Daniel Finley, Ph.D.

Daniel Finley, Ph.D.

Professor of Cell Biology (HMS)
C-404B
617-432-3492
Finley Lab

Dan Finley, Ph.D., received his undergraduate degree from Harvard University in biochemistry, and his graduate degree from MIT, with a focus on molecular biology. He stayed at MIT for his postdoctoral training before joining the Department of Cell Biology at HMS in 1988. He also currently sits on the Scientific Advisory Boards of Proteostasis and X-Chem Pharmaceuticals, and is a consultant for Genentech.

The Finley lab is interested in the ubiquitin-proteasome pathway and related regulatory systems. Specific topics include the mechanism of the proteasome, ubiquitin-like proteins, antizyme, and nonproteolytic functions of ubiquitination.

Harvard Medical School

Dept of Cell Biology, C-404B

240 Longwood Avenue

Boston, MA 02115

Lab Phone: 617-432-3492

Antizyme targets cyclin D1 for degradation. A novel mechanism for cell growth repression.
Authors: Authors: Newman RM, Mobascher A, Mangold U, Koike C, Diah S, Schmidt M, Finley D, Zetter BR.
J Biol Chem
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Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome.
Authors: Authors: Elsasser S, Chandler-Militello D, Müller B, Hanna J, Finley D.
J Biol Chem
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Localization to the proteasome is sufficient for degradation.
Authors: Authors: Janse DM, Crosas B, Finley D, Church GM.
J Biol Chem
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Ubiquitin as a central cellular regulator.
Authors: Authors: Finley D, Ciechanover A, Varshavsky A.
Cell
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Ubiquitin depletion as a key mediator of toxicity by translational inhibitors.
Authors: Authors: Hanna J, Leggett DS, Finley D.
Mol Cell Biol
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A proteomics approach to understanding protein ubiquitination.
Authors: Authors: Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP.
Nat Biotechnol
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Proteasome disassembly and downregulation is correlated with viability during stationary phase.
Authors: Authors: Bajorek M, Finley D, Glickman MH.
Curr Biol
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Rpn6p, a proteasome subunit from Saccharomyces cerevisiae, is essential for the assembly and activity of the 26 S proteasome.
Authors: Authors: Santamaria PG, Finley D, Ballesta JP, Remacha M.
J Biol Chem
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Proteasome subunit Rpn1 binds ubiquitin-like protein domains.
Authors: Authors: Elsasser S, Gali RR, Schwickart M, Larsen CN, Leggett DS, Müller B, Feng MT, Tübing F, Dittmar GA, Finley D.
Nat Cell Biol
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Multiple associated proteins regulate proteasome structure and function.
Authors: Authors: Leggett DS, Hanna J, Borodovsky A, Crosas B, Schmidt M, Baker RT, Walz T, Ploegh H, Finley D.
Mol Cell
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