Contact Information
Lab Summary Lab Members View our Publications Read our Research Contact Information Important Links

Click a category to view publications:

Mass and Heat Transfer Textbook

  1. Russell, T.W.F., Robinson, A.S., and Wagner, N.J., (2008) Mass and Heat Transfer: Analysis of Mass Contactors and Heat Exchangers, Cambridge University Press, Cambridge, UK (


G-protein Coupled Receptors (7-Helix Transmembrane Proteins)

  1. O'Malley MA, Mancini JD†, Young CL, McCusker EC, Raden D, Robinson A.S*. (2009) “Progress toward heterologous expression of active G-protein-coupled receptors in Saccharomyces cerevisiae: Linking cellular stress response with translocation and trafficking.” Protein Sci. 18(11):2356-70. PubMed Summary
  2. McCusker, E., and Robinson, A.S.*, (2008) Refolding of G protein α subunits from inclusion bodies expressed in Escherichia coli, Protein Exp. Purif., Apr;58(2): 342-55. Epub 2007 Dec 8. PubMed Summary
  3. McCusker, E., Bane, S.E., O’Malley, M., and Robinson, A.S.* (2007), “Heterologous GPCR expression: A bottleneck to obtaining crystal structures”, Biotech Progress, May-Jun;23(3):540-7.PubMed Summary
  4. O’Malley, M., Lazarova, T., Britton, Z.T., and Robinson, A.S. * (2007) “High-level expression in Saccharomyces cerevisiae enables isolation and spectroscopic characterization of functional human adenosine A2a receptor”, J. Struct Biol., 159(2): 166-178.PubMed Summary
  5. Bane, S.E., Velasquez, J.E. †, and Robinson, A.S. * (2007) “Expression and purification of milligram levels of inactive G-protein coupled receptors in E. coli”, Protein Expression and Purification, 52(2):348:355.PubMed Summary
  6. Niebauer, R. T., and Robinson, A.S. * (2006) “Exceptional total and functional yields of the human adenosine (A2a) receptor expressed in the yeast Saccharomyces cerevisiae”, Prot. Exp. Purif., 46, p. 204-211. PubMed Summary
  7. Wedekind, A.L. †, O’Malley, M., Niebauer, R.T., and Robinson, A.S. * (2006) Optimization of the Human Adenosine A2a Receptor Yields in Saccharomyces cerevisiae, Biotechnology Progress, 22(5):1249-55. PubMed Summary
  8. Niebauer, R. T. and Robinson, A.S.(2004) “Saccharomyces cerevisiae protein expression: From protein production to protein engineering” in Expression Technologies, Horizon Scientific Press. PubMed Summary
  9. Niebauer, R.T., Wedekind, A. and Robinson, A.S. * (2004) “Decreases in yeast expression yields of the human adenosine receptor are a result of translational or post-translational events”, Protein Exp. Purif., 37 (1) 134-143.PubMed Summary
  10. Butz, J., Niebauer, R. T., and Robinson, A.S. (2003), “Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-Protein coupled receptor expression in yeast,” Biotech. Bioeng, 84 (3) 292-304.PubMed Summary

