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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2012, Volume 109, Issue 27, pp. 10757 - 10758
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 07/2012, Volume 109, Issue 27, p. E1839
In the course of apoptosis, activated caspases cleave ~500 to ~1,000 different proteins in a mammalian cell. The dynamics of apoptosis involve a number of... 
Proteins | Proteases | Mutation | Metabolism | Apoptosis
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2004, Volume 101, Issue 40, pp. 14373 - 14378
Posttranslational modification by the ubiquitin homologue, small ubiquitin-like modifier 1 (SUMO-1), has been established as an important regulatory mechanism.... 
Proteins | Chemical equilibrium | Spectroscopy | Enzymes | Biological Sciences | Addition | Consensus sequence | Ubiquitins | Amino acids | Nuclear interactions | Post translational modification | Posttranslational modification | RanBP2 | Nup358 | Ubc9 | Protein-protein interaction | DOMAIN | COACTIVATOR | UBIQUITIN-BINDING | posttranslational modification | ENZYME UBC9 | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTIONAL REPRESSION | RECEPTOR | RANGAP1 | E3 LIGASE | Nup3S8 | NMR | NUCLEAR-PORE COMPLEX | protein-protein interaction | Consensus Sequence | Humans | Nuclear Pore Complex Proteins - chemistry | Molecular Sequence Data | GTPase-Activating Proteins - metabolism | SUMO-1 Protein - chemistry | Nuclear Magnetic Resonance, Biomolecular | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Molecular Chaperones | Mutagenesis, Site-Directed | Nuclear Pore Complex Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | GTPase-Activating Proteins - chemistry | Static Electricity | Amino Acid Motifs | Macromolecular Substances | Small Ubiquitin-Related Modifier Proteins - chemistry | Protein Processing, Post-Translational | SUMO-1 Protein - metabolism | In Vitro Techniques | Cells | Research
Journal Article
Journal Article
Methods in Molecular Biology, ISSN 1064-3745, 2012, Volume 832, pp. 1 - 11
Many intracellular proteins are metabolically unstable or can become unstable during their lifetime in a cell. The in vivo half-lives of specific proteins... 
Arg/N-end rule pathway | Ubiquitin | N-end rule | N-recognin | Proteolysis | Ac/N-end rule pathway | Saccharomyces cerevisiae - metabolism | Neoplasm Proteins | Saccharomyces cerevisiae Proteins | Ubiquitin - metabolism | Ubiquitin-Protein Ligases - metabolism | Proteasome Endopeptidase Complex - metabolism
Conference Proceeding
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2005, Volume 102, Issue 27, pp. 9559 - 9564
Journal Article
Journal Article
Current Biology, ISSN 0960-9822, 07/2003, Volume 13, Issue 13, pp. R501 - R502
Journal Article
Current Biology, ISSN 0960-9822, 07/2003, Volume 13, Issue 13, pp. R501 - R502
Journal Article
2000, ISBN 0121822281, Volume 327
Book Chapter
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2014, Volume 111, Issue 46, p. E4936
  The arginyltransferase Ate1 is a component of the N-end rule pathway, which recognizes proteins containing N-terminal degradation signals called N-degrons,... 
Proteins | Proteases | Genes | Primates | Genomes | Ribonucleic acid--RNA | Monkeys & apes
Journal Article
99.