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Volumn 19, Issue 8, 2009, Pages 929-949

Predicting intrinsic disorder in proteins: An overview

Author keywords

Intrinsic disorder; Prediction method; Protein

Indexed keywords

PROTEIN;

EID: 68749093787     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2009.87     Document Type: Review
Times cited : (368)

References (130)
  • 1
    • 0001189176 scopus 로고
    • Studies on denaturation of proteins. XIII. A theory of denaturation
    • Wu H. Studies on denaturation of proteins. XIII. A theory of denaturation. Chin J Physiol 1931; 1:219-234.
    • (1931) Chin J Physiol , vol.1 , pp. 219-234
    • Wu, H.1
  • 2
    • 0028948518 scopus 로고
    • Wu and the frst theory of protein denaturation (1931)
    • Edsall JT. Hsien Wu and the frst theory of protein denaturation (1931). Adv Protein Chem 1995; 46:1-5.
    • (1995) Adv Protein Chem , vol.46 , pp. 1-5
    • Hsien, E.J.T.1
  • 3
    • 52249085709 scopus 로고    scopus 로고
    • The unfoldomics decade: An update on intrinsically disordered proteins
    • Dunker AK, Oldfield CJ, Meng J, et al. The unfoldomics decade: an update on intrinsically disordered proteins. BMC Genomics 2008; 9:S1.
    • (2008) BMC Genomics , vol.9
    • Dunker, A.K.1    Oldfield, C.J.2    Meng, J.3
  • 5
    • 33847795359 scopus 로고    scopus 로고
    • Intrinsic disorder and functional proteomics
    • Radivojac P, Iakoucheva LM, Oldfeld CJ, et al. Intrinsic disorder and functional proteomics. Biophys J 2007; 92:1439-1456.
    • (2007) Biophys J , vol.92 , pp. 1439-1456
    • Radivojac, P.1    Iakoucheva, L.M.2    Oldfeld, C.J.3
  • 6
    • 34249282661 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions
    • Vucetic S, Xie H, Iakoucheva LM, et al. Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions. J Proteome Res 2007; 6:1899-1916.
    • (2007) J Proteome Res , vol.6 , pp. 1899-1916
    • Vucetic, S.1    Xie, H.2    Iakoucheva, L.M.3
  • 7
    • 33847768609 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions
    • Xie H, Vucetic S, Iakoucheva LM, et al. Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. J Proteome Res 2007; 6:1882-1898.
    • (2007) J Proteome Res , vol.6 , pp. 1882-1898
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3
  • 8
    • 33847783298 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifcations, and diseases associated with intrinsically disordered proteins
    • Xie H, Vucetic S, Iakoucheva LM, et al. Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifcations, and diseases associated with intrinsically disordered proteins. J Proteome Res 2007; 6:1917-1932.
    • (2007) J Proteome Res , vol.6 , pp. 1917-1932
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3
  • 9
    • 41149178980 scopus 로고    scopus 로고
    • A careful disorderliness in the proteome: Sites for interaction and targets for future therapies
    • Russell RB, Gibson TJ. A careful disorderliness in the proteome: sites for interaction and targets for future therapies. FEBS Lett 2008; 582:1271-1275.
    • (2008) FEBS Lett , vol.582 , pp. 1271-1275
    • Russell, R.B.1    Gibson, T.J.2
  • 10
    • 40949117264 scopus 로고    scopus 로고
    • Intrinsic disorder in protein-protein interaction networks: Case studies of complexes involving p53 and 14-3-3
    • Oldfeld CJ, Meng J, Yang JY, et al. Intrinsic disorder in protein-protein interaction networks: case studies of complexes involving p53 and 14-3-3. BMC Genomics 2008; 9:S1.
    • (2008) BMC Genomics , vol.9
    • Oldfeld, C.J.1    Meng, J.2    Yang, J.Y.3
  • 11
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • Oldfeld CJ, Meng J, Yang J Y, et al. Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics 2008; 9:S1.
    • (2008) BMC Genomics , vol.9
    • Oldfeld, C.J.1    Meng, J.2    Yang, J.Y.3
  • 12
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa P, Csermely P. The role of structural disorder in the function of RNA and protein chaperones. Faseb J 2004; 18:1169-1175.
    • (2004) Faseb J , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 13
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specifc binding of proteins to DNA
    • Spolar RS, Record MT Jr. Coupling of local folding to site-specifc binding of proteins to DNA. Science 1994; 263:777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 14
    • 33947445379 scopus 로고
    • A Theory of the structure and process of formation of antibodies
    • Pauling L. A Theory of the structure and process of formation of antibodies. J Am Chem Soc 1940; 62:2643-2657.
    • (1940) J Am Chem Soc , vol.62 , pp. 2643-2657
    • Pauling, L.1
  • 15
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter M, Simon I, Friedrich P, Tompa P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J Mol Biol 2004; 338:1015-1026.
    • (2004) J Mol Biol , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 16
    • 64449083994 scopus 로고    scopus 로고
    • Reconciling binding mechanisms of intrinsically disordered proteins
    • Espinoza-Fonseca LM. Reconciling binding mechanisms of intrinsically disordered proteins. Biochem Biophys Res Commun 2009; 382:479-482.