PostDoctoral Fellows


Stress Response And Chaperone Interactions

  1. Spatara, ML and Robinson, A.S.* (2010) “Transgenic mouse and cell culture models demonstrate a lack of mechanistic connection between endoplasmic reticulum stress and tau dysfunction” Journal of Neuroscience Research, Feb 8. [Epub ahead of print]. PubMed summary
  2. Xu, P. and Robinson, A.S.* (2009) “Decreased secretion and unfolded protein response up-regulation are correlated with intracellular retention for single-chain antibody variants produced in yeast” Biotech & Bioeng, 104(1):20-9. PubMed summary
  3. Hildebrandt, S.,Raden, D, Petzold, L, Robinson, A.S., and Doyle III, F.J.* (2008) “A top-down approach to mechanistic biological modeling: application to the single-chain antibody folding pathway”, Biophysical Journal, 95(8):3535-58. Epub 2008 Jul 18. PubMed Summary
  4. Famá, M.C., Raden, D., Zacchi, N., Lemos, D.R., Robinson, A.S., and Silberstein, S. * (2007) “The Saccharomyces cerevisiae YFR041C/ERJ5 gene encoding a type I membrane protein with a J domain is required to preserve the folding capacity of the endoplasmic reticulum” Biochim Biophys Acta, 1773(2):232-42.
  5. Griesemer, M., Young, C., Raden, D., Petzold, L., Robinson, A.S., Doyle, F.J. * (2007) “Computational Modeling of  Chaperone Interactions in the Endoplasmic Reticulum of Saccharomyces cerevisiae.” Proc. Int. Conf. Foundations of Systems Biology, Stuttgart, Germany.
  6. Yuraszeck, T., Raden, D, Robinson, A.S., and Doyle, F.J.* (2007) “Microarray Analysis of the Unfolded Protein Response in S. cerevisiae Reveals Evidence of Down-regulation.” Proc. Int. Conf. Foundations of Systems Biology, Stuttgart, Germany.
  7. Xu, P., Raden, D., Doyle, F.J. III, and Robinson, A.S. * (2005) “Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding”, Metabolic Engineering, 7 (4) 269-279.PubMed summary
  8. Raden, D., Hildebrandt, S, Xu, P., Bell, E. †, Doyle, III, F.J. and Robinson, A.S. * (2005), “Analysis of cellular response to protein overexpression.” IEE Proceedings: Systems Biology 152 (4) 285-289. PubMed summary
  9. Hildebrandt, S., D. Raden, E. Bell†, Robinson, A.S. , and F.J. Doyle III* (2005) “Modeling the Unfolded Protein Response in Saccharomyces Cerevisiae”, Proc. Int. Conf. Foundations of Systems Biology, Santa Barbara, California.
  10. Kauffman, K., Pridgen, E.M., Doyle, F.J. III, Dhurjati, P., and Robinson, A.S. (2002) “Decreased Protein Expression and Oscillating BiP Levels Result during Heterologous Protein Expression in S. cerevisiae,” Biotech. Prog., 18, 942-940. DOI: 10.1021/bp025518g PubMed summary
  11. Kauffman, K., Dhurjati, P. , Robinson, A.S. and F.J. Doyle III , “Framework for Modeling Information Flow in Biological Processes: Application to the Unfolded Protein Response.” Proc. IFAC Conf. Comput. Appl. Biotech (CAB), 2001.
  12. Robinson, A.S., Bockhaus, J.A., Voegler, A.C.and Wittrup, K.D. (1996) “Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiaeJ. Biol. Chem. 271, 10017-10022.PubMed summary
  13. Robinson, A.S. and Lauffenburger, D.A.(1996) “Model for ER Chaperone Dynamics and Secretory Protein Interactions.” AIChE J. 42, 1443-1453.
  14. Robinson, A.S. and K.D. Wittrup (1995) “Constitutive Overexpression of Secreted Heterologous Proteins Decreases Extractable BiP and PDI Levels in Saccharomyces cerevisiae.” Biotech Prog.  11, 171-177. PubMed summary
  15. Wittrup , K.D., Robinson, A.S., Parekh, R.N. and Forrester, K.J. (1994) “Existence of an Optimal Expression Level for Secretion of Foreign Proteins in Yeast.” Ann. N.Y. Acad. Sci.  745, 321-330.
  16. Robinson, A.S., V. Hines, and K.D. Wittrup (1994) “Overexpression of Protein Disulfide Isomerase Increases Secretion of Foreign Proteins in the Yeast Saccharomyces cerevisiae.” Bio/Tech. 12, 381-384. PubMed summary
  17. "Foreign Proteins in Eucaryotic Cells.”  in Protein Folding:  In vivo and In vitro.  ACS Symposium Series 526.  Jeffrey Cleland, Ed., 121-132.
  18. Robinson, A.S. and Wittrup, K.D. . “Methods for Increasing Secretion of Overexpressed Proteins.” Patent # 5,773,245.  Filed 10/92.  Accepted 6/30/98.

