메뉴 건너뛰기




Volumn 3, Issue 7, 2007, Pages 1335-1346

Natively unstructured loops differ from other loops

Author keywords

[No Author keywords available]

Indexed keywords

FORECASTING;

EID: 34547599318     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.0030140     Document Type: Article
Times cited : (86)

References (85)
  • 3
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson HJ, Wright PE (2002) Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 12: 54-60.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 4
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter M, Simon I, Friedrich P, Tompa P (2004) Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J Mol Biol 338: 1015-1026.
    • (2004) J Mol Biol , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 5
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6: 197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 6
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker AK, Cortese MS, Romero P, Iakoucheva LM, Uversky VN (2005) Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J 272: 5129-5148.
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 7
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27: 527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 8
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity-linking function and disorder
    • Dunker AK, Obradovic Z (2001) The protein trinity-linking function and disorder. Nat Biotechnol 19: 805-806.
    • (2001) Nat Biotechnol , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 9
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson HJ, Wright PE (2004) Unfolded proteins and protein folding studied by NMR. Chem Rev 104: 3607-3622.
    • (2004) Chem Rev , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 12
  • 13
    • 28444480251 scopus 로고    scopus 로고
    • Comparisons of NMR spectral quality and success in crystallization demonstrate that NMR and X-ray crystallography are complementary methods for small protein structure determination
    • Snyder DA, Chen Y, Denissova NG, Acton T, Aramini JM, et al. (2005) Comparisons of NMR spectral quality and success in crystallization demonstrate that NMR and X-ray crystallography are complementary methods for small protein structure determination. J Am Chem Soc 127: 16505-16511.
    • (2005) J Am Chem Soc , vol.127 , pp. 16505-16511
    • Snyder, D.A.1    Chen, Y.2    Denissova, N.G.3    Acton, T.4    Aramini, J.M.5
  • 14
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41: 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 15
    • 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, Rydberg EH, Man O, et al. (2005) FoldIndex: A simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 21: 3435-3438.
    • (2005) Bioinformatics , vol.21 , pp. 3435-3438
    • Prilusky, J.1    Felder, C.E.2    Zeev-Ben-Mordehai, T.3    Rydberg, E.H.4    Man, O.5
  • 16
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • Linding R, Russell RB, Neduva V, Gibson TJ (2003) GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res 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
  • 17
    • 10844222539 scopus 로고    scopus 로고
    • Sequence patterns associated with disordered regions in proteins
    • Lise S, Jones DT (2005) Sequence patterns associated with disordered regions in proteins. Proteins 58: 144-150.
    • (2005) Proteins , vol.58 , pp. 144-150
    • Lise, S.1    Jones, D.T.2
  • 18
    • 0035451226 scopus 로고    scopus 로고
    • A conserved helix-unfolding motif in the naturally unfolded proteins
    • Zetina CR (2001) A conserved helix-unfolding motif in the naturally unfolded proteins. Proteins 44: 479-483.
    • (2001) Proteins , vol.44 , pp. 479-483
    • Zetina, C.R.1
  • 20
    • 0242458482 scopus 로고    scopus 로고
    • Protein disorder prediction: Implications for structural proteomics
    • Linding R, Jensen LJ, Diella F, Bork P, Gibson TJ, et al. (2003) Protein disorder prediction: Implications for structural proteomics. Structure 11: 1453-1459.
    • (2003) Structure , vol.11 , pp. 1453-1459
    • Linding, R.1    Jensen, L.J.2    Diella, F.3    Bork, P.4    Gibson, T.J.5
  • 21
    • 0242362157 scopus 로고    scopus 로고
    • Prediction of disordered regions in proteins from position specific score matrices
    • Jones DT, Ward JJ (2003) Prediction of disordered regions in proteins from position specific score matrices. Proteins 53: 573-578.
