Author

J. Puffal

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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Microbiology· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:bacteria (other)· 3 Research Focus:cell type annotation· 3 Assay:proteomics· 3 Research Focus:cell signaling & trafficking· 1 Research Focus:development & morphogenesis· 1 Organism:human· 1

Frequent Co-Authors

Y. S. Morita· 4 shared J. R. Brenner· 2 shared T. A. Gray· 2 shared A. Garcia-Heredia· 1 shared A. H. Dills· 1 shared C. A. Z. Rokicki· 1 shared C. E. Sein· 1 shared D. B. Moody· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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4 shared papersMicrobiology

Y. S. Morita

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Author profile →

4 papers

Recent·Most cited

Compartmentalized Cell Envelope Biosynthesis in Mycobacterium tuberculosis

J. Puffal, I. L. Sparks, J. R. Brenner, X. Li, J. D. Leszyk, J. Hayashi, S. A. Shaffer, Y. S. Morita

This paper identifies the conserved intracellular membrane domain (IMD) in Mycobacterium tuberculosis, showing it is a specialized compartment for synthesizing virulence-related lipids.

bioRxiv · Jan 7, 2022Microbiology

Fluorescence Imaging-Based Discovery of Membrane Domain-Associated Proteins in Mycobacterium smegmatis

C. A. Z. Rokicki, J. R. Brenner, A. H. Dills, J. J. Judd, J. C. Kester, J. Puffal, J. T. Wade, T. A. Gray, K. M. Derbyshire, S. Fortune, Y. S. Morita

The paper uses fluorescence imaging to verify and discover new proteins associated with the intracellular membrane domain in Mycobacterium smegmatis.

bioRxiv · Feb 17, 2021Microbiology

The mycobacterial cell wall partitions the plasma membrane to organize its own synthesis

A. Garcia-Heredia, T. Kado, C. E. Sein, J. Puffal, S. H. Osman, J. Judd, T. A. Gray, Y. S. Morita, M. S. Siegrist

The paper shows that in Mycobacterium smegmatis, peptidoglycan precursors are synthesized in distinct plasma membrane domains that are separate from sites of cell wall assembly, and this partitioning is essential for ordered synthesis.

bioRxiv · Jul 6, 2020 · PreprintMicrobiology

Demethylmenaquinone methyl transferase is a membrane domain-associated protein essential for menaquinone homeostasis in Mycobacterium smegmatis

J. Puffal, J. A. Mayfield, D. B. Moody, Y. S. Morita

This study identifies MenG as an essential enzyme for menaquinone homeostasis in Mycobacterium smegmatis, showing its association with the intracellular membrane domain and its role in regulating menaquinone levels.

bioRxiv · Oct 25, 2018Microbiology