Publications – Bardwell Lab


2019 – 201820172016 2015 2014 2013 2012 2011 2010 2009 20082007 2006 2005 2004 2003 20022001 2000 1999 1998 1997 1995 1994 1993 1992 1991 1990 1989 1988 1987 1986 1985 1984


2021 Publications

pdf_icon Rishav M, Gadkari VV, Meinen BA, van Mierlo CPM, Ruotolo BT, Bardwell JCA. Mechanism of the small ATP-independent chaperone Spy is substrate specific. Nature Communications. 2021 February 8.

pdf_icon Dulchavsky M, Clark CT, Bardwell JCA, Stull F. A cytochrome c is the natural electron acceptor for nicotine oxidoreductase. Nature Chemical Biology. 2021 January 11.

2020 Publications

pdf_icon He W, Zhang J, Sachsenhauser V, Wang L, Bardwell JCA, Quan S. Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity. J Biol Chem. 2020 Aug 17:jbc.RA119.012300. doi: 10.1074/jbc.RA119.012300. Online ahead of print. Pubmed.

pdf_icon Lee C, Betschinger P, Wu K, Zyla DS, Glockshuber R, Bardwell JCA. A metabolite binding protein moonlights as a bile-responsive chaperone. EMBO J. 2020 Sep 3;e104231. doi: 10.15252/embj.2019104231. Online ahead of print.  Pubmed.

pdf_icon Sachsenhauser V, Deng X, Kim HH, Jankovic M, Bardwell JCA. Yeast Tripartite Biosensors Sensitive to Protein Stability and Aggregation Propensity. ACS Chem Biol. 2020 Apr 17;15(4):1078-1088. doi: 10.1021/acschembio.0c00083. Epub 2020 Mar 10. Pubmed.

2019 Publications

pdf_icon Rocchio S, Duman R, Omari KE, Mykhalylyk V, Orr C, Yan Z, Salmon L, Wagner A, Bardwell JCA, Horowitz S. Identifying dynamic ,partially occupied residues using anomalous scatteringActa Crys 2019. D75, 1084-1095.

pdf_icon Meinen BA, Gadkari VV, Stull F, Ruotolo BT, Bardwell JCA. SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins. Proc Natl Acad Sci U S A. 2019 Oct 28. pii: 201913316. doi: 10.1073/pnas.1913316116. Pubmed.

pdf_icon Wu K, Stull F, Lee C, Bardwell JCA. Protein folding while chaperone bound is dependent on weak interactions. Nat Commun 2019 Oct 23;10(1):4833. doi: 10.1038/s41467-019-12774-6. Pubmed.
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pdf_icon Yan Z, Hussain S, Xu W, Bernstein HD, Bardwell JCA. Chaperone OsmY facilitates the biogenesis of a major family of autotransporters. Mol Microbiol 2019 Aug 1 doi: 10.1111/mmi.14358. Pubmed.

pdf_icon Teixeira F, Tse E, Castro H, Makepeace KAT, Meinen BA, Borchers CH, Poole LB, Bardwell JC, Tomás AM, Southworth DR, Jakob U. Chaperone activation and client binding of a 2-cysteine peroxiredoxin. Nat Commun. 2019 Feb 8;10(1):659. doi: 10.1038/s41467-019-08565-8. Pubmed.


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2018 Publications

pdf_icon Stull F, Hipp H, Stockbridge RB, Bardwell JCA. In vivo chloride concentrations surge to proteotoxic levels during acid stress. Nature Chemical Biology 2018 Oct; 14, 1051-1058. Pubmed  This paper was the subject of a News and Views  citation in Nature Chemical Biology by Colin Kleanthous. 

