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Volumn 82, Issue 4, 2014, Pages 587-595

BCL:: Fold-Protein topology determination from limited NMR restraints

Author keywords

NOE; Protein structure prediction; RDC; Sparse data; Topology prediction

Indexed keywords

ISOLEUCINE; LEUCINE; MEMBRANE PROTEIN; METHYL GROUP; PROTON; VALINE;

EID: 84895526306     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24427     Document Type: Article
Times cited : (21)

References (27)
  • 1
    • 16244381696 scopus 로고    scopus 로고
    • Protein structure estimation from minimal restraints using Rosetta
    • Rohl CA. Protein structure estimation from minimal restraints using Rosetta. Methods Enzymol 2005;394:244-260.
    • (2005) Methods Enzymol , vol.394 , pp. 244-260
    • Rohl, C.A.1
  • 3
    • 78650427063 scopus 로고    scopus 로고
    • CABS-NMR-de novo tool for rapid global fold determination from chemical shifts, residual dipolar couplings and sparse methyl-methyl NOEs
    • Latek D, Kolinski A. CABS-NMR-de novo tool for rapid global fold determination from chemical shifts, residual dipolar couplings and sparse methyl-methyl NOEs. J Comput Chem 2011;32:536-544.
    • (2011) J Comput Chem , vol.32 , pp. 536-544
    • Latek, D.1    Kolinski, A.2
  • 8
    • 84869205629 scopus 로고    scopus 로고
    • BCL::Fold-de novo prediction of complex and large protein topologies by assembly of secondary structure elements
    • Karakas M, Woetzel N, Staritzbichler R, Alexander N, Weiner BE, Meiler J. BCL::Fold-de novo prediction of complex and large protein topologies by assembly of secondary structure elements. PLoS One 2012;7:e49240.
    • (2012) PLoS One , vol.7
    • Karakas, M.1    Woetzel, N.2    Staritzbichler, R.3    Alexander, N.4    Weiner, B.E.5    Meiler, J.6
  • 9
    • 67649967739 scopus 로고    scopus 로고
    • EM-fold: de novo folding of alpha-helical proteins guided by intermediate-resolution electron microscopy density maps
    • Lindert S, Staritzbichler R, Wotzel N, Karakas M, Stewart PL, Meiler J. EM-fold: de novo folding of alpha-helical proteins guided by intermediate-resolution electron microscopy density maps. Structure 2009;17:990-1003.
    • (2009) Structure , vol.17 , pp. 990-1003
    • Lindert, S.1    Staritzbichler, R.2    Wotzel, N.3    Karakas, M.4    Stewart, P.L.5    Meiler, J.6
  • 10
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen Y, Delaglio F, Cornilescu G, Bax A. TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 2009;44:213-223.
    • (2009) J Biomol NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 11
    • 0006747152 scopus 로고
    • Star dictionary definition language-initial specification
    • Hall SR, Cook APF. Star dictionary definition language-initial specification. J Chem Inform Comput Sci 1995;35:819-825.
    • (1995) J Chem Inform Comput Sci , vol.35 , pp. 819-825
    • Hall, S.R.1    Cook, A.P.F.2
  • 14
    • 0029806697 scopus 로고    scopus 로고
    • Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy
    • Johnson PE, Joshi MD, Tomme P, Kilburn DG, McIntosh LP. Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy. Biochemistry 1996;35:14381-14394.
    • (1996) Biochemistry , vol.35 , pp. 14381-14394
    • Johnson, P.E.1    Joshi, M.D.2    Tomme, P.3    Kilburn, D.G.4    McIntosh, L.P.5
  • 15
    • 34547179849 scopus 로고    scopus 로고
    • Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology
    • Shen Y, Bax A. Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology. J Biomol NMR 2007;38:289-302.
    • (2007) J Biomol NMR , vol.38 , pp. 289-302
    • Shen, Y.1    Bax, A.2
  • 16
