J. Bardwell

发表

Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm.

Hitoshi Nakamoto, Hitoshi Nakamoto, J. Bardwell, 2004, Biochimica et biophysica acta.

Snapshots of DsbA in Action: Detection of Proteins in the Process of Oxidative Folding

Thomas Zander, Jon Beckwith, J. Beckwith, 2004, Science.

Optimizing protein stability in vivo.

S. Radford, S. Warriner, J. Bardwell, 2009, Molecular cell.

Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular Modeling.

Logan S. Ahlstrom, Loïc Salmon, C. Brooks, 2016, Journal of the American Chemical Society.

Disulfide-linked protein folding pathways.

J. Bardwell, Bharath S Mamathambika, James C Bardwell, 2008, Annual review of cell and developmental biology.

Structure of Hsp15 reveals a novel RNA‐binding motif

J. Bardwell, P. Korber, B. Staker, 2000, The EMBO journal.

Building bridges: disulphide bond formation in the cell

J. Bardwell, J C Bardwell, 1994, Molecular microbiology.

Structural Organization of Procaryotic and Eucaryotic Hsp90. INFLUENCE OF DIVALENT CATIONS ON STRUCTURE AND FUNCTION (*)

J. Buchner, U. Jakob, J. Bardwell, 1995, The Journal of Biological Chemistry.

Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Ben A Meinen, C. Borchers, U. Jakob, 2019, Nature Communications.

Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Ben A Meinen, C. Borchers, U. Jakob, 2019, Nature Communications.

Conditional disorder in chaperone action.

U. Jakob, J. Bardwell, 2012, Trends in biochemical sciences.

An Engineered Pathway for the Formation of Protein Disulfide Bonds

George Georgiou, G. Georgiou, J. Collet, 2004, Science.

The CXXC Motif Is More than a Redox Rheostat*

J. Bardwell, Annekathrin von Hacht, Jonathan L Pan, 2007, Journal of Biological Chemistry.

Effect of Sequences of the Active-Site Dipeptides of DsbA and DsbC on In Vivo Folding of Multidisulfide Proteins inEscherichia coli

Paul H. Bessette, J. Bardwell, J. Swartz, 2001, Journal of bacteriology.

Reconstitution of a Disulfide Isomerization System*

J. Collet, M. Bader, J. Riemer, 2002, The Journal of Biological Chemistry.

The origami of thioredoxin‐like folds

J. Bardwell, Jonathan L Pan, Jonathan L. Pan, 2006, Protein science : a publication of the Protein Society.

Oxidative protein folding in bacteria

J. Collet, J. Bardwell, James C. A. Bardwell, 2002, Molecular microbiology.

Expression and characterization of RNase III and Era proteins. Products of the rnc operon of Escherichia coli.

D. Court, J. Bardwell, H. Takiff, 1990, The Journal of biological chemistry.

Protein folding while chaperone bound is dependent on weak interactions

J. Bardwell, Changhan Lee, Frederick W Stull, 2019, Nature Communications.

Electrostatic interactions are important for chaperone-client interaction in vivo.

J. Bardwell, Changhan Lee, Hyunhee Kim, 2018, Microbiology.

Disulfide Bonds Are Generated by Quinone Reduction*

M. Bader, J. Bardwell, Chang-an Yu, 2000, The Journal of Biological Chemistry.

DsbB Catalyzes Disulfide Bond Formation de Novo *

J. Bardwell, J. Regeimbal, James M. Regeimbal, 2002, The Journal of Biological Chemistry.

Disulfide bond formation involves a quinhydrone-type charge–transfer complex

B. Trumpower, J. Bardwell, D. Ballou, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Key Players Involved in Bacterial Disulfide‐Bond Formation

J. Bardwell, Jacqueline T Tan, Jacqueline T. Tan, 2004, Chembiochem : a European journal of chemical biology.

Protein refolding by pH-triggered chaperone binding and release

Titus M. Franzmann, U. Jakob, J. Bardwell, 2009, Proceedings of the National Academy of Sciences.

Identification of the Ubiquinone-binding Domain in the Disulfide Catalyst Disulfide Bond Protein B*

M. Bader, J. Bardwell, Linda P C Yu, 2002, The Journal of Biological Chemistry.

Ancient heat shock gene is dispensable

E. Craig, J. Bardwell, 1988, Journal of bacteriology.

Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity

J. Bardwell, Wei He, S. Quan, 2020, The Journal of Biological Chemistry.

Isolation of bacteria envelope proteins.