    • (2009) Biochem Biophys Res Commun , vol.382 , pp. 479-482
    • Espinoza-Fonseca, L.M.1
  • 18
    • 0031616362 scopus 로고    scopus 로고
    • Protein disorder and the evolution of molecular recognition: Theory, predictions and observations
    • Dunker AK, Garner E, Guilliot S, et al. Protein disorder and the evolution of molecular recognition: theory, predictions and observations. Pac Symp Biocomput 1998:473-484.
    • (1998) Pac Symp Biocomput , pp. 473-484
    • Dunker, A.K.1    Garner, E.2    Guilliot, S.3
  • 19
    • 33744814686 scopus 로고    scopus 로고
    • Functional profling by alternative splicing and intrinsic protein disorder
    • Romero R, Zaidi S, Fang YY, et al. Functional profling by alternative splicing and intrinsic protein disorder. Proc Natl Acad Sci USA 2006; 103:8390-8395.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8390-8395
    • Romero, R.1    Zaidi, S.2    Fang, Y.Y.3
  • 20
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem Sci 2002; 27:527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 21
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky VN. Natively unfolded proteins: a point where biology waits for physics. Protein Sci 2002; 11:739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 22
    • 35248852356 scopus 로고    scopus 로고
    • Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation
    • Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. J Mol Evol 2007; 65:277-288.
    • (2007) J Mol Evol , vol.65 , pp. 277-288
    • Daughdrill, G.W.1    Narayanaswami, P.2    Gilmore, S.H.3    Belczyk, A.4    Brown, C.J.5
  • 24
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright PE, Dyson HJ. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. J Mol Biol 1999; 293:321-331.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 25
    • 0029904487 scopus 로고    scopus 로고
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT Jr. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 1996; 35:13709-13715.
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT Jr. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 1996; 35:13709-13715.
  • 26
    • 22744437069 scopus 로고    scopus 로고
    • Natively disordered proteins: Functions and predictions
    • Romero P, Obradovic Z, Dunker AK. Natively disordered proteins: functions and predictions. Appl Bioinformatics 2004; 3:105-113.
    • (2004) Appl Bioinformatics , vol.3 , pp. 105-113
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 28
    • 67449092566 scopus 로고    scopus 로고
    • Characterisation of the structural features and interactions of sclerostin: Molecular insight into a key regulator of Wnt-mediated bone formation
    • Veverka V, Henry AJ, Slocombe PM, et al. Characterisation of the structural features and interactions of sclerostin: molecular insight into a key regulator of Wnt-mediated bone formation. J Biol Chem 2009; 284:10890-10900.
    • (2009) J Biol Chem , vol.284 , pp. 10890-10900
    • Veverka, V.1    Henry, A.J.2    Slocombe, P.M.3
  • 29
    • 0035808306 scopus 로고    scopus 로고
    • Structure-activity relationships in fexible protein domains: Regu- lation of rho GTPases by RhoGDI and D4 GDI
    • Golovanov AP, Chuang TH, DerMardirossian C, et al. Structure-activity relationships in fexible protein domains: regu- lation of rho GTPases by RhoGDI and D4 GDI. J Mol Biol 2001; 305:121-135.
    • (2001) J Mol Biol , vol.305 , pp. 121-135
    • Golovanov, A.P.1    Chuang, T.H.2    DerMardirossian, C.3
  • 30
    • 1942521630 scopus 로고    scopus 로고
    • Presence of transient helical segments in the galanin-like peptide evident from (1)H NMR, circular dichroism, and prediction studies
    • Dastmalchi S, Church WB, Morris MB, Iismaa TP, Mackay JP. Presence of transient helical segments in the galanin-like peptide evident from (1)H NMR, circular dichroism, and prediction studies. J Struct Biol 2004; 146:261-271.
    • (2004) J Struct Biol , vol.146 , pp. 261-271
    • Dastmalchi, S.1    Church, W.B.2    Morris, M.B.3    Iismaa, T.P.4    Mackay, J.P.5
  • 31
    • 0028848524 scopus 로고
    • Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex
    • Kissinger CR, Parge HE, Knighton DR, et al. Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature 1995; 378:641-644.
    • (1995) Nature , vol.378 , pp. 641-644
    • Kissinger, C.R.1    Parge, H.E.2    Knighton, D.R.3
  • 32
    • 33645292569 scopus 로고    scopus 로고
    • Calmodulin signaling: Analysis and prediction of a disorder-dependent molecular recognition
    • Radivojac P, Vucetic S, O'Connor TR, et al. Calmodulin signaling: analysis and prediction of a disorder-dependent molecular recognition. Proteins 2006; 63:398-410.
    • (2006) Proteins , vol.63 , pp. 398-410
    • Radivojac, P.1    Vucetic, S.2    O'Connor, T.R.3
  • 34
    • 0018539155 scopus 로고
    • The conformation properties of proteins in solution
    • Williams RJ. The conformation properties of proteins in solution. Biol Rev Camb Philos Soc 1979; 54:389-437.
    • (1979) Biol Rev Camb Philos Soc , vol.54 , pp. 389-437
    • Williams, R.J.1
  • 35
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 2000; 41:415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 38
    • 0035188314 scopus 로고    scopus 로고
    • Sequence complexity of disordered protein
    • Romero P, Obradovic Z, Li X, et al. Sequence complexity of disordered protein. Proteins 2001; 42:38-48.
