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Protein and Metabolic Engineering

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Publications (62 Total)

Columbia University (50 Total)

Smith, J.R., Amaya, K.R., Bredemeier, R.T., Banta, S., and Cropek, D.M. (2015) “Selective biomolecular photocatalytic decomposition using peptide-modified TiO2 nanoparticles" Applied Catalysis B: Environmental (In Press).

Patel, T.N., Park, A-H.A. and Banta, S. (2014) “Genetic Manipulation of Outer Membrane Permeability: Generating Porous Heterogeneous Catalyst Analogs in Escherichia coli” ACS Synthetic Biology 3(12) 848-854.

1. Patel TN, Park AH, and Banta S. Genetic manipulation of outer membrane permeability: generating porous heterogeneous catalyst analogs in Escherichia coli. ACS Synth Biol. 2014 Dec 19;3(12):848-54. DOI:10.1021/sb400202s |

Li, X., Mercado, R., Berlinger, S., Banta, S. and West, A.C. (2014) “Engineering Acidithiobacillus ferrooxidans growth media for enhanced electrochemical processing” AIChE Journal 60(12) 4008-4013.

DOI: 10.1002/aic.14628

Dooley, K., Bulutoglu, B. and Banta, S. (2014) “Doubling the cross-linking interface of a rationally-designed beta roll peptide for calcium-dependent proteinaceous hydrogel formation” Biomacromolecules 15(10) 3617-3624.

3. Dooley K, Bulutoglu B, and Banta S. Doubling the cross-linking interface of a rationally designed beta roll peptide for calcium-dependent proteinaceous hydrogel formation. Biomacromolecules. 2014 Oct 13;15(10):3617-24. DOI:10.1021/bm500870a |

Li, X., Mercado, R., Kernan, T., West, A.C., and Banta, S. (2014) “Addition of citrate to Acidithiobacillus ferrooxidans cultures enables precipitate-free growth at elevated pH and reduces ferric inhibition” Biotechnology and Bioengineering 111(10) 1940-1948.

4. Li X, Mercado R, Kernan T, West AC, and Banta S. Addition of citrate to Acidithiobacillus ferrooxidans cultures enables precipitate-free growth at elevated pH and reduces ferric inhibition. Biotechnol Bioeng. 2014 Oct;111(10):1940-8. DOI:10.1002/bit.25268 |

Patel, T.N., Park, A-H.A. and Banta, S. (2014) “Surface display of small peptides on Escherichia coli for enhanced calcite (CaCO3) precipitation rates” Biopolymers (Peptide Science) 102(2) 191-196.

doi:10.1002/bip.22466

Chandra, D., Sankalia, N., Arcibal, I., Banta, S., Cropek, D., and Karande, P. (2014) “Design of affinity peptides from natural protein ligands: A study of the cardiac troponin complex” Peptide Science 102(1) 97-106.

6. Chandra D, Sankalia N, Arcibal I, Banta S, Cropek D, and Karande P. Design of affinity peptides from natural protein ligands: A study of the cardiac troponin complex. Biopolymers. 2014 Jan;102(1):97-106. DOI:10.1002/bip.22436 |

Patel, T.N., Swanson, E.J., Park, A-H.A. and Banta, S. (2014) “An Automated Method for Measuring the Operational Stability of Biocatalysts with Carbonic Anhydrase Activity” Biochemical Engineering Journal 82 48-52.

doi:10.1016/j.bej.2013.11.003

Banta, S., Dooley, K., and Shur, O. (2013) “Replacing antibodies: Engineering new binding proteins” Annual Review of Biomedical Engineering 15 93-113.

8. Banta S, Dooley K, and Shur O. Replacing antibodies: engineering new binding proteins. Annu Rev Biomed Eng. 2013;15:93-113. DOI:10.1146/annurev-bioeng-071812-152412 |

Patel, T.N., Park, A-H. A., and Banta, S. (2013) “Periplasmic expression of carbonic anhydrase in Escherichia coli: A whole-cell biocatalyst for CO2 hydration” Biotechnology and Bioengineering 110(7) 1865-1873.

