container
The Bardwell Lab
HHMI
MCDB
Seite auf Deutsch ansehen

Publications

Gray MJ, Wholey WY, Wagner NO, Cremers CM, Mueller-Schickert A, Hock NT, Krieger AG, Smith EM, Bender RA, Bardwell JC, Jakob U. (March 2014) Polyphosphate is a primordial chaperone. Mol Cell. 6;53(5):689-99. Epub 2014 Feb 20. PMID:24560923. (Pubmed)

Bardwell JC, Schreiber G. (February 2014) Editorial overview: Folding and binding. Curr Opin Struct Biol. 2014 Feb;24:viii-x. Epub 2014 Feb 6. No abstract available. PMID:24508004. (Pubmed)

Quan S, Wang L, Petrotchenko EV, Makepeace KA, Horowitz S, Yang J, Zhang Y, Borchers CH, Bardwell JC. (February 2014) Super Spy variants implicate flexibility in chaperone action. Elife. 2014;3:e01584. Epub 2014 Feb 4. PMID:24497545. (Pubmed)

Foit L, George JS, Zhang BW, Brooks CL 3rd, Bardwell JC. (April 2013)  Chaperone activation by unfolding. Proc Natl Acad Sci U S A. 110(14):E1254-62. Epub 2013 Mar 4. PMCID:PMC3619340. (Pubmed)

Hailu TT, Foit L, Bardwell JC.. (March 2013)   In vivo detection and quantification of chemicals that enhance protein stability. Anal Biochem. 1;434(1):181-6. Epub 2012 Dec 5. PMCID:PMC3670414. . (Pubmed)

Shu Quan, Lili Wang, Evgeniy V Petrotchenko, Karl AT Makepeace, Scott Horowitz, Jianyi Yang, Yang Zhang, Christoph H Borchers, James CA Bardwell . (February 2013)  Super Spy variants implicate flexibility in chaperone action. eLife, Epub in process. eLife, Epub in process.

Shu Quan, Annie Hiniker, Jean-Francois Collet, and James C.A. Bardwell. (January 2013)  Isolation of bacteria Envelope Proteins. Methods in Molecular Biology. 966, 359-366. (Pubmed)

Foit L, Bardwell JC. . (January 2013)  A tripartite fusion system for the selection of protein variants with increased stability in vivo. Methods Mol Biol. 978:1-20. PMID:23423885. (Pubmed)

Quan S, Hiniker A, Collet JF, Bardwell JC. (January 2013) Isolation of bacteria envelope proteins. Methods Mol Biol. 966:359-66. PMID: 23299746.

Tsinatkeab T. Hailu, Linda Foit, James C.A. Bardwell. (March 2012)  In vivo detection and quantification of chemicals that enchance protein stability. Analytical Biochemistry. 434, 181-186. (Pubmed)

Evans ML, Schmidt JC, Ilbert M, Doyle SM, Quan S, Bardwell JC, Jakob U, Wickner S, Chapman MR. (January 2012) E. coli chaperones DnaK, Hsp33, and Spy inhibit bacterial functional amyloid assembly. Prion. 1;5(4). (Pubmed)

Shu Quan, and James C.A. Bardwell. (January 2012)  Chaperone Discovery. Bioessays. 34, 973-981. (Pubmed)

Bardwell JC, Jakob U . (January 2012) Conditional disorder in chaperone action. Trends Biochem Sci. 37(12):517-25. PMCID:PMC3508372.

Quan S, Bardwell JC. (January 2012) Chaperone discovery. Bioessays. 34(11):973-81. PMID: 22968800.

