James C. A. Bardwell - Publications

Affiliations: 
Biochemistry University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
Biochemistry

24/114 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
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
Low-probability matches
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  0.12
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  0.08
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  0.08
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  0.08
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  0.01
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  0.01
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  0.01
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  0.01
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: 10.1038/s41467-019-08565-8  0.04
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  0.01
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  0.01
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  0.01
2018 Stull F, Betton JM, Bardwell JCA. Periplasmic Chaperones and Prolyl Isomerases. Ecosal Plus. 8. PMID 29988001 DOI: 10.1128/ecosalplus.ESP-0005-2018  0.01
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  0.01
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  0.01
2018 Stull F, Bardwell JCA. Folding against the wind. Nature Chemical Biology. PMID 29507387 DOI: 10.1038/s41589-018-0016-5  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.04
2016 Horowitz S, Bardwell JC. RNAs as chaperones. Rna Biology. 0. PMID 27791471 DOI: 10.1080/15476286.2016.1247147  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.04
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  0.04
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  0.01
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  0.01
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  0.04
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  0.04
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  0.01
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  0.01
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  0.04
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  0.01
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  0.04
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  0.01
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  0.01
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  0.01
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  0.01
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  0.92
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  0.04
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.04
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  0.92
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  0.01
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  0.01
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  0.04
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  0.01
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  0.04
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  0.04
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  0.01
2005 Bardwell J. Thiol modifications in a snapshot. Nature Biotechnology. 23: 42-3. PMID 15637619 DOI: 10.1038/nbt0105-42  0.01
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  0.01
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  0.01
2004 Bardwell JC. The dance of disulfide formation. Nature Structural & Molecular Biology. 11: 582-3. PMID 15221018 DOI: 10.1038/nsmb0704-582  0.01
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  0.01
2003 Hiniker A, Bardwell JC. Disulfide bond isomerization in prokaryotes. Biochemistry. 42: 1179-85. PMID 12564920  0.01
2002 Bardwell JC. Disulfide bond formation, a race between FAD and oxygen. Developmental Cell. 3: 758-60. PMID 12479799  0.01
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  0.01
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  0.04
2002 Collet JF, Bardwell JC. Oxidative protein folding in bacteria. Molecular Microbiology. 44: 1-8. PMID 11967064  0.04
2002 Collet JF, Bardwell JC. Disulfides out of thin air. Nature Structural Biology. 9: 2-3. PMID 11753423 DOI: 10.1038/nsb0102-2  0.04
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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  0.01
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