9. Patel TN, Park AH, and Banta S. Periplasmic expression of carbonic anhydrase in Escherichia coli: a new biocatalyst for CO(2) hydration. Biotechnol Bioeng. 2013 Jul;110(7):1865-73. DOI:10.1002/bit.24863 |

Liu, F., Banta, S., and Chen, W. (2013) “Functional assembly of a multi-enzyme cascade on the surface-displayed trifunctional scaffold for enhanced NADH production” Chemical Communications 49(36) 3766-3768.

10. Liu F, Banta S, and Chen W. Functional assembly of a multi-enzyme methanol oxidation cascade on a surface-displayed trifunctional scaffold for enhanced NADH production. Chem Commun (Camb). 2013 May 8;49(36):3766-8. DOI:10.1039/c3cc40454d |

Shur, O., Dooley, K. Blenner, M., Baltimore, M., and Banta, S. (2013) “A designed, phase changing RTX-based peptide for efficient bioseparations” BioTechniques 54(4) 197-206.

11. Shur O, Dooley K, Blenner M, Baltimore M, and Banta S. A designed, phase changing RTX-based peptide for efficient bioseparations. Biotechniques. 2013 Apr;54(4):197-8, 200, 202, 204, 206. DOI:10.2144/000114010 |

Campbell, E., Chuang, S., and Banta, S. (2013) “Modular exchange of substrate-binding loops alters both substrate and cofactor specificity in a member of the aldo-keto reductase superfamily” Protein Engineering, Design and Selection 26(3) 181-186.

12. Campbell E, Chuang S, and Banta S. Modular exchange of substrate-binding loops alters both substrate and cofactor specificity in a member of the aldo-keto reductase superfamily. Protein Eng Des Sel. 2013 Mar;26(3):181-6. DOI:10.1093/protein/gzs095 |

Shur, O., and Banta, S. (2013) “Rearranging and concatenating a native RTX domain to understand sequence modularity” Protein Engineering, Design and Selection 26(3) 171-180.

13. Shur O and Banta S. Rearranging and concatenating a native RTX domain to understand sequence modularity. Protein Eng Des Sel. 2013 Mar;26(3):171-80. DOI:10.1093/protein/gzs092 |

Kim, Y.H., Campbell, E., Yu, J., Minteer, S.D., and Banta, S. (2013) “Complete oxidation of methanol in biobattery devices using a hydrogel created from three modified dehydrogenases” Angewandte Chemie International Edition 52(5) 1437-1440 (Designated as a “Hot Paper” by the Editors).

14. Kim YH, Campbell E, Yu J, Minteer SD, and Banta S. Complete oxidation of methanol in biobattery devices using a hydrogel created from three modified dehydrogenases. Angew Chem Int Ed Engl. 2013 Jan 28;52(5):1437-40. DOI:10.1002/anie.201207423 |

Sahin, A., Lin, W.-T., Khunjar, W.O., Chandran, K., Banta, S., and West, A.C., (2013) “Electrochemical reduction of nitrite to ammonia for use in a bioreactor” Journal of the Electrochemical Society 160(1) G19-G26.

doi:10.1149/2.042301jes

Khunjar, W.O., Sahin, A., West, A.C., Chandran, K., and Banta, S. (2012) “Biomass production from electricity using ammonia as an electron carrier in a reverse microbial fuel cell” PLoS ONE 7(9) e44846.

16. Khunjar WO, Sahin A, West AC, Chandran K, and Banta S. Biomass production from electricity using ammonia as an electron carrier in a reverse microbial fuel cell. PLoS One. 2012;7(9):e44846. DOI:10.1371/journal.pone.0044846 |

Felsovalyi, F., Patel, T., Mangiagalli, P., Kumar, S.K., and Banta, S. (2012) “Effect of thermal stability on protein adsorption to silica using homologous aldo-keto reductases” Protein Science 21(8) 1113-1125

17. Felsovalyi F, Patel T, Mangiagalli P, Kumar SK, and Banta S. Effect of thermal stability on protein adsorption to silica using homologous aldo-keto reductases. Protein Sci. 2012 Aug;21(8):1113-25. DOI:10.1002/pro.2099 |

Dooley, K., Kim, Y.H., Lu, H.D., Tu, R., and Banta, S. (2012) “Engineering of an Environmentally Responsive Beta Roll Peptide for Use as a Calcium-Dependent Cross-Linking Domain for Peptide Hydrogel Formation” Biomacromolecules 13(6) 1758-1764.

