2025

MP Hughes. Rethinking Cellular Organization: phase separation as a unifying principle in molecular biology. JMB, 2025. doi.org/10.1016/j.jmb.2025.169367

2024

Z Yang, BA Johnson, VA Meliopoulos, X Ju, P Zhang, MP Hughes, J Wu, KP Koreski, JE Clary, TC Chang, G Wu, J Hixon, J Duffner, K Wong, R Lemieux, KG Lokugamage, RE Alvarado, PA Crocquet-Valdes, DH Walker, KS Plante, JA Plante, SC Weaver, HJ Kim, R Meyers, S Schultz-Cherry, Q Ding, VD Menachery, JP Taylor. Interaction between host G3BP and viral nucleocapsid protein regulates SARS-Cov-2 replication and pathogenicity. Cell Reports, 2024. doi.org/10.1016/j.celrep.2024.113965

J Lu, P Ge, MR Sawaya, MP Hughes, DR Boyer, Q Cao, R Abskharon, D Cascio, E Tayeb-Fligelman, DS Eisenberg. Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation. JBC, 2024. doi.org/10.1016/j.jbc.2023.105531

2022

KA Murray, MP Hughes, CJ Hu, MR Sawaya, L Salwinski, H Pan, SW French, PM Seidler, DS Eisenberg. Identifying amyloid-related disease by mapping mutations in low-complexity protein domains to pathologies. Nat Struct Mol Biol, 2022. doi.org/10.1038/s41594-022-00774-y

GM Rosenberg, KA Murray, L Salwinski, MP Hughes, R Abskharon, DS Eisenberg.Bioinformati identificaion of previously uncrecognized amyloidogenic proteins. JBC, 2022. doi.org/10.1016/j.jbc.2022.101920

KA Murray, D Evans, MP Hughes, MR Sawaya, CJ Hu, KN Houk, D Eisenberg.Extended β‑strands contribute to reversible amyloid formation. ACS nano, 2022. doi.org/10.1021/acsnano.1c08043

2021

MR Sawaya, MP Hughes, JA ROdriguez, R Riek, DS Eisenberg. The expanding amyloid family: Structure, stability, function, and pathogenesis. Cell, 2021. doi.org/10.1016/j.cell.2021.08.013

Jiahui Lu, Cao Qin, MP Hughes, MR Sawaya, DR Boyer, D Cascio, DS Eisenberg. CryoEM structure of the low-complexity domain of hnRNPA2 reveals distinct differences from pathogeneic amyloid. Nat Comm, 2021. doi.org/10.1038/s41467-020-17905-y

2020

DR Boyer, B Li, C Sun, W Fan, K Zhou, MP Hughes, MR Sawaya, Lin Jiang, Eisenberg DS. The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure. PNAS, 2020.

TJ Litberg, B Docter, MP Hughes, J Bourne, S Horowitz. DNA Facilitates Oligomerization and Prevents Aggregation via DNA Networks. Biophysical journal, 2020.

J Lu, Q Cao, MP Hughes, MR Sawaya, DR Boyer, D Cascio, DS Eisenberg. CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid. Nat Commun (2020).

2018

TO Vogler, JR Wheeler, ED Nguyen, MP Hughes, KA Britson, Evan Lester, Bhalchandra Rao, ND Betta, ON Whitney, TE Ewachiw, E Gomes, James Shorter, TE Lloyd, DS Eisenberg, JP Taylor, AM Johnson, BB Olwin, Roy Parker. TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle. Nature563, 508–513 (2018).

Smriti Sangwan, Michael R Sawaya, Kevin A Murray, Michael P Hughes, David S Eisenberg. Atomic structures of corkscrew‐forming segments of SOD1 reveal varied oligomer conformations. Protein Science, 2018.

MP Hughes, MR Sawaya, DR Boyer, Lukasz Goldschmidt, JA Rodriguez, Duilio Cascio, Lisa Chong, Tamir Gonen, DS Eisenberg. Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks. Science, 2018.

Michael Patrick Hughes. Protein structure in reversible amyloid formed by low-complexity regions. UCLA. ProQuest ID: Hughes_ucla_0031D_16909.

2013

L Jiang, C Liu, D Leibly, M Landau, M Zhao, MP Hughes, DS Eisenberg. Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta. elife, 2013.