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Retraction Note: A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo

Dario Mizrachi
Michael-Paul Robinson
Matthew P. DeLisa
Amendments and Corrections19 Jan 2024
Nature Chemical Biology

Volume: 20, P: 392
Isolation of full-length IgG antibodies from combinatorial libraries expressed in the cytoplasm of Escherichia coli

Discovery of full-length antibodies can be slow and labor intensive. Here, the authors describe a robust genetic assay for facile isolation of IgG antibodies from combinatorial libraries expressed in the cytoplasm of redox-engineered bacteria.

Michael-Paul Robinson
Jinjoo Jung
Matthew P. DeLisa
ResearchOpen Access14 Jun 2023
Nature Communications

Volume: 14, P: 1-12
Efficient expression of full-length antibodies in the cytoplasm of engineered bacteria

Current methods for production of monoclonal antibodies often require refolding steps or secretion across biological membranes. Here, Robinson et al. describe engineered E. colistrains for efficient production of functional immunoglobulin G antibodies in the bacterial cytoplasm.

Michael-Paul Robinson
Na Ke
Mehmet Berkmen
ResearchOpen Access27 Aug 2015
Nature Communications

Volume: 6, P: 1-9
RETRACTED ARTICLE: A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo

The design of a water-soluble variant of the integral membrane protein DsbB and its coexpression with an export-defective copy of DsbA facilitates disulfide-bond formation in the Escherichia coli cytoplasm in a quinone-dependent fashion.

Dario Mizrachi
Michael-Paul Robinson
Matthew P DeLisa
Research19 Jun 2017
Nature Chemical Biology

Volume: 13, P: 1022-1028