J. Collet, J. Bardwell, A. Hiniker, 2013, Methods in molecular biology.

Correction for Lee et al., RNA design rules from a massive open laboratory

Logan S. Ahlstrom, Amanda A Winburn, Firas Khatib, 2015, Proceedings of the National Academy of Sciences.

Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli.

E. Craig, J. Bardwell, 1987, Proceedings of the National Academy of Sciences of the United States of America.

ERRATUM Ancient Heat Shock Gene Is Dispensable

E. Craig, J. Bardwell, 2022 .

The bonds that tie: Catalyzed disulfide bond formation

J. Beckwith, J. Bardwell, 1993, Cell.

A cytochrome c is the natural electron acceptor for nicotine oxidoreductase

J. Bardwell, Frederick W Stull, Mark Dulchavsky, 2020, Nature Chemical Biology.

Identifying dynamic, partially occupied residues using anomalous scattering

Loïc Salmon, J. Bardwell, A. Wagner, 2019, bioRxiv.

Symmetry‐Directed Self‐Assembly of a Tetrahedral Protein Cage Mediated by de Novo‐Designed Coiled Coils

S. Badieyan, B. Ruotolo, J. Bardwell, 2017, Chembiochem : a European journal of chemical biology.

Forces Driving Chaperone Action

J. Bardwell, S. Horowitz, P. Koldewey, 2016, Cell.

Forces Driving Chaperone Action Graphical

J. Bardwell, S. Horowitz, P. Koldewey, 2016 .

The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein.

J. King, C. Georgopoulos, E. Craig, 1986, The Journal of biological chemistry.

rRNA Methyltransferase Rescues a Null Mutation in a Heat-Induced Overexpression of Two Different GTPases

U. Jakob, J. Bardwell, Jacqueline T Tan, 2002 .

A Comparative Analysis of Mucormycosis in Immunosuppressed hosts Including Patients with Uncontrolled Diabetes in the Southwest United States.

J. Bardwell, T. Zangeneh, M. Al-Obaidi, 2021, The American journal of medicine.

Cytosolic Selection Systems To Study Protein Stability

J. Bardwell, Ajamaluddin Malik, Antje Mueller-Schickert, 2014, Journal of bacteriology.

Super Spy variants implicate flexibility in chaperone action

Yang Zhang, C. Borchers, Jianyi Yang, 2014, eLife.

Disulfide bond catalysts in Escherichia coli.

J. Bardwell, T. Zander, N. Phadke, 1998, Methods in enzymology.

The enzyme pseudooxynicotine amine oxidase from Pseudomonas putida S16 is not an oxidase, but a dehydrogenase

J. Bardwell, T. Barkman, Zhiyao Zhang, 2022, The Journal of biological chemistry.

Evidence for Conformational Changes within DsbD: Possible Role for Membrane-Embedded Proline Residues

D. Vertommen, J. Collet, J. Bardwell, 2006, Journal of bacteriology.

RNAs as chaperones

J. Bardwell, S. Horowitz, 2016, RNA biology.

A metabolite binding protein moonlights as a bile‐responsive chaperone

R. Glockshuber, D. Żyła, J. Bardwell, 2020, The EMBO journal.

In vivo chloride concentrations surge to proteotoxic levels during acid stress

J. Bardwell, R. Stockbridge, Frederick W Stull, 2018, Nature Chemical Biology.

Disulfide bond isomerization in prokaryotes.

J. Bardwell, S. Gleiter, 2008, Biochimica et biophysica acta.

Activation of the redox-regulated molecular chaperone Hsp33--a two-step mechanism.

H. Lilie, J. H. Hoffmann, U. Jakob, 2001, Structure.

Mutational Analysis of the Disulfide Catalysts DsbA and DsbB

J. Bardwell, Jacqueline T Tan, Ying Lu, 2005, Journal of bacteriology.

Elaborating a coiled‐coil‐assembled octahedral protein cage with additional protein domains

Ben A Meinen, J. Bardwell, E. Marsh, 2018, Protein science : a publication of the Protein Society.

Protein unfolding as a switch from self-recognition to high-affinity client binding

C. Borchers, D. Reichmann, U. Jakob, 2016, Nature Communications.

The dance of disulfide formation

J. Bardwell, 2004, Nature Structural &Molecular Biology.

SERF, a family of tiny highly conserved, highly charged proteins with enigmatic functions

Bikash R. Sahoo, J. Bardwell, 2022, The FEBS journal.

Identification of a protein required for disulfide bond formation in vivo

J. Beckwith, J. Bardwell, K. McGovern, 1991, Cell.

Selecting Conformational Ensembles Using Residual Electron and Anomalous Density (READ).

Logan S. Ahlstrom, Loïc Salmon, J. Bardwell, 2018, Methods in molecular biology.

