James Bardwell, Ph.D.

Rowena G Matthews Collegiate Professor, Molecular, Cellular and Developmental Biology
Professor, Molecular, Cellular and Developmental Biology
Professor, Biological Chemistry

4004 Natural Science Bldg. Box 1048



Molecular, Cellular and Developmental Biology, College of LSA
Biological Chemistry, Medical School

Areas of Interest

Proteins start life as linear amino acid sequences and end up as beautifully folded, active structures. Dr. Bardwell's laboratory focuses on recently discovered machinery that drives protein folding in the cell. Two types of folding helpers are being studied, the catalysts responsible for disulfide bond formation and the heat shock proteins, which chaperone protein folding. Powerful genetic, structural, and biophysical tools are being used to generate a detailed picture of how these folding machines work.

Dr. Bardwell received his Ph.D. from the University of Wisconsin at Madison in 1987 and was a post doctoral fellow at Harvard Medical School. He has been a Fellow of the Alexander von Humboldt Foundation and held a Visiting Professor appointment in Regensburg, Germany.

Laboratory Staff

Scott Horowitz, Postdoctoral Fellow
Christopher Lennon, Postdoctoral Fellow

Honors & Awards

1999 Literature, Science and Arts Excellence in Research Award
1997-2001 Pew Scholar
1993-1995 Alexander von Humboldt Fellowship
1989-1993 Helen Hay Whitney Fellowship, NSERC Postgraduate Scholarship

Published Articles or Reviews

Shu Quan, Annie Hiniker, Jean-Francois Collet, and James C.A. Bardwell. (January 2013) Isolation of bacteria Envelope Proteins. Methods in Molecular Biology. 966, 359-366. (Pubmed)

Tsinatkeab T. Hailu, Linda Foit, James C.A. Bardwell. (March 2012) In vivo detection and quantification of chemicals that enchance protein stability. Analytical Biochemistry. 434, 181-186. (Pubmed)

Evans ML, Schmidt JC, Ilbert M, Doyle SM, Quan S, Bardwell JC, Jakob U, Wickner S, Chapman MR. (January 2012) E. coli chaperones DnaK, Hsp33, and Spy inhibit bacterial functional amyloid assembly. Prion. 1;5(4). (Pubmed)

Shu Quan, and James C.A. Bardwell. (January 2012) Chaperone Discovery. Bioessays. 34, 973-981. (Pubmed)

Ren G, Bardwell JC. (June 2011) Engineered pathways for correct disulfide bond oxidation. Antioxid Redox Signal. 14(12):2399-412. (Pubmed)

Quan S, Koldewey P, Tapley T, Kirsch N, Ruane KM, Pfizenmaier J, Shi R, Hofmann S, Foit L, Ren G, Jakob U, Xu Z, Cygler M, Bardwell JC. (March 2011) Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat Struct Mol Biol. 18(3):262-9. (Pubmed)

Foit L, Mueller-Schickert A, Mamathambika BS, Gleiter S, Klaska CL, Ren G, Bardwell JC. (March 2011) Genetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor. Antioxid Redox Signal. 14(6):973-84. (Pubmed)

Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. (January 2010) Protein refolding by pH-triggered chaperone binding and release. Proc Natl Acad Sci U S A. 107(3):1071-6. (Pubmed)

Foit L, Morgan GJ, Kern MJ, Steimer LR, von Hacht AA, Titchmarsh J, Warriner SL, Radford SE, Bardwell JC.. (December 2009) Optimizing protein stability in vivo. Mol Cell. Dec 11;36(5):861-71. (Pubmed)

Ren G, Stephan D, Xu Z, Zheng Y, Tang D, Harrison RS, Kurz M, Jarrott R, Shouldice SR, Hiniker A, Martin JL, Heras B, Bardwell JC.. (May 2009) Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J Biol Chem. 284(15):10150-9. (Pubmed)

Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC.. (April 2009) Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Proc Natl Acad Sci U S A. 106(14):5557-62. (Pubmed)

Mamathambika BS, Bardwell JC. (April 2008) Disulfide-linked protein folding pathways. Annu Rev Cell Dev Biol. 24:211-35. Review. (Pubmed)

Pan JL, Sliskovic I, Bardwell JC.. (April 2008) Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway. J Mol Biol. 377(5):1433-42. (Pubmed)

Vertommen D, Depuydt M, Pan J, Leverrier P, Knoops L, Szikora JP, Messens J, Bardwell JC, Collet JF.. (January 2008) The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner. Mol Microbiol. 67(2):336-49. (Pubmed)

Gleiter S, Bardwell JC.. (January 2008) Disulfide bond isomerization in prokaryotes. Biochim Biophys Acta. 1783(4):530-4. (Pubmed)

