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Sec6l-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
The human cytomegalovirus genome encodes proteins that trigger destruction of newly synthesized major histocompatibility complex (MHC) class I molecules, which involves the Sec6l complex, in what appears to be a reversal of the reaction by which it translocates nascent chains into the endoplasmic reticulum.
The Human Cytomegalovirus US11 Gene Product Dislocates MHC Class I Heavy Chains from the Endoplasmic Reticulum to the Cytosol
Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools.
Nucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase
- Sarah E. Ewald, A. Engel, Jiyoun Lee, Miqi Wang, M. Bogyo, G. Barton
- BiologyThe Journal of experimental medicine
- 11 April 2011
TLR3, TLR7, and TLR9 are cleaved in the same step-wise manner in all immune cell types examined.
A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor.
Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors.
- M. Bogyo, J. McMaster, M. Gaczynska, D. Tortorella, A. Goldberg, H. Ploegh
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 24 June 1997
125I-NIP-L3VS covalently modifies the HSlV subunit of the Escherichia coli protease complex HslV/HslU, a reaction that requires ATP, and supports a catalytic mechanism shared with that of the eukaryotic proteasome.
Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum.
A forward chemical genetic screen using a highly focused library of more than 1,200 covalent serine and cysteine protease inhibitors to identify compounds that block host cell rupture by P. falciparum suggests that two mechanistically distinct proteases function to regulate processing of downstream substrates required for efficient release of parasites from host red blood cells.
Cathepsin V, a Novel and Potent Elastolytic Activity Expressed in Activated Macrophages*
- Y. Yasuda, Zhenqiang Li, D. Greenbaum, M. Bogyo, E. Weber, D. Brömme
- BiologyJournal of Biological Chemistry
- 27 August 2004
It is demonstrated that macrophages express a third elastolytic cysteine protease, cathepsin V, which exhibits the most potent elastase activity yet described among human proteases and that cathePSin V is present in atherosclerotic plaque specimens.
Tumor cell-derived and macrophage-derived cathepsin B promotes progression and lung metastasis of mammary cancer.
It is shown that mouse mammary tumor virus-polyoma middle T antigen (PyMT) transgenic mice deficient for the cysteine protease cathepsin B (CTSB) exhibited a significantly delayed onset and reduced growth rate of mammary cancers compared with wild-type PyMT mice.