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
Proteasome subunit Rpn13 is a novel ubiquitin receptor.
Authors: Authors: Husnjak K, Elsasser S, Zhang N, Chen X, Randles L, Shi Y, Hofmann K, Walters KJ, Finley D, Dikic I.
Nature
View full abstract on Pubmed
Nature
View full abstract on Pubmed
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction.
Authors: Authors: Schreiner P, Chen X, Husnjak K, Randles L, Zhang N, Elsasser S, Finley D, Dikic I, Walters KJ, Groll M.
Nature
View full abstract on Pubmed
Nature
View full abstract on Pubmed
Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins.
Authors: Authors: Goh AM, Walters KJ, Elsasser S, Verma R, Deshaies RJ, Finley D, Howley PM.
BMC Biochem
View full abstract on Pubmed
BMC Biochem
View full abstract on Pubmed
Measurement of muon neutrino quasielastic scattering on carbon.
Authors: Authors: Aguilar-Arevalo AA, Bazarko AO, Brice SJ, Brown BC, Bugel L, Cao J, Coney L, Conrad JM, Cox DC, Curioni A, Djurcic Z, Finley DA, Fleming BT, Ford R, Garcia FG, Garvey GT, Green C, Green JA, Hart TL, Hawker E, Imlay R, Johnson RA, Kasper P, Katori T, Kobilarcik T, Kourbanis I, Koutsoliotas S, Laird EM, Link JM, Liu Y, Liu Y, Louis WC, Mahn KB, Marsh W, Martin PS, McGregor G, Metcalf W, Meyers PD, Mills F, Mills GB, Monroe J, Moore CD, Nelson RH, Nienaber P, Ouedraogo S, Patterson RB, Perevalov D, Polly CC, Prebys E, Raaf JL, Ray H, Roe BP, Russell AD, Sandberg V, Schirato R, Schmitz D, Shaevitz MH, Shoemaker FC, Smith D, Sorel M, Spentzouris P, Stancu I, Stefanski RJ, Sung M, Tanaka HA, Tayloe R, Tzanov M, Van de Water R, Wascko MO, White DH, Wilking MJ, Yang HJ, Zeller GP, Zimmerman ED.
Phys Rev Lett
View full abstract on Pubmed
Phys Rev Lett
View full abstract on Pubmed
Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites.
Authors: Authors: Kleijnen MF, Roelofs J, Park S, Hathaway NA, Glickman M, King RW, Finley D.
Nat Struct Mol Biol
View full abstract on Pubmed
Nat Struct Mol Biol
View full abstract on Pubmed
Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry.
Authors: Authors: Smith DM, Chang SC, Park S, Finley D, Cheng Y, Goldberg AL.
Mol Cell
View full abstract on Pubmed
Mol Cell
View full abstract on Pubmed
A proteasome for all occasions.
Search for electron neutrino appearance at the Delta m2 approximately 1 eV2 scale.
Authors: Authors: Aguilar-Arevalo AA, Bazarko AO, Brice SJ, Brown BC, Bugel L, Cao J, Coney L, Conrad JM, Cox DC, Curioni A, Djurcic Z, Finley DA, Fleming BT, Ford R, Garcia FG, Garvey GT, Green C, Green JA, Hart TL, Hawker E, Imlay R, Johnson RA, Kasper P, Katori T, Kobilarcik T, Kourbanis I, Koutsoliotas S, Laird EM, Link JM, Liu Y, Liu Y, Louis WC, Mahn KB, Marsh W, Martin PS, McGregor G, Metcalf W, Meyers PD, Mills F, Mills GB, Monroe J, Moore CD, Nelson RH, Nienaber P, Ouedraogo S, Patterson RB, Perevalov D, Polly CC, Prebys E, Raaf JL, Ray H, Roe BP, Russell AD, Sandberg V, Schirato R, Schmitz D, Shaevitz MH, Shoemaker FC, Smith D, Sorel M, Spentzouris P, Stancu I, Stefanski RJ, Sung M, Tanaka HA, Tayloe R, Tzanov M, Van de Water R, Wascko MO, White DH, Wilking MJ, Yang HJ, Zeller GP, Zimmerman ED.
Phys Rev Lett
View full abstract on Pubmed
Phys Rev Lett
View full abstract on Pubmed
A ubiquitin stress response induces altered proteasome composition.
Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities.
Authors: Authors: Crosas B, Hanna J, Kirkpatrick DS, Zhang DP, Tone Y, Hathaway NA, Buecker C, Leggett DS, Schmidt M, King RW, Gygi SP, Finley D.
Cell
View full abstract on Pubmed
Cell
View full abstract on Pubmed