    • (2001) Proteins , vol.42 , pp. 38-48
    • Romero, P.1    Obradovic, Z.2    Li, X.3
  • 39
    • 14544299774 scopus 로고    scopus 로고
    • Optimizing long intrinsic disorder predictors with protein evolutionary information
    • Peng K, Vucetic S, Radivojac P, et al. Optimizing long intrinsic disorder predictors with protein evolutionary information. J Bioinform Comput Biol 2005; 3:35-60.
    • (2005) J Bioinform Comput Biol , vol.3 , pp. 35-60
    • Peng, K.1    Vucetic, S.2    Radivojac, P.3
  • 40
    • 30344485673 scopus 로고    scopus 로고
    • Exploiting heterogeneous sequence properties improves prediction of protein disorder
    • Obradovic Z, Peng K, Vucetic S, Radivojac P, Dunker AK. Exploiting heterogeneous sequence properties improves prediction of protein disorder. Proteins 2005; 61:176-182.
    • (2005) Proteins , vol.61 , pp. 176-182
    • Obradovic, Z.1    Peng, K.2    Vucetic, S.3    Radivojac, P.4    Dunker, A.K.5
  • 42
    • 24044515001 scopus 로고    scopus 로고
    • FoldIndex: A simple tool to predict whether a given protein sequence is intrinsically unfolded
    • Prilusky J, Felder CE, Zeev-Ben-Mordehai T. FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 2005; 21:3435-3438.
    • (2005) Bioinformatics , vol.21 , pp. 3435-3438
    • Prilusky, J.1    Felder, C.E.2    Zeev-Ben-Mordehai, T.3
  • 43
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • Linding R, Russell RB, Neduva V, Gibson TJ. GlobPlot: exploring protein sequences for globularity and disorder. Nucleic Acids Res 2003; 31:3701-3708.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 44
    • 0242458482 scopus 로고    scopus 로고
    • Protein disorder prediction: Implications for structural proteomics
    • Linding R, Jensen LJ, Diella F, et al. Protein disorder prediction: implications for structural proteomics. Structure 2003; 11:1453-1459.
    • (2003) Structure , vol.11 , pp. 1453-1459
    • Linding, R.1    Jensen, L.J.2    Diella, F.3
  • 45
    • 0242362157 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins from position specific score matrices
    • Jones DT, Ward JJ. Prediction of disordered regions in proteins from position specific score matrices. Proteins 2003; 53:573-578.
    • (2003) Proteins , vol.53 , pp. 573-578
    • Jones, D.T.1    Ward, J.J.2
  • 46
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffn LJ, Buxton BF, Jones DT. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 2004; 337:635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffn, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 48
    • 23144444979 scopus 로고    scopus 로고
    • Protein structure prediction servers at University College London
    • Bryson K, McGuffn LJ, Marsden RL, et al. Protein structure prediction servers at University College London. Nucleic Ac- ids Res 2005; 33:36-38.
    • (2005) Nucleic Ac- ids Res , vol.33 , pp. 36-38
    • Bryson, K.1    McGuffn, L.J.2    Marsden, R.L.3
  • 50
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztányi Z, Csizmók V, Tompa P, Simon I. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 2005; 347:827-839.
    • (2005) J Mol Biol , vol.347 , pp. 827-839
    • Dosztányi, Z.1    Csizmók, V.2    Tompa, P.3    Simon, I.4
  • 51
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 2005; 21:3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 53
    • 33751381791 scopus 로고    scopus 로고
    • FoldUn-fold: Web server for the prediction of disordered regions in protein chain
    • Galzitskaya OV, Garbuzynskiy SO, Lobanov MY. FoldUn-fold: web server for the prediction of disordered regions in protein chain. Bioinformatics 2006; 22:2948-2949.
    • (2006) Bioinformatics , vol.22 , pp. 2948-2949
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Lobanov, M.Y.3
  • 54
    • 34547681771 scopus 로고    scopus 로고
    • Expected packing density allows prediction of both amyloidogenic and disordered regions in protein chains
    • 15 pp
    • Galzitskaya OV, Garbuzynskiy SO, Lobanov MY. Expected packing density allows prediction of both amyloidogenic and disordered regions in protein chains. J Phys 2007; 19:285225 (15 pp).
    • (2007) J Phys , vol.19 , pp. 285225
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Lobanov, M.Y.3
  • 55
    • 20744437001 scopus 로고    scopus 로고
    • RONN: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • Yang ZR, Thomson R, McNeil P, Esnouf RM. RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 2005; 21:3369-3376.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 56
    • 27944488680 scopus 로고    scopus 로고
    • Accurate prediction of protein disordered regions by mining protein structure data
    • Cheng J, Sweredoski MJ, Baldi P. Accurate prediction of protein disordered regions by mining protein structure data. Data Mining and Knowledge Discovery 2005; 11:213-222.
    • (2005) Data Mining and Knowledge Discovery , vol.11 , pp. 213-222
    • Cheng, J.1    Sweredoski, M.J.2    Baldi, P.3
  • 57
    • 33746952996 scopus 로고    scopus 로고
    • Protein disorder prediction by condensed PSSM considering propensity for order or disorder
    • Su CT, Chen CY, Ou YY. Protein disorder prediction by condensed PSSM considering propensity for order or disorder. BMC Bioinformatics 2006; 7:319.
