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James C. A. Bardwell - Publications

Affiliations: 
Biochemistry University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
Biochemistry
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Year Citation  Score
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  0.364
2018 Stull F, Betton JM, Bardwell JCA. Periplasmic Chaperones and Prolyl Isomerases. Ecosal Plus. 8. PMID 29988001 DOI: 10.1128/ecosalplus.ESP-0005-2018  0.352
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  0.31
2016 Docter BE, Horowitz S, Gray MJ, Jakob U, Bardwell JC. Do nucleic acids moonlight as molecular chaperones? Nucleic Acids Research. PMID 27105849 DOI: 10.1093/Nar/Gkw291  0.305
2016 Groitl B, Horowitz S, Makepeace KA, Petrotchenko EV, Borchers CH, Reichmann D, Bardwell JC, Jakob U. Protein unfolding as a switch from self-recognition to high-affinity client binding. Nature Communications. 7: 10357. PMID 26787517 DOI: 10.1038/Ncomms10357  0.311
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  0.313
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  0.327
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  0.332
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  0.302
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  0.342
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  0.371
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  0.334
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  0.336
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  0.342
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  0.358
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  0.3
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  0.365
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  0.369
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  0.371
2007 Hiniker A, Ren G, Heras B, Zheng Y, Laurinec S, Jobson RW, Stuckey JA, Martin JL, Bardwell JCA. Laboratory evolution of one disulfide isomerase to resemble another Proceedings of the National Academy of Sciences of the United States of America. 104: 11670-11675. PMID 17609373 DOI: 10.1073/pnas.0704692104  0.312
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  0.527
2004 Tan JT, Bardwell JC. Key players involved in bacterial disulfide-bond formation. Chembiochem : a European Journal of Chemical Biology. 5: 1479-87. PMID 15515098 DOI: 10.1002/Cbic.200400036  0.452
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  0.337
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  0.307
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  0.311
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  0.333
2002 Tan J, Jakob U, Bardwell JC. Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase. Journal of Bacteriology. 184: 2692-8. PMID 11976298 DOI: 10.1128/Jb.184.10.2692-2698.2002  0.522
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  0.308
2001 Goldstone D, Haebel PW, Katzen F, Bader MW, Bardwell JCA, Beckwith J, Metcalf P. DsbC activation by the N-terminal domain of DsbD Proceedings of the National Academy of Sciences of the United States of America. 98: 9551-9556. PMID 11493705 DOI: 10.1073/pnas.171315498  0.311
2001 Bessette PH, Qiu J, Bardwell JC, Swartz JR, Georgiou G. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli. Journal of Bacteriology. 183: 980-8. PMID 11208797 DOI: 10.1128/Jb.183.3.980-988.2001  0.328
2000 Kadokura H, Bader M, Tian H, Bardwell JC, Beckwith J. Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 97: 10884-9. PMID 11005861 DOI: 10.1073/pnas.97.20.10884  0.356
