David Fushman

Affiliations: 
Chemistry and Biochemistry University of Maryland, College Park, College Park, MD 
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"David Fushman"
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Wydorski PM, Osipiuk J, Lanham BT, et al. (2023) Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin. Nature Communications. 14: 2366
Gama Lima Costa R, Fushman D. (2022) Reweighting methods for elucidation of conformation ensembles of proteins. Current Opinion in Structural Biology. 77: 102470
Osipiuk J, Wydorski PM, Lanham BT, et al. (2021) Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin. Biorxiv : the Preprint Server For Biology
Boughton AJ, Zhang D, Singh RK, et al. (2021) Polyubiquitin and ubiquitin-like signals share common recognition sites on proteasomal subunit Rpn1. The Journal of Biological Chemistry. 100450
Liao TJ, Jang H, Fushman D, et al. (2020) SOS1 interacts with Grb2 through regions that induce closed nSH3 conformations. The Journal of Chemical Physics. 153: 045106
Magnussen HM, Ahmed SF, Sibbet GJ, et al. (2020) Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain. Nature Communications. 11: 2094
Liao TJ, Jang H, Nussinov R, et al. (2020) High-affinity Interactions of the nSH3/cSH3 Domains of Grb2 with the C-terminal Proline-rich Domain of SOS1. Journal of the American Chemical Society
Wu X, Liu S, Sagum C, et al. (2019) Crosstalk between Lys63- and Lys11-polyubiquitin signaling at DNA damage sites is driven by Cezanne. Genes & Development
Boughton AJ, Krueger S, Fushman D. (2019) Branching via K11 and K48 Bestows Ubiquitin Chains with a Unique Interdomain Interface and Enhanced Affinity for Proteasomal Subunit Rpn1. Structure (London, England : 1993)
Nawatha M, Rogers JM, Bonn SM, et al. (2019) De novo macrocyclic peptides that specifically modulate Lys48-linked ubiquitin chains. Nature Chemistry
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