Ren G, Bardwell JC. (June 2011) Engineered pathways for correct disulfide bond oxidation. Antioxid Redox Signal. 14(12):2399-412. (Pubmed)

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. (March 2011) Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat Struct Mol Biol. 18(3):262-9. (Pubmed)

Foit L, Mueller-Schickert A, Mamathambika BS, Gleiter S, Klaska CL, Ren G, Bardwell JC. (March 2011) Genetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor. Antioxid Redox Signal. 14(6):973-84. (Pubmed)

Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. (January 2010) Protein refolding by pH-triggered chaperone binding and release. Proc Natl Acad Sci U S A. 107(3):1071-6. (Pubmed)

Foit L, Morgan GJ, Kern MJ, Steimer LR, von Hacht AA, Titchmarsh J, Warriner SL, Radford SE, Bardwell JC.. (December 2009) Optimizing protein stability in vivo. Mol Cell. Dec 11;36(5):861-71. (Pubmed)

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.. (May 2009) Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J Biol Chem. 284(15):10150-9. (Pubmed)

Tapley TL, K├Ârner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC.. (April 2009) Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Proc Natl Acad Sci U S A. 106(14):5557-62. (Pubmed)

Mamathambika BS, Bardwell JC. (April 2008) Disulfide-linked protein folding pathways. Annu Rev Cell Dev Biol. 24:211-35. Review. (Pubmed)

Pan JL, Sliskovic I, Bardwell JC.. (April 2008) Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway. J Mol Biol. 377(5):1433-42. (Pubmed)

Vertommen D, Depuydt M, Pan J, Leverrier P, Knoops L, Szikora JP, Messens J, Bardwell JC, Collet JF.. (January 2008) The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner. Mol Microbiol. 67(2):336-49. (Pubmed)

Gleiter S, Bardwell JC.. (January 2008) Disulfide bond isomerization in prokaryotes. Biochim Biophys Acta. 1783(4):530-4. (Pubmed)

Masip L, Klein-Marcuschamer D, Quan S, Bardwell JC, Georgiou G. (January 2008) Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant. J Biol Chem. 283(2):840-8. (Pubmed)

Mac TT, von Hacht A, Hung KC, Dutton RJ, Boyd D, Bardwell JC, Ulmer TS. (January 2008) Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase. J Biol Chem. 283:824-832. PMID:18003611.

Quan S, Schneider I, Pan J, Von Hacht A, Bardwell JC. (September 2007) The CXXC motif is more than a redox rheostat. J Biol Chem. 282(39):38823-33. (Pubmed)

Tapley TL, Eichner T, Gleiter S, Ballou DP, Bardwell JC. (April 2007) Kinetic characterization of the disulfide bond-forming enzyme DsbB. J Biol Chem. 282(14):10263-71. (Pubmed)

Hiniker A, Ren G, Heras B, Zheng Y, Laurinec S, Jobson RW, Stuckey JA, Martin JL, Bardwell JC. (January 2007) Laboratory evolution of one disulfide isomerase to resemble another. Proc Natl Acad Sci USA. 104:11670-11675. PMCID: PMC1906722.

Hiniker A, Vertommen D, Bardwell JC, Collet JF. (November 2006) Evidence for Conformational Changes within DsbD: Possible Role for Membrane-Embedded Proline Residues. J. Bacteriol. Oct;188(20):7317-20. (Pubmed)

Pan JL, Bardwell JC. (October 2006) The origami of thioredoxin-like folds. Protein Sci. Oct;15(10):2217-27. (Pubmed)

Hiniker A, Collet JF, Bardwell JC. (October 2005) Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. J. Biol. Chem. Oct 7;280(40):33785-91. Epub 2005 Aug 8. (Pubmed)

Collet JF, Peisach D, Bardwell JC, Xu Z. (July 2005) The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutant. Protein Sci. Jul;14(7):1863-9. (Pubmed)

Collet, J-F. and Bardwell J.C.A. . (April 2005) The Catalysis of disulfide bond formation in Prokaryotes. In Protein Folding Handbook, Buchner/Kiefhaber Eds. Wiley-VCH.