    • (2003) Proteins , vol.53 , pp. 573-578
    • Jones, D.T.1    Ward, J.J.2
  • 22
    • 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 (2005) RONN: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 21: 3369-3376.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 23
    • 27944488680 scopus 로고    scopus 로고
    • Accurate prediction of protein disordered regions by mining protein structure data
    • Maimon O, Rorkach L, editors, New York: Springer. pp
    • Cheng J, Sweredoski MJ, Baldi P (2005) Accurate prediction of protein disordered regions by mining protein structure data. In: Maimon O, Rorkach L, editors. Data mining and knowledge discovery. New York: Springer. pp. 213-222.
    • (2005) Data mining and knowledge discovery , pp. 213-222
    • Cheng, J.1    Sweredoski, M.J.2    Baldi, P.3
  • 24
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337: 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 25
    • 0242267501 scopus 로고    scopus 로고
    • Evaluation of disorder predictions in CASP5
    • Melamud E, Moult J (2003) Evaluation of disorder predictions in CASP5. Proteins 53 (Supplement 6): 561-565.
    • (2003) Proteins , vol.53 , Issue.SUPPL.EMENT 6 , pp. 561-565
    • Melamud, E.1    Moult, J.2
  • 26
    • 30344451365 scopus 로고    scopus 로고
    • Assessment of disorder predictions in CASP6
    • Jin Y, Dunbrack RL Jr (2005) Assessment of disorder predictions in CASP6. Proteins 61 (Supplement 7): 167-175.
    • (2005) Proteins , vol.61 , Issue.SUPPL.EMENT 7 , pp. 167-175
    • Jin, Y.1    Dunbrack Jr, R.L.2
  • 27
    • 0036968309 scopus 로고    scopus 로고
    • Loopy proteins appear conserved in evolution
    • Liu J, Tan H, Rost B (2002) Loopy proteins appear conserved in evolution. J Mol Biol 322: 53-64.
    • (2002) J Mol Biol , vol.322 , pp. 53-64
    • Liu, J.1    Tan, H.2    Rost, B.3
  • 28
    • 33746630984 scopus 로고    scopus 로고
    • Gu J, Gribskov M, Bourne PE (2006) Wiggle-predicting functionally flexible regions from primary sequence. PLoS Comput Biol 2: e90.
    • Gu J, Gribskov M, Bourne PE (2006) Wiggle-predicting functionally flexible regions from primary sequence. PLoS Comput Biol 2: e90.
  • 29
    • 0041620131 scopus 로고    scopus 로고
    • NORSp: Predictions of long regions without regular secondary structure
    • Liu J, Rost B (2003) NORSp: Predictions of long regions without regular secondary structure. Nucleic Acids Res 31: 3833-3835.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3833-3835
    • Liu, J.1    Rost, B.2
  • 30
    • 16244363308 scopus 로고    scopus 로고
    • How to use protein 1D structure predicted by PROFphd
    • Walker JE, editor, Totowa New Jersey, Humana. pp
    • Rost B (2005) How to use protein 1D structure predicted by PROFphd. In: Walker JE, editor. The proteomics protocols handbook. Totowa (New Jersey): Humana. pp. 875-901.
    • (2005) The proteomics protocols handbook , pp. 875-901
    • Rost, B.1
  • 31
    • 0035782925 scopus 로고    scopus 로고
    • Protein secondary structure prediction continues to rise
    • Rost B (2001) Protein secondary structure prediction continues to rise. J Struct Biol 134: 204-218.
    • (2001) J Struct Biol , vol.134 , pp. 204-218
    • Rost, B.1
  • 32
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile based neural networks
    • Rost B (1996) PHD: Predicting one-dimensional protein structure by profile based neural networks. Methods Enzymol 266: 525-539.
    • (1996) Methods Enzymol , vol.266 , pp. 525-539
    • Rost, B.1
  • 33
    • 0032521218 scopus 로고    scopus 로고
    • Marrying structure and genomics
    • Rost B (1998) Marrying structure and genomics. Structure 6: 259-263.
    • (1998) Structure , vol.6 , pp. 259-263
    • Rost, B.1
  • 34
    • 0032921818 scopus 로고    scopus 로고
    • Structural genomics: Keystone for a human proteome project
    • Montelione GT, Anderson S (1999) Structural genomics: Keystone for a human proteome project. Nat Struct Biol 6: 11-12.