pdf_icon Cristie-David AS, Koldewey P, Meinen BA, Bardwell JCA, Marsh ENG. Elaborating a coiled coil-assembled octahedral protein cage with additional protein domains. Protein Sci. 2018 Aug 16. doi: 10.1002/pro.3497. Pubmed

pdf_icon Lee C, Kim H, Bardwell JCA. Electrostatic interactions are important for chaperone-client interaction in vivo. Microbiology. 2018 Jul;164(7):992-997. doi: 10.1099/mic.0.000676. Pubmed

pdf_icon Salmon L, Ahlstrom LS, Bardwell JCA, Horowitz S. Selecting Conformational Ensembles Using Residual Electron and Anomalous Density (READ). Methods Mol Biol. 2018;1764:491-504. doi: 10.1007/978-1-4939-7759-8_31 Pubmed

pdf_icon Stull F, Betton J, Bardwell J. 2018. Periplasmic Chaperones and Prolyl Isomerases, EcoSal Plus 2018; doi:10.1128/ecosalplus.ESP-0005-2018. Pubmed.

pdf_icon Stull F, Bardwell JC. Folding against the wind. Nature Chemical Biology 2018 Apr;14(4):329-330. doi: 10.1038/s41589-018-0016-5. Pubmed

pdf_icon Sachsenhauser V, Bardwell JC. Directed evolution to improve protein folding in vivo. Curr Opin Struct Biol. 2018 Feb;48:117-123. doi: 10.1016/ Pubmed

pdf_icon Salmon L, Stull F, Sayle S, Cato C, Akgül Ş, Foit L, Ahlstrom LS, Eisenmesser EZ, Al-Hashimi HM, Bardwell JCA, Horowitz S. The Mechanism of HdeA Unfolding and Chaperone ActivationJ Mol Biol. 2018 Jan 5;430(1):33-40. doi: 10.1016/j.jmb.2017.11.002. Epub 2017 Nov 11. Pubmed

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2017 Publications

pdf_icon Badieyan S, Sciore A, Eschweiler J, Koldewey P, Cristie-David AS, Ruotolo BT, Bardwell JCA, Su M, Marsh N. Symmetry-directed Self-assembly of a Tetrahedral Protein Cage Mediated by De Novo-designed Coiled Coils. Chembiochem. 2017 Aug 1. doi: 10.1002/cbic.201700406. [Epub ahead of print] Pubmed 

pdf_icon Horowitz S, Koldewey P, Stull F, Bardwell JC. Folding while bound to chaperones. Curr Opin Struct Biol. 2017 Jul 19;48:1-5. doi: 10.1016/ [Epub ahead of print] Pubmed

pdf_icon Koldewey P, Horowitz S, Bardwell JCA. Chaperone-client interactions: Non-specificity engenders multifunctionality. J Biol Chem. 2017 Jul 21;292(29):12010-12017. doi: 10.1074/jbc.R117.796862. Epub 2017 Jun 15. Pubmed

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2016 Publications

pdf_icon Dahl JU, Koldewey P, Bardwell JC, Jakob U. Detection of the pH-dependent Activity of Escherichia coli Chaprone HdeB In Vitro and In Vivo. J Vis Exp. 2016 Oct 23;(116). doi: 10.3791/54527. Pubmed 

pdf_icon Horowitz S, Bardwell JC. (2016) RNAs as Chaperones. RNA Biology. 2016 Oct 28:1-4. [Epub ahead of print]Pubmed

pdf_icon Johansson KE, Johansen NT, Christensen S, Horowitz S, Bardwell JC, Olsen JG, Willemoës M, Lindorff-Larsen K, Ferkinghoff-Borg J, Hamelryck T, Winther JR. (2016) Computational redesign of thioredoxin is hypersensitive towards minor conformational changes in the backbone template. J Mol Biol. 2016 Sep 19. pii: S0022-2836(16)30378-3. doi: 10.1016/j.jmb.2016.09.013. [Epub ahead of print]. Pubmed

pdf_icon Horowitz S, Koepnick B, Martin R, Tymieniecki A, Winburn AA, Cooper S, Flatten J, Rogawski DS, Koropatkin NM, Hailu TT, Jain N, Koldewey P, Ahlstrom LS, Chapman MR, Sikkema AP, Skiba MA, Maloney FP, Beinlich FR; Foldit Players; University of Michigan students, Popović Z, Baker D, Khatib F, Bardwell JC. (2016). Determining crystal structures through crowdsourcing and coursework. Nat. Commun.2016 Sep 16;7:12549. doi: 10.1038/ncomms12549.Pubmed
This paper was the subject of a Marketplace Tech interview.

