Rapid degradation of a large fraction of newly synthesized proteins by proteasomes

By U. Schubert, L. C. Antón, J. Gibbs, C. Norbury, J. Yewdell, J. Bennink. Nature, 2000

1,690 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Parasitology

View Paper: https://www.semanticscholar.org/paper/06f479de8c40c51ccbe591c004ee358beea7e3cc

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In Immunology

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Christopher M. Dobson

Citations in the corpus

PPPYEPTAP Motif Is the Late Domain of Human T-Cell Leukemia Virus Type 1 Gag and Mediates Its Functional Interaction with Cellular Proteins Nedd4 and Tsg101 (2003, background): “It was hypothesized that the inhibition of retroviral budding is due to accumulation of polyubiquitinated proteins, possibly polyubiquitinated defective Gag proteins normally destined to degradation (54).”
Towards a systems understanding of MHC class I and MHC class II antigen presentation (2011, background): “This contradiction was solved by the observation that a large fraction of proteins (varying from 30% to 70% of all proteins made) is immediately degraded after synthesis before forming functional protein”
Immunoproteasome assembly and antigen presentation in mice lacking both PA28α and PA28β (2001, background): “source of MHC class I-binding peptides (Reits et al., 2000; Schubert et al., 2000).”
Protein degradation and protection against misfolded or damaged proteins (2003, background): “A large fraction of newly synthesized proteins is rapidly degrade”
p62 links the autophagy pathway and the ubiqutin–proteasome system upon ubiquitinated protein degradation (2016, neutral): “homeostasis, cell cycle control [3], inflammation, oxidative stress, apoptosis [4] and immunity [1].”
Radiation modulates the peptide repertoire, enhances MHC class I expression, and induces successful antitumor immunotherapy (2006, background): “Many of these peptides are generated by the proteasome from newly synthesized but rapidly degraded proteins called rapidly degraded proteins (RDPs) or defective ribosomal products (1, 2).”
In and out of the ER: protein folding, quality control, degradation, and related human diseases. (2007, background): “These values range from upwards of 30% in one study (341) to substantially less in another (383).”
Systematic and quantitative assessment of the ubiquitin modified proteome (2011, positive): “Errors in cotranslational folding of proteins or translation may account for a significant fraction of the flux through the UPS (Schubert et al., 2000; Vabulas and Hartl, 2005).”