18. Dooley K, Kim YH, Lu HD, Tu R, and Banta S. Engineering of an environmentally responsive beta roll peptide for use as a calcium-dependent cross-linking domain for peptide hydrogel formation. Biomacromolecules. 2012 Jun 11;13(6):1758-64. DOI:10.1021/bm3002446 |

Campbell, E., Meredith, M., Minteer, S.D., and Banta, S., (2012) “An Enzymatic biofuel cell utilizing a biomimetic cofactor” Chemical Communications 48(13) 1898-1900.

19. Campbell E, Meredith M, Minteer SD, and Banta S. Enzymatic biofuel cells utilizing a biomimetic cofactor. Chem Commun (Camb). 2012 Feb 11;48(13):1898-900. DOI:10.1039/c2cc16156g |

Holland, J.T., Lau, C., Brozik, S., Atanassov, P., and Banta, S., (2011) “Protein engineering of a glucose oxidase for direct electron transfer via targeted gold nanoparticle conjugation” Journal of the American Chemical Society 133(48) 19262-19265.

20. Holland JT, Lau C, Brozik S, Atanassov P, and Banta S. Engineering of glucose oxidase for direct electron transfer via site-specific gold nanoparticle conjugation. J Am Chem Soc. 2011 Dec 7;133(48):19262-5. DOI:10.1021/ja2071237 |

Wu, J., Park, J.P., Dooley, K., Cropek, D.M., West, A.C. and Banta, S. (2011) “Rapid development of new protein biosensors utilizing peptides obtained via phage display” PLoS ONE 6(10) e24948.

21. Wu J, Park JP, Dooley K, Cropek DM, West AC, and Banta S. Rapid development of new protein biosensors utilizing peptides obtained via phage display. PLoS One. 2011;6(10):e24948. DOI:10.1371/journal.pone.0024948 |

Sahin, A., Dooley, K., Cropek, D.M., West, A.C., and Banta, S. (2011) “A dual enzyme electrochemical assay for the detection of organophosphorus compounds using organophosphorus hydrolase and horseradish peroxidase” Sensors and Actuators B: Chemical 158(1) 353-360.

doi:10.1016/j.snb.2011.06.034

Felsovalyi, F., Mangiagalli, P., Bureau, C., Kumar, S.K., and Banta, S. (2011) “Reversibility of the Adsorption of Lysozyme on Silica” Langmuir 27(19) 11873-11882.

23. Felsovalyi F, Mangiagalli P, Bureau C, Kumar SK, and Banta S. Reversibility of the adsorption of lysozyme on silica. Langmuir. 2011 Oct 4;27(19):11873-82. DOI:10.1021/la202585r |

Szilvay, G.R., Brocato, S., Ivnitski, D., Li, C., De La Iglesia, P., Lau, C., Chi, E., Werner-Washburne, M., Banta, S., and Atanassov, P. (2011) “Engineering of a redox protein for DNA-directed assembly” Chemical Communications 47(26) 7464-7466.

24. Szilvay GR, Brocato S, Ivnitski D, Li C, De La Iglesia P, Lau C, Chi E, Werner-Washburne M, Banta S, and Atanassov P. Engineering of a redox protein for DNA-directed assembly. Chem Commun (Camb). 2011 Jul 14;47(26):7464-6. DOI:10.1039/c1cc11951f |

Kang, W.H., Simon, M.J., Gao, S., Banta, S., and Morrison III, B. (2011) “Attenuation of astrocyte activation by TAT mediated-delivery of a peptide JNK inhibitor” Journal of Neurotrauma 28(7) 1219-1228.

