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 |
0.367 |
|
2018 |
Stull F, Betton JM, Bardwell JCA. Periplasmic Chaperones and Prolyl Isomerases. Ecosal Plus. 8. PMID 29988001 DOI: 10.1128/ecosalplus.ESP-0005-2018 |
0.353 |
|
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 |
0.311 |
|
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 |
0.306 |
|
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 |
0.314 |
|
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 |
0.314 |
|
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 |
0.328 |
|
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 |
0.334 |
|
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 |
0.303 |
|
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 |
0.343 |
|
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 |
0.337 |
|
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 |
0.343 |
|
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 |
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 |
0.301 |
|
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 |
0.301 |
|
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 |
0.37 |
|
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 |
0.372 |
|
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 |
0.314 |
|
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 |
0.532 |
|
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 |
0.457 |
|
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 |
0.339 |
|
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 |
0.312 |
|
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 |
0.334 |
|
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 |
0.528 |
|
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 |
0.309 |
|
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 |
0.329 |
|
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 |
0.555 |
|
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 |
0.362 |
|
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 |
0.55 |
|
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 |
0.359 |
|
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 |
0.392 |
|
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 |
0.361 |
|
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 |
0.307 |
|
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 |
0.356 |
|
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 |
0.334 |
|
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