메뉴 건너뛰기




Volumn 523, Issue , 2013, Pages 213-235

Evolution-based design of proteins

Author keywords

Evolution; Folding; Protein design; SCA; Sector

Indexed keywords

SERINE PROTEINASE; TRYPTOPHAN;

EID: 84874029754     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394292-0.00010-2     Document Type: Chapter
Times cited : (39)

References (27)
  • 2
    • 0025363984 scopus 로고
    • Deciphering the message in protein sequences: Tolerance to amino acid substitutions
    • J.U. Bowie, J.F. Reidhaar-Olson, W.A. Lim, and R.T. Sauer Deciphering the message in protein sequences: Tolerance to amino acid substitutions Science 247 1990 1306 1310
    • (1990) Science , vol.247 , pp. 1306-1310
    • Bowie, J.U.1    Reidhaar-Olson, J.F.2    Lim, W.A.3    Sauer, R.T.4
  • 3
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • DOI 10.1126/science.278.5335.82
    • B.I. Dahiyat, and S.L. Mayo De novo protein design: Fully automated sequence selection Science 278 1997 82 87 (Pubitemid 27446279)
    • (1997) Science , vol.278 , Issue.5335 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 4
    • 0041387567 scopus 로고    scopus 로고
    • A large scale test of computational protein design: Folding and stability of nine completely redesigned globular proteins
    • DOI 10.1016/S0022-2836(03)00888-X
    • G. Dantas, B. Kuhlman, D. Callender, M. Wong, and D. Baker A large scale test of computational protein design: Folding and stability of nine completely redesigned globular proteins Journal of Molecular Biology 332 2003 449 460 (Pubitemid 37013512)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.2 , pp. 449-460
    • Dantas, G.1    Kuhlman, B.2    Callender, D.3    Wong, M.4    Baker, D.5
  • 6
    • 58149229162 scopus 로고    scopus 로고
    • An in vitro microfluidic approach to generating protein-interaction networks
    • D. Gerber, S.J. Maerkl, and S.R. Quake An in vitro microfluidic approach to generating protein-interaction networks Nature Methods 6 2009 71 74
    • (2009) Nature Methods , vol.6 , pp. 71-74
    • Gerber, D.1    Maerkl, S.J.2    Quake, S.R.3
  • 7
    • 68749107059 scopus 로고    scopus 로고
    • Protein sectors: Evolutionary units of three-dimensional structure
    • N. Halabi, O. Rivoire, S. Leibler, and R. Ranganathan Protein sectors: Evolutionary units of three-dimensional structure Cell 138 2009 774 786
    • (2009) Cell , vol.138 , pp. 774-786
    • Halabi, N.1    Rivoire, O.2    Leibler, S.3    Ranganathan, R.4
  • 8
    • 0032553587 scopus 로고    scopus 로고
    • High-resolution protein design with backbone freedom
    • P.B. Harbury, J.J. Plecs, B. Tidor, T. Alber, and P.S. Kim High-resolution protein design with backbone freedom Science 282 1998 1462 1467 (Pubitemid 28538602)
    • (1998) Science , vol.282 , Issue.5393 , pp. 1462-1467
    • Harbury, P.B.1    Plecs, J.J.2    Tidor, B.3    Alber, T.4    Kim, P.S.5
  • 10
    • 79952474660 scopus 로고    scopus 로고
    • A miniaturized technique for assessing protein thermodynamics and function using fast determination of quantitative cysteine reactivity
    • D.G. Isom, P.R. Marguet, T.G. Oas, and H.W. Hellinga A miniaturized technique for assessing protein thermodynamics and function using fast determination of quantitative cysteine reactivity Proteins 79 2011 1034 1047
    • (2011) Proteins , vol.79 , pp. 1034-1047
    • Isom, D.G.1    Marguet, P.R.2    Oas, T.G.3    Hellinga, H.W.4
  • 12
    • 78650021707 scopus 로고    scopus 로고
    • Scalable gene synthesis by selective amplification of DNA pools from high-fidelity microchips
    • S. Kosuri, N. Eroshenko, E.M. Leproust, M. Super, J. Way, and J.B. Li Scalable gene synthesis by selective amplification of DNA pools from high-fidelity microchips Nature Biotechnology 28 2010 1295 1299
    • (2010) Nature Biotechnology , vol.28 , pp. 1295-1299
    • Kosuri, S.1    Eroshenko, N.2    Leproust, E.M.3    Super, M.4    Way, J.5    Li, J.B.6
  • 13
    • 0345306764 scopus 로고    scopus 로고
    • Design of a Novel Globular Protein Fold with Atomic-Level Accuracy
    • DOI 10.1126/science.1089427
    • B. Kuhlman, G. Dantas, G.C. Ireton, G. Varani, B.L. Stoddard, and D. Baker Design of a novel globular protein fold with atomic-level accuracy Science 302 2003 1364 1368 (Pubitemid 37452172)
    • (2003) Science , vol.302 , Issue.5649 , pp. 1364-1368
    • Kuhlman, B.1    Dantas, G.2    Ireton, G.C.3    Varani, G.4    Stoddard, B.L.5    Baker, D.6
  • 15
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • DOI 10.1126/science.286.5438.295
