Author

A. Sulpizio

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· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:bacteria (other)· 2 Research Focus:cell signaling & trafficking· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Organism:E. coli· 1 Approach:genetic perturbation / CRISPR· 1

Frequent Co-Authors

Y. Mao· 3 shared J.-H. Shin· 2 shared M. B. Smolka· 2 shared M. Wan· 2 shared A. Akturk· 1 shared A. E. Connolly-Sporing· 1 shared A. Kang· 1 shared A. Kelley· 1 shared

Activity by Year

2019-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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3 shared papersBiochemistry

Y. Mao

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Engineered chimeras unveil swappable modular features of fatty acid and polyketide synthase acyl carrier proteins

Y. I. Cho, C. L. Armstrong, A. Sulpizio, K. K. Acheampong, K. N. Banks, O. Bardhan, S. J. Churchill, A. E. Connolly-Sporing, C. E. W. Crawford, P. L. Cruz Parrilla, S. M. Curtis, L. M. De La Ossa, S. C. Epstein, C. J. Farrehi, G. S. Hamrick, , L. K. Charkoudian

This study designs chimeric acyl carrier proteins to swap modular features between different ACPs, enabling compatibility with specific enzymes for synthetic pathway engineering.

bioRxiv · Dec 30, 2021Biochemistry

Structural basis of peptidoglycan endopeptidase regulation

J.-H. Shin, A. Sulpizio, A. Kelley, L. Alvarez, S. Murphy, F. Cava, Y. Mao, M. A. Saper, T. Doerr

This study solves the crystal structure of ShyA, a peptidoglycan endopeptidase, revealing a regulatory mechanism involving conformational changes that activate its catalytic activity.

bioRxiv · Nov 17, 2019Microbiology

Deubiquitination of phosphoribosyl-ubiquitin conjugates by PDE domain-containing Legionella effectors

M. Wan, A. Sulpizio, A. Akturk, W. H. J. Beck, M. Lanz, V. M. Faca, M. B. Smolka, J. P. Vogel, Y. Mao

This paper identifies DupA and DupB as deubiquitinases that reverse PR-ubiquitination, a novel modification mediated by Legionella effectors, and shows their role in modulating host-pathogen interactions.

bioRxiv · Aug 23, 2019Biochemistry

Protein polyglutamylation catalyzed by the bacterial Calmodulin-dependent pseudokinase SidJ

A. Sulpizio, M. E. Minelli, M. Wan, P. D. Burrowes, X. Wu, E. J. Sanford, J.-H. Shin, B. Williams, M. L. Goldberg, M. B. Smolka, Y. Mao

This study identifies SidJ as a bacterial pseudokinase that catalyzes polyglutamylation of SdeA, a Legionella effector, in a CaM-dependent manner, suppressing ADP-ribosylation.

bioRxiv · Aug 20, 2019Biochemistry