2000 Bügl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA, Bardwell JC, Jakob U. RNA methylation under heat shock control. Molecular Cell. 6: 349-60. PMID 10983982 DOI: 10.1016/S1097-2765(00)00035-6  0.548
2000 Shao F, Bader MW, Jakob U, Bardwell JC. DsbG, a protein disulfide isomerase with chaperone activity. The Journal of Biological Chemistry. 275: 13349-52. PMID 10788443 DOI: 10.1074/Jbc.275.18.13349  0.361
2000 Staker BL, Korber P, Bardwell JC, Saper MA. Structure of Hsp15 reveals a novel RNA-binding motif. The Embo Journal. 19: 749-57. PMID 10675344 DOI: 10.1093/Emboj/19.4.749  0.544
2000 Korber P, Stahl JM, Nierhaus KH, Bardwell JC. Hsp15: a ribosome-associated heat shock protein. The Embo Journal. 19: 741-8. PMID 10675343 DOI: 10.1093/emboj/19.4.741  0.355
1999 Korber P, Zander T, Herschlag D, Bardwell JCA. A new heat shock protein that binds nucleic acids Journal of Biological Chemistry. 274: 249-256. PMID 9867837 DOI: 10.1074/Jbc.274.1.249  0.388
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  0.36
1998 Guddat LW, Bardwell JC, Glockshuber R, Huber-Wunderlich M, Zander T, Martin JL. Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. Protein Science : a Publication of the Protein Society. 6: 1893-900. PMID 9300489 DOI: 10.1002/pro.5560060910  0.306
1993 Bardwell JC, Lee JO, Jander G, Martin N, Belin D, Beckwith J. A pathway for disulfide bond formation in vivo. Proceedings of the National Academy of Sciences of the United States of America. 90: 1038-42. PMID 8430071 DOI: 10.1073/Pnas.90.3.1038  0.342
1991 Bardwell JC, McGovern K, Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell. 67: 581-9. PMID 1934062 DOI: 10.1016/0092-8674(91)90532-4  0.355
1988 Bardwell JC, Craig EA. Ancient heat shock gene is dispensable. Journal of Bacteriology. 170: 2977-83. PMID 3290192 DOI: 10.1128/Jb.170.7.2977-2983.1988  0.353
1987 Bardwell JC, Craig EA. Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 84: 5177-81. PMID 3299380 DOI: 10.1073/Pnas.84.15.5177  0.331
Low-probability matches (unlikely to be authored by this person)
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  0.3
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  0.299
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  0.299
2002 Collet JF, Bardwell JC. Oxidative protein folding in bacteria. Molecular Microbiology. 44: 1-8. PMID 11967064  0.296
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  0.296
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  0.296
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  0.296
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  0.29
2024 Sahoo BR, Kocman V, Clark N, Myers N, Deng X, Wong EL, Yang HJ, Kotar A, Guzman BB, Dominguez D, Plavec J, Bardwell JCA. Protein G-quadruplex interactions and their effects on phase transitions and protein aggregation. Nucleic Acids Research. PMID 38572746 DOI: 10.1093/nar/gkae229  0.289
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  0.289
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  0.287
2016 Horowitz S, Bardwell JC. RNAs as chaperones. Rna Biology. 0. PMID 27791471 DOI: 10.1080/15476286.2016.1247147  0.285
1996 Grauschopf U, Winther JR, Korber P, Zander T, Dallinger P, Bardwell JC. Why is DsbA such an oxidizing disulfide catalyst? Cell. 83: 947-55. PMID 8521518 DOI: 10.1016/0092-8674(95)90210-4  0.284
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  0.284
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  0.282
2001 Jakob U, Eser M, Bardwell JC. Redox switch of hsp33 has a novel zinc-binding motif. The Journal of Biological Chemistry. 275: 38302-10. PMID 10976105 DOI: 10.1074/Jbc.M005957200  0.282