pdf_icon Sciore A, Su M, Koldewey P, Eschweiler JD, Diffley KA, Linhares BM, Ruotolo BT, Bardwell JC, Skiniotis G, Marsh EN. (2016) Flexible, symmetry-directted approach to assembling protein cages.PNAS. 2016 Aug 2;113(31):8681-6. doi: 10.1073/pnas.1606013113. Epub 2016 Jul 18. Pubmed

pdf_icon Loïc Salmon, Logan S. Ahlstrom, Scott Horowitz, Alex Dickson,Charles L. Brooks, and James C. A. Bardwell. (2016) Capturing a dynamic chaperone-substrate interaction using NMR-informed molecular modelingJACS. DOI:10.1021/jacs.6b02382 Epub July 14, 2016 (Pubmed)

pdf_icon Koldewey P, Stull F, Horowitz S, Martin R, Bardwell JCA. (2016) Forces Driving Chaperone Action.  Cell. 2016 Jun 9. pii: S0092-8674(16)30657-2. doi: 10.1016/j.cell.2016.05.054. [Epub ahead of print](Pubmed)   This paper was the subject of a News and Viewspdf_icon  citation in NSMB by Patricia L. Clark and Adrian H. Elcock.

pdf_icon Horowitz S, Salmon L, Koldewey P, Ahlstrom L, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL, Bardwell JCA. (2016) Visualizing Chaperone-assisted Folding. Nature Struct. Mol. Biol. 2016 Jul;23(7):691-7. doi: 10.1038/nsmb.3237. Epub 2016 May 30. (Pubmed)  This paper was the subject of a News and Views  citation in NSMB by Patricia L. Clark and Adrian H. Elcock.
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pdf_icon Docter BE, Horowitz S, Gray MJ, Jakob U, and Bardwell JCA (2016) Do Nucleic Acids Moonlight as Molecular Chaperones? Nucleic Acids Research. 2016 Jun 2;44(10):4835-45. doi: 10.1093/nar/gkw291. Epub 2016 Apr 21. (Pubmed) Access the recommendation on F1000Prime

pdf_icon Groitl B, Horowitz S, Makepeace KA, Petrotchenko EV, Borchers CH, Reichmann D, Bardwell JC, Jakob U. (2016) Protein unfolding as a switch from self-recognition to high-affinity client binding.  Nat Commun. 2016 Jan 20;7:10357. doi: 10.1038/ncomms10357. PMID: 26787517 (Pubmed)

pdf_icon Stull F, Koldewey P, Humes JR, Radford SE, Bardwell JC. (2016). Substrate protein folds while it is bound to the ATP-independent chaperone Spy.  Nat Struct Mol Biol. 2016 Jan;23(1):53-8. doi: 10.1038/nsmb.3133. Epub 2015 Nov 30. PMID: 26619265 (Pubmed)   This paper was the subject of a News and Views  citation in NSMB by Patricia L. Clark and Adrian H. Elcock.

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2015 Publications

pdf_icon Chatelle C, Kraemer S, Ren G, Chmura H, Marechal N, Boyd D, Roggemans C, Ke N, Riggs P, Bardwell J, Berkmen M. (2015) Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase. Antioxid Redox Signal. 2015 Oct 20;23(12):945-57. doi: 10.1089/ars.2014.6235. Epub 2015 Jul 20. (Pubmed)

pdf_icon Lennon CW, Thamsen M, Friman ET, Cacciaglia A, Sachsenhauser V, Sorgenfrei FA, Wasik MA, Bardwell JC. (2015) Folding Optimization In Vivo Uncovers New Chaperones. J Mol Biol. Sep 11;427(18):2983-94. doi: 10.1016/j.jmb.2015.05.013. Epub 2015 May 21. PMID: 26003922 (Pubmed)

pdf_icon Dahl JU, Koldewey P, Salmon L, Horowitz S, Bardwell JC, Jakob U. (2015) HdeB functions as an acid-protective chaperone in bacteria. J Biol Chem. 2015 Apr 17;290(16):9950. PMID: 25888567 (Pubmed)

pdf_icon Bardwell JC, Foit L, Malik A, Baumann T, Kern M. (2015) Methods and Compositions for Increasing Biological Molecule Stability.  United States Patent No. US 8,986,997 B2.  2015 Mar 24.

