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W. Hayes McDonald

Researcher at Vanderbilt University

Publications -  116
Citations -  12031

W. Hayes McDonald is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Gene & Proteome. The author has an hindex of 51, co-authored 110 publications receiving 11219 citations. Previous affiliations of W. Hayes McDonald include Howard Hughes Medical Institute & University of British Columbia.

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Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26S Proteasome

TL;DR: These findings reveal an unexpected coupling between substrate deubiquitination and degradation and suggest a unifying rationale for the presence of the lid in eukaryotic proteasomes.
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Phytophthora Genome Sequences Uncover Evolutionary Origins and Mechanisms of Pathogenesis

Brett M. Tyler, +68 more
- 01 Sep 2006 - 
TL;DR: Comparison of the two species' genomes reveals a rapid expansion and diversification of many protein families associated with plant infection such as hydrolases, ABC transporters, protein toxins, proteinase inhibitors, and, in particular, a superfamily of 700 proteins with similarity to known oömycete avirulence genes.
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Sirt3-Mediated Deacetylation of Evolutionarily Conserved Lysine 122 Regulates MnSOD Activity in Response to Stress

TL;DR: Infestation of Sirt3⁻/⁻ MEFs with lenti-MnSOD(K122-R) inhibited in vitro immortalization by an oncogene (Ras), inhibited IR-induced genomic instability, and decreased mitochondrial superoxide, suggesting acetylation directly regulates function.
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Shotgun identification of protein modifications from protein complexes and lens tissue

TL;DR: This work describes a process for the analysis of posttranslational modifications that is simple, robust, general, and can be applied to complicated protein mixtures and lens tissue from a patient with congenital cataracts.
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Mus81-Eme1 Are Essential Components of a Holliday Junction Resolvase

TL;DR: It is reported that Mus81 and an associated protein Eme1 are components of an endonuclease that resolves Holliday junctions into linear duplex products and constitute strong evidence that Mus 81 and Eme 1 are subunits of a nuclear Holliday junction resolvase.