    • (2006) BMC Bioinformatics , vol.7 , pp. 319
    • Su, C.T.1    Chen, C.Y.2    Ou, Y.Y.3
  • 58
    • 34547574473 scopus 로고    scopus 로고
    • iPDA: Integrated protein disorder analyzer
    • Su CT, Chen CY, Hsu CM. iPDA: integrated protein disorder analyzer. Nucleic Acids Res 2007; 35:465-472.
    • (2007) Nucleic Acids Res , vol.35 , pp. 465-472
    • Su, C.T.1    Chen, C.Y.2    Hsu, C.M.3
  • 59
    • 33747868721 scopus 로고    scopus 로고
    • Spritz: A server for the prediction of intrinsically disordered regions in protein sequences using kernel machines
    • Vullo A, Bortolami O, Pollastri G, Tosatto SC. Spritz: a server for the prediction of intrinsically disordered regions in protein sequences using kernel machines. Nucleic Acids Res 2006; 34:164-168.
    • (2006) Nucleic Acids Res , vol.34 , pp. 164-168
    • Vullo, A.1    Bortolami, O.2    Pollastri, G.3    Tosatto, S.C.4
  • 60
    • 34547588389 scopus 로고    scopus 로고
    • PrDOS: Prediction of disordered protein regions from amino acid sequence
    • Ishida T, Kinoshita K. PrDOS: prediction of disordered protein regions from amino acid sequence. Nucleic Acids Res 2007; 35:460-464.
    • (2007) Nucleic Acids Res , vol.35 , pp. 460-464
    • Ishida, T.1    Kinoshita, K.2
  • 61
    • 13644257647 scopus 로고    scopus 로고
    • Comparing and combining predictors of mostly disordered proteins
    • Oldfield CJ, Cheng Y, Cortese MS, et al. Comparing and combining predictors of mostly disordered proteins. Biochemistry 2005; 44:1989-2000.
    • (2005) Biochemistry , vol.44 , pp. 1989-2000
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3
  • 62
    • 23644449725 scopus 로고    scopus 로고
    • The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded
    • Bourhis JM, Receveur-Brechot V, Oglesbee M, et al. The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. Protein Sci 2005; 14:1975-1992.
    • (2005) Protein Sci , vol.14 , pp. 1975-1992
    • Bourhis, J.M.1    Receveur-Brechot, V.2    Oglesbee, M.3
  • 63
    • 4744349987 scopus 로고    scopus 로고
    • Combining prediction, computation and experiment for the characterization of protein disorder
    • Bracken C, Iakoucheva LM, Romero PR, Dunker AK. Combining prediction, computation and experiment for the characterization of protein disorder. Curr Opin Struct Biol 2004; 14:570-576.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 570-576
    • Bracken, C.1    Iakoucheva, L.M.2    Romero, P.R.3    Dunker, A.K.4
  • 64
    • 3242802943 scopus 로고    scopus 로고
    • Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E
    • Callaghan AJ, Aurikko JP, Ilag LL, et al. Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. J Mol Biol 2004; 340:965-979.
    • (2004) J Mol Biol , vol.340 , pp. 965-979
    • Callaghan, A.J.1    Aurikko, J.P.2    Ilag, L.L.3
  • 65
    • 0037705413 scopus 로고    scopus 로고
    • The C-termi-nal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein
    • Longhi S, Receveur-Brechot V, Karlin D, et al. The C-termi-nal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. J Biol Chem 2003; 278:18638-18648.
    • (2003) J Biol Chem , vol.278 , pp. 18638-18648
    • Longhi, S.1    Receveur-Brechot, V.2    Karlin, D.3
  • 66
    • 1642512502 scopus 로고    scopus 로고
    • The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner
    • Bourhis JM, Johansson K, Receveur-Brechot V, et al. The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner. Virus Res 2004; 99:157-167.
    • (2004) Virus Res , vol.99 , pp. 157-167
    • Bourhis, J.M.1    Johansson, K.2    Receveur-Brechot, V.3
  • 68
    • 33645097025 scopus 로고    scopus 로고
    • Recognition of enolase in the Escherichia coli RNA degradosome
    • Chandran V, Luisi BF. Recognition of enolase in the Escherichia coli RNA degradosome. J Mol Biol 2006; 358:8-15.
    • (2006) J Mol Biol , vol.358 , pp. 8-15
    • Chandran, V.1    Luisi, B.F.2
  • 69
    • 51049119258 scopus 로고    scopus 로고
    • Multiple intrinsically disordered sequences alter DNA binding by the homeodomain of the Drosophila hox protein ultrabithorax
    • Liu Y, Matthews KS, Bondos SE. Multiple intrinsically disordered sequences alter DNA binding by the homeodomain of the Drosophila hox protein ultrabithorax. J Biol Chem 2008; 283:20874-20887.
    • (2008) J Biol Chem , vol.283 , pp. 20874-20887
    • Liu, Y.1    Matthews, K.S.2    Bondos, S.E.3
  • 70
    • 0036017388 scopus 로고    scopus 로고
    • Evolutionary rate heterogeneity in proteins with long disordered regions
    • Brown CJ, Takayama S, Campen AM, et al. Evolutionary rate heterogeneity in proteins with long disordered regions. J Mol Evol 2002; 55:104-110.