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2014 Publications

pdf_icon Malik A, Mueller-Schickert A, Bardwell JC. (2014) Cytosolic selection systems to study protein stability. J Bacteriol.J Bacteriol. 2014 Dec;196(24):4333-43. doi: 10.1128/JB.02215-14. Epub 2014 Sep 29. PMID: 25266385. (Pubmed)

pdf_icon Horowitz S, Koldewey P, Bardwell JC. (2014) Undergraduates improve upon published crystal structure in class assignment.Biochemistry and Molecular Biology Education. Biochem Mol Biol Educ. 2014 Sep-Oct;42(5):398-404. doi: 10.1002/bmb.20811. Epub 2014 Jul 18. PMID: 25044946

pdf_icon Gray MJ, Wholey WY, Wagner NO, Cremers CM, Mueller-Schickert A, Hock NT, Krieger AG, Smith EM, Bender RA, Bardwell JC, Jakob U. (2014) Polyphosphate is a primordial chaperone. Mol Cell. 6;53(5):689-99. Epub 2014 Feb 20. PMID:24560923. (Pubmed)Access the recommendation on F1000Prime

pdf_icon Bardwell JC, Schreiber G. (2014) Editorial overview: Folding and binding. Curr Opin Struct Biol. 2014 Feb;24:viii-x. Epub 2014 Feb 6. No abstract available. PMID:24508004. (Pubmed)

pdf_icon Quan S, Wang L, Petrotchenko EV, Makepeace KA, Horowitz S, Yang J, Zhang Y, Borchers CH, Bardwell JC. (2014) Super Spy variants implicate flexibility in chaperone action. Elife. 2014;3:e01584. Epub 2014 Feb 4. PMID:24497545. (Pubmed)
“Discussed in the podcast Flexible Friends”

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2013 Publications

pdf_icon Foit L, George JS, Zhang BW, Brooks CL 3rd, Bardwell JC. (2013)  Chaperone activation by unfolding. Proc Natl Acad Sci U S A. 110(14):E1254-62. Epub 2013 Mar 4. PMCID:PMC3619340. (Pubmed) This paper was the subject of a Commentarypdf_icon  by Karan S. Hingorani and Lila M. Gierasch. Access the recommendation on F1000Prime

pdf_icon Hailu TT, Foit L, Bardwell JC.. (2013)   In vivo detection and quantification of chemicals that enhance protein stability. Anal Biochem. 1;434(1):181-6. Epub 2012 Dec 5. PMCID:PMC3670414. . (Pubmed)

pdf_icon Foit L, Bardwell JC. . (2013)  A tripartite fusion system for the selection of protein variants with increased stability in vivo.Methods Mol Biol. 978:1-20. PMID:23423885. (Pubmed)

pdf_icon Quan S, Hiniker A, Collet JF, Bardwell JC. (2013) Isolation of bacteria envelope proteins. Methods Mol Biol. 966:359-66. PMID: 23299746. (Pubmed)

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2012 Publications

pdf_icon Evans ML, Schmidt JC, Ilbert M, Doyle SM, Quan S, Bardwell JC, Jakob U, Wickner S, Chapman MR. (2012) E. coli chaperones DnaK, Hsp33, and Spy inhibit bacterial functional amyloid assembly. Prion. 2011 Oct-Dec;5(4):323-34. doi: 10.4161/pri.18555. Epub 2011 Oct 1.
PMID: 22156728(Pubmed)

pdf_icon Bardwell JC, Jakob U . (2012) Conditional disorder in chaperone action. Trends Biochem Sci. 37(12):517-25. PMCID:PMC3508372.

pdf_icon Quan S, Bardwell JC. (2012) Chaperone discovery. Bioessays. 34(11):973-81. PMID: 22968800.

