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James Bardwell - Publications

Affiliations: 
University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
Genetics, Microbiology Biology, Molecular Biology
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64 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2022 Mitra R, Wu K, Lee C, Bardwell JCA. ATP-Independent Chaperones. Annual Review of Biophysics. PMID 35167761 DOI: 10.1146/annurev-biophys-090121-082906  0.308
2021 Mitra R, Gadkari VV, Meinen BA, van Mierlo CPM, Ruotolo BT, Bardwell JCA. Mechanism of the small ATP-independent chaperone Spy is substrate specific. Nature Communications. 12: 851. PMID 33558474 DOI: 10.1038/s41467-021-21120-8  0.322
2020 Lee C, Betschinger P, Wu K, Żyła DS, Glockshuber R, Bardwell JC. A metabolite binding protein moonlights as a bile-responsive chaperone. The Embo Journal. e104231. PMID 32882062 DOI: 10.15252/embj.2019104231  0.354
2020 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. The Journal of Biological Chemistry. PMID 32817055 DOI: 10.1074/Jbc.Ra119.012300  0.693
2020 Sachsenhauser V, Deng X, Kim HH, Jankovic M, Bardwell JCA. Yeast tripartite biosensors sensitive to protein stability and aggregation propensity. Acs Chemical Biology. PMID 32105441 DOI: 10.1021/acschembio.0c00083  0.341
2019 Wu K, Stull F, Lee C, Bardwell JCA. Protein folding while chaperone bound is dependent on weak interactions. Nature Communications. 10: 4833. PMID 31645566 DOI: 10.1038/s41467-019-12774-6  0.308
2019 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. Nature Communications. 10: 659. PMID 30737390 DOI: 10.2210/Pdb6E0G/Pdb  0.361
2018 Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL, Bardwell JCA. Reply to 'Misreading chaperone-substrate complexes from random noise'. Nature Structural & Molecular Biology. PMID 30297780 DOI: 10.1038/S41594-018-0145-2  0.615
2018 Cristie-David AS, Koldewey P, Meinen BA, Bardwell JCA, Marsh ENG. Elaborating a coiled coil-assembled octahedral protein cage with additional protein domains. Protein Science : a Publication of the Protein Society. PMID 30113093 DOI: 10.1002/Pro.3497  0.341
2018 Stull F, Betton JM, Bardwell JCA. Periplasmic Chaperones and Prolyl Isomerases. Ecosal Plus. 8. PMID 29988001 DOI: 10.1128/ecosalplus.ESP-0005-2018  0.418
2017 Sachsenhauser V, Bardwell JC. Directed evolution to improve protein folding in vivo. Current Opinion in Structural Biology. 48: 117-123. PMID 29278775 DOI: 10.1016/j.sbi.2017.12.003  0.321
2017 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 : a European Journal of Chemical Biology. PMID 28763578 DOI: 10.1002/Cbic.201700406  0.334
2017 Horowitz S, Koldewey P, Stull F, Bardwell JC. Folding while bound to chaperones. Current Opinion in Structural Biology. 48: 1-5. PMID 28734135 DOI: 10.1016/J.Sbi.2017.06.009  0.359
2017 Koldewey P, Horowitz S, Bardwell JCA. Chaperone-client interactions: non-specificity engenders multi-functionality. The Journal of Biological Chemistry. PMID 28620048 DOI: 10.1074/Jbc.R117.796862  0.329
2016 Dahl JU, Koldewey P, Bardwell JC, Jakob U. Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo. Journal of Visualized Experiments : Jove. PMID 27805614 DOI: 10.3791/54527  0.328
