Author

Y. Y. Dong

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Chu· 2 shared E. P. Carpenter· 2 shared N. A. Burgess-Brown· 2 shared A. C. Pike· 1 shared A. C. W. Pike· 1 shared A. Quigley· 1 shared A. Sajid· 1 shared B. G. Davis· 1 shared

Activity by Year

2018-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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2 shared papersBiochemistry

A. Chu

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2 papers

Recent·Most cited

A new paradigm for Prelamin A proteolytic processing by ZMPSTE24: the upstream SY^LL cleavage occurs first and there is no CaaX processing by ZMPSTE24

L. Nie, E. Spear, T. D. Babatz, A. Quigley, Y. Y. Dong, A. Chu, B. Rotty, R. Chalk, S. M. M. Mukhopadhyay, N. A. Burgess-Brown, A. C. W. Pike, S. G. Young, S. Michaelis, E. P. Carpenter

This study challenges the established order of prelamin A processing by ZMPSTE24, showing that SY^LL cleavage occurs first and independently of C-terminal modifications.

bioRxiv · May 13, 2020 · PreprintBiochemistry

Structures of DPAGT1 explain glycosylation disease mechanisms and advance TB antibiotic design

Y. Y. Dong, H. Wang, A. C. Pike, S. J. Cochrane, S. Hamedzade, F. J. Wyszynsk, S. R. Bushell, S. F. Royer, D. A. Widdick, A. Sajid, H. I. Boshoff, R. Lucas, W.-M. Liu, S. S. Lee, T. Machida, , E. P. Carpenter

This paper determines the structures of DPAGT1 with substrates and inhibitors, revealing catalytic mechanisms and disease-causing mutations, and designs non-toxic antibiotics for tuberculosis.

bioRxiv · Apr 2, 2018Biochemistry