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2011 Publications

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

pdf_icon 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. (2011) Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat Struct Mol Biol. 18(3):262-9. (PubmedThis paper was the subject of a  “News and Views”  citation in Nature by Evan T. Powers and Willian E. Balch.Access the recommendation on F1000Prime

pdf_icon Foit L, Mueller-Schickert A, Mamathambika BS, Gleiter S, Klaska CL, Ren G, Bardwell JC. (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)

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2010 Publications

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

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2009 Publications

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

pdf_icon 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.. (2009) Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J Biol Chem. 284(15):10150-9. (Pubmed)

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

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2008 Publications

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

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

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

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

pdf_icon Masip L, Klein-Marcuschamer D, Quan S, Bardwell JC, Georgiou G. (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)

pdf_icon Mac TT, von Hacht A, Hung KC, Dutton RJ, Boyd D, Bardwell JC, Ulmer TS. (2008) Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase. J Biol Chem. 283:824-832. PMID:18003611.

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2007 Publications

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

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

pdf_icon Hiniker A, Ren G, Heras B, Zheng Y, Laurinec S, Jobson RW, Stuckey JA, Martin JL, Bardwell JC. (2007) Laboratory evolution of one disulfide isomerase to resemble another. Proc Natl Acad Sci USA. 104:11670-11675. PMCID: PMC1906722.Access the recommendation on F1000Prime

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2006 Publications

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

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

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2005 Publications

pdf_icon Hiniker A, Collet JF, Bardwell JC. (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)

pdf_icon Collet JF, Peisach D, Bardwell JC, Xu Z. (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)

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

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

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

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

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2004 Publications

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

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

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

pdf_icon Kadokura H, Tian H, Zander T, Bardwell JC, and Beckwith J. (2004) Snapshots of DsbA in Action: detection of proteins in the process of oxidative folding. Science. 303(5657):534-537. (Pubmed)Access the recommendation on F1000Prime

pdf_icon Masip L, Pan JL, Haldar S, Penner-Hahn J, Georgiou G, Bardwell JC, and Collet Jean-Francois. (2004) An Engineered pathway for the formation of protein disulfide bonds. Science. 303:1185 – 1189. (Pubmed)Access the recommendation on F1000Prime

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

pdf_icon Hiniker, A. and Bardwell J.C.A.. (2004) Disulfide relays between and within proteins: the Erolp structure. Trends in Biochem. Sci. 29:516-9.

pdf_icon Nakamoto, H. and Bardwell J.C.A.. (2004) Catalysis of Disulfide Bond Formation and Isomerization in the Bacterial Periplasm.Biochim. Biophys. Acta. 1694:111-9.

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2003 Publications

pdf_icon Regeimbal J, Gleiter S, Trumpower BL, Yu CA, Diwakar M, Ballou DP, Bardwell JC. (2003) Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proc Natl Acad Sci U S A. 2003 Nov 25; 100(24):13779-84.Access the recommendation on F1000Prime

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

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

Goulding CW, Apostol MI, Gleiter S, Parseghian A, Bardwell J, Gennaro M, and Eisenberg D. (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.. (2003) Disulfide bond isomerization in prokaryotes. Biochemistry. Feb 11;42(5): 1179-85. (Pubmed)

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2002 Publications

Bardwell J.C.. (2002) Disulfide bond formation, a race between FAD and oxygen. Dev. Cell. Dec;3(6):758-60. (Pubmed)

Regeimbal J. and Bardwell J.C.. (2002) DsbB catalyzes disulfide bond formation de novo. J. Biol. Chem. Sep 6;277(36):32706-13. (Pubmed)Access the recommendation on F1000Prime

Collet J.F., Reimer J., Bader M.W., and Bardwell J.C.. (2002) Reconstitution of a disulfide isomerization system. J. Biol. Chem. Jul 26;277(30):26886-92. (Pubmed)

Tan J., Jakob U., and Bardwell J.C.. (2002) Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA. J. Bacteriol. May;184(10):2692-8. (Pubmed)

Collet J.F. and Bardwell J.C.. (2002) Oxidative protein folding in bacteria. Mol. Microbiol. Apr;44(1):1-8. (Pubmed)

Xie T, Yu L, Bader MW, Bardwell JC, and Yu CA. (2002) Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. J. Biol. Chem. Jan 18;277(3):1649-52. (Pubmed)

Collet J.F. and Bardwell J.C.. (2002) Disulfides out of thin air. Nat. Struct. Biol. . Jan;9(1):2-3. (Pubmed)

