J
Jon Beckwith
Researcher at Harvard University
Publications - 297
Citations - 36449
Jon Beckwith is an academic researcher from Harvard University. The author has contributed to research in topics: Escherichia coli & Periplasmic space. The author has an hindex of 101, co-authored 297 publications receiving 35324 citations. Previous affiliations of Jon Beckwith include Kyoto University & Laboratory of Molecular Biology.
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Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter.
TL;DR: The tight regulation of the PBAD promoter is exploited to study the phenotypes of null mutations of essential genes and the use of pBAD vectors as an expression system is explored.
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TnphoA: a transposon probe for protein export signals.
Colin Manoil,Jon Beckwith +1 more
TL;DR: A derivative of transposon Tn5 is constructed that permits the generation of hybrid proteins composed of alkaline phosphatase lacking its signal peptide fused to amino-terminal sequences of other proteins, and should help localize export signals within the structure of a protein, such as a transmembrane protein, as well as identify new chromosomal genes for secreted and trans Membrane proteins.
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Identification of a protein required for disulfide bond formation in vivo
TL;DR: The results suggest that disulfide bond formation is facilitated by DsbA in vivo, and may represent in vivo folding intermediates that chase slowly into stable oxidized forms.
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Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
TL;DR: It is demonstrated that the cytoplasm can be rendered sufficiently oxidizing to allow efficient formation of native disulfide bonds without compromising cell viability.
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The Role of the Thioredoxin and Glutaredoxin Pathways in Reducing Protein Disulfide Bonds in the Escherichia coliCytoplasm
TL;DR: E. coli requires either a functional thioredoxin or glutaredoxin system to reduce disulfide bonds which appear after each catalytic cycle in the essential enzyme ribonucleotide reductase and perhaps to reduce non-native disulfides in cytoplasmic proteins.