    • (1999) Nat Struct Biol , vol.6 , pp. 11-12
    • Montelione, G.T.1    Anderson, S.2
  • 35
    • 3042726394 scopus 로고    scopus 로고
    • Automatic target selection for structural genomics on eukaryotes
    • Liu J, Hegyi H, Acton TB, Montelione GT, Rost B (2004) Automatic target selection for structural genomics on eukaryotes. Proteins 56: 188-200.
    • (2004) Proteins , vol.56 , pp. 188-200
    • Liu, J.1    Hegyi, H.2    Acton, T.B.3    Montelione, G.T.4    Rost, B.5
  • 36
    • 3042728092 scopus 로고    scopus 로고
    • The protein target list of the Northeast Structural Genomics Consortium
    • Wunderlich Z, Acton TB, Liu J, Kornhaber G, Everett J, et al. (2004) The protein target list of the Northeast Structural Genomics Consortium. Proteins 56: 181-187.
    • (2004) Proteins , vol.56 , pp. 181-187
    • Wunderlich, Z.1    Acton, T.B.2    Liu, J.3    Kornhaber, G.4    Everett, J.5
  • 37
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 38
    • 30044445169 scopus 로고    scopus 로고
    • Solution structure of the human immunodeficiency virus type 1 p6 protein
    • Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, et al. (2005) Solution structure of the human immunodeficiency virus type 1 p6 protein. J Biol Chem 280: 42515-42527.
    • (2005) J Biol Chem , vol.280 , pp. 42515-42527
    • Fossen, T.1    Wray, V.2    Bruns, K.3    Rachmat, J.4    Henklein, P.5
  • 41
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I (2005) The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 347: 827-839.
    • (2005) J Mol Biol , vol.347 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 43
    • 33746952996 scopus 로고    scopus 로고
    • Protein disorder prediction by condensed PSSM considering propensity for order or disorder
    • Su CT, Chen CY, Ou YY (2006) Protein disorder prediction by condensed PSSM considering propensity for order or disorder. BMC Bioinformatics 7: 319.
    • (2006) BMC Bioinformatics , vol.7 , pp. 319
    • Su, C.T.1    Chen, C.Y.2    Ou, Y.Y.3
  • 45
    • 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 (2005) IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21: 3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 47
    • 0038268061 scopus 로고    scopus 로고
    • SPINE 2: A system for collaborative structural proteomics within a federated database framework
    • Goh CS, Lan N, Echols N, Douglas SM, Milburn D, et al. (2003) SPINE 2: A system for collaborative structural proteomics within a federated database framework. Nucleic Acids Res 31: 2833-2838.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2833-2838
    • Goh, C.S.1    Lan, N.2    Echols, N.3    Douglas, S.M.4    Milburn, D.5
  • 49
    • 0034613297 scopus 로고    scopus 로고
    • Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70
    • Booth V, Koth CM, Edwards AM, Arrowsmith CH (2000) Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70. J Biol Chem 275: 31266-31268.
    • (2000) J Biol Chem , vol.275 , pp. 31266-31268
    • Booth, V.1    Koth, C.M.2    Edwards, A.M.3    Arrowsmith, C.H.4
  • 50
    • 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 CD, Blanch EW, Holt C, Jakes R, Goedert M, et al. (2002) 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 269: 148-156.
    • (2002) Eur J Biochem , vol.269 , pp. 148-156
    • Syme, C.D.1    Blanch, E.W.2    Holt, C.3    Jakes, R.4    Goedert, M.5
  • 51
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT (2000) The PSIPRED protein structure prediction server. Bioinformatics 16: 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 53
    • 3042810008 scopus 로고    scopus 로고
    • Sequence-based prediction of protein domains
    • Liu J, Rost B (2004) Sequence-based prediction of protein domains. Nucleic Acids Res 32: 3522-3530.