    • S.W. Lockless, and R. Ranganathan Evolutionarily conserved pathways of energetic connectivity in protein families Science 286 1999 295 299 (Pubitemid 29484693)
    • (1999) Science , vol.286 , Issue.5438 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 18
    • 0035122917 scopus 로고    scopus 로고
    • Predicting the emergence of antibiotic resistance by directed evolution and structural analysis
    • DOI 10.1038/84981
    • M.C. Orencia, J.S. Yoon, J.E. Ness, W.P.C. Stemmer, and R.C. Stevens Predicting the emergence of antibiotic resistance by directed evolution and structural analysis Nature Structural and Molecular Biology 8 2001 238 242 (Pubitemid 32180050)
    • (2001) Nature Structural Biology , vol.8 , Issue.3 , pp. 238-242
    • Orencia, M.C.1    Yoon, J.S.2    Ness, J.E.3    Stemmer, W.P.C.4    Stevens, R.C.5
  • 19
    • 0025370163 scopus 로고
    • Functionally acceptable substitutions in two α-helical regions of repressor
    • DOI 10.1002/prot.340070403
    • J.F. Reidhaar-Olson, and R.T. Sauer Functionally acceptable substitutions in two alpha-helical regions of lambda repressor Proteins 7 1990 306 316 (Pubitemid 20218368)
    • (1990) Proteins: Structure, Function and Genetics , vol.7 , Issue.4 , pp. 306-316
    • Reidhaar-Olson, J.F.1    Sauer, R.T.2
  • 20
    • 84455167671 scopus 로고    scopus 로고
    • Hot spots for allosteric regulation on protein surfaces
    • K.A. Reynolds, R.N. McLaughlin, and R. Ranganathan Hot spots for allosteric regulation on protein surfaces Cell 147 2011 1564 1575
    • (2011) Cell , vol.147 , pp. 1564-1575
    • Reynolds, K.A.1    McLaughlin, R.N.2    Ranganathan, R.3
  • 21
    • 25644442464 scopus 로고    scopus 로고
    • Natural-like function in artificial WW domains
    • DOI 10.1038/nature03990, PII N03990
    • W.P. Russ, D.M. Lowery, P. Mishra, M.B. Yaffe, and R. Ranganathan Natural-like function in artificial WW domains Nature 437 2005 579 583 (Pubitemid 41613558)
    • (2005) Nature , vol.437 , Issue.7058 , pp. 579-583
    • Russ, W.P.1    Lowery, D.M.2    Mishra, P.3    Yaffe, M.B.4    Ranganathan, R.5
  • 22
    • 1642304065 scopus 로고    scopus 로고
    • Structural determinants of allosteric ligand activation in RXR heterodimers
    • DOI 10.1016/S0092-8674(04)00119-9, PII S0092867404001199
    • A.I. Shulman, C. Larson, D.J. Mangelsdorf, and R. Ranganathan Structural determinants of allosteric ligand activation in RXR heterodimers Cell 116 2004 417 429 (Pubitemid 38366318)
    • (2004) Cell , vol.116 , Issue.3 , pp. 417-429
    • Shulman, A.I.1    Larson, C.2    Mangelsdorf, D.J.3    Ranganathan, R.4
  • 24
    • 25644452032 scopus 로고    scopus 로고
    • Evolutionary information for specifying a protein fold
    • DOI 10.1038/nature03991, PII N03991
    • M. Socolich, S.W. Lockless, W.P. Russ, H. Lee, K.H. Gardner, and R. Ranganathan Evolutionary information for specifying a protein fold Nature 437 2005 512 518 (Pubitemid 41613543)
    • (2005) Nature , vol.437 , Issue.7058 , pp. 512-518
    • Socolich, M.1    Lockless, S.W.2    Russ, W.P.3    Lee, H.4    Gardner, K.H.5    Ranganathan, R.6
  • 25
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • DOI 10.1038/nsb881
    • G.M. Suel, S.W. Lockless, M.A. Wall, and R. Ranganathan Evolutionarily conserved networks of residues mediate allosteric communication in proteins Nature Structural Biology 10 2003 59 69 (Pubitemid 36034178)
    • (2003) Nature Structural Biology , vol.10 , Issue.1 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 26
    • 0035903602 scopus 로고    scopus 로고
    • Investigating and engineering enzymes by genetic selection
    • DOI 10.1002/1521-3773(20010917)40:18<3310::AID-ANIE3310>3.0.CO;2-P
    • S.V. Taylor, P. Kast, and D. Hilvert Investigating and engineering enzymes by genetic selection Angewandte Chemie (International Ed. in English) 40 2001 3310 3335 (Pubitemid 32916593)
    • (2001) Angewandte Chemie - International Edition , vol.40 , Issue.18 , pp. 3310-3335
    • Taylor, S.V.1    Kast, P.2    Hilvert, D.3
  • 27
    • 33645666942 scopus 로고    scopus 로고
    • Darwinian evolution can follow only very few mutational paths to fitter proteins
    • D.M. Weinreich, N.F. Delaney, M.A. Depristo, and D.L. Hartl Darwinian evolution can follow only very few mutational paths to fitter proteins Science 312 2006 111 114
    • (2006) Science , vol.312 , pp. 111-114
    • Weinreich, D.M.1    Delaney, N.F.2    Depristo, M.A.3    Hartl, D.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.