25. Kang WH, Simon MJ, Gao S, Banta S, and Morrison B 3rd. Attenuation of astrocyte activation by TAT-mediated delivery of a peptide JNK inhibitor. J Neurotrauma. 2011 Jul;28(7):1219-28. DOI:10.1089/neu.2011.1879 |

Shur, O., Wu, J., Cropek, D.M., and Banta, S. (2011) “Monitoring the conformational changes of an intrinsically disordered peptide using a Quartz Crystal Microbalance” Protein Science 20(5) 925-930.

26. Shur O, Wu J, Cropek DM, and Banta S. Monitoring the conformational changes of an intrinsically disordered peptide using a quartz crystal microbalance. Protein Sci. 2011 May;20(5):925-30. DOI:10.1002/pro.625 |

Gao, S., Simon, M.J., Hue, C.D., Morrison III, B., and Banta, S. (2011) “An unusual cell penetrating peptide identified using a plasmid display-based functional selection platform” ACS Chemical Biology 6(5) 484-491 (Recommended by Faculty of 1000, Featured in Biotechniques News).

27. Gao S, Simon MJ, Hue CD, Morrison B 3rd, and Banta S. An unusual cell penetrating peptide identified using a plasmid display-based functional selection platform. ACS Chem Biol. 2011 May 20;6(5):484-91. DOI:10.1021/cb100423u |

Simon, M.J., Kang, W.H., Gao, S., Banta, S., and Morrison III, B. (2011) “TAT is not capable of transcellular delivery across an intact endothelial monolayer in vitro” Annals of Biomedical Engineering 39(1) 394-401.

28. Simon MJ, Kang WH, Gao S, Banta S, and Morrison B 3rd. TAT is not capable of transcellular delivery across an intact endothelial monolayer in vitro. Ann Biomed Eng. 2011 Jan;39(1):394-401. DOI:10.1007/s10439-010-0144-x |

Glykys, D.J., Szilvay, G.R., Tortosa, P., Suarez Diez, M., Jaramillo, A., and Banta, S. (2011) “Pushing the limits of automatic computational protein design: computational design, expression, and characterization of a large synthetic protein based on a fungal laccase scaffold” Systems and Synthetic Biology 5(1-2) 45-58.

29. Glykys DJ, Szilvay GR, Tortosa P, Suárez Diez M, Jaramillo A, and Banta S. Pushing the limits of automatic computational protein design: design, expression, and characterization of a large synthetic protein based on a fungal laccase scaffold. Syst Synth Biol. 2011 Jun;5(1-2):45-58. DOI:10.1007/s11693-011-9080-9 |

Gao, S., Simon, M.J., Morrison III, B., and Banta, S. (2010) “A plasmid display platform for the selection of peptides exhibiting a functional cell-penetrating phenotype” Biotechnology Progress 26(6) 1796-1800.

30. Gao S, Simon MJ, Morrison B 3rd, and Banta S. A plasmid display platform for the selection of peptides exhibiting a functional cell-penetrating phenotype. Biotechnol Prog. 2010 Nov-Dec;26(6):1796-800. DOI:10.1002/btpr.490 |

Simon, M.J., Kang, W.H., Gao, S., Banta, S., and Morrison III, B. (2010) “Increased delivery of TAT across an endothelial monolayer following ischemic injury” Neuroscience Letters 486(1) 1-4.

31. Simon MJ, Kang WH, Gao S, Banta S, and Morrison B 3rd. Increased delivery of TAT across an endothelial monolayer following ischemic injury. Neurosci Lett. 2010 Dec 3;486(1):1-4. DOI:10.1016/j.neulet.2010.09.029 |

Wu, J., Cropek, D.M., West, A.C. and Banta, S. (2010) “Development of a troponin I biosensor using a peptide obtained through phage display” Analytical Chemistry 82(19) 8235-8243.

32. Wu J, Cropek DM, West AC, and Banta S. Development of a troponin I biosensor using a peptide obtained through phage display. Anal Chem. 2010 Oct 1;82(19):8235-43. DOI:10.1021/ac101657h |

Campbell, E., Wheeldon, I.R., and Banta, S. (2010) “Broadening the cofactor specificity of a thermostable alcohol dehydrogenase using rational protein design introduces novel kinetic transient behavior” Biotechnology and Bioengineering 107(5) 763-774.

