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 (www.cambridge.org/9780521886703).

 

1. Naranjo, A.N., Chevalier, A., Cousins, G.D., Ayettey, E., McCusker, E.C., Wenk, C., and Robinson, A.S. (2015) "Conserved disulfide bond is not essential for the adenosine A2A receptor: extracellular cysteines influence receptor distribution within the cell and ligand-binding recognition", BBA Biomembranes, 1848: 603-614 Available on-line Dec 5 2014
2. Blocker, K.M., Britton, Z.T., Naranjo, A.N., McNeely, P.M., Young, C.L., and Robinson, A.S. (2015) "Recombinant G protein-coupled receptor expression in Saccharomyces cerevisiae for protein characterization", in “Membrane Proteins – Production and Function Characterization”, Methods Enzymol., 556:165-83 
3. McNeely, P.M., Naranjo, A.N., and Robinson, A.S. (2012) "Structure-function studies with G-protein coupled receptors as a paradigm for improving drug discovery and therapeutic development", Biotechnology Journal, 7(12): 1451-1461.
4. Britton, Z.T., Hanle, E., and Robinson, A.S. (2012) "An Expression and Purification System for the Biosynthesis of Adenosine Receptor Peptides for Biophysical and Structural Characterization", Protein Exp. Purif., 84:224-235
5. O’Malley, M.A., Helgeson, M.E., Wagner, N.J., and Robinson, A.S. (2011) “Toward Rational Design of Protein Detergent Complexes: Determinants of Mixed Micelles that are Critical for the in vitro Stabilization of a G-protein Coupled Receptor”, Biophysical Journal, 101 (8): 1938-1948
   
6. Robinson, A.S., ed (2011) "Production of Membrane Proteins – Strategies for Expression and Isolation", Wiley VCH.
7. O’Malley, M.A., Naranjo, A.N., Lazarova, T., and Robinson, A.S.* (2010) “Analysis of Adenosine A2a Receptor Stability: Effects of Ligands and Disulfide Bonds,” Biochemistry, Nov 2;49(43):9181-9.
8. O'Malley, M.A., Helgeson, M.E., Wagner, N.J., and Robinson, A.S.* (2011) "The morphology and composition of cholesterol-rich micellar nanostructures determine transmembrane protein (GPCR) Activity", Biophysical Journal, 100(2): L11-13.
9. Robinson, A.S* (2011) “New Tools for Breaking Barriers to GPCR Expression in E. coli” Journal of Molecular Biology. 408 (4): 597-598.
10. Britton, Z., Young, C.L., Can, O., McNeely, P., Naranjo, A.N., and Robinson, A. S.* (2011), “Membrane protein expression in yeast Saccharomyces cerevisiae” in Production of Membrane Proteins – Strategies for Expression and Isolation, Wiley VCH, Robinson, A.S., ed.
11. O'Malley, M.A., Mancini, J.D.†, Young, C.L., McCusker, E.C., Raden, D., and 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.
12. 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.
13. 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.
14. 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.
15. 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.
16. 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.
17. 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.
18. Niebauer, R. T. and Robinson, A.S.(2004) “Saccharomyces cerevisiae protein expression: From protein production to protein engineering” in Expression Technologies, Horizon Scientific Press.
19. 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.
20. 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.

 

1. Young, C.L. and Robinson, A.S.* (2014) "Protein Folding and Secretion: Mechanistic Insights Advancing Recombinant Protein Production in S. cerevisiae", Current Opinion in Biotechnology, 30: 168-177.
2. Griesemer, M., Young, C., Robinson, A.S., Petzold, L.* (2014) "BiP Clustering Facilitates Protein Folding in the Endoplasmic Reticulum", PLOS Computational Biology, 10(7):1-16
3. Young, C.L., Raden, D.L., Robinson, A.S. (2013) "Analysis of ER Resident Proteins in S. cerevisiae: Implementation of H/KDEL Retrieval Sequences", Traffic, 14(4):365-81
4. Young, C.L., Raden, D.L., Caplan, J., Czymmek, K., Robinson, A.S. (2012) “Cassette Series Designed for Live-Cell Imaging of Proteins and High Resolution Techniques in Yeast”, Yeast, Mar;29(3-4):119-36.
5. Young, C.L., Britton, Z.T., Robinson, A.S. (2012) “Recombinant Protein Expression and Purification: A Comprehensive Review of Affinity Tags and Microbial Applications” Biotechnology Journal, May;7(5):620-34.
6. Young C.L., Yuraszeck T., Robinson A.S.* (2011) “Decreased secretion and unfolded protein response upregulation,” Methods Enzymol. 491:235-60.
7. Griesemer, M., Young, C.L., Doyle III, F.J., Robinson, A.S. and Petzold, L.* (2011) Spatial Localization of Chaperone Distribution in the Endoplasmic Reticulum of Yeast, IET Systems Biology, 6(2):54-63.
8. 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, 88(9):1951-61.
9. Yuraszeck, T.M., Neveu, P., Rodriguez-Fernandez, M., Robinson, A.S., Kosik, K.S., Doyle III, F.J.* (2010) "Vulnerabilities in the Tau Network and The Role of Ultrasensitive Points in Tau Pathophysiology", PLoS Computational Biology, 6(11): e1000997. doi:10.1371/journal.pcbi.1000997 (with cover art).
10. 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.
11. 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.
12. 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.
13. 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.
14. 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.
15. 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.
16. 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.
17. 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.
18. 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
19. 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.
20. Robinson, A.S., Bockhaus, J.A., Voegler, A.C.and Wittrup, K.D. (1996) “Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae” J. Biol. Chem. 271, 10017-10022.
21. Robinson, A.S. and Lauffenburger, D.A.(1996) “Model for ER Chaperone Dynamics and Secretory Protein Interactions.” AIChE J. 42, 1443-1453.
22. 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.
23. 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.
24. 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.
25. "Foreign Proteins in Eucaryotic Cells.”  in Protein Folding:  In vivo and In vitro.  ACS Symposium Series 526.  Jeffrey Cleland, Ed., 121-132.
26. 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.