In vivo detection and quantification of chemicals that enhance protein stability.

J. Bardwell, Linda Foit, Tsinatkeab T. Hailu, 2013, Analytical biochemistry.

Infection of Aortic Endograft caused by Coccidioidomycosis.

J. Bardwell, Fariba M. Donovan, T. Zangeneh, 2019, The American journal of medicine.

Pulmonary Mucormycosis in a Heart Transplant Patient.

J. Bardwell, T. Zangeneh, J. Márquez, 2020, American Journal of Medicine.

Copper Stress Causes an in Vivo Requirement for the Escherichia coli Disulfide Isomerase DsbC*

J. Collet, J. Bardwell, A. Hiniker, 2005, Journal of Biological Chemistry.

Kinetic Characterization of the Disulfide Bond-forming Enzyme DsbB*

J. Bardwell, D. Ballou, S. Gleiter, 2007, Journal of Biological Chemistry.

Chaperone OsmY facilitates the biogenesis of a major family of autotransporters

J. Bardwell, H. Bernstein, Sunyia Hussain, 2019, Molecular microbiology.

Trigger factor both holds and folds its client proteins

J. Bardwell, Kevin Wu, T. Minshull, 2022, Nature communications.

Consensus sequence for Escherichia coli heat shock gene promoters.

C. Gross, E. Craig, J. Bardwell, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Polyphosphate is a primordial chaperone.

R. Bender, U. Jakob, J. Bardwell, 2014, Molecular cell.

In Vivo Substrate Specificity of Periplasmic Disulfide Oxidoreductases*

J. Bardwell, A. Hiniker, 2004, Journal of Biological Chemistry.

The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD‐independent manner

D. Vertommen, J. Collet, L. Knoops, 2007, Molecular microbiology.

E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly

M. Chapman, Jens C. Schmidt, U. Jakob, 2011, Prion.

Oxidative Protein Folding Is Driven by the Electron Transport System

M. Bader, J. Bardwell, D. Ballou, 1999, Cell.

Gram-positive DsbE Proteins Function Differently from Gram-negative DsbE Homologs

D. Eisenberg, C. Goulding, J. Bardwell, 2004, Journal of Biological Chemistry.

Genetic selection designed to stabilize proteins uncovers a chaperone called Spy

Miroslaw Cygler, Ursula Jakob, Philipp Koldewey, 2011, Nature Structural &Molecular Biology.

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.

J. Bardwell, Jonathan L Pan, I. Sliskovic, 2008, Journal of molecular biology.

A pathway for disulfide bond formation in vivo.

D. Belin, J. Beckwith, J. Bardwell, 1993, Proceedings of the National Academy of Sciences of the United States of America.

A glimpse into TriC’s magic chamber of secrets

J. Bardwell, 2022, Cell.

Chaperone-client interactions: Non-specificity engenders multifunctionality

J. Bardwell, S. Horowitz, P. Koldewey, 2017, The Journal of Biological Chemistry.

Polyphosphate drives bacterial heterochromatin formation

Peter L. Freddolino, Ben A Meinen, J. Biteen, 2021, Science advances.

Folding Optimization In Vivo Uncovers New Chaperones.

Frieda A. Sorgenfrei, J. Bardwell, Frieda A Sorgenfrei, 2015, Journal of molecular biology.

Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous.

E. Craig, J. Bardwell, Elizabeth A. Craig, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Chaperone discovery

J. Bardwell, S. Quan, 2012, BioEssays : news and reviews in molecular, cellular and developmental biology.

Protein folding occurs while bound to the ATP-independent chaperone Spy

S. Radford, J. Bardwell, P. Koldewey, 2015, Nature Structural &Molecular Biology.

Trigger factor both holds and folds its client proteins

J. Bardwell, Kevin Wu, T. Minshull, 2022, Nature Communications.

Mechanism of the small ATP-independent chaperone Spy is substrate specific

Ben A Meinen, B. Ruotolo, C. V. van Mierlo, 2021, Nature Communications.

Supplementary InformationJB2

J. Bardwell, Changhan Lee, Frederick W Stull, 2019 .

Periplasmic Chaperones and Prolyl Isomerases.

J. Betton, J. Bardwell, Frederick W Stull, 2018, EcoSal Plus.

Folding while bound to chaperones.

J. Bardwell, S. Horowitz, P. Koldewey, 2018, Current opinion in structural biology.

Directed evolution to improve protein folding in vivo

Veronika Sachsenhauser, James CA Bardwell, J. Bardwell, 2017, Current opinion in structural biology.