2016 Sciore A, Su M, Koldewey P, Eschweiler JD, Diffley KA, Linhares BM, Ruotolo BT, Bardwell JC, Skiniotis G, Marsh EN. Flexible, symmetry-directed approach to assembling protein cages. Proceedings of the National Academy of Sciences of the United States of America. PMID 27432965 DOI: 10.1073/Pnas.1606013113  0.311
2016 Koldewey P, Stull F, Horowitz S, Martin R, Bardwell JC. Forces Driving Chaperone Action. Cell. PMID 27293188 DOI: 10.1016/J.Cell.2016.05.054  0.331
2016 Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL, Bardwell JC. Visualizing chaperone-assisted protein folding. Nature Structural & Molecular Biology. PMID 27239796 DOI: 10.1038/Nsmb.3237  0.708
2016 Stull F, Koldewey P, Humes JR, Radford SE, Bardwell JC. Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Nature Structural & Molecular Biology. 23: 53-8. PMID 26619265 DOI: 10.1038/nsmb.3133  0.362
2015 Chatelle C, Kraemer S, Ren G, Chmura H, Marechal N, Boyd D, Roggemans C, Ke N, Riggs P, Bardwell J, Berkmen M. Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase. Antioxidants & Redox Signaling. 23: 945-57. PMID 26191605 DOI: 10.1089/Ars.2014.6235  0.482
2015 Lennon CW, Thamsen M, Friman ET, Cacciaglia A, Sachsenhauser V, Sorgenfrei FA, Wasik MA, Bardwell JC. Folding Optimization In Vivo Uncovers New Chaperones. Journal of Molecular Biology. 427: 2983-94. PMID 26003922 DOI: 10.1016/j.jmb.2015.05.013  0.356
2014 Malik A, Mueller-Schickert A, Bardwell JC. Cytosolic selection systems to study protein stability. Journal of Bacteriology. 196: 4333-43. PMID 25266385 DOI: 10.1128/JB.02215-14  0.316
2014 Gray MJ, Wholey WY, Wagner NO, Cremers CM, Mueller-Schickert A, Hock NT, Krieger AG, Smith EM, Bender RA, Bardwell JC, Jakob U. Polyphosphate is a primordial chaperone. Molecular Cell. 53: 689-99. PMID 24560923 DOI: 10.1016/J.Molcel.2014.01.012  0.359
2014 Quan S, Wang L, Petrotchenko EV, Makepeace KA, Horowitz S, Yang J, Zhang Y, Borchers CH, Bardwell JC. Super Spy variants implicate flexibility in chaperone action. Elife. 3: e01584. PMID 24497545 DOI: 10.7554/Elife.01584  0.694
2013 Foit L, George JS, Zhang BW, Brooks CL, Bardwell JC. Chaperone activation by unfolding. Proceedings of the National Academy of Sciences of the United States of America. 110: E1254-62. PMID 23487787 DOI: 10.1073/Pnas.1222458110  0.319
2013 Foit L, Bardwell JC. A tripartite fusion system for the selection of protein variants with increased stability in vivo. Methods in Molecular Biology (Clifton, N.J.). 978: 1-20. PMID 23423885 DOI: 10.1007/978-1-62703-293-3_1  0.314
2013 Quan S, Hiniker A, Collet JF, Bardwell JC. Isolation of bacteria envelope proteins. Methods in Molecular Biology (Clifton, N.J.). 966: 359-66. PMID 23299746 DOI: 10.1007/978-1-62703-245-2_22  0.727
2013 Foit L, Zhang B, George J, Brunetti L, Brooks C, Bardwell J. Acid-Induced Activation of the Periplasmic Chaperone HdeA Biophysical Journal. 104: 569a-570a. DOI: 10.1016/J.Bpj.2012.11.3163  0.323
2012 Quan S, Bardwell JC. Chaperone discovery. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 34: 973-81. PMID 22968800 DOI: 10.1002/bies.201200059  0.712
2011 Evans ML, Schmidt JC, Ilbert M, Doyle SM, Quan S, Bardwell JC, Jakob U, Wickner S, Chapman MR. E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly. Prion. 5: 323-34. PMID 22156728 DOI: 10.4161/Pri.18555  0.67
2011 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. Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nature Structural & Molecular Biology. 18: 262-9. PMID 21317898 DOI: 10.1038/Nsmb.2016  0.723
