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  1. 1.   Purification of inclusion bodies using PEG precipitation under denaturing conditions to produce recombinant therapeutic proteins from Escherichia coli
  2. Chen, Huanhuan; Li, Ninghuan; Xie, Yueqing; Jiang, Hua; Yang, Xiaoyi; Cagliero, Cedric; Shi, Siwei; Zhu, Chencen; Luo, Han; Chen, Junsheng; Zhang, Lei; Zhao, Menglin; Feng, Lei; Lu, Huili; Zhu, Jianwei
  3. Applied Microbiology and Biotechnology. 2017, Jul; 101(13): 5267-5278.
  1. 2.   Potential Role of alpha-Synuclein and Metallothionein in Lead-Induced Inclusion Body Formation
  2. Zuo, P. J.; Qu, W.; Cooper, R. N.; Goyer, R. A.; Diwan, B. A.; Waalkes, M. P.
  3. Toxicological Sciences. 2009 111(1): 100-108.
  1. 3.   Recombinant production of anti-HIV protein, griffithsin, by auto-induction in a fermentor culture
  2. Giomarelli, B.; Schumacher, K. M.; Taylor, T. E.; Sowder, R. C.; Hartley, J. L.; McMahon, J. B.; Mori, T.
  3. Protein Expression and Purification. 2006, MAY; 47(1): 194-202.
  1. 4.   Enhanced soluble protein expression using two new fusion tags
  2. Chatterjee, D. K.; Esposito, D.
  3. Protein Expression and Purification. 2006, MAR; 46(1): 122-129.
  1. 5.   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. 6.   Immunogenetic risk and protective factors for the idiopathic inflammatory myopathies - Distinct HLA-A, -B, -Cw,-DRB1 and -DQA1 allelic profiles and motifs define clinicopothologic groups in Caucasians
  2. O'Hanlon, T. P.; Carrick, D. M.; Arnett, F. C.; Reveille, J. D.; Carrington, M.; Gao, X. J.; Oddis, C. V.; Morel, P. A.; Malley, J. D.; Malley, K.; Dreyfuss, J.; Shamim, E. A.; Rider, L. G.; Chanock, S. J.; Foster, C. B.; Bunch, T.; Plotz, P. H.; Love, L. A.; Miller, F. W.
  3. Medicine. 2005, NOV; 84(6): 338-349.
  1. 7.   Metallothionein-I/II double knockout mice are hypersensitive to lead-induced kidney carcinogenesis: Role of inclusion body formation
  2. Waalkes, M. P.; Liu, J.; Goyer, R. A.; Diwan, B. A.
  3. Cancer Research. 2004, NOV 1; 64(21): 7766-7772.
  1. 8.   Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins
  2. Fox, J. D.; Kapust, R. B.; Waugh, D. S.
  3. Protein Science. 2001 10(3): 622-630.
  1. 9.   Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
  2. Kapust, R. B.; Waugh, D. S.
  3. Protein Science. 1999 8(8): 1668-1674.
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