    • (2004) Nucleic Acids Res , vol.32 , pp. 3522-3530
    • Liu, J.1    Rost, B.2
  • 54
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A, et al. (1998) A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391: 43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5
  • 55
    • 0035932969 scopus 로고    scopus 로고
    • Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45
    • Zhou P, Lugovskoy AA, McCarty JS, Li P, Wagner G (2001) Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. Proc Natl Acad Sci U S A 98: 6051-6055.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6051-6055
    • Zhou, P.1    Lugovskoy, A.A.2    McCarty, J.S.3    Li, P.4    Wagner, G.5
  • 56
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky VN, Oldfield CJ, Dunker AK (2005) Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18: 343-384.
    • (2005) J Mol Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 57
    • 33748074139 scopus 로고    scopus 로고
    • Haynes C, Oldfield CJ, Ji F, Klitgord N, Cusick ME, et al. (2006) Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes. PLoS Comput Biol 2: e100.
    • Haynes C, Oldfield CJ, Ji F, Klitgord N, Cusick ME, et al. (2006) Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes. PLoS Comput Biol 2: e100.
  • 58
    • 33745686603 scopus 로고    scopus 로고
    • What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?
    • Ekman D, Light S, Bjorklund AK, Elofsson A (2006) What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae? Genome Biol 7: R45.
    • (2006) Genome Biol , vol.7
    • Ekman, D.1    Light, S.2    Bjorklund, A.K.3    Elofsson, A.4
  • 59
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • Patil A, Nakamura H (2006) Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks. FEBS Lett 580: 2041-2045.
    • (2006) FEBS Lett , vol.580 , pp. 2041-2045
    • Patil, A.1    Nakamura, H.2
  • 60
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P (2005) The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 579: 3346-3354.
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 61
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink AL (2005) Natively unfolded proteins. Curr Opin Struct Biol 15: 35-41.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 63
    • 33744814686 scopus 로고    scopus 로고
    • Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms
    • Romero PR, Zaidi S, Fang YY, Uversky VN, Radivojac P, et al. (2006) Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms. Proc Natl Acad Sci U S A 103: 8390-8395.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8390-8395
    • Romero, P.R.1    Zaidi, S.2    Fang, Y.Y.3    Uversky, V.N.4    Radivojac, P.5
  • 66
    • 9144264169 scopus 로고    scopus 로고
    • A map of the interactome network of the metazoan C. elegans
    • Li S, Armstrong CM, Bertin N, Ge H, Milstein S, et al. (2004) A map of the interactome network of the metazoan C. elegans. Science 303: 540-543.
    • (2004) Science , vol.303 , pp. 540-543
    • Li, S.1    Armstrong, C.M.2    Bertin, N.3    Ge, H.4    Milstein, S.5
  • 68
    • 0031787022 scopus 로고    scopus 로고
    • 100,000 protein structures for the biologist
    • Sali A (1998) 100,000 protein structures for the biologist. Nat Struct Biol 5: 1029-1032.
    • (1998) Nat Struct Biol , vol.5 , pp. 1029-1032
    • Sali, A.1
  • 69
    • 0344109574 scopus 로고    scopus 로고
    • Structural genomics taking shape
    • Gaasterland T (1998) Structural genomics taking shape. Trends Genet 14: 135.
    • (1998) Trends Genet , vol.14 , pp. 135
    • Gaasterland, T.1
  • 70
    • 12344271154 scopus 로고    scopus 로고
    • Survey of current protein family databases and their application in comparative, structural and functional genomics
    • Redfern O, Grant A, Maibaum M, Orengo C (2005) Survey of current protein family databases and their application in comparative, structural and functional genomics. J Chromatogr B Analyt Technol Biomed Life Sci 815: 97-107.
    • (2005) J Chromatogr B Analyt Technol Biomed Life Sci , vol.815 , pp. 97-107
    • Redfern, O.1    Grant, A.2    Maibaum, M.3    Orengo, C.4
  • 71
    • 2442499624 scopus 로고    scopus 로고
    • CHOP proteins into structural domain-like fragments
    • Liu J, Rost B (2004) CHOP proteins into structural domain-like fragments. Proteins 55: 678-688.
    • (2004) Proteins , vol.55 , pp. 678-688
    • Liu, J.1    Rost, B.2
  • 72
    • 3242891265 scopus 로고    scopus 로고
    • CHOP: Parsing proteins into structural domains
    • Liu J, Rost B (2004) CHOP: Parsing proteins into structural domains. Nucleic Acids Res 32: W569-W571.
