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Volumn 20, Issue 11, 2011, Pages 1929-1934

High-resolution structure prediction of a circular permutation loop

Author keywords

Circular permutation; Computational protein design; Protein structure prediction; RosettaRemodel

Indexed keywords

ARTICLE; BINDING AFFINITY; CIRCULAR PERMUTATION LOOP; CRYSTAL STRUCTURE; GEL PERMEATION CHROMATOGRAPHY; MATHEMATICAL ANALYSIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE;

EID: 80052337644     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.725     Document Type: Article
Times cited : (5)

References (29)
  • 1
    • 0345306764 scopus 로고    scopus 로고
    • Design of a Novel Globular Protein Fold with Atomic-Level Accuracy
    • DOI 10.1126/science.1089427
    • Kuhlman B, Dantas G, Ireton GC, Varani G, Stoddard BL, Baker D (2003) Design of a novel globular protein fold with atomic-level accuracy. Science 302:1364-1368. (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
  • 2
    • 0032553587 scopus 로고    scopus 로고
    • High-resolution protein design with backbone freedom
    • Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS (1998) High-resolution protein design with backbone freedom. Science 282:1462-1467. (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
  • 4
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • DOI 10.1126/science.278.5335.82
    • Dahiyat BI, Mayo SL (1997) De novo protein design: fully automated sequence selection. Science 278:82-87. (Pubitemid 27446279)
    • (1997) Science , vol.278 , Issue.5335 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 6
    • 65249171530 scopus 로고    scopus 로고
    • Design of protein-interaction specificity gives selective bZIP-binding peptides
    • Grigoryan G, Reinke AW, Keating AE (2009) Design of protein-interaction specificity gives selective bZIP-binding peptides. Nature 458:859-864.
    • (2009) Nature , vol.458 , pp. 859-864
    • Grigoryan, G.1    Reinke, A.W.2    Keating, A.E.3
  • 9
    • 78650413957 scopus 로고    scopus 로고
    • Circular permutation: A different way to engineer enzyme structure and function
    • Yu Y, Lutz S (2011) Circular permutation: a different way to engineer enzyme structure and function. Trends Biotechnol 29:18-25.
    • (2011) Trends Biotechnol , vol.29 , pp. 18-25
    • Yu, Y.1    Lutz, S.2
  • 11
    • 34548861782 scopus 로고    scopus 로고
    • Protein-Protein Docking with Backbone Flexibility
    • DOI 10.1016/j.jmb.2007.07.050, PII S0022283607010030
    • Wang C, Bradley P, Baker D (2007) Protein-protein docking with backbone flexibility. J Mol Biol 373: 503-519. (Pubitemid 47445567)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.2 , pp. 503-519
    • Wang, C.1    Bradley, P.2    Baker, D.3
  • 12
    • 0037406075 scopus 로고    scopus 로고
    • Cyclic coordinate descent: A robotics algorithm for protein loop closure
    • DOI 10.1110/ps.0242703
    • Canutescu AA, Dunbrack RL, Jr (2003) Cyclic coordinate descent: a robotics algorithm for protein loop closure. Protein Sci 12:963-972. (Pubitemid 36505431)
    • (2003) Protein Science , vol.12 , Issue.5 , pp. 963-972
    • Canutescu, A.A.1    Dunbrack Jr., R.L.2
  • 14
    • 78149378424 scopus 로고    scopus 로고
    • Tying up the loose ends: Circular permutation decreases the proteolytic susceptibility of recombinant proteins
    • Whitehead TA, Bergeron LM, Clark DS (2009) Tying up the loose ends: circular permutation decreases the proteolytic susceptibility of recombinant proteins. Protein Eng Des Sel 22:607-613.
    • (2009) Protein Eng des Sel , vol.22 , pp. 607-613
    • Whitehead, T.A.1    Bergeron, L.M.2    Clark, D.S.3
  • 16
    • 25844525807 scopus 로고    scopus 로고
    • Improving the catalytic activity of Candida antarctica lipase B by circular permutation
    • DOI 10.1021/ja053932h
    • Qian Z, Lutz S (2005) Improving the catalytic activity of Candida antarctica lipase B by circular permutation. J Am Chem Soc 127:13466-13467. (Pubitemid 41401178)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.39 , pp. 13466-13467
    • Qian, Z.1    Lutz, S.2
  • 17
    • 0042847339 scopus 로고    scopus 로고
    • Circular permutation of 5-aminolevulinate synthase: Effect on folding, conformational stability, and structure
    • DOI 10.1074/jbc.M207011200
    • Cheltsov AV, Guida WC, Ferreira GC (2003) Circular permutation of 5-aminolevulinate synthase: effect on folding, conformational stability, and structure. J Biol Chem 278:27945-27955. (Pubitemid 36899989)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 27945-27955
    • Cheltsov, A.V.1    Guida, W.C.2    Ferreira, G.C.3
  • 20
    • 50649095790 scopus 로고    scopus 로고
    • Macromolecular modeling with rosetta
    • Das R, Baker D (2008) Macromolecular modeling with rosetta. Ann Rev Biochem 77:363-382.
    • (2008) Ann Rev Biochem , vol.77 , pp. 363-382
    • Das, R.1    Baker, D.2
  • 22
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath JW (1999) The finer things in X-ray diffraction data collection. Acta Cryst D55:1718-1725.
    • (1999) Acta Cryst , vol.D55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 27
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.