Author

M. P. Hughes

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· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Research Focus:cell type annotation· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Assay:cryo-EM· 1 Research Focus:differential expression· 1 Organism:Drosophila· 1

Frequent Co-Authors

D. S. Eisenberg· 2 shared A. A. Rahim· 1 shared A. Dowsey· 1 shared A. E. Burrows· 1 shared A. Philips· 1 shared A. Sharaireh· 1 shared A. Tierney· 1 shared B. A. Johnson· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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2 shared papersBiochemistry

D. S. Eisenberg

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication

Z. Yang, B. A. Johnson, V. A. Meliopoulos, X. Ju, P. Zhang, M. P. Hughes, J. Wu, K. P. Koreski, T.-C. Chang, G. Wu, J. Hixon, J. Duffner, K. Wong, R. Lemieux, K. G. Lokugamage, , J. P. Taylor

This study identifies the role of G3BP1-N interaction in SARS-CoV-2 replication by showing that disrupting this interaction reduces viral replication and pathogenesis.

bioRxiv · Jun 29, 2023 · PreprintCell Biology

CLN7 mutation causes aberrant redistribution of protein isoforms and contributes to Batten disease pathobiology

A. Sharaireh, M. Guevara Ferrer, S. Herranz-Martin, M. Garcia-Macia, A. Philips, A. Tierney, M. P. Hughes, O. Coombe-Tennant, H. Nelvagel, A. E. Burrows, S. Fielding, L. M. FitzPatrick, C. D. Thornton, S. Storch, S. E. Mole, , T. R. McKay

This study shows CLN7 mutations cause nuclear and endolysosomal protein distribution defects in Batten disease, leading to apoptosis and neuroinflammation, suggesting combinatorial therapies may be needed.

bioRxiv · Apr 21, 2022 · PreprintCell Biology

The prevalence and distribution in genomes of low-complexity, amyloid-like, reversible, kinked segment (LARKS), a common structural motif in amyloid-like fibrils

M. P. Hughes, L. Goldschmidt, D. S. Eisenberg

The paper identifies LARKS as a common structural motif in amyloid-like fibrils across six organisms and shows their abundance in M. tuberculosis, D. melanogaster, and H. sapiens.

bioRxiv · Dec 8, 2020Biochemistry

The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure

D. R. Boyer, B. Li, C. Sun, W. Fan, K. Zhou, M. P. Hughes, M. R. Sawaya, L. Jiang, D. S. Eisenberg

This study determines the cryoEM structure of α-synuclein fibrils with the E46K mutation, revealing a more stable and pathogenic fibril structure compared to wild-type.

bioRxiv · Dec 8, 2019Biochemistry