rev Biophys Biomol Struct , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 6
    • 0033231014 scopus 로고    scopus 로고
    • A 'distributed degron' allows regulated entry into the ER degradation pathway
    • DOI 10.1093/emboj/18.21.5994
    • Gardner RG, Hampton RY. 1999. A 'distributed degron' allows regulated entry into the ER degradation pathway. EMBO J 18:5994-6004. (Pubitemid 29515676)
    • (1999) EMBO Journal , vol.18 , Issue.21 , pp. 5994-6004
    • Gardner, R.G.1    Hampton, R.Y.2
  • 7
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • DOI 10.1038/nature02263
    • Goldberg AL. 2003. Protein degradation and protection against misfolded or damaged proteins. Nature 426:895-899. (Pubitemid 38056882)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 895-899
    • Goldberg, A.L.1
  • 8
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: From transcript synthesis to protein degradation
    • DOI 10.1126/science.1163581
    • Gsponer J, Futschik ME, Teichmann SA, Babu MM. 2008. Tight regulation of unstructured proteins: From transcript synthesis to protein degradation. Science 322:1365-1368. (Pubitemid 352775246)
    • (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
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, Hayer-Hartl M. 2009. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 16:574-581.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 10
    • 41849150019 scopus 로고    scopus 로고
    • Intrinsically disordered proteins display no preference for chaperone binding in vivo
    • Hegyi H, Tompa P. 2008. Intrinsically disordered proteins display no preference for chaperone binding in vivo. PLoS Comput Biol 4(3):e1000017.
    • (2008) PLoS Comput Biol , vol.4 , Issue.3
    • Hegyi, H.1    Tompa, P.2
  • 11
    • 77956501272 scopus 로고    scopus 로고
    • A transient and low-populated protein-folding intermediate at atomic resolution
    • Korzhnev DM, Religa TL, Banachewicz W, Fersht AR, Kay LE. 2010. A transient and low-populated protein-folding intermediate at atomic resolution. Science 329:1312-1316.
    • (2010) Science , vol.329 , pp. 1312-1316
    • Korzhnev, D.M.1    Religa, T.L.2    Banachewicz, W.3    Fersht, A.R.4    Kay, L.E.5
  • 12
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • DOI 10.1016/S1097-2765(01)00209-X
    • Lee C, Schwartz MP, Prakash S, Iwakura M, Matouschek A. 2001. ATPdependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol Cell 7:627-637. (Pubitemid 32706354)
    • (2001) Molecular Cell , vol.7 , Issue.3 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 13
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of Longevity in Caenorhabditis elegans by Heat Shock Factor and Molecular Chaperones
    • DOI 10.1091/mbc.E03-07-0532
    • Morley JF, Morimoto RI. 2004. Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. Mol Biol Cell 15:657-664. (Pubitemid 38146482)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.2 , pp. 657-664
    • Morley, J.F.1    Morimoto, R.I.2
  • 16
    • 77950618150 scopus 로고    scopus 로고
    • Molecular simulations of protein disorder
    • Rauscher S, Pomès R. 2010. Molecular simulations of protein disorder. Biochem Cell Biol 88:269-290.
    • (2010) Biochem Cell Biol , vol.88 , pp. 269-290
    • Rauscher, S.1    Pomès, R.2
  • 17
    • 2942591945 scopus 로고    scopus 로고
    • The cancer/testis genes: Review, standardization, and commentary
    • Scanlan MJ, Simpson AJ, Old LJ. 2004. The cancer/testis genes: Review, standardization, and commentary. Cancer Immun 4:1-15.
    • (2004) Cancer Immun , vol.4 , pp. 1-15
    • Scanlan, M.J.1    Simpson, A.J.2    Old, L.J.3
  • 21
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited. A polypeptide chain at the folding - Misfolding - Nonfolding cross-roads: Which way to go?
    • DOI 10.1007/s00018-003-3096-6
    • Uversky VN. 2003. Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go? Cell Mol Life Sci 60:1852-1871. (Pubitemid 37222583)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.9 , pp. 1852-1871
    • Uversky, V.N.1
  • 22
    • 77949916296 scopus 로고    scopus 로고
    • Understanding protein non-folding
    • Uversky VN, Dunker K. 2010. Understanding protein non-folding. Biochim Biophys Acta 1804:1231-1264.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1231-1264
    • Uversky, V.N.1    Dunker, K.2
  • 23
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky VN, Oldfield CJ, Dunker AK. 2008. Intrinsically disordered proteins in human diseases: Introducing the D2 concept. Annu Rev Biophys 37:215-246.
    • (2008) Annu Rev Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 24
    • 55849136903 scopus 로고    scopus 로고
    • Global protein stability profiling in mammalian cells
    • Yen HC, Xu Q, Chou DM, Zhao Z, Elledge SJ. 2008. Global protein stability profiling in mammalian cells. Science 322:918-923.
    • (2008) Science , vol.322 , pp. 918-923
    • Yen, H.C.1    Xu, Q.2    Chou, D.M.3    Zhao, Z.4    Elledge, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.