Caspase activation inhibits proteasome function during apoptosis (Q40569376)

21 September 2017

title

Caspase activation inhibits proteasome function during apoptosis (English)

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21 September 2017

4

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21 September 2017

5

Aaron Ciechanover

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21 September 2017

Xiao-Ming Sun

1

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21 September 2017

Michael Butterworth

series ordinal

2

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21 September 2017

Marion MacFarlane

series ordinal

3

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21 September 2017

Gerald M Cohen

series ordinal

6

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21 September 2017

publication date

1 April 2004

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21 September 2017

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21 September 2017

volume

14

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21 September 2017

issue

1

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21 September 2017

page(s)

81-93

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Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2

21 September 2017

cites work

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7 January 2021

Proteasome inhibitor-induced apoptosis of B-chronic lymphocytic leukaemia cells involves cytochrome c release and caspase activation, accompanied by formation of an approximately 700 kDa Apaf-1 containing apoptosome complex

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7 January 2021

The proteasome: paradigm of a self-compartmentalizing protease

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7 January 2021

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7 January 2021

Protein complexes activate distinct caspase cascades in death receptor and stress-induced apoptosis

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7 January 2021

The base of the proteasome regulatory particle exhibits chaperone-like activity

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7 January 2021

Proteasome involvement and accumulation of ubiquitinated proteins in cerebellar granule neurons undergoing apoptosis

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7 January 2021

Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver

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7 January 2021

Preservation of caspase-3 subunits from degradation contributes to apoptosis evoked by lactacystin: any single lysine or lysine pair of the small subunit is sufficient for ubiquitination

1 reference

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7 January 2021

The ubiquitin-proteasome pathway: on protein death and cell life

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Regulation of cellular polyamines by antizyme

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7 January 2021

Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Proteasome subunit Rpn1 binds ubiquitin-like protein domains

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Regulatory subunit interactions of the 26S proteasome, a complex problem

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7 January 2021

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

1 reference

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7 January 2021

A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.

1 reference

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7 January 2021

A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems

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7 January 2021

Deadly encounter: ubiquitin meets apoptosis

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Multiple associated proteins regulate proteasome structure and function

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

1 reference

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7 January 2021

Active caspases and cleaved cytokeratins are sequestered into cytoplasmic inclusions in TRAIL-induced apoptosis

1 reference

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7 January 2021

Mechanisms of resistance to TRAIL-induced apoptosis in primary B cell chronic lymphocytic leukaemia.

1 reference

https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Degradation of ornithine decarboxylase by the 26S proteasome

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

The role of the ubiquitin-proteasome pathway in apoptosis

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Mechanisms of apoptosis

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Identification of ubiquitin-like protein-binding subunits of the 26S proteasome

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Caspases: preparation and characterization

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Bcl-2 and Bcl-xL inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac/DIABLO and subsequent inactivation of X-linked inhibitor-of-apoptosis protein

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death

1 reference

https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

The role of mitochondrial factors in apoptosis: a Russian roulette with more than one bullet.

1 reference

https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

1 reference

https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

A proteasome howdunit: the case of the missing signal

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

A cryptic protease couples deubiquitination and degradation by the proteasome

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https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate

1 reference

https://api.crossref.org/works/10.1016/S1097-2765(04)00156-X

7 January 2021

10.1016/S1097-2765(04)00156-X

Identifiers

DOI

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21 September 2017

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