2011 Ren G, Bardwell JC. Engineered pathways for correct disulfide bond oxidation. Antioxidants & Redox Signaling. 14: 2399-412. PMID 21250836 DOI: 10.1089/ars.2010.3782  0.417
2011 Foit L, Mueller-Schickert A, Mamathambika BS, Gleiter S, Klaska CL, Ren G, Bardwell JC. Genetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor. Antioxidants & Redox Signaling. 14: 973-84. PMID 21110786 DOI: 10.1089/ars.2010.3712  0.393
2009 Foit L, Morgan GJ, Kern MJ, Steimer LR, von Hacht AA, Titchmarsh J, Warriner SL, Radford SE, Bardwell JC. Optimizing protein stability in vivo. Molecular Cell. 36: 861-71. PMID 20005848 DOI: 10.1016/j.molcel.2009.11.022  0.349
2009 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. Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. The Journal of Biological Chemistry. 284: 10150-9. PMID 19181668 DOI: 10.1074/Jbc.M809509200  0.397
2008 Mamathambika BS, Bardwell JC. Disulfide-linked protein folding pathways. Annual Review of Cell and Developmental Biology. 24: 211-35. PMID 18588487 DOI: 10.1146/annurev.cellbio.24.110707.175333  0.419
2008 Gleiter S, Bardwell JC. Disulfide bond isomerization in prokaryotes. Biochimica Et Biophysica Acta. 1783: 530-4. PMID 18342631 DOI: 10.1016/j.bbamcr.2008.02.009  0.351
2008 Pan JL, Sliskovic I, Bardwell JC. Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway. Journal of Molecular Biology. 377: 1433-42. PMID 18325532 DOI: 10.1016/j.jmb.2008.01.058  0.404
2008 Vertommen D, Depuydt M, Pan J, Leverrier P, Knoops L, Szikora JP, Messens J, Bardwell JC, Collet JF. The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner. Molecular Microbiology. 67: 336-49. PMID 18036138 DOI: 10.1111/j.1365-2958.2007.06030.x  0.681
2008 Masip L, Klein-Marcuschamer D, Quan S, Bardwell JC, Georgiou G. Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant. The Journal of Biological Chemistry. 283: 840-8. PMID 18003618 DOI: 10.1074/Jbc.M705147200  0.707
2008 Mac TT, von Hacht A, Hung KC, Dutton RJ, Boyd D, Bardwell JC, Ulmer TS. Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase. The Journal of Biological Chemistry. 283: 824-32. PMID 18003611 DOI: 10.1074/jbc.M707863200  0.378
2007 Quan S, Schneider I, Pan J, Von Hacht A, Bardwell JC. The CXXC motif is more than a redox rheostat. The Journal of Biological Chemistry. 282: 28823-33. PMID 17675287 DOI: 10.1074/Jbc.M705291200  0.732
2006 Hiniker A, Vertommen D, Bardwell JC, Collet JF. Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues. Journal of Bacteriology. 188: 7317-20. PMID 17015672 DOI: 10.1128/JB.00383-06  0.586
2006 Pan JL, Bardwell JC. The origami of thioredoxin-like folds. Protein Science : a Publication of the Protein Society. 15: 2217-27. PMID 17008712 DOI: 10.1110/ps.062268106  0.357
2005 Hiniker A, Collet JF, Bardwell JC. Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. The Journal of Biological Chemistry. 280: 33785-91. PMID 16087673 DOI: 10.1074/jbc.M505742200  0.619
2005 Collet JF, Peisach D, Bardwell JC, Xu Z. The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutant. Protein Science : a Publication of the Protein Society. 14: 1863-9. PMID 15987909 DOI: 10.1110/Ps.051464705  0.622
2005 Tan J, Lu Y, Bardwell JC. Mutational analysis of the disulfide catalysts DsbA and DsbB. Journal of Bacteriology. 187: 1504-10. PMID 15687215 DOI: 10.1128/Jb.187.4.1504-1510.2005  0.329