Tan, J. Lu Y., and Bardwell J.C.A.. (March 2005) Mutational Anlysis of the disulfide catalysts DsbA and DsbB. J.Bacteriol. 187: 1504-10. (Pubmed)

Bardwell J.C.A.. (February 2005) The dance of disulfide formation. Nat. Struct. Mol. Biol. 11: 582-3. (Pubmed)

Bardwell J.C.A.. (January 2005) Thiol modifications in a snapshot. Nat. Biotechno. 23: 42-3. (Pubmed)

Nakamoto H, Bardwell JC.. (December 2004) Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochim. Biophys. Acta. Nov 11;1694(1-3):111-9. (Pubmed)

Tan JT, Bardwell JC.. (November 2004) Key players involved in bacterial disulfide-bond formation. Chembiochem. Nov 5;5(11):1479-87. (Pubmed)

Hiniker A, Bardwell JC.. (October 2004) Disulfide relays between and within proteins: the Ero1p structure. Trends Biochem. Sci. Oct;29(10):516-9. (Pubmed)

Kadokura H, Tian H, Zander T, Bardwell JC, and Beckwith J. (August 2004) Snapshots of DsbA in Action: detection of proteins in the process of oxidative folding. Science. 303(5657):534-537. (Pubmed)

Masip L, Pan JL, Haldar S, Penner-Hahn J, Georgiou G, Bardwell JC, and Collet Jean-Francois. (August 2004) An Engineered pathway for the formation of protein disulfide bonds. Science. 303:1185 - 1189. (Pubmed)

Hiniker A and Bardwell JC. (July 2004) in vivo substrate specificity of periplasmic disulfide oxidoreductases. J. Biol. Chem. Mar 26;279(13):12967-73. Epub 2004 Jan 15. (Pubmed)

Collet J-F. and Bardwell J.C.A.. (December 2003) Oxidative folding in Bacteria. NATO Science series. (Pubmed)

Collet J.F., D'Souza J.C., Jakob U., Bardwell J.C.. (November 2003) Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. J. Biol. Chem. 278(46):45325-32. (Pubmed)

Regeimbal J., Gleiter, S., Trumpower, B.L., Yu, C.A., Diwakar, M., Ballou, D.P., and Bardwell, J.C.. (November 2003) Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proc. Nat. Acad. of Sci USA. 100(24):13779-84. (Pubmed)

Goulding CW, Apostol MI, Gleiter S, Parseghian A, Bardwell J, Gennaro M, and Eisenberg D. (November 2003) Gram-positive DsbE proteins function differently from gram-negative DsbE homologs: A structure function analysis of DsbE from Mycobacterium tuberculosis. J. Biol. Chem. 2004 Jan 30;279(5):3516-24. Epub 2003 Nov 3. (Pubmed)

Hiniker A. and Bardwell J.C.. (February 2003) Disulfide bond isomerization in prokaryotes. Biochemistry. Feb 11;42(5): 1179-85. (Pubmed)

Bardwell J.C.. (December 2002) Disulfide bond formation, a race between FAD and oxygen. Dev. Cell. Dec;3(6):758-60. (Pubmed)

Regeimbal J. and Bardwell J.C.. (September 2002) DsbB catalyzes disulfide bond formation de novo. J. Biol. Chem. Sep 6;277(36):32706-13. (Pubmed)

Collet J.F., Reimer J., Bader M.W., and Bardwell J.C.. (July 2002) Reconstitution of a disulfide isomerization system. J. Biol. Chem. Jul 26;277(30):26886-92. (Pubmed)

Tan J., Jakob U., and Bardwell J.C.. (May 2002) Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA. J. Bacteriol. May;184(10):2692-8. (Pubmed)

Collet J.F. and Bardwell J.C.. (April 2002) Oxidative protein folding in bacteria. Mol. Microbiol. Apr;44(1):1-8. (Pubmed)

Xie T, Yu L, Bader MW, Bardwell JC, and Yu CA. (January 2002) Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. J. Biol. Chem. Jan 18;277(3):1649-52. (Pubmed)

Collet J.F. and Bardwell J.C.. (January 2002) Disulfides out of thin air. Nat. Struct. Biol. . Jan;9(1):2-3. (Pubmed)

Bader, MW and Bardwell JC. (September 2001) Catalysis of disulfide bond formation and isomerization in Escherichia coli. Adv. Protein Chem. 59:283-301. (Pubmed)

