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  1. 1.   Galectin-1 as a fusion partner for the production of soluble and folded human beta-1,4-galactosyltransferase-T7 in E. coil
  2. Pasek, M.; Boeggeman, E.; Ramakrishnan, B.; Qasba, P. K.
  3. Biochemical and Biophysical Research Communications. 2010, Apr; 394(3): 679-684.
  1. 2.   Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners
  2. Nallamsetty, S.; Waugh, D. S.
  3. Protein Expression and Purification. 2006, JAN; 45(1): 175-182.
  1. 3.   Gateway vectors for the production of combinatorially-tagged His(6)-MBP fusion proteins in the cytoplasm and periplasm of Escherichia Coli
  2. Nallamsetty, S.; Austin, B. P.; Penrose, K. J.; Waugh, D. S.
  3. Protein Science. 2005, DEC; 14(12): 2964-2971.
  1. 4.   Structure-based discovery of nonpeptidic small organic compounds to block the T cell response to myelin basic protein
  2. Koehler, N. K. U.; Yang, C. Y.; Varady, J.; Lu, Y. P.; Wu, X. W.; Liu, M.; Yin, D. X.; Bartels, M.; Xu, B. Y.; Roller, P. P.; Long, Y. Q.; Li, P.; Kattah, M.; Cohn, M. L.; Moran, K.; Tilley, E.; Richert, J. R.; Wang, S. M.
  3. Journal of Medicinal Chemistry. 2004, OCT 7; 47(21): 4989-4997.
  1. 5.   Expression of the murine leukemia virus protease in fusion with maltose-binding protein in Escherichia coli
  2. Feher, A.; Boross, P.; Sperka, T.; Oroszlan, S.; Tozser, J.
  3. Protein Expression and Purification. 2004 35(1): 62-68.
  1. 6.   Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers
  2. Fox, J. D.; Routzahn, K. M.; Bucher, M. H.; Waugh, D. S.
  3. Febs Letters. 2003 537(1-3): 53-57.
  1. 8.   Removal of Affinity Tags with TEV Protease.
  2. Raran-Kurussi, Sreejith; Cherry, Scott; Zhang, Di; Waugh, David
  3. Methods in molecular biology (Clifton, N.J.). 2017 1586: 221-230.
  1. 9.   Expression and Purification of Recombinant Proteins in Escherichia coli with a His6 or Dual His6-MBP Tag.
  2. Raran-Kurussi, Sreejith; Waugh, David
  3. Methods in molecular biology (Clifton, N.J.). 2017 1607: 1-15.
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