The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis

No abstract is available for this paper.

• Publication year

  2008

• Venue

  Apoptosis

• Publication date

  2008-02-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1007/s10495-007-0164-7PMID 18060501
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity

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• The Subunit CSN6 of the COP9 Signalosome Is Cleaved during Apoptosis*

  2007influential reference
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• CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha.

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• The cell cycle inhibitor p57Kip2 promotes cell death via the mitochondrial apoptotic pathway

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• Regulation of neddylation and deneddylation of cullin1 in SCFSkp2 ubiquitin ligase by F-box protein and substrate.

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• Proteasome inhibitor induces apoptosis through induction of endoplasmic reticulum stress

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  2005influential reference
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• The COP9 Signalosome: Its Possible Role in the Ubiquitin System

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• Caspase activation inhibits proteasome function during apoptosis.

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• The COP9 signalosome.

  2003cited by this paper
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  2003cited by this paper
• Degradation of p57Kip2 mediated by SCFSkp2-dependent ubiquitylation

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• Deadly encounter: ubiquitin meets apoptosis

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  2000influential reference
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  1999cited by this paper
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  1997cited by this paper
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  1996influential reference

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  2023influential citation
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  2019cites this paper
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  2018cites this paper
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  2017cites this paper
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  2011cites this paper
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  2011cites this paper
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  2010cites this paper
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