James J. Driscoll - Concepedia

Author

James J. Driscoll

Also Known As

Driscoll,James;Ignatz-Hoover,James;, J Driscoll, J J Driscoll, J. Driscoll, J. J. DRISCOLL, James Driscoll, James J Driscoll, James J. Driscoll, James Joseph Driscoll, S. Tripathy

285

Publications

4.7K

Citations

H-Index

Concepts

All Affiliations

Harvard University University of Cincinnati Medical Center University of Cincinnati Boston University Case Western Reserve University

About

James J. Driscoll is an author at Harvard University specializing in medicine, proteomics, and natural sciences.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	16	16	2K
2	Natural Sciences	10	11	1.7K
3	Engineering	3	3	43
4	Health Sciences	1	1	19
5	Allergy	1	1	45

James J. Driscoll

Publications

2.7K

Citations

H-Index

Page 1

	Year	Citations
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome James J. Driscoll, Michael G. Brown, Daniel Finley, Nature Peptidase ActivitiesProtein ExpressionBiochemistryProtein FoldingNatural Sciences	1993	448
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 Ubiquitin-conjugate-degrading EnzymeProteasome Substrates1500-Kda Proteolytic ComplexProteasomeMolecular Biology	1990	326
Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes Michael G. Brown, James J. Driscoll, John J. Monaco Nature Multicatalytic ProteinaseProtein ChemistryProtein AssemblyBiochemistryProtein Folding	1991	314
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, Nature BiochemistryMhc ClassProtein FoldingMedicineNatural Sciences	1992	210
Involvement of the proteasome in various degradative processes in mammalian cells. Wallace J. Matthews, James J. Driscoll, Keiji Tanaka, Proceedings of the National Academy of Sciences ApoptosisProteasomeRedox BiologyOxidative StressBioanalysis	1989	163
The sumoylation pathway is dysregulated in multiple myeloma and is associated with adverse patient outcome James J. Driscoll, Dheeraj Pelluru, Konstantinos Lefkimmiatis, Blood	2009	125
Pharmacologic screens reveal metformin that suppresses GRP78-dependent autophagy to enhance the anti-myeloma effect of bortezomib Sajjeev Jagannathan, M A Y Abdel-Malek, Ehsan Malek, Leukemia ImmunologyGrp78-dependent AutophagyCell DeathPharmacotherapyTumor Biology	2015	109
Skeletal muscle proteasome can degrade proteins in an ATP-dependent process that does not require ubiquitin. James J. Driscoll, Alfred L. Goldberg Proceedings of the National Academy of Sciences Muscle FunctionProteasomeMolecular BiologyCytoskeletonProtein Refolding	1989	95
Comparison of cell lines deficient in antigen presentation reveals a functional role for TAP-1 alone in antigen processing. R. Gabathuler, Gregor S. D. Reid, G Kolaitis, The Journal of Experimental Medicine Cmt.64 DefectImmunologyImmunoeditingPathologyImmunodominance	1994	89
Molecular chaperone GRP78 enhances aggresome delivery to autophagosomes to promote drug resistance in multiple myeloma Mohamed A.Y. Abdel Malek, Sajjeev Jagannathan, Ehsan Malek, Oncotarget	2014	80

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