Author

M. B. Campana

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 Cell Biology· 1

Signature Assays, Organisms & Methods

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Assay:proteomics· 3 Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Organism:human· 2 Approach:deep learning· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1

Frequent Co-Authors

T. R. Davis· 2 shared A. Neumann· 1 shared E. D. Larson· 1 shared E. R. Cleverdon· 1 shared E. R. Curtis· 1 shared F. J. Irudayanathan· 1 shared H. Hehnly· 1 shared J. Hougland· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersBiochemistry

T. R. Davis

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Author profile →

3 papers

Recent·Most cited

PDGFRα/β heterodimer activation negatively affects downstream ERK1/2 signaling and cellular proliferation

M. B. Campana, M. R. Perkins, M. C. McCabe, A. Neumann, E. D. Larson, K. A. Fantauzzo

PDGFR/{beta} heterodimer binding to MYO1D promotes rapid internalization, inhibiting ERK1/2 phosphorylation and reducing cell proliferation.

bioRxiv · Dec 27, 2023Cell Biology

A remarkably specific ligand reveals ghrelin O-acyltransferase interacts with extracellular peptides and exhibits unexpected cellular localization for a secretory pathway enzyme

M. B. Campana, T. R. Davis, E. R. Cleverdon, M. Bates, N. Krishnan, E. R. Curtis, M. D. Childs, M. R. Pierce, S. X. Novak, Y. Morales-Rodriguez, M. Sieburg, H. Hehnly, L. G. Luyt, J. Hougland

This study identifies a specific ligand that shows GOAT interacts with extracellular ghrelin and facilitates its internalization, revealing new insights into its catalytic mechanism and signaling role.

bioRxiv · Jun 1, 2021 · PreprintBiochemistry

Molecular architecture of a membrane-spanning hormone acyltransferase required for metabolic regulation

M. B. Campana, F. J. Irudayanathan, T. R. Davis, K. R. McGovern-Gooch, R. Loftus, M. Ashkar, N. Escoffery, M. Navarro, M. A. Sieburg, S. nangia, J. L. Hougland

The paper presents a structural model of GOAT, an MBOAT enzyme, using co-evolutionary constraints and computational modeling validated by biochemistry, revealing a novel acylation mechanism within a transmembrane channel.

bioRxiv · Feb 28, 2019 · PreprintBiochemistry