Reply to Vangala et al.: Complete inhibition of the proteasome reduces new proteasome production by causing Nrf1 aggregation

Current Biology

Volumn 26, Issue 18, 2016, Pages R836-R837

  Sha, Zhe ^a   Goldberg, Alfred L ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR RESPIRATORY FACTOR 1; PROTEASOME; PROTEASOME INHIBITOR;

ANIMAL; GENETICS; PROTEIN DEGRADATION; UBIQUITINATION;

ANIMALS; NUCLEAR RESPIRATORY FACTOR 1; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEASOME INHIBITORS; PROTEOLYSIS; UBIQUITINATION;

EID: 84992049114     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2016.08.030     Document Type: Letter

References (10)

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2. 2 Sha, Z., Goldberg, A.L., Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97. Curr. Biol. 24 (2014), 1573–1583.
3. 3 Steffen, J., Seeger, M., Koch, A., Kruger, E., Proteasomal degradation is transcriptionally controlled by TCF11 via an ERAD-dependent feedback loop. Mol. Cell 40 (2010), 147–158.
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6. 6 Lehrbach, N.J., Ruvkun, G., Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic protease DDI-1. eLife, 5, 2016, 10.7554/eLife.17721.
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