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  0.28
2024 Mitra R, Usher ET, Dedeoğlu S, Crotteau MJ, Fraser OA, Yennawar NH, Gadkari VV, Ruotolo BT, Holehouse AS, Salmon L, Showalter SA, Bardwell JCA. Molecular insights into the interaction between a disordered protein and a folded RNA. Proceedings of the National Academy of Sciences of the United States of America. 121: e2409139121. PMID 39589885 DOI: 10.1073/pnas.2409139121  0.28
2022 Sahoo BR, Bardwell JCA. SERF, a family of tiny highly conserved, highly charged proteins with enigmatic functions. The Febs Journal. PMID 35694898 DOI: 10.1111/febs.16555  0.28
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  0.279
2024 Mitra R, Usher ET, Dedeoğlu S, Crotteau MJ, Fraser OA, Yennawar NH, Gadkari VV, Ruotolo BT, Holehouse AS, Salmon L, Showalter SA, Bardwell JCA. Molecular insights into the interaction between a disordered protein and a folded RNA. Biorxiv : the Preprint Server For Biology. PMID 38915483 DOI: 10.1101/2024.06.12.598678  0.278
2024 Sahoo BR, Subramanian V, Bardwell JCA. Backbone 1H, 13C, and 15N chemical shift assignments for human SERF2. Biomolecular Nmr Assignments. PMID 38466543 DOI: 10.1007/s12104-024-10167-5  0.278
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  0.273
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  0.273
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  0.271
1995 Jakob U, Meyer I, Bügl H, André S, Bardwell JC, Buchner J. Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function. The Journal of Biological Chemistry. 270: 14412-9. PMID 7782303 DOI: 10.1074/Jbc.270.24.14412  0.268
1997 Guddat LW, Bardwell JC, Zander T, Martin JL. The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding. Protein Science : a Publication of the Protein Society. 6: 1148-56. PMID 9194175 DOI: 10.1002/pro.5560060603  0.268
2009 Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC. Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Proceedings of the National Academy of Sciences of the United States of America. 106: 5557-62. PMID 19321422 DOI: 10.1073/Pnas.0811811106  0.267
2023 Sahoo BR, Kocman V, Clark N, Myers N, Deng X, Wong EL, Yang HJ, Kotar A, Guzman BB, Dominguez D, Plavec J, Bardwell JCA. Effects of protein G-quadruplex interactions on phase transitions and protein aggregation. Biorxiv : the Preprint Server For Biology. PMID 37790366 DOI: 10.1101/2023.09.21.558871  0.267
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  0.265
2013 Foit L, Zhang B, George J, Brunetti L, Brooks C, Bardwell JC. Structural Studies on the Activation and Substrate Binding of a Conditionally Disordered Acid-Activated Chaperone Biophysical Journal. 104: 5a. DOI: 10.1016/J.Bpj.2012.11.050  0.264
2018 Lee C, Kim H, Bardwell JCA. Electrostatic interactions are important for chaperone-client interaction in vivo. Microbiology (Reading, England). PMID 29870331 DOI: 10.1099/mic.0.000676  0.261
1998 Guddat LW, Bardwell JC, Martin JL. Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization. Structure (London, England : 1993). 6: 757-67. PMID 9655827 DOI: 10.1016/S0969-2126(98)00077-X  0.261
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  0.259
2010 Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. Protein refolding by pH-triggered chaperone binding and release. Proceedings of the National Academy of Sciences of the United States of America. 107: 1071-6. PMID 20080625 DOI: 10.1073/Pnas.0911610107  0.258
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  0.257