Goldstone D., Haebel P.W., Katzen F., Bader M.W., Bardwell J.C., Beckwith J., and Metcalf P. . (August 2001) DsbC activation by the N-terminal domain of DsbD. Proc. Natl. Acad. Sci. USA. . Aug 14;98(17):9551-6. (Pubmed)

Graumann J, Lilie H, Tang X, Tucker KA, Hoffman JH, Vijayalakshmi J, Saper M, Bardwell JC, and Jakob U. (May 2001) Activation of the redox-regulated molecular chaperone Hsp33-a two-step mechanism. Structure (Camb). May 9;9(5):377-87. (Pubmed)

Bader M.W., Hiniker A., Regeimbal J., Goldstone D., Haebel P.W., Riemer J., Metcalf P., and Bardwell J.C.. (April 2001) Turning a disulfide into an oxidase: DsbC mutants that imitate DsbA. EMBO J. Apr 2;20(7):1555-62. (Pubmed)

Bessette PH, Qiu J, Bardwell JC, Swartz JR, and Georgiou G. (February 2001) Effects of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide protein in Escherichia coli. J. Bacteriol. Feb;183(3):980-8. (Pubmed)

Jakob U, Eser M, and Bardwell JC. (December 2000) Redox switch of hsp33 has a novel zinc-binding motif. J. Biol. Chem. Dec 8;275(34):38302-10. (Pubmed)

Kadokura H., Bader M., Tian H., Bardwell J.C., and Beckwith J. (September 2000) Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain in Escherichia coli. Proc. Natl. Acad. Sci. USA. Sep 26;97(20):10884-9. (Pubmed)

Bader M.W., Xie T., Yu C.A., and Bardwell J.C.. (August 2000) Disulfide bonds are generated by quinone reduction. J Biol Chem. Aug 25;275(34):26082-8. (Pubmed)

Bugl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA, Bardwell JC, and Jakob U. (August 2000) RNA methylation under heat shock control. Mol. Cell. Aug;6(2):349-60. (Pubmed)

Shao F., Bader M.W., Jakob U., and Bardwell J.C.. (May 2000) DsbG, a protein disulfide isomerase with chaperone activtity. J. Biol. Chem. May 5;275(18):13349-52. (Pubmed)

Wong C, Sridhara S, Bardwell JC, and Jakob U. (March 2000) Heating greatly speeds Coomassie blue staining and destaining. Biotechniques. Mar;28(3):426-28,430,432. (Pubmed)

Korber P., Stahl J.M., Nierhaus K.H., and Bardwell J.C.. (February 2000) Hsp15: a ribosome-associated heat shock protein. EMBO J. Feb 15;19(4):741-8. (Pubmed)

Staker BL, Korber P, Bardwell JC, and Saper MA.. (January 2000) Structure of Hsp15 reveals a novel RNA-binding motif. EMBO J. Feb 15;19(4):749-57. (Pubmed)

Bader M, Winther JR, and Bardwell JC. (April 1999) Protein oxidation: prime suspect found 'not guilty'. Nat Cell Biol. . Jul;1(3):E57-8. (Pubmed)

Bader M., Muse W., Ballou D.P., Gassner C., and Bardwell J.C.. (March 1999) Oxidative protein folding is driven by the electron transport chain. Cell. Jul 23;98(2):217-27. (Pubmed)

Jakob U., Muse W., Eser M., and Bardwell J.C.. (February 1999) Chaperone activity with a redox switch. Cell. Feb 5;96(3):341-52. (Pubmed)

Korber P., Zander T., Herschlag D., and Bardwell J.C.. (January 1999) A new heat shock protein that binds nucleic acids. J Biol Chem. Jan 1;274(1):249-56. (Pubmed)

Guddat LW, Bardwell JC, and Martin JL.. (December 1998) Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stability. Structure. Jun 15;6(6):757-767. (Pubmed)

Bader M, Muse W, Zander T, and Bardwell J.. (August 1998) Reconstitution of a protein disulfide catalytic system. J Biol Chem. Apr 24;273(17):10302-7. (Pubmed)