33. Campbell E, Wheeldon IR, and Banta S. Broadening the cofactor specificity of a thermostable alcohol dehydrogenase using rational protein design introduces novel kinetic transient behavior. Biotechnol Bioeng. 2010 Dec 1;107(5):763-74. DOI:10.1002/bit.22869 |

Lu, H.D., Wheeldon, I.R., and Banta, S. (2010) “Catalytic biomaterials: Engineering organophosphate hydrolase to form self-assembling enzymatic hydrogels” Protein Engineering, Design and Selection 23(7) 559-566.

34. Lu HD, Wheeldon IR, and Banta S. Catalytic biomaterials: engineering organophosphate hydrolase to form self-assembling enzymatic hydrogels. Protein Eng Des Sel. 2010 Jul;23(7):559-66. DOI:10.1093/protein/gzq026 |

Blenner, M.A., Shur, O., Szilvay, G.R., Cropek, D.M., and Banta, S. (2010) “Calcium-induced folding of a beta roll motif requires C-terminal entropic stabilization” Journal of Molecular Biology 400(2) 244-256.

35. Blenner MA, Shur O, Szilvay GR, Cropek DM, and Banta S. Calcium-induced folding of a beta roll motif requires C-terminal entropic stabilization. J Mol Biol. 2010 Jul 9;400(2):244-56. DOI:10.1016/j.jmb.2010.04.056 |

Banta, S., Wheeldon, I.R., and Blenner, M. (2010) “Protein engineering in the development of functional hydrogels” Annual Review of Biomedical Engineering 12 176-186.

36. Banta S, Wheeldon IR, and Blenner M. Protein engineering in the development of functional hydrogels. Annu Rev Biomed Eng. 2010 Aug 15;12:167-86. DOI:10.1146/annurev-bioeng-070909-105334 |

Park, J.P., Cropek, D.M., and Banta, S. (2010) “High affinity peptides for the recognition of the heart disease biomarker troponin I using phage display” Biotechnology and Bioengineering 105(4) 678-686.

37. Park JP, Cropek DM, and Banta S. High affinity peptides for the recognition of the heart disease biomarker troponin I identified using phage display. Biotechnol Bioeng. 2010 Mar 1;105(4):678-86. DOI:10.1002/bit.22597 |

Szilvay, G.R., Blenner, M.A., Shur, O., Cropek, D.M., and Banta, S. (2009) “A FRET-based method for probing the calcium-dependent conformational behavior of an intrinsically disordered beta roll domain from the Bordetella pertussis adenylate cyclase” Biochemistry 48(47) 11273-11282.

38. Szilvay GR, Blenner MA, Shur O, Cropek DM, and Banta S. A FRET-based method for probing the conformational behavior of an intrinsically disordered repeat domain from Bordetella pertussis adenylate cyclase. Biochemistry. 2009 Dec 1;48(47):11273-82. DOI:10.1021/bi901447j |

Wheeldon, I.R., Campbell, E. and Banta, S. (2009) “A chimeric fusion protein engineered with disparate functionalities— enzymatic activity and self assembly” Journal of Molecular Biology 392(1) 129-142.

39. Wheeldon IR, Campbell E, and Banta S. A chimeric fusion protein engineered with disparate functionalities-enzymatic activity and self-assembly. J Mol Biol. 2009 Sep 11;392(1):129-42. DOI:10.1016/j.jmb.2009.06.075 |

Chockalingam, K., Lu, H.D., and Banta, S. (2009) “Development of a bacteriophage-based system for the selection of short structured peptides” Analytical Biochemistry 388(1) 122-127.

40. Chockalingam K, Lu HD, and Banta S. Development of a bacteriophage-based system for the selection of structured peptides. Anal Biochem. 2009 May 1;388(1):122-7. DOI:10.1016/j.ab.2009.01.042 |

Simon, M.J., Gao, S., Kang, W.H., Banta, S., and Morrison III, B. (2009) “TAT-mediated intracellular protein delivery to primary brain cells is dependent on glycosaminoglycan expression” Biotechnology and Bioengineering 104(1) 10-19.