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2001 Publications

Bader, MW and Bardwell JC. (2001) Catalysis of disulfide bond formation and isomerization in Escherichia coli. Adv. Protein Chem. 59:283-301. (Pubmed)

Goldstone D., Haebel P.W., Katzen F., Bader M.W., Bardwell J.C., Beckwith J., and Metcalf P. . (2001) DsbC activation by the N-terminal domain of DsbD. Proc. Natl. Acad. Sci. USA. . Aug 14;98(17):9551-6. (Pubmed)

Graumann J, Lilie H, Tang X, Tucker KA, Hoffman JH, Vijayalakshmi J, Saper M, Bardwell JC, and Jakob U. (2001) Activation of the redox-regulated molecular chaperone Hsp33-a two-step mechanism. Structure (Camb). May 9;9(5):377-87. (Pubmed)

Bader M.W., Hiniker A., Regeimbal J., Goldstone D., Haebel P.W., Riemer J., Metcalf P., and Bardwell J.C.. (2001) Turning a disulfide into an oxidase: DsbC mutants that imitate DsbA. EMBO J. Apr 2;20(7):1555-62. (Pubmed)

Bessette PH, Qiu J, Bardwell JC, Swartz JR, and Georgiou G. (2001) Effects of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide protein in Escherichia coli. J. Bacteriol. Feb;183(3):980-8. (Pubmed)

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2000 Publications

Jakob U, Eser M, and Bardwell JC. (2000) Redox switch of hsp33 has a novel zinc-binding motif. J. Biol. Chem. Dec 8;275(34):38302-10. (Pubmed)

Kadokura H., Bader M., Tian H., Bardwell J.C., and Beckwith J. (2000) Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain in Escherichia coli. Proc. Natl. Acad. Sci. USA. Sep 26;97(20):10884-9. (Pubmed)

Bader M.W., Xie T., Yu C.A., and Bardwell J.C.. (2000) Disulfide bonds are generated by quinone reduction. J Biol Chem.Aug 25;275(34):26082-8. (Pubmed)

Bugl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA, Bardwell JC, and Jakob U. (2000) RNA methylation under heat shock control. Mol. Cell. Aug;6(2):349-60. (Pubmed)

Shao F., Bader M.W., Jakob U., and Bardwell J.C.. (2000) DsbG, a protein disulfide isomerase with chaperone activtity. J. Biol. Chem. May 5;275(18):13349-52. (Pubmed)

Wong C, Sridhara S, Bardwell JC, and Jakob U. (2000) Heating greatly speeds Coomassie blue staining and destaining.Biotechniques. Mar;28(3):426-28,430,432. (Pubmed)

Korber P., Stahl J.M., Nierhaus K.H., and Bardwell J.C.. (2000) Hsp15: a ribosome-associated heat shock protein. EMBO J.Feb 15;19(4):741-8. (Pubmed)

Staker BL, Korber P, Bardwell JC, and Saper MA.. (2000) Structure of Hsp15 reveals a novel RNA-binding motif. EMBO J.Feb 15;19(4):749-57. (Pubmed)

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1999 Publications

Bader M, Winther JR, and Bardwell JC. (1999) Protein oxidation: prime suspect found ‘not guilty’. Nat Cell Biol. . Jul;1(3):E57-8. (Pubmed)

Bader M., Muse W., Ballou D.P., Gassner C., and Bardwell J.C.. (1999) Oxidative protein folding is driven by the electron transport chain. Cell. Jul 23;98(2):217-27. (Pubmed)

Jakob U., Muse W., Eser M., and Bardwell J.C.. (1999) Chaperone activity with a redox switch. Cell. Feb 5;96(3):341-52. (Pubmed)

Korber P., Zander T., Herschlag D., and Bardwell J.C.. (1999) A new heat shock protein that binds nucleic acids. J Biol Chem. Jan 1;274(1):249-56. (Pubmed)

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1998 Publications

Guddat LW, Bardwell JC, and Martin JL.. (1998) Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stability. Structure. Jun 15;6(6):757-767. (Pubmed)

Bader M, Muse W, Zander T, and Bardwell J.. (1998) Reconstitution of a protein disulfide catalytic system. J Biol Chem. Apr 24;273(17):10302-7. (Pubmed)

