| 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 |
|
| 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 |
|
| 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 |
|
| 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 |
|
| 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 |
|
| 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 |
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 |
|
| 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 |
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 |
|
| 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 |
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| Hide low-probability matches. |