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Biology and Biochemistry

D-Index
67
Citations
16381
World Ranking
8207
National Ranking
3710

Overview

James C. A. Bardwell is affiliated with the University of Michigan-Ann Arbor in the United States. Their research primarily falls within the field of Biochemistry, Genetics and Molecular Biology, with a particular focus on Molecular Biology, Cell Biology, Immunology, Biochemistry, and Genetics.

The key topics covered in their work include:

  • RNA and protein synthesis mechanisms
  • RNA Research and Splicing
  • Protein Structure and Dynamics
  • Heat shock proteins research
  • Mitochondrial Function and Pathology
  • DNA and Nucleic Acid Chemistry
  • RNA modifications and cancer

Several frequent co-authors collaborate with Bardwell, including Bikash R. Sahoo, Rishav Mitra, Xiexiong Deng, Kevin Wu, and Mark Dulchavsky.

Their work has been published multiple times in notable venues, with recurrent publications in:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Biophysical Journal
  • Nature Communications
  • Nature Chemical Biology
  • Journal of Biological Chemistry

Recent papers by Bardwell demonstrate a focus on bacterial chromatin dynamics, chaperone mechanisms, and enzymatic interactions, including:

  • Polyphosphate drives bacterial heterochromatin formation, 2021, Science Advances
  • ATP-Independent Chaperones, 2022, Annual Review of Biophysics
  • Trigger factor both holds and folds its client proteins, 2022, Nature Communications
  • Mechanism of the small ATP-independent chaperone Spy is substrate specific, 2021, Nature Communications
  • A cytochrome c is the natural electron acceptor for nicotine oxidoreductase, 2021, Nature Chemical Biology

Best Publications

  • Identification of a protein required for disulfide bond formation in vivo

    James C.A. Bardwell;Karen McGovern;Jon Beckwith

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

    James C. A. Bardwell;Elizabeth A. Craig

  • Chaperone Activity with a Redox Switch

    Ursula Jakob;Wilson B Muse;Markus Eser;James C.A. Bardwell

  • A pathway for disulfide bond formation in vivo.

    James C.A. Bardwell;Jie Oh Lee;Georg Jander;Nancy Martin

  • Oxidative Protein Folding Is Driven by the Electron Transport System

    Martin Bader;Wilson Muse;David P Ballou;Christian Gassner

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

    Jennifer L. Martin;Jennifer L. Martin;James C. A. Bardwell;James C. A. Bardwell;James C. A. Bardwell;John Kuriyan

  • Consensus sequence for Escherichia coli heat shock gene promoters

    Deborah W. Cowing;James C. A. Bardwell;Elizabeth A. Craig;Carol Woolford

  • Why is DsbA such an oxidizing disulfide catalyst

    Ulla Grauschopf;Jakob R. Winther;Philipp Korber;Thomas Zander

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

    Andre Zapun;James C. A. Bardwell;Thomas E. Creighton

  • Polyphosphate Is a Primordial Chaperone

    Michael J. Gray;Wei Yun Wholey;Nico O. Wagner;Claudia M. Cremers

  • Building bridges: disulphide bond formation in the cell

    James C. A. Bardwell

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

    James C. A. Bardwell;Elizabeth A. Craig

  • RNA methylation under heat shock control

    Hans Bügl;Eric B. Fauman;Bart L. Staker;Fuzhong Zheng

  • Oxidative protein folding in bacteria

    Jean Francois Collet;James C A Bardwell

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

    Hiroshi Kadokura;Hongping Tian;Hongping Tian;Thomas Zander;Thomas Zander;James C. A. Bardwell;James C. A. Bardwell

  • Autoregulation of RNase III operon by mRNA processing.

    J. C. A. Bardwell;P. Regnier;Su-Min Chen;Y. Nakamura

  • Ancient heat shock gene is dispensable.

    J C Bardwell;E A Craig

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

    Hitoshi Nakamoto;James C A Bardwell

  • Disulfide-Linked Protein Folding Pathways

    Bharath S. Mamathambika;James C. Bardwell

  • In vivo substrate specificity of periplasmic disulfide oxidoreductases.

    Annie Hiniker;James C.A. Bardwell

Frequent Co-Authors

Ursula Jakob
Ursula Jakob University of Michigan–Ann Arbor
Jean-François Collet
Jean-François Collet Université Catholique de Louvain
Jennifer L. Martin
Jennifer L. Martin University of Wollongong
Jon Beckwith
Jon Beckwith Harvard University
Charles L. Brooks
Charles L. Brooks University of Michigan–Ann Arbor
Brandon T. Ruotolo
Brandon T. Ruotolo University of Michigan–Ann Arbor
Elizabeth A. Craig
Elizabeth A. Craig University of Wisconsin–Madison
E. Neil G. Marsh
E. Neil G. Marsh University of Michigan–Ann Arbor
Christoph H. Borchers
Christoph H. Borchers McGill University
George Georgiou
George Georgiou The University of Texas at Austin

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