41. Simon MJ, Gao S, Kang WH, Banta S, and Morrison B 3rd. TAT-mediated intracellular protein delivery to primary brain cells is dependent on glycosaminoglycan expression. Biotechnol Bioeng. 2009 Sep 1;104(1):10-9. DOI:10.1002/bit.22377 |

Gao, S., Simon, M.J., Morrison III, B., and Banta, S. (2009) “Bifunctional chimeric fusion proteins engineered for DNA delivery: Optimization of the protein to DNA ratio” Biochimica et Biophysica Acta (General Subjects) 1790(3) 198-207.

42. Gao S, Simon MJ, Morrison B 3rd, and Banta S. Bifunctional chimeric fusion proteins engineered for DNA delivery: optimization of the protein to DNA ratio. Biochim Biophys Acta. 2009 Mar;1790(3):198-207. DOI:10.1016/j.bbagen.2009.01.001 |

Glykys, D.J., and Banta, S. (2009) “Metabolic control analysis of an enzymatic biofuel cell” Biotechnology and Bioengineering 102(6) 1624-1635.

43. Glykys DJ and Banta S. Metabolic control analysis of an enzymatic biofuel cell. Biotechnol Bioeng. 2009 Apr 15;102(6):1624-35. DOI:10.1002/bit.22199 |

Chen, X.J., West, A.C., Cropek, D.M., and Banta, S. (2008) “Detection of the superoxide radical anion using various alkanethiol monolayers and immobilized cytochrome c” Analytical Chemistry 80(24) 9622-9629.

44. Chen XJ, West AC, Cropek DM, and Banta S. Detection of the superoxide radical anion using various alkanethiol monolayers and immobilized cytochrome c. Anal Chem. 2008 Dec 15;80(24):9622-9. DOI:10.1021/ac800796b |

Wheeldon, I.R., Gallaway, J.W., Calabrese Barton, S., and Banta, S. (2008) “Bioelectrocatalytic hydrogels from electron-conducting metallopolypeptides coassembled with bifunctional enzymatic building blocks” Proceedings of the National Academy of Sciences of the United States of America 105(40) 15275-15280.

45. Wheeldon IR, Gallaway JW, Barton SC, and Banta S. Bioelectrocatalytic hydrogels from electron-conducting metallopolypeptides coassembled with bifunctional enzymatic building blocks. Proc Natl Acad Sci U S A. 2008 Oct 7;105(40):15275-80. DOI:10.1073/pnas.0805249105 |

Blenner M.A., and Banta, S. (2008) “Characterization of the 4D5Flu single chain antibody with a stimulus-responsive elastin-like peptide linker: A potential reporter of peptide linker conformation” Protein Science 17(3) 527-536.

46. Blenner MA and Banta S. Characterization of the 4D5Flu single-chain antibody with a stimulus-responsive elastin-like peptide linker: a potential reporter of peptide linker conformation. Protein Sci. 2008 Mar;17(3):527-36. DOI:10.1110/ps.073257308 |

Gallaway, J., Wheeldon, I.R., Rincon, R., Atanassov, P., Banta, S., and Calabrese Barton, S. (2008) “Oxygen-Reducing Enzyme Cathodes Produced from SLAC, a Small Laccase from Streptomyces coelicolor, For Use at Neutral pH” Biosensors and Bioelectronics 23(8) 1229-1235.

47. Gallaway J, Wheeldon I, Rincon R, Atanassov P, Banta S, and Barton SC. Oxygen-reducing enzyme cathodes produced from SLAC, a small laccase from Streptomyces coelicolor. Biosens Bioelectron. 2008 Mar 14;23(8):1229-35. DOI:10.1016/j.bios.2007.11.004 |

Wheeldon, I.R., Calabrese Barton, S., and Banta, S. (2007) “Bioactive Proteinaceous Hydrogels from Designed Bi-functional Building Blocks” Biomacromolecules 8(10) 2990-2994.

