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Daniel N. Bolon

Researcher at University of Massachusetts Medical School

Publications -  87
Citations -  4686

Daniel N. Bolon is an academic researcher from University of Massachusetts Medical School. The author has contributed to research in topics: Protease & Influenza A virus. The author has an hindex of 34, co-authored 78 publications receiving 4071 citations. Previous affiliations of Daniel N. Bolon include California Institute of Technology & Massachusetts Institute of Technology.

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Sculpting the Proteome with AAA+ Proteases and Disassembly Machines

TL;DR: Exciting progress has been made in understanding how AAA(+) machines recognize specific proteins as targets and then carry out ATP-dependent dismantling of the tertiary and/or quaternary structure of these molecules during the processes of protein degradation and the disassembly of macromolecular complexes.
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Enzyme-like proteins by computational design

TL;DR: The development and initial experimental validation of a computational design procedure aimed at generating enzyme-like protein catalysts called “protozymes” are reported, suggesting a possible mechanism for examining the relationships between protein fold and the evolvability of protein function.
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Experimental illumination of a fitness landscape.

TL;DR: Deep sequencing technology is exploited to experimentally determine the fitness of all possible individual point mutants under controlled conditions for a nine-amino acid region of Hsp90 in yeast, consistent with a nearly neutral model of molecular evolution.
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Analyses of the Effects of All Ubiquitin Point Mutants on Yeast Growth Rate

TL;DR: The results indicate that core mutations may frequently cause functional defects through subtle disturbances to structure or dynamics in ubiquitin function.
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Asymmetric Interactions of ATP with the AAA+ ClpX6 Unfoldase: Allosteric Control of a Protein Machine

TL;DR: These studies further emphasize commonalities between distant AAA+ family members, including protein and DNA translocases, helicases, motor proteins, clamp loaders, and other ATP-dependent enzymes.