PostDoctoral Fellows


 Protein Aggregation and Refolding

  1. Spatara, ML, Roberts, CJ, and Robinson, A.S.* (2009) “Kinetic folding studies of the P22 tailspike beta-helix domain reveal multiple unfolded states.” Biophys Chem. 141(2-3):214-21. PubMed summary
  2. Webber T, Gurung S, Saul J, Baker T, Spatara M, Freyer M, Robinson A.S., and Gage MJ* (2009) “The C-terminus of the P22 tailspike protein acts as an independent oligomerization domain for monomeric proteins.”, Biochem J. 2009 May 1;419(3):595-602. PubMed summary
  3. Gage, M.J, Lefebvre, B.G., and Robinson, A.S.* (2006) “Determinants of Protein Folding and Aggregation in P22 Tailspike,” in Misbehaving Proteins, ACS Publications, eds. Regina Murphy and Amos Tsai.
  4. Kim, J. and Robinson, A.S. * (2006) Dissociation of intermolecular disulfide bonds in P22 tailspike protein intermediates in the presence of SDS, Protein Science, 15 (7), p. 1791-3. PubMed summary
  5. Gage, M.J., Zak, J. and Robinson, A.S. * (2005) “Three Amino Acids that are Critical to Formation and Stability of the P22 Tailspike Trimer”, Protein Science, 14 (9) 2333-43. PubMed summary
  6. Lefebvre, B.G., Gage, M.J., and Robinson, A.S. (2004) “Maximizing Recovery of Native Protein from Aggregates by Optimizing Pressure Treatment,” Biotechnology Progress, 20, 2, p. 623-629.  10.1021/bp034221v.PubMed summary
  7. Lefebvre, B.G., Comolli, N.K., Gage, M.J. and A.S. Robinson * (2004), “Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive mutants of P22 tailspike,” Protein Sci., 13 (6) 1538-46.PubMed summary
  8. Danek, B.L. and Robinson, A.S.* (2004) “P22 tailspike trimer assembly is governed by interchain redox associations,” Biochem. Biophys. Acta, 1700(1):105-16. [5]PubMed Summary
  9. Gage, M.J. and Robinson, A. S. (2003) “C-terminal Hydrophobic Interactions Play a Critical role in Oligomeric Assembly of the P22 Tailspike Trimer,” Protein Sci., 12, 12, p. 2732-47. PubMed Summary
  10. Lefebvre, B.G., and Robinson, A.S. (2003), “Pressure treatment of tailspike aggregates rapidly produces on-pathway folding intermediates,” Biotech. Bioeng, 82, 5, p. 595-604. DOI: 10.1002/bit.10607 PubMed Summary
  11. Danek, B.L., and Robinson, A. S. (2003) “Non-native interactions between cysteines direct productive assembly of P22 tailspike protein,” Biophys J., 85, 5, p. 1-11.
  12. Sinacola, J. and Robinson, A. S. (2002) “Rapid refolding and polishing of single-chain antibodies from E. coli inclusion bodies” Protein Exp. Purif., Vol. 26, No. 2, Nov 2002, pp. 301-308. DOI: 10.1016/S1046-5928(02)00538-7.PubMed Summary
  13. Haase-Pettingell, C., Betts, S., Raso, S.W., Stuart, L., Robinson, A.S. and J. King (2001), “Role for Cysteine Residues in the In Vivo Folding and Assembly of the Phage P22 Tailspike,” Protein Sci. 10, 397-410.
  14. Robinson, A.S. and J. King , (1997) “Disulfide-Bonded Intermediate on the Folding and Assembly Pathway of a Non-Disulfide Bonded Protein.” Nature Struct. Biol., 4, 450-455.
  15. Foguel, D., Robinson, C.R., Caetano de Sousa Jr., P., Silva, J. L., Robinson A.S. (1999), “Hydrostatic Pressure Rescues Protein Aggregates”, Biotech. Bioeng. 63, 552-558.PubMed Summary
  16. Robinson, A.S., D. Foguel, J.L. Silva, C.R. Robinson. “Use of Hydrostatic Pressure to Inhibit and Reverse Protein Aggregation and Facilitate Protein Refolding.” US Patent # 7,615,617. Filed 10/99. Issued 11/10/09.
  17. King , J., Haase-Pettingell, C., Robinson, A. S., Speed, M and Mitraki, A. (1996) “Thermolabile Folding Intermediates: Inclusion Body Precursors and Chaperonin Substrates” FASEB J., 10, 57-66.PubMed Summary