Zander T, Phadke ND, and Bardwell JC. (1998) Disulfide bond catalysts in Escherichia coli. Methods Enzymol. 290:59-74. (Pubmed)

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1997 Publications

Guddat LW, Bardwell JC, Glockshuber R, Huber-Wunderlich M, Zander T, and Martin JL. (1997) Structural analysis of three His32 mutants of DsbA: support for an electrostatic role in His32 in DsbA stability. Protein Sci. Sep;6(9):1893-900. (Pubmed)

Guddat LW, Bardwell JC, Zander T, and Martin JL.. (1997) The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding. Protein Sci. Jun;6(6):1148-56. (Pubmed)

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1995 Publications

Grauschopf U, Winther JR, Korber P, Zander T, Dallinger P, and Bardwell JC. (1995) Why is DsbA such an oxidizing disulfide catalyst?. Cell. Dec 15;83(6):947-55. (Pubmed)

Jakob U, Meyer I, Bugl H, Andre S, Bardwell JC, and Buchner J.. (1995) Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function. J Biol Chem. Jun 16;270(24):14412-9. (Pubmed)

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1994 Publications

Bardwell JC.. (1994) Building bridges:disulphide bond formation in the cell. Mol Microbiol. Oct;14(2):199-205. (Pubmed)

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1993 Publications

Bardwell JC and Beckwith J.. (1993) The bonds that tie: catalyzed disulfide bond formation. Cell. Sep 10;74(5):769-71. (Pubmed)

Zapun A, Bardwell JC, and Creighton TE. (1993) The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry. May 18;32(19):5082-92. (Pubmed)

Martin JL, Waksman G, Bardwell JC, Beckwith J, and Kuriyan J.. (1993) Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo. J Mol Biol. Apr 5;230(3):1097-100. (Pubmed)

Bardwell JC, Lee JO, Jander G, Martin N, Belin D, and Beckwith J.. (1993) A pathway for disulfide bond formation in vivo.Proc Natl Acad Sci USA. Feb 1;90(3):1038-42. (Pubmed)

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1991 Publications

Bardwell JC, McGovern K, and Beckwith J.. (1991) Identification of a protein required for disulfide bond formation in vivo. Cell.Nov 1;67(3):581-9. (Pubmed)

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1990 Publications

Yeung T, Mullin DA, Chen KS, Craig EA, Bardwell JC, and Walker JR. (1990) Sequence and expression of the Escherichia coli recR locus. J Bacteriol. Oct;172(10):6042-7. (Pubmed)

Chen SM, Takiff HE, Barber AM, Dubois GC, Bardwell JC, and Court DL.. (1990) Expression and characterization of RNase III and Era proteins. Products of the rnc operon of Escherichia coli. J Biol Chem. Feb 15;265(5):2888-95. (Pubmed)

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1989 Publications

Bardwell JC, Regnier P, Chem SM, Nakamura Y, Grunberg-Manago M, Court DL.. (1989) Autoregulation of RNase III operon by mRNA processing. EMBO J. Nov;8(11):3401-7. (Pubmed)

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1988 Publications

Bardwell JC and Craig EA. (1988) Ancient heat shock gene is dispensable. J Bacteriol. Jul;170(7):2977-83. (Pubmed)

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1987 Publications

Bardwell JC and Craig EA.. (1987) Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli. Proc Natl Acad Sci USA. Aug;84(15):5177-81. (Pubmed)

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1986 Publications

Bardwell JC, Tilly K, Craig E, King J, Zylicz M, and Georgopoulos C.. (1986) The nucleotide sequence of the Escherichia coliK12 dnaJ+ gene.  A gene that encodes a heat shock protein. J Biol Chem. Feb 5;261(4):1782-5. (Pubmed)

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1985 Publications

Cowing DW, Bardwell JC, Craig EA, Woolford C, Hendrix RW, and Gross CA. (1985) Consensus sequence for Escherichia coli heat shock gene promoters. Proc Natl Acad Sci USA. May;82(9):2679-83. (Pubmed)

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1984 Publications

Bardwell JC and Craig EA.. (1984) Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proc Natl Acad Sci USA. Feb;81(3):848-52. (Pubmed)

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