2001 Bader MW, Hiniker A, Regeimbal J, Goldstone D, Haebel PW, Riemer J, Metcalf P, Bardwell JC. Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. The Embo Journal. 20: 1555-62. PMID 11285220 DOI: 10.1093/Emboj/20.7.1555  0.257
2019 Yan Z, Hussain S, Xu W, Bernstein HD, Bardwell JCA. Chaperone OsmY facilitates the biogenesis of a major family of autotransporters. Molecular Microbiology. PMID 31369167 DOI: 10.1111/Mmi.14358  0.257
2001 Graumann J, Lilie H, Tang X, Tucker KA, Hoffmann JH, Vijayalakshmi J, Saper M, Bardwell JC, Jakob U. Activation of the redox-regulated molecular chaperone Hsp33--a two-step mechanism. Structure (London, England : 1993). 9: 377-87. PMID 11377198 DOI: 10.1016/S0969-2126(01)00599-8  0.252
2024 Sahoo BR, Deng X, Wong EL, Clark N, Yang H, Subramanian V, Guzman BB, Harris SE, Dehury B, Miyashita E, Hoff JD, Kocaman V, Saito H, Dominguez D, Plavec J, ... Bardwell JCA, et al. Visualizing liquid-liquid phase transitions. Biorxiv : the Preprint Server For Biology. PMID 39554013 DOI: 10.1101/2023.10.09.561572  0.249
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  0.245
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  0.245
2016 Salmon L, Ahlstrom LS, Horowitz S, Dickson A, Brooks CL, Bardwell JC. Capturing a dynamic chaperone-substrate interaction using NMR-informed molecular modeling. Journal of the American Chemical Society. PMID 27415450 DOI: 10.1021/Jacs.6B02382  0.242
2016 Ahlstrom LS, Salmon L, Horowitz S, Dickson A, Brooks CL, Bardwell JC. NMR-Informed Molecular Modeling Uncovers the Conformational Landscape of Chaperone Binding with Unfolded Substrate Biophysical Journal. 110: 369a. DOI: 10.1016/J.Bpj.2015.11.1989  0.238
2015 Dahl JU, Koldewey P, Salmon L, Horowitz S, Bardwell JC, Jakob U. HdeB functions as an acid-protective chaperone in bacteria. The Journal of Biological Chemistry. 290: 65-75. PMID 25391835 DOI: 10.1074/Jbc.M114.612986  0.233
2000 Bader MW, Xie T, Yu CA, Bardwell JC. Disulfide bonds are generated by quinone reduction. The Journal of Biological Chemistry. 275: 26082-8. PMID 10854438 DOI: 10.1074/Jbc.M003850200  0.233
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  0.224
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  0.222
2016 Johansson KE, Johansen NT, Christensen S, Horowitz S, Bardwell JC, Olsen JG, Willemoës M, Lindorff-Larsen K, Ferkinghoff-Borg J, Hamelryck T, Winther JR. Computational redesign of thioredoxin is hypersensitive towards minor conformational changes in the backbone template. Journal of Molecular Biology. PMID 27659562 DOI: 10.1016/J.Jmb.2016.09.013  0.22
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  0.219
1984 Bardwell JC, Craig EA. Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proceedings of the National Academy of Sciences of the United States of America. 81: 848-52. PMID 6322174 DOI: 10.1073/Pnas.81.3.848  0.218
2022 Wu K, Minshull TC, Radford SE, Calabrese AN, Bardwell JCA. Trigger factor both holds and folds its client proteins. Nature Communications. 13: 4126. PMID 35840586 DOI: 10.1038/s41467-022-31767-6  0.215
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  0.214
2013 Hailu TT, Foit L, Bardwell JC. In vivo detection and quantification of chemicals that enhance protein stability. Analytical Biochemistry. 434: 181-6. PMID 23219982 DOI: 10.1016/j.ab.2012.11.022  0.212
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  0.209
2017 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 Activation. Journal of Molecular Biology. PMID 29138002 DOI: 10.1016/J.Jmb.2017.11.002  0.207
2018 Stull F, Hipp H, Stockbridge RB, Bardwell JCA. In vivo chloride concentrations surge to proteotoxic levels during acid stress. Nature Chemical Biology. 14: 1051-1058. PMID 30323217 DOI: 10.1038/s41589-018-0143-z  0.2