    • (2002) J Mol Evol , vol.55 , pp. 104-110
    • Brown, C.J.1    Takayama, S.2    Campen, A.M.3
  • 71
    • 57149085681 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: Controlled chaos
    • Uversky VN, Dunker AK. Intrinsically disordered proteins: controlled chaos. Science 2008; 322: 1340-1341
    • (2008) Science , vol.322 , pp. 1340-1341
    • Uversky, V.N.1    Dunker, A.K.2
  • 72
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: From transcript synthesis to protein degradation
    • Gsponer J, Futschik ME, Teichmann SA, Babu MM. Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science 2008; 322:1365-1368.
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 73
    • 3142670846 scopus 로고    scopus 로고
    • Overproduction, crystallization and preliminary crystallographic analysis of a novel human DNA-repair enzyme that recognizes oxidative DNA damage
    • Bandaru V, Cooper W, Wallace SS, Doublie S. Overproduction, crystallization and preliminary crystallographic analysis of a novel human DNA-repair enzyme that recognizes oxidative DNA damage. Acta Crystallogr D Biol Crystallogr 2004; 60:1142-1144.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1142-1144
    • Bandaru, V.1    Cooper, W.2    Wallace, S.S.3    Doublie, S.4
  • 74
    • 60849128834 scopus 로고    scopus 로고
    • Large-scale analysis of thermostable, mammalian proteins provides insights into the intrinsically disordered proteome
    • Galea CA, High AA, Obenauer JC, et al. Large-scale analysis of thermostable, mammalian proteins provides insights into the intrinsically disordered proteome. J Proteome Res 2009; 8:211-226.
    • (2009) J Proteome Res , vol.8 , pp. 211-226
    • Galea, C.A.1    High, A.A.2    Obenauer, J.C.3
  • 75
    • 26844566629 scopus 로고    scopus 로고
    • Uncovering the unfoldome: Enriching cell extracts for unstructured proteins by acid treatment
    • Cortese MS, Baird JP, Uversky VN, Dunker AK. Uncovering the unfoldome: enriching cell extracts for unstructured proteins by acid treatment. J Proteome Res 2005; 4:1610-1618.
    • (2005) J Proteome Res , vol.4 , pp. 1610-1618
    • Cortese, M.S.1    Baird, J.P.2    Uversky, V.N.3    Dunker, A.K.4
  • 76
    • 33750097976 scopus 로고    scopus 로고
    • Proteomic studies of the intrinsically unstructured mammalian proteome
    • Galea CA, Pagala VR, Obenauer JC, et al. Proteomic studies of the intrinsically unstructured mammalian proteome. J Proteome Res 2006; 5:2839-2848.
    • (2006) J Proteome Res , vol.5 , pp. 2839-2848
    • Galea, C.A.1    Pagala, V.R.2    Obenauer, J.C.3
  • 77
    • 49849101215 scopus 로고    scopus 로고
    • Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities
    • Szollosi E, Bokor M, Bodor A, et al. Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. J Proteome Res 2008; 7:2291-2299.
    • (2008) J Proteome Res , vol.7 , pp. 2291-2299
    • Szollosi, E.1    Bokor, M.2    Bodor, A.3
  • 78
    • 57449088165 scopus 로고    scopus 로고
    • Proteomics studies confirm the presence of alternative protein isoforms on a large scale
    • Tress ML, Bodenmiller B, Aebersold R, Valencia A. Proteomics studies confirm the presence of alternative protein isoforms on a large scale. Genome Biol 2008; 9:R162.
    • (2008) Genome Biol , vol.9
    • Tress, M.L.1    Bodenmiller, B.2    Aebersold, R.3    Valencia, A.4
  • 79
    • 34247640113 scopus 로고    scopus 로고
    • Predicting protein disorder and induced folding: From theoretical principles to practical applications
    • Bourhis JM, Canard B, Longhi S. Predicting protein disorder and induced folding: from theoretical principles to practical applications. Curr Protein Pept Sci 2007; 8:135-149.
    • (2007) Curr Protein Pept Sci , vol.8 , pp. 135-149
    • Bourhis, J.M.1    Canard, B.2    Longhi, S.3
  • 81
    • 33748258328 scopus 로고    scopus 로고
    • A practical overview of protein disorder prediction methods
    • Ferron F, Longhi S, Canard B, Karlin D. A practical overview of protein disorder prediction methods. Proteins 2006; 65:1-14.
    • (2006) Proteins , vol.65 , pp. 1-14
    • Ferron, F.1    Longhi, S.2    Canard, B.3    Karlin, D.4
  • 83
    • 0242267501 scopus 로고    scopus 로고
    • Evaluation of disorder predictions in CASP5
    • Melamud E, Moult J. Evaluation of disorder predictions in CASP5. Proteins 2003; 53:561-565.
    • (2003) Proteins , vol.53 , pp. 561-565
    • Melamud, E.1    Moult, J.2
  • 84
    • 30344451365 scopus 로고    scopus 로고
    • Assessment of disorder predictions in CASP6
    • Jin Y, Dunbrack RL Jr. Assessment of disorder predictions in CASP6. Proteins 2005; 61:167-175.
    • (2005) Proteins , vol.61 , pp. 167-175
    • Jin, Y.1    Dunbrack Jr., R.L.2
  • 85
    • 36749081458 scopus 로고    scopus 로고
    • Assessment of disorder predictions in CASP7
    • Bordoli L, Kiefer F, Schwede T. Assessment of disorder predictions in CASP7. Proteins 2007; 69:129-136.
