James J. Driscoll

MHC-linked LMP gene products specifically alter peptidase activities of the proteasome

James J. Driscoll, Michael G. Brown, Daniel Finley et al. · Nature · 1993 · 448 citations

Peptidase Activities, Protein Expression, Biochemistry +9

The proteasome (multicatalytic protease) is a component of the 1500-kDa proteolytic complex which degrades ubiquitin-conjugated proteins.

James J. Driscoll, Alfred L. Goldberg · Journal of Biological Chemistry · 1990 · 326 citations · Full text

Ubiquitin-conjugate-degrading Enzyme, Proteasome Substrates, 1500-Kda Proteolytic Complex +16

Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes

Michael G. Brown, James J. Driscoll, John J. Monaco · Nature · 1991 · 314 citations

Multicatalytic Proteinase, Protein Chemistry, Protein Assembly +12

Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules

Danièle Arnold, James J. Driscoll, Matthew J. Androlewicz et al. · Nature · 1992 · 210 citations

Biochemistry, Mhc Class, Protein Folding +11

Involvement of the proteasome in various degradative processes in mammalian cells.

Wallace J. Matthews, James J. Driscoll, Keiji Tanaka et al. · Proceedings of the National Academy of Sciences · 1989 · 163 citations · Full text

Apoptosis, Proteasome, Redox Biology +18