Troy E. Messick
Wistar Institute
39 Papers
143 Citations
Troy E. Messick is an academic researcher from Wistar Institute. The author has contributed to research in topics: Epstein–Barr virus & Biology. The author has an hindex of 14, co-authored 33 publications. Previous affiliations of Troy E. Messick include University of Pennsylvania.
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Papers
MERIT40 controls BRCA1–Rap80 complex integrity and recruitment to DNA double-strand breaks
Genze Shao,Jeffrey Patterson-Fortin,Troy E. Messick,Dan Feng,Niraj M. Shanbhag,Yingqun Wang,Roger A. Greenberg +6 more
TL;DR: This work has identified MERIT40 (Mediator of Rap80 Interactions and Targeting 40 kD)/(C19orf62) as a Rap80-associated protein that is essential for BRCA1-Rap80 complex protein interactions, stability, and DSB targeting.
The ubiquitin landscape at DNA double-strand breaks
TL;DR: It is proposed that, in order to accommodate parallel processes involved in DSB repair and checkpoint signaling, DSB-associated ubiquitin structures must be nonuniform, using different linkages for distinct functional outputs.
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Structure-based design of small-molecule inhibitors of EBNA1 DNA binding blocks Epstein-Barr virus latent infection and tumor growth.
Troy E. Messick,Garry R. Smith,Samantha S. Soldan,Mark E. McDonnell,Julianna S. Deakyne,Kimberly A. Malecka,Lois Tolvinski,A. Pieter J. van den Heuvel,Bai-Wei Gu,Joel A. Cassel,Donna H. Tran,Benjamin R. Wassermann,Yan Zhang,Venkata Velvadapu,Edward R. Zartler,Philippe Busson,Allen B. Reitz,Paul M. Lieberman +17 more
TL;DR: EBNA1 inhibitors developed by fragment-based drug design block EBNA1 DNA binding and EBV-dependent tumor cell growth in vivo and show favorable pharmacological properties and have the potential to be further developed for the treatment ofEBV-associated malignancies.
Differential regulation of JAMM domain deubiquitinating enzyme activity within the RAP80 complex
TL;DR: Findings reveal that JAMM domain DUB activity and K63-Ub levels are regulated by multiple mechanisms within the cell, including common regulatory mechanisms and potential competition between K 63-Ub-related signaling in cytoplasmic and nuclear compartments.
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Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex.
Jonathan J. Ipsaro,Sandra L. Harper,Troy E. Messick,Ronen Marmorstein,Alfonso Mondragón,David W. Speicher +5 more
TL;DR: To provide further insights into spectrin assembly and tetramer site mutations, a crystal structure of the spectrin tetramerization domain complex has been determined and mapping of hereditary anemia-related mutations onto the structure demonstrate that most, but not all, local hereditaryAnemia mutations map to the interacting domains.
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