PostDoctoral Fellows


Extermophilic Protein Expression - beta Glucosidase (CelB) and Pyrolysin

  1. Powers, S.L. and Robinson, A. S.* (2007) “PDI Improves Secretion of Redox-Inactive b-glucosidase”, Biotech Prog., Mar-Apr;23(2):364-9. E-pub Feb 22, DOI: 10.1021/bp060287p PubMed Summary
  2. Powers, S.L., Robinson, C.R., and Robinson, A.S. * (2007) Denaturation of an Extremely Stable Hyperthermophilic Protein Occurs via a Dimeric Intermediate, Extremophiles, 11(1):179-89. PubMed Summary
  3. Smith, J.D., Richardson, N.E. and Robinson, A. S.* (2005) “Elevated expression temperature in a mesophilic host results in increased secretion of a hyperthermophilic enzyme and decreased cell stress,” Biochem. Biophys. Acta, 1752 (1) 18-25. PubMed Summary
  4. Smith, J.D., Tang, B.C., and Robinson, A. S.(2004) “Protein disulfide isomerase, but not binding protein, overexpression enhances secretion of a non-disulfide-bonded protein in yeast”, Biotech. Bioeng., 85, 3, p. 340-50.PubMed Summary
  5. Smith, J.D. and Robinson, A. S. (2002) “Expression of an archael enzyme in a eucaryotic host: A secretion bottleneck at the ER,” Biotech. Bioeng., 79, 7, p. 713-723. DOI: 10.1002/bit.10367
  6. Blumentals, I. I., Robinson, A. S. and Kelly, R. M.. (1990). "Characterization of Sodium Dodecyl Sulfate Resistant Proteolytic Activity in the Hyperthermophilic Archaebacterium Pyrococcus furiosus." Appl. Envir. Microbiol. 56, 1992-1998. PubMed Summary
  7. Blumentals, I.I., S.H. Brown, R.N. Schicho, A.K. Skaja [Robinson], H.R. Costantino, and R.M. Kelly . (1990) “The Hyperthermophilic Archaebacterium, Pyrococcus furiosus:  Development of Culturing Protocols, Perspectives on Scale-Up, and Potential Applications.” Ann. N.Y. Acad. Sci., 589, 301-314. PubMed Summary
  8. Kelly, R.M., Robinson,A.K.S., I.I. Blumentals, S.H. Brown, and C.B. Anfinsen.  “Proteolytic Enzymes from Hyperthermophilic Bacteria and Processes for Their Production.” 
    Patent # 5,242,817.  Filed 9/12/89.  Accepted 9/7/93.  Licensed to Takara Shuzo.

PostDoctoral Fellows



  1. Blumentals, I. I., Kelly, R. M., A. K. Skaja [Robinson] and J. Shiloach. (1987) "Effect of Culturing Conditions on the Production of Exotoxin A by Pseudomonas aeruginosa."  Ann N Y Acad. Sci. 506, 663-668. PubMed Summary
  2. Forsten-Williams*, K.F., Cassino, T.R, Delo, L.J., Bellis, A.D., Robinson, A.S., and Ryan, T.E., (2007) Enhanced Insulin-like Growth Factor-I (IGF-I) Cell Association at Reduced pH is Dependent on IGF Binding Protein-3 (IGFBP-3) Interaction, Journal of Cellular Physiology, 210(2):298-308.PubMed Summary

PostDoctoral Fellows


University of Delaware