Chemistry-based functional proteomics: mechanism-based activity-profiling tools for ubiquitin and ubiquitin-like specific proteases. Export

@article{citeulike:3816479, abstract = {Determining the biological function of newly discovered gene products requires the development of novel functional approaches. To facilitate this task, recent developments in proteomics include small molecular probes that target proteolytic enzyme families including serine, threonine, and cysteine proteases. For the families of ubiquitin (Ub) and ubiquitin-like (UBL)-specific proteases, such tools were lacking until recently. Here, we review the advances made in the development of protein-based active site-directed probes that target proteases specific for ubiquitin and ubiquitin-like proteins. Such probes were applied successfully to discover and characterize novel Ub/UBL-specific proteases. Ub/UBL processing and deconjugation are performed by a diverse set of proteases belonging to several different enzyme families, including members of the ovarian tumor domain (OTU) protease family. A further definition of this family of enzymes will benefit from a directed chemical proteomics approach. Some of the Ub/UBL-specific proteases react with multiple Ub/UBLs and members of the same protease family can recognize multiple Ub/UBLs, underscoring the need for tools that appropriately address enzyme specificity.}, author = {Hemelaar, J. and Galardy, P. J. and Borodovsky, A. and Kessler, B. M. and Ploegh, H. L. and Ovaa, H.}, citeulike-article-id = {3816479}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/15113103}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=15113103}, issn = {1535-3893}, journal = {Journal of proteome research}, keywords = {abpp, dub, ub}, number = {2}, pages = {268--276}, posted-at = {2008-12-22 04:54:18}, priority = {2}, title = {Chemistry-based functional proteomics: mechanism-based activity-profiling tools for ubiquitin and ubiquitin-like specific proteases.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/15113103}, volume = {3}, year = {2004} }

TY - JOUR ID - citeulike:3816479 L3 - citeulike-article-id:3816479 N2 - Determining the biological function of newly discovered gene products requires the development of novel functional approaches. To facilitate this task, recent developments in proteomics include small molecular probes that target proteolytic enzyme families including serine, threonine, and cysteine proteases. For the families of ubiquitin (Ub) and ubiquitin-like (UBL)-specific proteases, such tools were lacking until recently. Here, we review the advances made in the development of protein-based active site-directed probes that target proteases specific for ubiquitin and ubiquitin-like proteins. Such probes were applied successfully to discover and characterize novel Ub/UBL-specific proteases. Ub/UBL processing and deconjugation are performed by a diverse set of proteases belonging to several different enzyme families, including members of the ovarian tumor domain (OTU) protease family. A further definition of this family of enzymes will benefit from a directed chemical proteomics approach. Some of the Ub/UBL-specific proteases react with multiple Ub/UBLs and members of the same protease family can recognize multiple Ub/UBLs, underscoring the need for tools that appropriately address enzyme specificity. IS - 2 JF - Journal of proteome research SN - 1535-3893 EP - 276 TI - Chemistry-based functional proteomics: mechanism-based activity-profiling tools for ubiquitin and ubiquitin-like specific proteases. VL - 3 SP - 268 KW - abpp KW - dub KW - ub AU - Hemelaar, J AU - Galardy, PJ AU - Borodovsky, A AU - Kessler, BM AU - Ploegh, HL AU - Ovaa, H PY - 2004///r UR - http://view.ncbi.nlm.nih.gov/pubmed/15113103 ER -