Search Results - "Bardwell, J C"

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  1. 1

    Gas-phase Ortho-to-para Ratio of Formaldehyde Formed at Low Temperatures in Laboratory Ices by Yocum, K. M., Wilkins, O. H., Bardwell, J. C., Milam, S. N., Gerakines, P. A.

    Published in Astrophysical journal. Letters (01-12-2023)
    “…Abstract The ortho-to-para ratio (OPR) of formaldehyde (H 2 CO) has been used as a probe to estimate the formation temperature of molecules in interstellar,…”
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  2. 2

    A Pathway for Disulfide Bond Formation in vivo by BARDWELL, J. C. A, JIE-OH LEE, JANDER, G, MARTIN, N, BELIN, D, BECKWITH, J

    “…Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We describe here mutations in the gene for a second protein, DsbB,…”
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  3. 3

    Ancient heat shock gene is dispensable by BARDWELL, J. C. A, CRAIG, E. A

    Published in Journal of Bacteriology (01-07-1988)
    “…A correction has been published Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious…”
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  4. 4

    Eukaryotic Mr 83,000 Heat Shock Protein Has a Homologue in Escherichia coli by James C. A. Bardwell, Craig, Elizabeth A.

    “…We have isolated a gene from Escherichia coli homologous to the gene encoding the Mr 83,000 Drosophila heat shock protein (hsp83). In E. coli the protein…”
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  5. 5

    Identification of a protein required for disulfide bond formation in vivo by Bardwell, J C, McGovern, K, Beckwith, J

    Published in Cell (01-11-1991)
    “…We describe a mutation (dsbA) that renders Escherichia coli severely defective in disulfide bond formation. In dsbA mutant cells, pulse-labeled beta-lactamase,…”
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  6. 6

    Consensus Sequence for Escherichia coli Heat Shock Gene Promoters by Cowing, Deborah W., James C. A. Bardwell, Craig, Elizabeth A., Woolford, Carol, Hendrix, Roger W., Gross, Carol A.

    “…We have identified promoters for the Escherichia coli heat shock operons dnaK and groE and the gene encoding heat shock protein C62.5. Transcription from each…”
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    The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein by Bardwell, J C, Tilly, K, Craig, E, King, J, Zylicz, M, Georgopoulos, C

    Published in The Journal of biological chemistry (05-02-1986)
    “…The Escherichia coli dnaJ gene product is required for bacteriophage lambda DNA replication at all temperatures. It is also essential for bacterial viability…”
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  9. 9

    Crystal structure of the DsbA protein required for disulphide bond formation in vivo by Martin, Jennifer L, Bardwell, James C. A, Kuriyan, John

    Published in Nature (London) (30-09-1993)
    “…Proteins that contain disulphide bonds are often slow to fold in vitro because the oxidation and correct pairing of the cysteine residues is rate limiting. The…”
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    Effectiveness of larval defenses against spider predation in cranberry ecosystems by Bardwell, C.J. (University of Massachusetts, Amherst, MA.), Averill, A.L

    Published in Environmental entomology (01-10-1996)
    “…Two laboratory experiments, a choice test and observations of individual spider-larva interactions, were conducted to determine how the morphological or…”
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  12. 12

    The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding by Guddat, Luke W., Martin, Jennifer L., Bardwell, James C.A., Zander, Thomas

    Published in Protein science (01-06-1997)
    “…DsbA is a protein‐folding catalyst from the periplasm of Escherichia coli that interacts with newly translocated polypeptide substrate and catalyzes the…”
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  13. 13

    Structural analysis of three His32 mutants of DsbA: Support for an electrostatic role of His32 in DsbA stability by Guddat, Luke W., Bardwell, James C. A., Glockshuber, Rudi, Huber‐Wunderlich, Martina, Zander, Thomas, Martin, Jennifer L.

    Published in Protein science (01-09-1997)
    “…DsbA, a 21‐kDa protein from Escherichia coli, is a potent oxidizing disulfide catalyst required for disulfide bond formation in secreted proteins. The active…”
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  14. 14

    Sequence and expression of the Escherichia coli recR locus by YEUNG, T, MULLIN, D. A, KEN-SHIUNG CHEN, CRAIG, E. A, BARDWELL, J. C. A, WALKER, J. R

    Published in Journal of Bacteriology (01-10-1990)
    “…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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  15. 15

    Major Heat Shock Gene of Drosophila and the Escherichia coli Heat-Inducible dnaK Gene are Homologous by James C. A. Bardwell, Craig, Elizabeth A.

    “…The Escherichia coli dnaK gene is homologous to the major heat shock-induced gene in Drosophila (Hsp70). The primary DNA sequence of the entire protein-coding…”
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  16. 16

    Autoregulation of RNase III operon by mRNA processing by Bardwell, J.C., Régnier, P., Chen, S.M., Nakamura, Y., Grunberg‐Manago, M., Court, D.L.

    Published in The EMBO journal (01-11-1989)
    “…RNase III has been implicated in the control of gene expression by the processing of mRNA. We have found that the rnc operon is autoregulated; rnc‐ mutant…”
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  17. 17

    Expression and characterization of RNase III and Era proteins. Products of the rnc operon of Escherichia coli by Chen, S M, Takiff, H E, Barber, A M, Dubois, G C, Bardwell, J C, Court, D L

    Published in The Journal of biological chemistry (15-02-1990)
    “…The synthesis rates of ribonuclease III (RNase III) and Era proteins are relatively low, and expression of the era gene is translationally coupled with…”
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  18. 18

    Chaperone Activity with a Redox Switch by Jakob, Ursula, Muse, Wilson, Eser, Markus, Bardwell, James C.A

    Published in Cell (05-02-1999)
    “…Hsp33, a member of a newly discovered heat shock protein family, was found to be a very potent molecular chaperone. Hsp33 is distinguished from all other known…”
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  19. 19

    Oxidative protein folding in bacteria by Collet, Jean‐Francois, Bardwell, James C. A.

    Published in Molecular microbiology (01-04-2002)
    “…Summary Ten years ago it was thought that disulphide bond formation in prokaryotes occurred spontaneously. Now two pathways involved in disulphide bond…”
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  20. 20

    Redox Switch of Hsp33 Has a Novel Zinc-binding Motif by Jakob, U, Eser, M, Bardwell, J C

    Published in The Journal of biological chemistry (08-12-2000)
    “…The chaperone activity of the heat shock protein Hsp33 is regulated by reversible disulfide bond formation. Oxidized Hsp33 is active, and reduced Hsp33 is…”
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