48. Wheeldon IR, Barton SC, and Banta S. Bioactive proteinaceous hydrogels from designed bifunctional building blocks. Biomacromolecules. 2007 Oct;8(10):2990-4. DOI:10.1021/bm700858p |

Chockalingam, K., Blenner, M., and Banta, S. (2007) “Design and Application of Stimulus-Responsive Peptide Systems” Protein Engineering, Design and Selection 20(4) 155-161.

49. Chockalingam K, Blenner M, and Banta S. Design and application of stimulus-responsive peptide systems. Protein Eng Des Sel. 2007 Apr;20(4):155-61. DOI:10.1093/protein/gzm008 |

Harvard University (7 Total)

Casali, M., Banta, S., Zambonelli, C., Megeed, Z., and Yarmush, M.L. (2008) ”Site-directed mutagenesis of the hinge peptide from the Hemagglutinin protein: Enhancement of the pH-responsive conformational change” Protein Engineering, Design and Selection 21(6) 395-404.

50. Casali M, Banta S, Zambonelli C, Megeed Z, and Yarmush ML. Site-directed mutagenesis of the hinge peptide from the hemagglutinin protein: enhancement of the pH-responsive conformational change. Protein Eng Des Sel. 2008 Jun;21(6):395-404. DOI:10.1093/protein/gzn018 |

Banta, S.*, Megeed, Z.*, Casali, M., Rege, K., and Yarmush, M.L. (2007) “Engineering Protein and Peptide Building Blocks for Nanotechnology” Journal of Nanoscience and Nanotechnology 7(2) 387-401 (*co-first authors).

51. Banta S, Megeed Z, Casali M, Rege K, and Yarmush ML. Engineering protein and peptide building blocks for nanotechnology. J Nanosci Nanotechnol. 2007 Feb;7(2):387-401. DOI:10.1166/jnn.2007.153 |

Banta, S.*, Vemula, M.*, Yokoyama, T., Jayaraman, A., Berthiaume, F., and Yarmush, M.L. (2007) “Contribution of Gene Expression to Metabolic Fluxes in Hypermetabolic Livers Induced Through Burn Injury and Cecal Ligation and Puncture in Rats” Biotechnology and Bioengineering 97(1) 118-137 (*co-first authors) (Featured in Editor’s Spotlight ).

52. Banta S, Vemula M, Yokoyama T, Jayaraman A, Berthiaume F, and Yarmush ML. Contribution of gene expression to metabolic fluxes in hypermetabolic livers induced through burn injury and cecal ligation and puncture in rats. Biotechnol Bioeng. 2007 May 1;97(1):118-37. DOI:10.1002/bit.21200 |

Banta, S., Yokoyama, T., Berthiaume, F., and Yarmush, M.L. (2005) “Effects of Dehydroepiandrosterone administration on rat hepatic metabolism following thermal injury” Journal of Surgical Research 127(2) 93-105.

53. Banta S, Yokoyama T, Berthiaume F, and Yarmush ML. Effects of dehydroepiandrosterone administration on rat hepatic metabolism following thermal injury. J Surg Res. 2005 Aug;127(2):93-105. DOI:10.1016/j.jss.2005.01.001 |

Yokoyama, T., Banta, S., Berthiaume, F., Nagrath, D., Tompkins, R.G., and Yarmush, M.L. (2005) “Evolution of intrahepatic carbon, nitrogen, and energy metabolism in a D-galactosamine-induced rat liver failure model” Metabolic Engineering 7(2) 88-103.

54. Yokoyama T, Banta S, Berthiaume F, Nagrath D, Tompkins RG, and Yarmush ML. Evolution of intrahepatic carbon, nitrogen, and energy metabolism in a D-galactosamine-induced rat liver failure model. Metab Eng. 2005 Mar;7(2):88-103. DOI:10.1016/j.ymben.2004.09.003 |

Banta, S., Yokoyama, T., Berthiaume, F., and Yarmush, M.L. (2004) “Quantitative effects of thermal injury and insulin on the metabolism of the skeletal muscle using the perfused rat hindquarter preparation” Biotechnology and Bioengineering 88(5) 613-629.