1985 Cowing DW, Bardwell JCA, Craig EA, Woolford C, Hendrix RW, Gross CA. Consensus sequence for Escherichia coli heat shock gene promoters Proceedings of the National Academy of Sciences of the United States of America. 82: 2679-2683. PMID 3887408 DOI: 10.1073/Pnas.82.9.2679  0.199
1990 Yeung T, Mullin DA, Chen KS, Craig EA, Bardwell JCA, Walker JR. Sequence and expression of the Escherichia coli recR locus Journal of Bacteriology. 172: 6042-6047. PMID 1698765 DOI: 10.1128/Jb.172.10.6042-6047.1990  0.199
2012 Bardwell JC, Jakob U. Conditional disorder in chaperone action. Trends in Biochemical Sciences. 37: 517-25. PMID 23018052 DOI: 10.1016/J.Tibs.2012.08.006  0.193
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  0.189
2018 Salmon L, Ahlstrom LS, Bardwell JCA, Horowitz S. Selecting Conformational Ensembles Using Residual Electron and Anomalous Density (READ). Methods in Molecular Biology (Clifton, N.J.). 1764: 491-504. PMID 29605935 DOI: 10.1007/978-1-4939-7759-8_31  0.188
2022 Bardwell JCA. A glimpse into TriC's magic chamber of secrets. Cell. 185: 4679-4681. PMID 36493750 DOI: 10.1016/j.cell.2022.11.007  0.186
2019 Rocchio S, Duman R, El Omari K, Mykhaylyk V, Orr C, Yan Z, Salmon L, Wagner A, Bardwell JCA, Horowitz S. Identifying dynamic, partially occupied residues using anomalous scattering. Acta Crystallographica. Section D, Structural Biology. 75: 1084-1095. PMID 31793902 DOI: 10.1107/S2059798319014475  0.182
2022 Ade C, Marcelino TF, Dulchavsky M, Wu K, Bardwell JCA, Städler B. Microreactor equipped with naturally acid-resistant histidine ammonia lyase from an extremophile. Materials Advances. 3: 3649-3662. PMID 36238657 DOI: 10.1039/d2ma00051b  0.182
1993 Bardwell JC, Beckwith J. The bonds that tie: catalyzed disulfide bond formation. Cell. 74: 769-71. PMID 8374949 DOI: 10.1016/0092-8674(93)90455-Y  0.179
2003 Hiniker A, Bardwell JC. Disulfide bond isomerization in prokaryotes. Biochemistry. 42: 1179-85. PMID 12564920  0.176
2022 Choudhary V, Wu K, Zhang Z, Dulchavsky M, Barkman T, Bardwell JCA, Stull F. The enzyme pseudooxynicotine amine oxidase from Pseudomonas putida S16 is not an oxidase, but a dehydrogenase. The Journal of Biological Chemistry. 102251. PMID 35835223 DOI: 10.1016/j.jbc.2022.102251  0.173
2019 Meinen BA, Gadkari VV, Stull F, Ruotolo BT, Bardwell JCA. SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins. Proceedings of the National Academy of Sciences of the United States of America. PMID 31659041 DOI: 10.1073/Pnas.1913316116  0.17
2017 Cristie-David AS, Sciore A, Badieyan S, Escheweiler JD, Koldewey P, Bardwell JCA, Ruotolo BT, Marsh ENG. Evaluation of de novo-designed coiled coils as off-the-shelf components for protein assembly Molecular Systems Design & Engineering. 2: 140-148. DOI: 10.1039/C7ME00012J  0.17
2014 Bardwell JCA, Schreiber G. Editorial overview: Folding and binding Current Opinion in Structural Biology. 24: 8-10. PMID 24508004 DOI: 10.1016/j.sbi.2014.01.012  0.167
2007 Tapley TL, Eichner T, Gleiter S, Ballou DP, Bardwell JCA. Kinetic characterization of the disulfide bond-forming enzyme DsbB Journal of Biological Chemistry. 282: 10263-10271. PMID 17267399 DOI: 10.1074/Jbc.M611541200  0.162
2015 Dahl JU, Koldewey P, Salmon L, Horowitz S, Bardwell JC, Jakob U. HdeB functions as an acid-protective chaperone in bacteria. The Journal of Biological Chemistry. 290: 9950. PMID 25888567 DOI: 10.1074/Jbc.A114.612986  0.162
2004 Bardwell JC. The dance of disulfide formation. Nature Structural & Molecular Biology. 11: 582-3. PMID 15221018 DOI: 10.1038/nsmb0704-582  0.156
