Author

G. A. Cornwall

Texas Tech University Health Sciences Center

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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Biophysics· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Organism:mouse· 2 Assay:proteomics· 2 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

R. B. Sutton· 2 shared A. Snow· 1 shared C. Myers· 1 shared F. M. Harsini· 1 shared G. R. Atkins· 1 shared I. L. Scott· 1 shared J. Villarreal· 1 shared J. Williams· 1 shared

Activity by Year

2023-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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2 shared papersCell Biology

R. B. Sutton

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3 papers

Recent·Most cited

DNA modulates structural transitions and oligomerization kinetics of the functional amyloid CRES

Ritika Kukreja, Marella D. Canny, G. A. Cornwall, Michael P. Latham

The paper shows DNA binding accelerates CRES amyloid formation by altering oligomerization pathways and kinetics, suggesting a regulatory mechanism for functional amyloid diversity.

Journal of the American Chemical Society · Dec 24, 2025Peer-reviewedBiophysics

The Mouse Epididymal Amyloid Matrix: A Mammalian Counterpart of a Bacterial Biofilm

C. Myers, G. R. Atkins, J. Villarreal, R. B. Sutton, G. A. Cornwall

The paper identifies the mouse epididymal amyloid matrix as a structural and functional analog of bacterial biofilms, protecting spermatozoa through components like eDNA, eRNA, and mucin-like polysaccharides.

iScience · Jun 1, 2024Peer-reviewedCell Biology

Pathogenic Mutations in the C2A Domain of Dysferlin form Amyloid that Activates the Inflammasome.

I. L. Scott, M. J. Dominguez, A. Snow, F. M. Harsini, J. Williams, K. L. Fuson, R. Thapa, P. Bhattacharjee, G. A. Cornwall, P. A. Keyel, R. B. Sutton

This study shows that C2A domain mutations in dysferlin cause amyloid formation, which activates the NLRP3 inflammasome and leads to inflammation and muscle dysfunction in Limb-Girdle Muscular Dystrophy Type-2B/2R.

bioRxiv · Apr 24, 2023 · PreprintBiophysics