Author

B. Sessa

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 Cancer Biology· 1 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:mouse· 2 Assay:bulk RNA-seq· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:development & morphogenesis· 1 Research Focus:differential expression· 1 Research Focus:gene regulatory network inference· 1

Frequent Co-Authors

A. K. Singh· 1 shared B. H. Edani· 1 shared B. Siciliano· 1 shared E. J. Park· 1 shared K. A. Grabinsko· 1 shared L. Surmacz· 1 shared M. Y. Lee· 1 shared N.-T. Rahman· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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1 shared paperCancer Biology

A. K. Singh

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3 papers

Recent·Most cited

Loss of cis-PTase function in the liver promotes a highly penetrant form of fatty liver disease that rapidly transitions to hepatocellular carcinoma

A. K. Singh, B. Sessa

This study shows that loss of NgBR/cis-PTase function in the liver leads to fatty liver disease that progresses to hepatocellular carcinoma with 100% penetrance, and DGAT2 inhibition prevents this progression.

bioRxiv · Nov 13, 2023 · PreprintCancer Biology

Endothelial Nitric Oxide Synthase (eNOS) S1176 phosphorylation status governs atherosclerotic lesion formation

T. D. Nguyen, N.-T. Rahman, B. Sessa, M. Y. Lee

This study shows that phosphorylation of eNOS at S1176 by Akt determines atherosclerotic lesion formation, with phospho-mimic mutants reducing plaque while unphosphorylatable mutants increase it.

bioRxiv · Jan 13, 2022Physiology

Structural elucidation of the heterodimeric cis-prenyltransferase NgBR/DHDDS complex reveals novel insights in regulation of protein glycosylation

B. H. Edani, K. A. Grabinsko, R. Zhang, E. J. Park, B. Siciliano, L. Surmacz, Y. Ha, B. Sessa

The paper reports the crystal structure of the human NgBR/DHDDS complex, revealing how it stabilizes the active site and is regulated by phospholipids in protein glycosylation.

bioRxiv · Jun 3, 2020Biochemistry