 

1. Wu, H., Truncali, K., Ritchie, J., Kroe-Barrett, R., Singh, S., Robinson, A.S., Roberts, C.J.* (2015) "Weak protein interactions and pH- and temperature-dependent aggregation of human Fc1", mAbs, in press
2. Wu, H., Kroe-Barrett, R., Singh, S., Robinson, A.S., Roberts, C.J.* (2014) "Competing aggregation pathways for monoclonal antibodies", FEBS Letters, 588(6): 936-941.
3. Maurer, R.W., Hunter, A.K., Robinson, A.S.*, and Roberts, C.J.* (2014) "Aggregates of alpha-chymotrypsinogen anneal to access more stable states", Biotechnology & Bioengineering, 111 (4): 782-791.
4. Maurer, R.W., Hunter, A.K., Wang, X., Wang, W.K., Robinson, A.S., and Roberts, C.J.* (2013) "Folding and aggregation of a multi-domain engineered immunotoxin", Biochemical Engineering Journal, 81: 8-14. 
5. Blanco, M., Sahin, E., Robinson, A.S., Roberts, C.* (2013) "Coarse-Grained Model for Colloidal Protein Interactions, B22, and Protein Cluster Formation", The Journal of Physical Chemistry, Part B, Dec 19;117(50):16013-28
6. Costanzo, J.A., O’Brien, C.J., Tiller, K.†, Tamargo, E.†, Robinson, A.S., Roberts, C.J., and Fernandez, E.J.* (2013) "Computational Design to Control Protein Aggregation Rates Through Conformational Stability", Protein Eng, Des, & Sel, 27 (5): 157-167
7. Morozova, O.A, March, Z.M.†, Robinson, A.S., Colby, D.W.* (2013) "Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein", Biochemistry, 52(40):6960-7.
8. Sahin, E., Jordan, J.L., Spatara, M.L., Naranjo, A.N., Weiss IV, W.F., Robinson, A.S, Fernandez, E.J.*, Roberts, C.J.* (2011) “Computational Design and Biophysical Characterization of Aggregation-Resistant Point Mutations for γD Crystallin Illustrate a Balance of Conformational Stability and Intrinsic Aggregation Propensity”, Biochemistry, Feb 8;50(5):628-39.
9. 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.
10. 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.
11. 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.
12. 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.
13. 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.
14. 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.
15. 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.
16. 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]
17. 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.
18. 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
19. 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.
20. 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.
21. 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.
22. 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.
23. 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.
24. 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.
25. 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.

 

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
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.
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.
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.
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.
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.
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.

 

1. St. Amand, M.M., Radhakrishnan, D., Robinson, A.S., Ogunnaike, B.A.* (2014) "Identification of Manipulated Variables for a Glycosulation Control Strategy", Biotech Bioeng, Oct;111(10):1957-70.
2. St. Amand, M.M., Tran, K.†, Radhakrishnan, D., Robinson, A.S., Ogunnaike, B.A.* (2014) "Controllability Analysis of Protein Glycosylation in CHO cells", PLoS One, 9(2): e87973
3. St. Amand, M., Ogunnaike, B.A., and Robinson, A.S.* (2014) "Development of At-Line Assay to Monitor Charge Variants of mAbs During Production", Biotechnology Progress, 30: 249–255. 
4. 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.
5. 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.