    • (2004) Nucleic Acids Res , vol.32
    • Liu, J.1    Rost, B.2
  • 73
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost B (1994) Conservation and prediction of solvent accessibility in protein families. Proteins 20: 216-226.
    • (1994) Proteins , vol.20 , pp. 216-226
    • Rost, B.1
  • 75
    • 0036139410 scopus 로고    scopus 로고
    • EVA: Continuous automatic evaluation of protein structure prediction servers
    • Eyrich V, Martí-Renom MA, Przybylski D, Fiser A, Pazos F, et al. (2001) EVA: Continuous automatic evaluation of protein structure prediction servers. Bioinformatics 17: 1242-1243.
    • (2001) Bioinformatics , vol.17 , pp. 1242-1243
    • Eyrich, V.1    Martí-Renom, M.A.2    Przybylski, D.3    Fiser, A.4    Pazos, F.5
  • 76
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost B (1999) Twilight zone of protein sequence alignments. Protein Eng 12: 85-94.
    • (1999) Protein Eng , vol.12 , pp. 85-94
    • Rost, B.1
  • 77
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • Sander C, Schneider R (1991) Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins 9: 56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 78
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaeffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res 25: 3389-33402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-33402
    • Altschul, S.F.1    Madden, T.L.2    Schaeffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 79
    • 0036467068 scopus 로고    scopus 로고
    • Alignments grow, secondary structure prediction improves
    • Przybylski D, Rost B (2002) Alignments grow, secondary structure prediction improves. Proteins 46: 195-205.
    • (2002) Proteins , vol.46 , pp. 195-205
    • Przybylski, D.1    Rost, B.2
  • 80
    • 16244398103 scopus 로고    scopus 로고
    • Mimicking cellular sorting improves prediction of subcellular localization
    • Nair R, Rost B (2005) Mimicking cellular sorting improves prediction of subcellular localization. J Mol Biol 348: 85-100.
    • (2005) J Mol Biol , vol.348 , pp. 85-100
    • Nair, R.1    Rost, B.2
  • 81
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost B, Sander C (1993) Prediction of protein secondary structure at better than 70% accuracy. J Mol Biol 232: 584-599.
    • (1993) J Mol Biol , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 82
    • 24344503079 scopus 로고    scopus 로고
    • Protein flexibility and rigidity predicted from sequence
    • Schlessinger A, Rost B (2005) Protein flexibility and rigidity predicted from sequence. Proteins 61: 115-126.
    • (2005) Proteins , vol.61 , pp. 115-126
    • Schlessinger, A.1    Rost, B.2
  • 83
    • 0038356582 scopus 로고    scopus 로고
    • Predict protein-protein interaction sites from local sequence information
    • Ofran Y, Rost B (2003) Predict protein-protein interaction sites from local sequence information. FEBS Lett 544: 236-239.
    • (2003) FEBS Lett , vol.544 , pp. 236-239
    • Ofran, Y.1    Rost, B.2
  • 84
    • 33645288849 scopus 로고    scopus 로고
    • PROFbval: Predict flexible and rigid residues in proteins
    • Schlessinger A, Yachdav G, Rost B (2006) PROFbval: Predict flexible and rigid residues in proteins. Bioinformatics 22: 891-893.
    • (2006) Bioinformatics , vol.22 , pp. 891-893
    • Schlessinger, A.1    Yachdav, G.2    Rost, B.3
  • 85
    • 10744220076 scopus 로고    scopus 로고
    • Using multiple structure alignments, fast model building, and energetic analysis in fold recognition and homology modeling
    • Petrey D, Xiang Z, Tang CL, Xie L, Gimpelev M, et al. (2003) Using multiple structure alignments, fast model building, and energetic analysis in fold recognition and homology modeling. Proteins 53 (Supplement 6): 430-435.
    • (2003) Proteins , vol.53 , Issue.SUPPL.EMENT 6 , pp. 430-435
    • Petrey, D.1    Xiang, Z.2    Tang, C.L.3    Xie, L.4    Gimpelev, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.