Author

E. C. Carroll

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· 4 Immunology· 2 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:cell signaling & trafficking· 4 Assay:protein structure· 4 Organism:human· 3 Research Focus:protein folding & dynamics· 3 Approach:biophysical modeling· 1 Organism:C. elegans· 1 Research Focus:cancer & tumor microenvironment· 1

Frequent Co-Authors

J. E. Gestwicki· 4 shared A. N. Akbar· 2 shared C. M. Nadel· 2 shared L. A. Callender· 2 shared O. T. Johnson· 2 shared S. M. Henson· 2 shared S. Marqusee· 2 shared A. J. Samelson· 1 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 11 mutual co-author links

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4 shared papersBiochemistry

J. E. Gestwicki

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Author profile →

8 papers

Recent·Most cited

Interaction with the membrane-anchored protein CHIC2 constrains the ubiquitin ligase activity of CHIP

M. D. Callahan, M. Hodul, E. C. Carroll, M. Ravalin, C. M. Nadel, A. R. de Silva, A. R. Cupo, L. E. McDermott, J. C. Nix, R. C. Page, A. W. Kao, J. E. Gestwicki

This study identifies CHIC2 as a chaperone-independent regulator of CHIP, showing it attenuates CHIP's ubiquitin ligase activity and contributes to neurodegeneration in C. elegans.

bioRxiv · Jul 17, 2023 · PreprintBiochemistry

CRISPR screens in iPSC-derived neurons reveal principles of tau proteostasis

A. J. Samelson, N. Ariqat, J. McKetney, G. Rohanitazangi, C. Parra Bravo, R. Bose, K. J. Travaglini, V. L. Lam, D. Goodness, G. Dixon, E. Marzette, J. Jin, R. Tian, E. Tse, R. Abskharon, , M. Kampmann

The paper uses CRISPR screens in iPSC-derived neurons to identify factors controlling tau aggregation, finding new pathways and potential therapeutic targets for tauopathies.

bioRxiv · Jun 16, 2023Cell Biology

Conformationally responsive dyes enable protein-adaptive Differential Scanning Fluorometry

T. Wu, J. C. Yu, A. Suresh, Z. J. Gale-Day, M. G. Alteen, A. S. Woo, Z. Millbern, O. T. Johnson, E. C. Carroll, C. L. Partch, D. Fourches, N. R. Vinueza, D. J. Vocadlo, J. E. Gestwicki

This paper introduces paDSF, a protein-adaptive Differential Scanning Fluorometry method that improves compatibility with proteins and expands observable processes.

bioRxiv · Jan 23, 2023 · PreprintBiochemistry

Two distinct classes of co-chaperones compete for the EEVD motif in heat shock protein 70 (Hsp70) to tune its activity

O. T. Johnson, C. M. Nadel, E. C. Carroll, T. Arhar, J. E. Gestwicki

The paper identifies two co-chaperones that compete for the EEVD motif of Hsp70, influencing its activity by determining whether bound proteins are folded or degraded.

bioRxiv · Oct 18, 2021 · PreprintBiochemistry

Mechanistic basis for ubiquitin modulation of a protein energy landscape

E. C. Carroll, N. R. Latorraca, J. M. Lindner, B. C. Maguire, J. G. Pelton, S. Marqusee

This study investigates how ubiquitination at different sites affects the energy landscape of a model protein, revealing distinct thermodynamic mechanisms for destabilization and protection.

bioRxiv · Dec 6, 2020Biophysics

GATA3 controls mitochondrial biogenesis in primary human CD4+ T cells during DNA damage

L. A. Callender, J. Schroth, E. C. Carroll, L. E. L. Romano, E. Hendy, A. Kelly, P. Lavender, A. N. Akbar, J. P. Chapple, S. M. Henson

This study identifies a novel mechanism by which GATA3 regulates mitochondrial biogenesis in primary human CD4+ T cells in response to DNA damage.

bioRxiv · May 15, 2020 · PreprintImmunology

Ubiquitination modulates a protein energy landscape site-specifically with consequences for proteasomal degradation

E. C. Carroll, E. R. Greene, A. Martin, S. Marqusee

This study shows that ubiquitination at specific sites destabilizes protein structure and enhances proteasomal degradation, even in well-folded proteins.

bioRxiv · Nov 15, 2019Biochemistry

Mitochondrial mass governs the extent of T cell senescence

L. A. Callender, E. C. Carroll, E. A. Bober, A. N. Akbar, E. Solito, S. M. Henson

This study shows that mitochondrial mass differences between CD4+ and CD8+ T cells drive their distinct susceptibility to senescence, with reduced mitochondrial function inducing a CD8+ -like phenotype in CD4+ T cells.

bioRxiv · May 4, 2019Immunology