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© 1992 Nature Publishing Group
© 1992 Nature Publishing Group
© 1992 Nature Publishing Group
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Autoregulation of the 26S proteasome by in situ ubiquitination.
Numerous proteins with unique characteristics are degraded by the 26S proteasome following monoubiquitination.
Protection against murine osteoarthritis by inhibition of the 26S proteasome and lysine-48 linked ubiquitination.
Dss1 is a 26S proteasome ubiquitin receptor.
Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome.
Ornithine decarboxylase and ornithine decarboxylase-inhibiting activity in rat thymocytes.
Long-range allosteric regulation of the human 26S proteasome by 20S proteasome-targeting cancer drugs.
Superinduction of ornithine decarboxylase by halogenated ribofuranosylbenzimidazoles.
The proteasome activity reporter GFP-Cl1 is degraded by autophagy in the aging model Podospora anserina.
N-Terminal Coiled-Coil Structure of ATPase Subunits of 26S Proteasome Is Crucial for Proteasome Function.
Ornithine decarboxylase activity: control by cyclic nucleotides.
A splice variant of the human phosphohistidine phosphatase 1 (PHPT1) is degraded by the proteasome.
Regulation by 1,4-diamines of the ornithine decarboxylase activity induced by ornithine in perifused tumor cells.
The regulation of mouse liver ornithine decarboxylase by metabolites.
On the translational control of ornithine decarboxylase expression by polyamines.
Ornithine decarboxylase activity is critical for cell transformation.
The Cdc48-Vms1 complex maintains 26S proteasome architecture.
Regulation of thyroid ornithine ornithine decarboxylase (ODC) by thyrotropin. I. The rat.
DNA damage modulates interactions between microRNAs and the 26S proteasome.
Characterization of the 26S proteasome network in Plasmodium falciparum.
The 26S proteasome and initiation of gene transcription.
The proteasome subunit RPN10 functions as a specific receptor for degradation of the 26S proteasome by macroautophagy in Arabidopsis.
Ubiquitin Receptor RPN10 in Arabidopsis.
Regulation of ornithine decarboxylase by ODC-antizyme in HTC cells.
Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination.
Ornithine decarboxylase (ODC), a key enzyme in polyamine biosynthesis, is the most rapidly turned over mammalian enzyme. We have shown that its degrad...
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Autoregulation of the 26S proteasome by in situ ubiquitination.
Numerous proteins with unique characteristics are degraded by the 26S proteasome following monoubiquitination.
Protection against murine osteoarthritis by inhibition of the 26S proteasome and lysine-48 linked ubiquitination.
Dss1 is a 26S proteasome ubiquitin receptor.
Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome.
Ornithine decarboxylase and ornithine decarboxylase-inhibiting activity in rat thymocytes.
Long-range allosteric regulation of the human 26S proteasome by 20S proteasome-targeting cancer drugs.
Superinduction of ornithine decarboxylase by halogenated ribofuranosylbenzimidazoles.
The proteasome activity reporter GFP-Cl1 is degraded by autophagy in the aging model Podospora anserina.
N-Terminal Coiled-Coil Structure of ATPase Subunits of 26S Proteasome Is Crucial for Proteasome Function.
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