Masip L, Klein-Marcuschamer D, Quan S, Bardwel JC, Georgiou G. (January 2008) Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant. J Biol Chem. 283(2):840-8. (Pubmed)

Quan S, Schneider I, Pan J, Von Hacht A, Bardwell JC. (September 2007) The CXXC motif is more than a redox rheostat. J Biol Chem. 282(39):38823-33. (Pubmed)

Tapley TL, Eichner T, Gleiter S, Ballou DP, Bardwell JC. (April 2007) Kinetic characterization of the disulfide bond-forming enzyme DsbB. J Biol Chem. 282(14):10263-71. (Pubmed)

Hiniker A, Vertommen D, Bardwell JC, Collet JF. (November 2006) Evidence for Conformational Changes within DsbD: Possible Role for Membrane-Embedded Proline Residues. J. Bacteriol. Oct;188(20):7317-20. (Pubmed)

Pan JL, Bardwell JC. (October 2006) The origami of thioredoxin-like folds. Protein Sci. Oct;15(10):2217-27. (Pubmed)

Hiniker A, Collet JF, Bardwell JC. (October 2005) Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. J. Biol. Chem. Oct 7;280(40):33785-91. Epub 2005 Aug 8. (Pubmed)

Collet JF, Peisach D, Bardwell JC, Xu Z. (July 2005) The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutant. Protein Sci. Jul;14(7):1863-9. (Pubmed)

Collet, J-F. and Bardwell J.C.A. . (April 2005) The Catalysis of disulfide bond formation in Prokaryotes. In Protein Folding Handbook, Buchner/Kiefhaber Eds. Wiley-VCH.

Tan, J. Lu Y., and Bardwell J.C.A.. (March 2005) Mutational Anlysis of the disulfide catalysts DsbA and DsbB. J.Bacteriol. 187: 1504-10. (Pubmed)

Bardwell J.C.A.. (February 2005) The dance of disulfide formation. Nat. Struct. Mol. Biol. 11: 582-3. (Pubmed)

Bardwell J.C.A.. (January 2005) Thiol modifications in a snapshot. Nat. Biotechno. 23: 42-3. (Pubmed)

Nakamoto H, Bardwell JC.. (December 2004) Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochim. Biophys. Acta. Nov 11;1694(1-3):111-9. (Pubmed)

Tan JT, Bardwell JC.. (November 2004) Key players involved in bacterial disulfide-bond formation. Chembiochem. Nov 5;5(11):1479-87. (Pubmed)

Hiniker A, Bardwell JC.. (October 2004) Disulfide relays between and within proteins: the Ero1p structure. Trends Biochem. Sci. Oct;29(10):516-9. (Pubmed)

Kadokura H, Tian H, Zander T, Bardwell JC, and Beckwith J. (August 2004) Snapshots of DsbA in Action: detection of proteins in the process of oxidative folding. Science. 303(5657):534-537. (Pubmed)

Masip L, Pan JL, Haldar S, Penner-Hahn J, Georgiou G, Bardwell JC, and Collet Jean-Francois. (August 2004) An Engineered pathway for the formation of protein disulfide bonds. Science. 303:1185 - 1189. (Pubmed)

Hiniker A and Bardwell JC. (July 2004) in vivo substrate specificity of periplasmic disulfide oxidoreductases. J. Biol. Chem. Mar 26;279(13):12967-73. Epub 2004 Jan 15. (Pubmed)

Collet J-F. and Bardwell J.C.A.. (December 2003) Oxidative folding in Bacteria. NATO Science series. (Pubmed)

J.F., D'Souza J.C., Jakob U., Bardwell J.C.. (November 2003) Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. J. Biol. Chem. 278(46):45325-32. (Pubmed)

Regeimbal J., Gleiter, S., Trumpower, B.L., Yu, C.A., Diwakar, M., Ballou, D.P., and Bardwell, J.C.. (November 2003) Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proc. Nat. Acad. of Sci USA. 100(24):13779-84. (Pubmed)

Goulding CW, Apostol MI, Gleiter S, Parseghian A, Bardwell J, Gennaro M, and Eisenberg D. (November 2003) Gram-positive DsbE proteins function differently from gram-negative DsbE homologs: A structure function analysis of DsbE from Mycobacterium tuberculosis. J. Biol. Chem. 2004 Jan 30;279(5):3516-24. Epub 2003 Nov 3. (Pubmed)

Hiniker A. and Bardwell J.C.. (February 2003) Disulfide bond isomerization in prokaryotes. Biochemistry. Feb 11;42(5): 1179-85. (Pubmed)

For a complete list of this person’s PubMed publications, click HERE

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