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The Journal of Biological Chemistry|February 15, 2000
The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasomeJ Lüders, J Demand, J HöhfeldMolecular and Cellular Biology|April 7, 1998
The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactorsJ Demand, J Lüders, J HöhfeldCurrent Biology : CB|October 26, 2001
Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome couplingJ Demand, S Alberti, C Patterson, et al.The Journal of Biological Chemistry|May 16, 2000
Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone functionJ Lüders, J Demand, O Papp, et al.AIDS (London, England)|April 26, 2000
Partner type and condom useM Macaluso, M J Demand, L M Artz, et al.Biochemical and Biophysical Research Communications|January 27, 1999
A dehydroalanyl residue can capture the 5'-deoxyadenosyl radical generated from S-adenosylmethionine by pyruvate formate-lyase-activating enzymeA F Wagner, J Demand, G Schilling, et al.Biological Chemistry|November 20, 1998
Cofactor-induced modulation of the functional specificity of the molecular chaperone Hsc70J Lüders, J Demand, S Schönfelder, et al.European Journal of Biochemistry|June 10, 2000
Assembly of heterodimeric luciferase after de novo synthesis of subunits in rabbit reticulocyte lysate involves hsc70 and hsp40 at a post-translational stageJ Tyedmers, M Kruse, M Lerner, et al.Pageof 1