Cell-free protein production and labeling protocol for NMR-based structural proteomics
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John L Markley | J. Markley | B. Volkman | F. Peterson | Betsy L Lytle | Francis C Peterson | Brian F Volkman | Dmitriy A Vinarov | Ejan M Tyler | B. Lytle | D. Vinarov | Ejan M. Tyler
[1] Yasuhiko Yoshida,et al. Cell‐free production and stable‐isotope labeling of milligram quantities of proteins , 1999, FEBS letters.
[2] M. McPherson,et al. PCR 2 : a practical approach , 2016 .
[3] J. Swartz,et al. Enhancing multiple disulfide bonded protein folding in a cell‐free system , 2004, Biotechnology and bioengineering.
[4] A. Palmer,et al. Nmr probes of molecular dynamics: overview and comparison with other techniques. , 2001, Annual review of biophysics and biomolecular structure.
[5] Shigeyuki Yokoyama,et al. Protein expression systems for structural genomics and proteomics. , 2003, Current opinion in chemical biology.
[6] T. Kigawa,et al. A highly efficient cell-free protein synthesis system from Escherichia coli. , 1996, European journal of biochemistry.
[7] R. Wetzel,et al. Inclusion body formation and protein stability in sequence variants of interleukin-1 beta. , 1993, The Journal of biological chemistry.
[8] Tomio Ogasawara,et al. A bilayer cell‐free protein synthesis system for high‐throughput screening of gene products , 2002, FEBS letters.
[9] A. Goldberg,et al. An increased content of protease La, the lon gene product, increases protein degradation and blocks growth in Escherichia coli. , 1987, The Journal of biological chemistry.
[10] Adam Godzik,et al. Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization , 2003, BMC Bioinformatics.
[11] E D Laue,et al. Dual amino acid-selective and site-directed stable-isotope labeling of the human c-Ha-Ras protein by cell-free synthesis , 1998, Journal of biomolecular NMR.
[12] M. Maurizi. Degradation in vitro of bacteriophage lambda N protein by Lon protease from Escherichia coli. , 1987, The Journal of biological chemistry.
[13] C. Sander,et al. Errors in protein structures , 1996, Nature.
[14] Dong-Myung Kim,et al. Prolonging Cell‐Free Protein Synthesis by Selective Reagent Additions , 2000, Biotechnology progress.
[15] P. Curmi,et al. Dictyostelium discoideum as expression host: isotopic labeling of a recombinant glycoprotein for NMR studies. , 2000, Protein expression and purification.
[16] J-M Betton,et al. Rapid translation system (RTS): a promising alternative for recombinant protein production. , 2003, Current protein & peptide science.
[17] T. Sawasaki,et al. A wheat germ cell‐free system is a novel way to screen protein folding and function , 2003, Protein science : a publication of the Protein Society.
[18] A. Bax,et al. Protein backbone angle restraints from searching a database for chemical shift and sequence homology , 1999, Journal of biomolecular NMR.
[19] J. Thornton,et al. PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .
[20] T. Sawasaki,et al. Efficient synthesis of a disulfide-containing protein through a batch cell-free system from wheat germ. , 2003, European journal of biochemistry.
[21] Tomio Ogasawara,et al. A cell-free protein synthesis system for high-throughput proteomics , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[22] C. Larsen,et al. The ubiquitin superfamily: members, features, and phylogenies. , 2002, Journal of proteome research.
[23] W. Jahnke,et al. Amino–acid-type selective isotope labeling of proteins expressed in Baculovirus-infected insect cells useful for NMR studies , 2003, Journal of biomolecular NMR.
[24] Y. Matsuo,et al. Structural genomics projects in Japan. , 2000, Progress in biophysics and molecular biology.
[25] W. Lubitz,et al. Lysis of Escherichia coli by induction of cloned ϕX174 genes , 2004, Molecular and General Genetics MGG.
[26] T. Holak,et al. A novel medium for expression of proteins selectively labeled with 15N-amino acids in Spodoptera frugiperda (Sf9) insect cells , 2003, Journal of biomolecular NMR.
[27] K Wüthrich,et al. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT , 1996, Journal of biomolecular NMR.
[28] E. Truve,et al. Protein Synthesis in Cell-Free Systems , 1998 .
[29] R. Andrew Byrd,et al. ASSOCIATION OF BIOMOLECULAR SYSTEMS VIA PULSED FIELD GRADIENT NMR SELF-DIFFUSION MEASUREMENTS , 1995 .
[30] T. Kigawa,et al. Effects of Escherichia coli ribosomal protein S12 mutations on cell-free protein synthesis. , 2004, European journal of biochemistry.
[31] D. Wemmer,et al. Protein Signal Assignments Using Specific Labeling and Cell-Free Synthesis , 2004, Journal of biomolecular NMR.
[32] S. Grzesiek,et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.
[33] M. Nilges,et al. Refinement of protein structures in explicit solvent , 2003, Proteins.
[34] Y Endo,et al. A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: plants apparently contain a suicide system directed at ribosomes. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[35] N. Dixon,et al. NMR analysis of in vitro‐synthesized proteins without purification: a high‐throughput approach , 2002, FEBS letters.
[36] Torsten Herrmann,et al. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. , 2002, Journal of molecular biology.
[37] T. Kigawa,et al. Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis , 1995, Journal of biomolecular NMR.
[38] Heinz Rüterjans,et al. High level cell-free expression and specific labeling of integral membrane proteins. , 2004, European journal of biochemistry.