Zander T, Phadke ND, and Bardwell JC. (January 1998) Disulfide bond catalysts in Escherichia coli. Methods Enzymol. 290:59-74. (Pubmed)

Guddat LW, Bardwell JC, Glockshuber R, Huber-Wunderlich M, Zander T, and Martin JL. (October 1997) Structural analysis of three His32 mutants of DsbA: support for an electrostatic role in His32 in DsbA stability. Protein Sci. Sep;6(9):1893-900. (Pubmed)

Guddat LW, Bardwell JC, Zander T, and Martin JL.. (February 1997) The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding. Protein Sci. Jun;6(6):1148-56. (Pubmed)

Grauschopf U, Winther JR, Korber P, Zander T, Dallinger P, and Bardwell JC. (December 1995) Why is DsbA such an oxidizing disulfide catalyst?. Cell. Dec 15;83(6):947-55. (Pubmed)

Jakob U, Meyer I, Bugl H, Andre S, Bardwell JC, and Buchner J.. (February 1995) Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function. J Biol Chem. Jun 16;270(24):14412-9. (Pubmed)

Bardwell JC.. (January 1994) Building bridges:disulphide bond formation in the cell. Mol Microbiol. Oct;14(2):199-205. (Pubmed)

Martin JL, Bardwell, and Kuriyan J.. (October 1993) Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature. Sep 30;365(6445):464-8. (Pubmed)

Bardwell JC and Beckwith J.. (September 1993) The bonds that tie: catalyzed disulfide bond formation. Cell. Sep 10;74(5):769-71. (Pubmed)

Zapun A, Bardwell JC, and Creighton TE. (May 1993) The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry. May 18;32(19):5082-92. (Pubmed)

Martin JL, Waksman G, Bardwell JC, Beckwith J, and Kuriyan J.. (April 1993) Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo. J Mol Biol. Apr 5;230(3):1097-100. (Pubmed)

Bardwell JC, Lee JO, Jander G, Martin N, Belin D, and Beckwith J.. (February 1993) A pathway for disulfide bond formation in vivo. Proc Natl Acad Sci USA. Feb 1;90(3):1038-42. (Pubmed)

Bardwell JC, McGovern K, and Beckwith J.. (November 1991) Identification of a protein required for disulfide bond formation in vivo. Cell. Nov 1;67(3):581-9. (Pubmed)

Yeung T, Mullin DA, Chen KS, Craig EA, Bardwell JC, and Walker JR. (October 1990) Sequence and expression of the Escherichia coli recR locus. J Bacteriol. Oct;172(10):6042-7. (Pubmed)

Chen SM, Takiff HE, Barber AM, Dubois GC, Bardwell JC, and Court DL.. (February 1990) Expression and characterization of RNase III and Era proteins. Products of the rnc operon of Escherichia coli. J Biol Chem. Feb 15;265(5):2888-95. (Pubmed)

Bardwell JC, Regnier P, Chem SM, Nakamura Y, Grunberg-Manago M, Court DL.. (November 1989) Autoregulation of RNase III operon by mRNA processing. EMBO J. Nov;8(11):3401-7. (Pubmed)

Bardwell JC and Craig EA. (July 1988) Ancient heat shock gene is dispensable. J Bacteriol. Jul;170(7):2977-83. (Pubmed)

Bardwell JC and Craig EA.. (October 1987) Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli. Proc Natl Acad Sci USA. Aug;84(15):5177-81. (Pubmed)

Bardwell JC, Tilly K, Craig E, King J, Zylicz M, and Georgopoulos C.. (February 1986) The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene.  A gene that encodes a heat shock protein. J Biol Chem. Feb 5;261(4):1782-5. (Pubmed)

Cowing DW, Bardwell JC, Craig EA, Woolford C, Hendrix RW, and Gross CA. (May 1985) Consensus sequence for Escherichia coli heat shock gene promoters. Proc Natl Acad Sci USA. May;82(9):2679-83. (Pubmed)

Bardwell JC and Craig EA.. (February 1984) Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proc Natl Acad Sci USA. Feb;81(3):848-52. (Pubmed)

contatiner