55. Banta S, Yokoyama T, Berthiaume F, and Yarmush ML. Quantitative effects of thermal injury and insulin on the metabolism of the skeletal muscle using the perfused rat hindquarter preparation. Biotechnol Bioeng. 2004 Dec 5;88(5):613-29. DOI:10.1002/bit.20258 |

Yarmush, M.L. and Banta, S. (2003) “Metabolic Engineering: Advances in Modeling and Intervention in Health and Disease” Annual Review of Biomedical Engineering 5 349-381.

56. Yarmush ML and Banta S. Metabolic engineering: advances in modeling and intervention in health and disease. Annu Rev Biomed Eng. 2003;5:349-81. DOI:10.1146/annurev.bioeng.5.031003.163247 |

Rutgers University (5 Total)

Sanli, G., Banta, S., Anderson, S., and Blaber, M. (2004) “Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase” Protein Science 13(2) 504-512.

57. Sanli G, Banta S, Anderson S, and Blaber M. Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase. Protein Sci. 2004 Feb;13(2):504-12. DOI:10.1110/ps.03450704 |

Banta, S., Boston, M., Jarnagin, A., and Anderson, S. (2002) “Mathematical modeling of in vitro enzymatic production of 2-keto-L-gulonic acid using NAD(H) or NADP(H) as cofactors” Metabolic Engineering 4(4) 273-284.

58. Banta S, Boston M, Jarnagin A, and Anderson S. Mathematical modeling of in vitro enzymatic production of 2-Keto-L-gulonic acid using NAD(H) or NADP(H) as cofactors. Metab Eng. 2002 Oct;4(4):273-84. DOI:10.1006/mben.2002.0231 |

Banta, S., and Anderson, S. (2002) “Verification of a novel NADH-binding motif: Combinatorial mutagenesis of three amino acids in the cofactor binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase” Journal of Molecular Evolution 55(6) 623-631.

59. Banta S and Anderson S. Verification of a novel NADH-binding motif: combinatorial mutagenesis of three amino acids in the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase. J Mol Evol. 2002 Dec;55(6):623-31. DOI:10.1007/s00239-002-2345-x |

Banta, S., Swanson, B.A., Wu, S., Jarnagin, A., and Anderson, S. (2002) “Optimizing an artificial metabolic pathway: Engineering the cofactor specificity of Corynebacterium 2,5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis” Biochemistry 41(20) 6226-6236.

60. Banta S, Swanson BA, Wu S, Jarnagin A, and Anderson S. Optimizing an artificial metabolic pathway: engineering the cofactor specificity of Corynebacterium 2,5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis. Biochemistry. 2002 May 21;41(20):6226-36. DOI:10.1021/bi015987b |

Banta, S., Swanson, B.A., Wu, S., Jarnagin, A., and Anderson, S. (2002) “Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase A” Protein Engineering 15(2) 131-140. (Featured on cover)

61. Banta S, Swanson BA, Wu S, Jarnagin A, and Anderson S. Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase A. Protein Eng. 2002 Feb;15(2):131-40. DOI:10.1093/protein/15.2.131 |

Book Chapters and Other Articles

Campbell, E., and Banta, S. (2014) “Protein Engineering for Enzymatic Fuel Cells” Enzymatic Fuel Cells: From Fundamentals to Applications Edited by H.R. Luckarifft, P.B. Atanassov and G.R. Johnson, Wiley & Sons

Atanassov, P., Apblett, C., Banta, S. Brozik, S., Calabrese Barton, S., Cooney, M., Liaw, B. Y., Mukerjee, S., and Minteer, S.D. (2007) "Enzymatic Biofuel Cells" Interface 16(2) 28-31

Banta, S. (2006) "Protein Engineering" The Biomedical Engineering Handbook, 3rd Ed, Edited by J.D. Bronzino, CRC Press, Boca Raton, Florida.

Banta, S. and Zupke, C. (2006) "Metabolic Engineering" The Biomedical Engineering Handbook, 3rd Ed, Edited by J.D. Bronzino, CRC Press, Boca Raton, Florida.