    • (2007) Proteins , vol.69 , pp. 129-136
    • Bordoli, L.1    Kiefer, F.2    Schwede, T.3
  • 86
    • 4143107222 scopus 로고    scopus 로고
    • Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers
    • Gunnasekaran K, Tsai CJ, Nussinov R. Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers. J Mol Biol 2004; 341:1327-1341.
    • (2004) J Mol Biol , vol.341 , pp. 1327-1341
    • Gunnasekaran, K.1    Tsai, C.J.2    Nussinov, R.3
  • 87
    • 36749037699 scopus 로고    scopus 로고
    • Mining alpha-helix-forming molecular recognition features with cross species sequence alignments
    • Cheng Y, Oldfield CJ, Meng J, et al. Mining alpha-helix-forming molecular recognition features with cross species sequence alignments. Biochemistry 2007; 46:13468-13477.
    • (2007) Biochemistry , vol.46 , pp. 13468-13477
    • Cheng, Y.1    Oldfield, C.J.2    Meng, J.3
  • 88
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • Oldfeld CJ, Cheng Y, Cortese MS, et al. Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 2005; 44:12454-12470.
    • (2005) Biochemistry , vol.44 , pp. 12454-12470
    • Oldfeld, C.J.1    Cheng, Y.2    Cortese, M.S.3
  • 89
    • 0000332920 scopus 로고    scopus 로고
    • Sequence data analysis for long disordered regions prediction in the calcineurin family
    • Romero P, Obradovic Z, Dunker AK. Sequence data analysis for long disordered regions prediction in the calcineurin family. Genome Inform 1997; 8:110-124.
    • (1997) Genome Inform , vol.8 , pp. 110-124
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 91
    • 6344277430 scopus 로고    scopus 로고
    • Reduced amino acid alphabet is suffcient to accurately recognize intrinsically disordered protein
    • Weathers EA, Paulaitis ME, Woolf TB, Hoh JH. Reduced amino acid alphabet is suffcient to accurately recognize intrinsically disordered protein. FEBS Lett 2004; 576:348-352.
    • (2004) FEBS Lett , vol.576 , pp. 348-352
    • Weathers, E.A.1    Paulaitis, M.E.2    Woolf, T.B.3    Hoh, J.H.4
  • 92
    • 0029909384 scopus 로고    scopus 로고
    • An iterative method for extracting energy-like quantities from protein structures
    • Thomas PD, Dill KA. An iterative method for extracting energy-like quantities from protein structures. Proc Natl Acad Sci USA 1996; 93:11628-11633.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11628-11633
    • Thomas, P.D.1    Dill, K.A.2
  • 94
    • 44449117551 scopus 로고    scopus 로고
    • Protein disorder prediction at multiple levels of sensitivity and specifcity
    • Hecker J, Yang JY, Cheng J. Protein disorder prediction at multiple levels of sensitivity and specifcity. BMC Genomics 2008; 9:S9.
    • (2008) BMC Genomics , vol.9
    • Hecker, J.1    Yang, J.Y.2    Cheng, J.3
  • 95
    • 0036558021 scopus 로고    scopus 로고
    • Viral RNA-polymerases - a predicted 2′-O-ribose methyltransferase domain shared by all Mononegavirales
    • Ferron F, Longhi S, Henrissat B, Canard B. Viral RNA-polymerases - a predicted 2′-O-ribose methyltransferase domain shared by all Mononegavirales. Trends Biochem Sci 2002; 27:222-224.
    • (2002) Trends Biochem Sci , vol.27 , pp. 222-224
    • Ferron, F.1    Longhi, S.2    Henrissat, B.3    Canard, B.4
  • 96
    • 0346752214 scopus 로고    scopus 로고
    • Structural disorder and modular organization in Paramyxovirinae N and P
    • Karlin D, Ferron F, Canard B, Longhi S. Structural disorder and modular organization in Paramyxovirinae N and P. J Gen Virol 2003; 84:3239-3252.
    • (2003) J Gen Virol , vol.84 , pp. 3239-3252
    • Karlin, D.1    Ferron, F.2    Canard, B.3    Longhi, S.4
  • 97
    • 14744282925 scopus 로고    scopus 로고
    • VaZyMolO: A tool to defne and classify modularity in viral proteins
    • Ferron F, Rancurel C, Longhi S, et al. VaZyMolO: a tool to defne and classify modularity in viral proteins. J Gen Virol 2005; 86:743-749.
    • (2005) J Gen Virol , vol.86 , pp. 743-749
    • Ferron, F.1    Rancurel, C.2    Longhi, S.3
  • 98
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997; 25:3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3
  • 99
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 1988; 16:10881-10890.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 100
    • 0030690133 scopus 로고    scopus 로고
    • Deciphering protein sequence information through hydrophobic cluster analysis (HCA): Current status and perspectives
    • Callebaut I, Labesse G, Durand P, et al. Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives. Cell Mol Life Sci 1997; 53:621-645.
    • (1997) Cell Mol Life Sci , vol.53 , pp. 621-645
    • Callebaut, I.1    Labesse, G.2    Durand, P.3
  • 101
    • 34548738213 scopus 로고    scopus 로고
    • POODLE-S: Web application for predicting protein disorder by using physicochemical features and reduced amino acid set of a position-specific scoring matrix
    • Shimizu K, Hirose S, Noguchi T. POODLE-S: web application for predicting protein disorder by using physicochemical features and reduced amino acid set of a position-specific scoring matrix. Bioinformatics 2007; 23:2337-2338.