Visualizing chaperone-assisted protein folding

Logan S. Ahlstrom, H. V. D. Bedem, Loïc Salmon, 2016 .

HdeB Functions as an Acid-protective Chaperone in Bacteria*

Loïc Salmon, U. Jakob, J. Bardwell, 2014, The Journal of Biological Chemistry.

Genetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor.

J. Bardwell, Linda Foit, Bharath S Mamathambika, 2011, Antioxidants & redox signaling.

Insight into Disulfide Bond Catalysis in Chlamydia from the Structure and Function of DsbH, a Novel Oxidoreductase*

D. Boyd, T. Ulmer, J. Bardwell, 2008, Journal of Biological Chemistry.

Disulfide relays between and within proteins: the Ero1p structure.

J. Bardwell, A. Hiniker, 2004, Trends in biochemical sciences.

Disulfide bond formation, a race between FAD and oxygen.

J. Bardwell, 2002, Developmental cell.

Disulfide Bond Formation in Prokaryotes and Eukaryotes

J. Bardwell, James M. Regeimbal, 2002 .

Disulfides out of thin air

J. Collet, J. Bardwell, 2002, Nature Structural Biology.

Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue*S⃞

Jennifer L. Martin, Zhaohui Xu, J. Bardwell, 2009, Journal of Biological Chemistry.

Do nucleic acids moonlight as molecular chaperones?

U. Jakob, J. Bardwell, M. Gray, 2016, Nucleic acids research.

RNA methylation under heat shock control.

E. Fauman, U. Jakob, J. Bardwell, 2000, Molecular cell.

Overexpression of Two Different GTPases Rescues a Null Mutation in a Heat-Induced rRNA Methyltransferase

U. Jakob, J. Bardwell, Jacqueline T Tan, 2002, Journal of bacteriology.

Disulfide Bond Formation Enzymes

J. Bardwell, 2007 .

Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA

M. Bader, J. Riemer, J. Bardwell, 2001, The EMBO journal.

Hsp15: a ribosome‐associated heat shock protein

K. Nierhaus, J. Bardwell, J. Stahl, 2000, The EMBO journal.

Evaluation of de novo-designed coiled coils as off-the-shelf components for protein assembly

S. Badieyan, B. Ruotolo, J. Bardwell, 2017 .

Sequence and expression of the Escherichia coli recR locus

E. Craig, D. Mullin, J. Bardwell, 1990, Journal of bacteriology.

Crystal structure of the DsbA protein required for disulphide bond formation in vivo

John Kuriyan, J. Kuriyan, Jennifer L. Martin, 1993, Nature.

Chaperone activation by unfolding

C. Brooks, J. Bardwell, Linda Foit, 2013, Proceedings of the National Academy of Sciences.

Thioredoxin 2, an Oxidative Stress-induced Protein, Contains a High Affinity Zinc Binding Site*

J. Collet, U. Jakob, J. Bardwell, 2003, Journal of Biological Chemistry.

HdeB functions as an acid-protective chaperone in bacteria.

Loïc Salmon, U. Jakob, J. Bardwell, 2015, The Journal of Biological Chemistry.

Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding

U. Jakob, J. Bardwell, J. Hupfeld, 2009, Proceedings of the National Academy of Sciences.

Computational Redesign of Thioredoxin Is Hypersensitive toward Minor Conformational Changes in the Backbone Template.

Kresten Lindorff-Larsen, Jesper Ferkinghoff-Borg, Thomas Hamelryck, 2016, Journal of molecular biology.

Structural analysis of three His32 mutants of DsbA: Support for an electrostatic role of His32 in DsbA stability

R. Glockshuber, L. Guddat, Jennifer L. Martin, 1997, Protein science : a publication of the Protein Society.

The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding

L. Guddat, Jennifer L. Martin, J. Bardwell, 1997, Protein science : a publication of the Protein Society.

DsbG, a Protein Disulfide Isomerase with Chaperone Activity*

M. Bader, U. Jakob, J. Bardwell, 2000, The Journal of Biological Chemistry.

Chaperone Activity with a Redox Switch

U. Jakob, J. Bardwell, W. Muse, 1999, Cell.

Redox Switch of Hsp33 Has a Novel Zinc-binding Motif*

U. Jakob, J. Bardwell, Markus Eser, 2000, The Journal of Biological Chemistry.

Yeast tripartite biosensors sensitive to protein stability and aggregation propensity.

J. Bardwell, Hyunhee Kim, V. Sachsenhauser, 2020, ACS chemical biology.

Heating greatly speeds Coomassie blue staining and destaining.