2004 Nakamoto H, Bardwell JC. Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochimica Et Biophysica Acta. 1694: 111-9. PMID 15546661 DOI: 10.1016/j.bbamcr.2004.02.012  0.347
2004 Hiniker A, Bardwell JC. Disulfide relays between and within proteins: the Ero1p structure. Trends in Biochemical Sciences. 29: 516-9. PMID 15450603 DOI: 10.1016/j.tibs.2004.08.002  0.329
2004 Masip L, Pan JL, Haldar S, Penner-Hahn JE, DeLisa MP, Georgiou G, Bardwell JC, Collet JF. An engineered pathway for the formation of protein disulfide bonds. Science (New York, N.Y.). 303: 1185-9. PMID 14976313 DOI: 10.1126/Science.1092612  0.653
2004 Kadokura H, Tian H, Zander T, Bardwell JCA, Beckwith J. Snapshots of DsbA in Action: Detection of Proteins in the Process of Oxidative Folding Science. 303: 534-537. PMID 14739460 DOI: 10.1126/science.1091724  0.313
2004 Hiniker A, Bardwell JC. In vivo substrate specificity of periplasmic disulfide oxidoreductases. The Journal of Biological Chemistry. 279: 12967-73. PMID 14726535 DOI: 10.1074/jbc.M311391200  0.326
2004 Goulding CW, Apostol MI, Gleiter S, Parseghian A, Bardwell J, Gennaro M, Eisenberg D. Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis. The Journal of Biological Chemistry. 279: 3516-24. PMID 14597624 DOI: 10.1074/Jbc.M311833200  0.491
2003 Regeimbal J, Gleiter S, Trumpower BL, Yu CA, Diwakar M, Ballou DP, Bardwell JC. Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proceedings of the National Academy of Sciences of the United States of America. 100: 13779-84. PMID 14612576 DOI: 10.1073/Pnas.1935988100  0.726
2003 Collet JF, D'Souza JC, Jakob U, Bardwell JC. Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. The Journal of Biological Chemistry. 278: 45325-32. PMID 12952960 DOI: 10.1074/Jbc.M307818200  0.625
2002 Regeimbal J, Bardwell JC. DsbB catalyzes disulfide bond formation de novo. The Journal of Biological Chemistry. 277: 32706-13. PMID 12072444 DOI: 10.1074/Jbc.M205433200  0.733
2002 Collet JF, Riemer J, Bader MW, Bardwell JC. Reconstitution of a disulfide isomerization system. The Journal of Biological Chemistry. 277: 26886-92. PMID 12004064 DOI: 10.1074/jbc.M203028200  0.575
2002 Collet JF, Bardwell JC. Oxidative protein folding in bacteria. Molecular Microbiology. 44: 1-8. PMID 11967064  0.674
2002 Collet JF, Bardwell JC. Disulfides out of thin air. Nature Structural Biology. 9: 2-3. PMID 11753423 DOI: 10.1038/nsb0102-2  0.507
2002 Xie T, Yu L, Bader MW, Bardwell JC, Yu CA. Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. The Journal of Biological Chemistry. 277: 1649-52. PMID 11698406 DOI: 10.1074/Jbc.M108697200  0.311
1999 Bader M, Winther JR, Bardwell JC. Protein oxidation: prime suspect found 'not guilty'. Nature Cell Biology. 1: E57-8. PMID 10559908 DOI: 10.1038/11025  0.343
1998 Bader M, Muse W, Zander T, Bardwell J. Reconstitution of a protein disulfide catalytic system. The Journal of Biological Chemistry. 273: 10302-7. PMID 9553083 DOI: 10.1074/Jbc.273.17.10302  0.514
1993 Zapun A, Bardwell JC, Creighton TE. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry. 32: 5083-92. PMID 8494885 DOI: 10.1021/bi00070a016  0.347
1993 Martin JL, Bardwell JCA, Kuriyan J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo Nature. 365: 464-468. PMID 8413591 DOI: 10.1038/365464A0  0.417
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