    • (2007) Bioinformatics , vol.23 , pp. 2337-2338
    • Shimizu, K.1    Hirose, S.2    Noguchi, T.3
  • 102
    • 34548567232 scopus 로고    scopus 로고
    • POO-DLE-L: A two-level SVM prediction system for reliably predicting long disordered regions
    • Hirose S, Shimizu K, Kanai S, Kuroda Y, Noguchi T. POO-DLE-L: a two-level SVM prediction system for reliably predicting long disordered regions. Bioinformatics 2007; 23:2046-2053.
    • (2007) Bioinformatics , vol.23 , pp. 2046-2053
    • Hirose, S.1    Shimizu, K.2    Kanai, S.3    Kuroda, Y.4    Noguchi, T.5
  • 103
    • 34547458990 scopus 로고    scopus 로고
    • IUP: Intrinsically unstructured protein predictor - a software tool for analyzing polypeptide sequences. BioInformatics and BioEngineering
    • Oct
    • Yang MQ, Yang J Y. IUP: intrinsically unstructured protein predictor - a software tool for analyzing polypeptide sequences. BioInformatics and BioEngineering, 2006. BIBE 2006. Sixth IEEE Symposium on 16-18 Oct.:3-11.
    • (2006) BIBE 2006. Sixth IEEE Symposium on 16-18 , pp. 3-11
    • Yang, M.Q.1    Yang, J.Y.2
  • 104
    • 34548750953 scopus 로고    scopus 로고
    • Natively unstructured regions in proteins identifed from contact predictions
    • Schlessinger A, Punta M, Rost B. Natively unstructured regions in proteins identifed from contact predictions. Bioinfor-matics 2007; 23:2376-2384.
    • (2007) Bioinfor-matics , vol.23 , pp. 2376-2384
    • Schlessinger, A.1    Punta, M.2    Rost, B.3
  • 105
  • 106
    • 52149105815 scopus 로고    scopus 로고
    • Using bayesian multinomial classifer to predict where a given protein sequence is intrinsically disordered
    • Bulashevska A, Eils R. Using bayesian multinomial classifer to predict where a given protein sequence is intrinsically disordered. J Theor Biol 2008; 254:799-803.
    • (2008) J Theor Biol , vol.254 , pp. 799-803
    • Bulashevska, A.1    Eils, R.2
  • 107
    • 44349150513 scopus 로고    scopus 로고
    • OnD-CRF: Predicting order and disorder in proteins using conditional random fields
    • Wang L, Sauer UH. OnD-CRF: predicting order and disorder in proteins using conditional random fields. Bioinformatics 2008; 24:1401-1402.
    • (2008) Bioinformatics , vol.24 , pp. 1401-1402
    • Wang, L.1    Sauer, U.H.2
  • 108
    • 67349162535 scopus 로고    scopus 로고
    • CDF it all: Consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions
    • Xue B, Oldfield CJ, Dunker AK, Uversky VN. CDF it all: consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions. FEBS Lett 2009; 583:1469-1474.
    • (2009) FEBS Lett , vol.583 , pp. 1469-1474
    • Xue, B.1    Oldfield, C.J.2    Dunker, A.K.3    Uversky, V.N.4
  • 109
    • 44349192171 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins based on the meta approach
    • Ishida T, Kinoshita K. Prediction of disordered regions in proteins based on the meta approach. Bioinformatics 2008; 24:1344-1348.
    • (2008) Bioinformatics , vol.24 , pp. 1344-1348
    • Ishida, T.1    Kinoshita, K.2
  • 110
    • 84885949386 scopus 로고    scopus 로고
    • Improved disorder prediction by combination of orthogonal approaches
    • Schlessinger A, Punta M, Yachdav G, Kajan L, Rost B. Improved disorder prediction by combination of orthogonal approaches. PLoS ONE 2009; 4:e4433.
    • (2009) PLoS ONE , vol.4
    • Schlessinger, A.1    Punta, M.2    Yachdav, G.3    Kajan, L.4    Rost, B.5
  • 111
    • 49549111841 scopus 로고    scopus 로고
    • Intrinsic disorder prediction from the analysis of multiple protein fold recognition models
    • McGuffn LJ. Intrinsic disorder prediction from the analysis of multiple protein fold recognition models. Bioinformatics 2008; 24:1798-1804.
    • (2008) Bioinformatics , vol.24 , pp. 1798-1804
    • McGuffn, L.J.1
  • 112
    • 52249108097 scopus 로고    scopus 로고
    • MeDor: A metaserver for predicting protein disorder
    • Lieutaud P, Canard B, Longhi S. MeDor: a metaserver for predicting protein disorder. BMC Genomics 2008; 9:S25.
    • (2008) BMC Genomics , vol.9
    • Lieutaud, P.1    Canard, B.2    Longhi, S.3
  • 113
    • 0033562880 scopus 로고    scopus 로고
    • New methods for accurate prediction of protein secondary structure
    • Chandonia JM, Karplus M. New methods for accurate prediction of protein secondary structure. Proteins 1999; 35:293-306.
    • (1999) Proteins , vol.35 , pp. 293-306
    • Chandonia, J.M.1    Karplus, M.2
  • 114
    • 34548118802 scopus 로고    scopus 로고
    • StrBioLib: A Java library for development of custom computational structural biology applications
    • Chandonia JM. StrBioLib: a Java library for development of custom computational structural biology applications. Bioinformatics 2007; 23:2018-2020.
