Author

T. D. Babatz

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· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

E. P. Carpenter· 2 shared L. Nie· 2 shared S. Michaelis· 2 shared A. C. W. Pike· 1 shared A. Chu· 1 shared A. Quigley· 1 shared B. Rotty· 1 shared E. D. Spear· 1 shared

Activity by Year

2020-2020 · peak 2/yr

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10 top collaborators · 39 mutual co-author links

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2 shared papersCell Biology

E. P. Carpenter

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2 papers

Recent·Most cited

Cleavage Site Specificity for Processing of Farnesylated Prelamin A by the Zinc Metalloprotease ZMPSTE24

T. D. Babatz, E. D. Spear, W. Xu, O. L. Sun, L. Nie, E. P. Carpenter, S. Michaelis

This study identifies sequence requirements for ZMPSTE24 cleavage of prelamin A, revealing preferences for hydrophobic residues at P1 and sensitivity of C-terminal residues.

bioRxiv · Aug 17, 2020Cell Biology

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