Cell‐free synthesis of proteins that require disulfide bonds using glucose as an energy source
暂无分享,去创建一个
[1] B. Wanner,et al. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[2] T. Kigawa,et al. Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis , 1995, Journal of biomolecular NMR.
[3] James Swartz,et al. Amino acid stabilization for cell-free protein synthesis by modification of the Escherichia coli genome. , 2004, Metabolic engineering.
[4] C. Williams,et al. Proton stoichiometry in the reduction of the FAD and disulfide of Escherichia coli thioredoxin reductase. Evidence for a base at the active site. , 1983, The Journal of biological chemistry.
[5] J. Swartz,et al. Efficient and scalable method for scaling up cell free protein synthesis in batch mode. , 2005, Biotechnology and bioengineering.
[6] Dong-Myung Kim,et al. Efficient production of a bioactive, multiple disulfide‐bonded protein using modified extracts of Escherichia coli , 2004, Biotechnology and bioengineering.
[7] J. Swartz,et al. Energizing cell-free protein synthesis with glucose metabolism. , 2005, Biotechnology and bioengineering.
[8] R. Raines,et al. The CXXC motif: a rheostat in the active site. , 1997, Biochemistry.
[9] W. Fischer,et al. Protein Disulfide Bond Formation in the Cytoplasm during Oxidative Stress* , 2004, Journal of Biological Chemistry.
[10] J. Swartz,et al. Enhancing multiple disulfide bonded protein folding in a cell‐free system , 2004, Biotechnology and bioengineering.
[11] L. Polgár. Ion-pair formation as a source of enhanced reactivity of the essential thiol group of D-glyceraldehyde-3-phosphate dehydrogenase. , 1975, European journal of biochemistry.
[12] J. Swartz,et al. Streamlining Escherichia Coli S30 Extract Preparation for Economical Cell‐Free Protein Synthesis , 2008, Biotechnology progress.
[13] J. Swartz,et al. An Economical Method for Cell‐Free Protein Synthesis using Glucose and Nucleoside Monophosphates , 2008, Biotechnology progress.
[14] M. Jewett,et al. Mimicking the Escherichia coli cytoplasmic environment activates long‐lived and efficient cell‐free protein synthesis , 2004, Biotechnology and bioengineering.
[15] James Swartz,et al. Maintaining rapid growth in moderate-density Escherichia coli fermentations. , 2005, Biotechnology and bioengineering.
[16] J. Swartz,et al. Cell‐free production of active E. coli thioredoxin reductase and glutathione reductase , 2004, FEBS letters.
[17] L. Polgár. On the mode of activation of the catalytically essential sulfhydryl group of papain. , 1973, European journal of biochemistry.
[18] J. Beckwith,et al. Conversion of a Peroxiredoxin into a Disulfide Reductase by a Triplet Repeat Expansion , 2001, Science.
[19] M. J. Coon,et al. Mechanism of action of pyruvate kinase. Role of sulfhydryl groups in catalytic activity as determined by disulfide interchange. , 1972, The Journal of biological chemistry.
[20] James A Thomas,et al. Aging and oxidation of reactive protein sulfhydryls , 2001, Experimental Gerontology.