Author

P. M. Walden

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Biochemistry· 1

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Organism:bacteria (other)· 1 Approach:experimental assay· 1 Research Focus:protein folding & dynamics· 1 Assay:structural biology· 1

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A. E. Whitten· 1 shared B. Heras· 1 shared G. King· 1 shared J. L. Martin· 1 shared M. Halili· 1 shared P. Lakshmanane· 1 shared

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2018-2018 · peak 1/yr

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1 shared paperBiochemistry

A. E. Whitten

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1 paper

Recent·Most cited

The atypical thiol-disulfide exchange protein alpha-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase

P. M. Walden, P. Lakshmanane, M. Halili, B. Heras, G. King, A. E. Whitten, J. L. Martin

This study characterizes the structure and function of DsbA2 from Wolbachia pipientis, revealing it as a homotrimeric disulfide isomerase with distinct activity compared to other DsbA enzymes.

bioRxiv · Sep 11, 2018Biochemistry