2016 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, ... ... Bardwell JC, et al. Determining crystal structures through crowdsourcing and coursework. Nature Communications. 7: 12549. PMID 27633552 DOI: 10.1038/Ncomms12549  0.156
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  0.155
2021 Beaufay F, Amemiya HM, Guan J, Basalla J, Meinen BA, Chen Z, Mitra R, Bardwell JCA, Biteen JS, Vecchiarelli AG, Freddolino PL, Jakob U. Polyphosphate drives bacterial heterochromatin formation. Science Advances. 7: eabk0233. PMID 34936433 DOI: 10.1126/sciadv.abk0233  0.142
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  0.14
2000 Wong C, Sridhara S, Bardwell JC, Jakob U. Heating greatly speeds Coomassie blue staining and destaining. Biotechniques. 28: 426-8, 430, 432. PMID 10723553 DOI: 10.2144/00283Bm07  0.136
2002 Bardwell JC. Disulfide bond formation, a race between FAD and oxygen. Developmental Cell. 3: 758-60. PMID 12479799  0.135
2014 Horowitz S, Koldewey P, Bardwell JC. Undergraduates improve upon published crystal structure in class assignment. Biochemistry and Molecular Biology Education : a Bimonthly Publication of the International Union of Biochemistry and Molecular Biology. 42: 398-404. PMID 25044946 DOI: 10.1002/Bmb.20811  0.125
2023 Dulchavsky M, Mitra R, Wu K, Li J, Boer K, Liu X, Zhang Z, Vasquez C, Clark CT, Funckes K, Shankar K, Bonnet-Zahedi S, Siddiq M, Sepulveda Y, Suhandynata RT, ... ... Bardwell JCA, et al. Directed evolution unlocks oxygen reactivity for a nicotine-degrading flavoenzyme. Nature Chemical Biology. PMID 37770699 DOI: 10.1038/s41589-023-01426-y  0.119
2005 Bardwell J. Thiol modifications in a snapshot. Nature Biotechnology. 23: 42-3. PMID 15637619 DOI: 10.1038/Nbt0105-42  0.115
2025 Kim H, Bell T, Lee K, Jeong J, Bardwell JC, Lee C. Identification of Host Genetic Factors Modulating β-Lactam Resistance in harboring plasmid-borne β-lactamase through Transposon-Sequencing. Emerging Microbes & Infections. 2493921. PMID 40231449 DOI: 10.1080/22221751.2025.2493921  0.108
2023 Marcelino T, Docampo MAR, Qian X, Ade C, Brodszkij E, Ceccato M, Foss M, Dulchavsky M, Bardwell JCA, Städler B. Surfaces Coated with Polymer Brushes Work as Carriers for Histidine Ammonia Lyase. Macromolecular Bioscience. e2200528. PMID 36971346 DOI: 10.1002/mabi.202200528  0.074
2021 Dulchavsky M, Clark CT, Bardwell JCA, Stull F. A cytochrome c is the natural electron acceptor for nicotine oxidoreductase. Nature Chemical Biology. PMID 33432238 DOI: 10.1038/s41589-020-00712-3  0.072
2016 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, ... ... Bardwell JC, et al. Corrigendum: Determining crystal structures through crowdsourcing and coursework. Nature Communications. 7: 13392. PMID 27779204 DOI: 10.1038/Ncomms13392  0.06
1989 Bardwell J, Régnier P, Chen S, Nakamura Y, Grunberg-Manago M, Court D. Autoregulation of RNase III operon by mRNA processing. The Embo Journal. 8: 3401-3407. DOI: 10.1002/j.1460-2075.1989.tb08504.x  0.06
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  0.048
2018 Stull F, Bardwell JCA. Folding against the wind. Nature Chemical Biology. PMID 29507387 DOI: 10.1038/s41589-018-0016-5  0.037
2002 Collet JF, Bardwell JC. Disulfides out of thin air. Nature Structural Biology. 9: 2-3. PMID 11753423 DOI: 10.1038/nsb0102-2  0.025
2021 Dulchavsky M, Clark CT, Bardwell JCA, Stull F. Author Correction: A cytochrome c is the natural electron acceptor for nicotine oxidoreductase. Nature Chemical Biology. PMID 33542535 DOI: 10.1038/s41589-021-00756-z  0.02
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