Found 19 results
Author Title [ Type(Desc)] Year
Book Chapter
[Nerli2019] Nerli S, Sgourakis NG.  2019.  CS-Rosetta. Biological NMR Part A, Methods in Enzymology. 614
Journal Article
[Raman2010b] Raman S, Huang YJ, Mao B, Rossi P, Aramini JM, Liu G, Montelione GT, Baker D.  2010.  Accurate Automated Protein NMR Structure Determination Using Unassigned NOESY Data. J. Am. Chem. Soc.. 132(1):202-207.
[Thompson2012] Thompson J, Sgourakis NG, Liu G, Rossi P, Tang Y, Mills JL, Szyperski T, Montelione GT, Baker D.  2012.  Accurate protein structure modeling using sparse NMR data and homologous structure information. Proceedings of the National Academy of Sciences. 109(25)
[Evangelidis2018] Evangelidis T, Nerli S, Nováček J, Brereton AE, P. Karplus A, Dotas RR, Venditti V, Sgourakis NG, Tripsianes K.  2018.  Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra. Nature Communications. 9
[Lange2014] Lange O.  2014.  Automatic NOESY assignment in CS-RASREC-Rosetta. Journal of Biomolecular NMR. 59(3)
[Rosato2012a] Rosato A, Aramini JM, Arrowsmith C, Bagaria A, Baker D, Cavalli A, Doreleijers JF, Eletsky A, Giachetti A, Guerry P et al..  2012.  Blind testing of routine, fully automated determination of protein structures from NMR data.. Structure. 20(2):227-236.
[Nerli2018] Nerli S, McShan AC, Sgourakis NG.  2018.  Chemical shift-based methods in NMR structure determination. Progress in Nuclear Magnetic Resonance Spectroscopy. 106-107
[shen2008a] Shen Y, Lange OF, Delaglio F, Rossi P, Aramini JM, Liu G, Eletsky A, Wu Y, Singarapu KK, Lemak A et al..  2008.  Consistent blind protein structure generation from NMR chemical shift data.. P. Natl. Acad. Sci. USA. 105(12):4685-4690.
[shen2009a] Shen Y, Vernon R, Baker D, Bax A.  2009.  De novo protein structure generation from incomplete chemical shift assignments. J Biomol NMR. 43(2):63-78.
[shen2010a] Shen Y, Bryan PN, He Y, Orban J, Baker D, Bax A.  2010.  De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds.. Protein Sci.. 19(2):349-356.
[Lange2012b] Lange OF, Rossi P, Sgourakis NG, Song Y, Lee H-W, Aramini JM, Ertekin A, Xiao R, Acton TB, Montelione GT et al..  2012.  Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples. Proc Nat Am Soc. (in press)
[Sgourakis2011a] Sgourakis NG, Lange OF, DiMaio F, Andre I, Fitzkee NC, Rossi P, Montelione GT, Bax A, Baker D.  2011.  Determination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings.. J. Am. Chem. Soc.. 133(16):6288-6298.
[Ramelot2009a] Ramelot TA, Raman S, Kuzin AP, Xiao R, Ma L-C, Acton TB, Hunt JF, Montelione GT, Baker D, Kennedy MA.  2009.  Improving NMR protein structure quality by Rosetta refinement: a molecular replacement study.. Proteins. 75(1):147-167.
[raman2010a] Raman S, Lange OF, Rossi P, Tyka M, Wang X, Aramini JM, Liu G, Ramelot TA, Eletsky A, Szyperski T et al..  2010.  NMR structure determination for larger proteins using backbone-only data.. Science. 327(5968):1014-1018.
[Schmitz2012a] Schmitz C, Vernon R, Otting G, Baker D, Huber T.  2012.  Protein structure determination from pseudocontact shifts using ROSETTA.. J Mol Biol. 416(5):668-677.
[Lange2012a] Lange OF, Baker D.  2012.  Resolution-adapted recombination of structural features significantly improves sampling in restraint-guided structure calculation.. Proteins. 80(3):884-895.
[Zhang2014] Zhang Z, Porter J, Tripsianes K, Lange OF.  2014.  Robust and highly accurate automatic NOESY assignment and structure determination with Rosetta. Journal of Biomolecular NMR. 59(3)
[Bouvignies2011a] Bouvignies G, Vallurupalli P, Hansen FD, Correia BE, Lange OF, Bah A, Vernon R, Dahlquist FW, Baker D, Kay LE.  2011.  Solution structure of a minor and transiently formed state of a T4 lysozyme mutant.. Nature. 477(7362):111-114.
[Warner2011a] Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, Pardi A.  2011.  Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set.. J Mol Biol. 411(1):83-95.