J. Bardwell, C. Wong, S. Sridhara, 2000, BioTechniques.

Why is DsbA such an oxidizing disulfide catalyst?

J. Winther, U. Grauschopf, J. Bardwell, 1995, Cell.

A New Heat Shock Protein That Binds Nucleic Acids*

D. Herschlag, J. Bardwell, T. Zander, 1999, The Journal of Biological Chemistry.

A tripartite fusion system for the selection of protein variants with increased stability in vivo.

J. Bardwell, Linda Foit, 2013, Methods in molecular biology.

Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Ben A Meinen, C. Borchers, U. Jakob, 2019, Nature Communications.

Flexible, symmetry-directed approach to assembling protein cages

G. Skiniotis, B. Ruotolo, J. Bardwell, 2016, Proceedings of the National Academy of Sciences.

Engineered pathways for correct disulfide bond oxidation.

J. Bardwell, Guoping Ren, 2011, Antioxidants & redox signaling.

Disulfide bond isomerization in prokaryotes.

J. Bardwell, A. Hiniker, 2003, Biochemistry.

The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.

T. Creighton, A. Zapun, J. Bardwell, 1993, Biochemistry.

SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins

Ben A Meinen, B. Ruotolo, J. Bardwell, 2019, Proceedings of the National Academy of Sciences.

The Mechanism of HdeA Unfolding and Chaperone Activation.

Logan S. Ahlstrom, E. Eisenmesser, Loïc Salmon, 2018, Journal of molecular biology.

Laboratory evolution of one disulfide isomerase to resemble another

Jennifer L. Martin, J. Stuckey, J. Bardwell, 2007, Proceedings of the National Academy of Sciences.

Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization.

L. Guddat, J. Bardwell, J. Martin, 1998, Structure.

Reconstitution of a Protein Disulfide Catalytic System*

M. Bader, J. Bardwell, T. Zander, 1998, The Journal of Biological Chemistry.

Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.

J. Beckwith, M. Bader, H. Kadokura, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Molecular Cell Polyphosphate Is a Primordial Chaperone

R. Bender, U. Jakob, J. Bardwell, 2022 .

DsbC activation by the N-terminal domain of DsbD

J. Beckwith, M. Bader, F. Katzen, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Determining crystal structures through crowdsourcing and coursework

Zoran Popović, Neha Jain, Scott Horowitz, 2016, Nature Communications.

Computational Redesign of Thioredoxin Is Hypersensitive toward Minor Conformational Changes in the Backbone Template.

K. E. Johansson, K. Lindorff-Larsen, T. Hamelryck, 2016, Journal of molecular biology.

Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase

D. Boyd, J. Bardwell, M. Berkmen, 2015, Antioxidants & redox signaling.

Protein oxidation: prime suspect found ‘not guilty’

J. Winther, M. Bader, J. Bardwell, 1999, Nature Cell Biology.

Catalysis of disulfide bond formation and isomerization in Escherichia coli.

M. Bader, J. Bardwell, 2001, Advances in protein chemistry.

Mitochondrial peroxiredoxin from Leishmania infantum after heat stress without unfolding client protein

Ben A Meinen, C. Borchers, U. Jakob, 2019 .

Laboratory Evolution of Escherichia coli Thioredoxin for Enhanced Catalysis of Protein Oxidation in the Periplasm Reveals a Phylogenetically Conserved Substrate Specificity Determinant*

G. Georgiou, D. Klein‐Marcuschamer, J. Bardwell, 2008, Journal of Biological Chemistry.

The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe‐2S] iron–sulfur cluster in an Escherichia coli thioredoxin mutant

Zhaohui Xu, D. Peisach, J. Collet, 2005, Protein science : a publication of the Protein Society.

mutant thioredoxinEscherichia colia [ 2 Fe2 S ] iron – sulfur cluster in an The crystal structure of TrxA ( CACA ) : Insights into the formation of

Zhaohui Xu, D. Peisach, J. Collet, 2005 .

Thiol modifications in a snapshot

J. Bardwell, 2005, Nature Biotechnology.

Protein G-quadruplex interactions and their effects on phase transitions and protein aggregation

Bikash R. Sahoo, J. Plavec, N. Clark, 2023, bioRxiv.

Directed evolution unlocks oxygen reactivity for a nicotine-degrading flavoenzyme

J. Bardwell, J. Momper, K. Shankar, 2023, Nature Chemical Biology.

Disulfide-linked protein folding pathways.

J. Bardwell, Bharath S Mamathambika, 2008, Annual review of cell and developmental biology.

Disulfide Bond Formation in Prokaryotes

J. Collet, J. Bardwell, 2008 .