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • Cornilescu G, Marquardt JL, Ottiger M, Bax A. Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase. J Am Chem Soc 1998;120:6836-6837.
    • (1998) J Am Chem Soc , vol.120 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 17
    • 84869223129 scopus 로고    scopus 로고
    • BCL::Score-knowledge based energy potentials for ranking protein models represented by idealized secondary structure elements
    • Woetzel N, Karakas M, Staritzbichler R, Muller R, Weiner BE, Meiler J. BCL::Score-knowledge based energy potentials for ranking protein models represented by idealized secondary structure elements. PLoS One 2012;7:e49242.
    • (2012) PLoS One , vol.7
    • Woetzel, N.1    Karakas, M.2    Staritzbichler, R.3    Muller, R.4    Weiner, B.E.5    Meiler, J.6
  • 18
    • 0033145058 scopus 로고    scopus 로고
    • Order matrix analysis of residual dipolar couplings using singular value decomposition
    • Losonczi JA, Andrec M, Fischer MW, Prestegard JH. Order matrix analysis of residual dipolar couplings using singular value decomposition. J Magn Reson 1999;138:334-342.
    • (1999) J Magn Reson , vol.138 , pp. 334-342
    • Losonczi, J.A.1    Andrec, M.2    Fischer, M.W.3    Prestegard, J.H.4
  • 19
    • 84967789667 scopus 로고
    • Recent results in field of liquid crystals
    • 102
    • Saupe A. Recent results in field of liquid crystals. Angew Chem-Int Ed 1968;7:97-102.
    • (1968) Angew Chem-Int Ed , vol.7 , pp. 97
    • Saupe, A.1
  • 20
    • 0033811768 scopus 로고    scopus 로고
    • DipoCoup: a versatile program for 3D-structure homology comparison based on residual dipolar couplings and pseudocontact shifts
    • Meiler J, Peti W, Griesinger C. DipoCoup: a versatile program for 3D-structure homology comparison based on residual dipolar couplings and pseudocontact shifts. J Biomol NMR 2000;17:283-294.
    • (2000) J Biomol NMR , vol.17 , pp. 283-294
    • Meiler, J.1    Peti, W.2    Griesinger, C.3
  • 21
    • 23144438711 scopus 로고    scopus 로고
    • PISCES: recent improvements to a PDB sequence culling server
    • Wang G, Dunbrack RL, Jr. PISCES: recent improvements to a PDB sequence culling server. Nucleic Acids Res 2005;33:W94-W98.
    • (2005) Nucleic Acids Res , vol.33
    • Wang, G.1    Dunbrack Jr, R.L.2
  • 22
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word JM, Lovell SC, Richardson JS, Richardson DC. Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. J Mol Biol 1999;285:1735-1747.
    • J Mol Biol , vol.1999 , Issue.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 23
    • 84879844572 scopus 로고    scopus 로고
    • BCL::MP-fold: folding membrane proteins through assembly of transmembrane helices
    • Structure 2013;21:1107-1117
    • Weiner BE, Woetzel N, Karakas M, Alexander N, Meiler J. BCL::MP-fold: folding membrane proteins through assembly of transmembrane helices. Structure, Structure 2013;21:1107-1117.
    • Structure
    • Weiner, B.E.1    Woetzel, N.2    Karakas, M.3    Alexander, N.4    Meiler, J.5
  • 25
    • 0034977013 scopus 로고    scopus 로고
    • A normalized root-mean-square distance for comparing protein three-dimensional structures
    • Carugo O, Pongor S. A normalized root-mean-square distance for comparing protein three-dimensional structures. Protein Sci 2001;10:1470-1473.
    • (2001) Protein Sci , vol.10 , pp. 1470-1473
    • Carugo, O.1    Pongor, S.2
  • 27
    • 60149096311 scopus 로고    scopus 로고
    • Properties and identification of human protein drug targets
    • Bakheet TM, Doig AJ. Properties and identification of human protein drug targets. Bioinformatics 2009;25:451-457.
    • (2009) Bioinformatics , vol.25 , pp. 451-457
    • Bakheet, T.M.1    Doig, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.