    • (2007) Bioinformatics , vol.23 , pp. 2018-2020
    • Chandonia, J.M.1
  • 115
    • 18744405418 scopus 로고    scopus 로고
    • Prediction of unfolded segments in a protein sequence based on amino acid composition
    • Coeytaux K, Poupon A. Prediction of unfolded segments in a protein sequence based on amino acid composition. Bioinformatics 2005; 21:1891-1900.
    • (2005) Bioinformatics , vol.21 , pp. 1891-1900
    • Coeytaux, K.1    Poupon, A.2
  • 116
    • 0242267500 scopus 로고    scopus 로고
    • Predicting intrinsic disorder from amino acid sequence
    • Obradovic Z, Peng K, Vucetic S, et al. Predicting intrinsic disorder from amino acid sequence. Proteins 2003; 53 Suppl 6:566-572.
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 566-572
    • Obradovic, Z.1    Peng, K.2    Vucetic, S.3
  • 117
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Kall L, Krogh A, Sonnhammer EL. A combined transmembrane topology and signal peptide prediction method. J Mol Biol 2004; 338:1027-1036.
    • (2004) J Mol Biol , vol.338 , pp. 1027-1036
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 120
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky VN, Oldfield CJ, Dunker AK. Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu Rev Biophys 2008; 37:215-246.
    • (2008) Annu Rev Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 122
    • 0041620131 scopus 로고    scopus 로고
    • NORSp: Predictions of long regions without regular secondary structure
    • Liu J, Rost B. NORSp: predictions of long regions without regular secondary structure. Nucleic Acids Res 2003; 31:3833-3835.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3833-3835
    • Liu, J.1    Rost, B.2
  • 123
    • 33746630984 scopus 로고    scopus 로고
    • Wiggle-predicting functionally fexible regions from primary sequence
    • Gu J, Gribskov M, Bourne PE. Wiggle-predicting functionally fexible regions from primary sequence. PLoS Comput Biol 2006; 2:e90.
    • (2006) PLoS Comput Biol , vol.2
    • Gu, J.1    Gribskov, M.2    Bourne, P.E.3
  • 124
    • 34447539760 scopus 로고    scopus 로고
    • Composition profler: A tool for discovery and visualization of amino acid composition differences
    • Vacic V, Uversky VN, Dunker AK, Lonardi S. Composition profler: a tool for discovery and visualization of amino acid composition differences. BMC Bioinformatics 2007; 8:211.
    • (2007) BMC Bioinformatics , vol.8 , pp. 211
    • Vacic, V.1    Uversky, V.N.2    Dunker, A.K.3    Lonardi, S.4
  • 125
    • 34547599318 scopus 로고    scopus 로고
    • Natively unstructured loops differ from other loops
    • Schlessinger A, Liu J, Rost B. Natively unstructured loops differ from other loops. PLoS Comput Biol 2007; 3:e140.
    • (2007) PLoS Comput Biol , vol.3
    • Schlessinger, A.1    Liu, J.2    Rost, B.3
  • 126
    • 52249124593 scopus 로고    scopus 로고
    • TOP-IDP-Scale: A new amino acid scale measuring propensity for intrinsic disorder
    • Campen A, Williams RM, Brown CJ, et al. TOP-IDP-Scale: a new amino acid scale measuring propensity for intrinsic disorder. Protein Pept Lett 2008; 15:956-963.
    • (2008) Protein Pept Lett , vol.15 , pp. 956-963
    • Campen, A.1    Williams, R.M.2    Brown, C.J.3
  • 127
    • 50949126750 scopus 로고    scopus 로고
    • DPROT: Prediction of disordered proteins using evolutionary information
    • Sethi D, Garg A, Raghava GP. DPROT: prediction of disordered proteins using evolutionary information. Amino Acids 2008; 35:599-605.
    • (2008) Amino Acids , vol.35 , pp. 599-605
    • Sethi, D.1    Garg, A.2    Raghava, G.P.3
  • 128
    • 47149116214 scopus 로고    scopus 로고
    • Identifcation of intrinsically unstructured proteins using hierarchical classifer
    • Yang J Y, Yang MQ. Identifcation of intrinsically unstructured proteins using hierarchical classifer. Int J Data Min Bioinform 2008; 2:121-133.
    • (2008) Int J Data Min Bioinform , vol.2 , pp. 121-133
    • Yang, J.Y.1    Yang, M.Q.2
  • 129
    • 60949104277 scopus 로고    scopus 로고
    • Predicting disordered regions in proteins using the profles of amino acid indices
    • Han P, Zhang X, Feng ZP. Predicting disordered regions in proteins using the profles of amino acid indices. BMC Bioinformatics 2009; 10:S42.
    • (2009) BMC Bioinformatics , vol.10
    • Han, P.1    Zhang, X.2    Feng, Z.P.3
  • 130
    • 60649095847 scopus 로고    scopus 로고
    • Large-scale prediction of long disordered regions in proteins using random forests
    • Han P, Zhang X, Norton RS, Feng ZP. Large-scale prediction of long disordered regions in proteins using random forests. BMC Bioinformatics 2009; 10:8.
    • (2009) BMC Bioinformatics , vol.10 , pp. 8
    • Han, P.1    Zhang, X.2    Norton, R.S.3    Feng, Z.P.4


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