(Q40527794)

21 September 2017

title

The biochemical mechanism of caspase-2 activation (English)

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21 September 2017

3

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21 September 2017

Baliga BC

1

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21 September 2017

Read SH

series ordinal

2

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21 September 2017

publication date

1 November 2004

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Cell Death & Differentiation

21 September 2017

published in

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21 September 2017

volume

11

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21 September 2017

issue

11

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21 September 2017

page(s)

1234-1241

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https://scigraph.springernature.com/pub.10.1038/sj.cdd.4401492

21 September 2017

exact match

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cites work

Prodomains--adaptors--oligomerization: the pursuit of caspase activation in apoptosis.

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7 January 2021

Mechanisms of caspase activation and inhibition during apoptosis

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7 January 2021

Caspase activation - stepping on the gas or releasing the brakes? Lessons from humans and flies

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https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Activation of initiator caspases through a stable dimeric intermediate

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https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Insights into the regulatory mechanism for caspase-8 activation

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https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Oligomerization is a general mechanism for the activation of apoptosis initiator and inflammatory procaspases.

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https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

A unified model for apical caspase activation

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https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Many cuts to ruin: a comprehensive update of caspase substrates

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https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Functional activation of Nedd2/ICH-1 (caspase-2) is an early process in apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Dimerization and autoprocessing of the Nedd2 (caspase-2) precursor requires both the prodomain and the carboxyl-terminal regions

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Chimeric caspase molecules with potent cell killing activity in apoptosis-resistant cells.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Role of prodomain in importin-mediated nuclear localization and activation of caspase-2

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

RAIDD is a new 'death' adaptor molecule

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Bcl-2 constitutively suppresses p53-dependent apoptosis in colorectal cancer cells

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Mitotic catastrophe constitutes a special case of apoptosis whose suppression entails aneuploidy.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

The NRIF3 family of transcriptional coregulators induces rapid and profound apoptosis in breast cancer cells

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Inhibition of apoptosis by the expression of antisense Nedd2.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Caspase-2 can trigger cytochrome C release and apoptosis from the nucleus.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Apoptosis. A cinderella caspase takes center stage

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Apaf-1/cytochrome c apoptosome: an essential initiator of caspase activation or just a sideshow?

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Processing of the Nedd2 precursor by ICE-like proteases and granzyme B.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is dependent on both Apaf-1 and caspase-9

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

1 reference

7 January 2021

Defects in regulation of apoptosis in caspase-2-deficient mice

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

A novel Apaf-1-independent putative caspase-2 activation complex

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor. A novel function for a caspase prodomain

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

DRONC, an ecdysone-inducible Drosophila caspase

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Apoptosis initiated by Bcl-2-regulated caspase activation independently of the cytochrome c/Apaf-1/caspase-9 apoptosome

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Apaf-1 and caspase-9 accelerate apoptosis, but do not determine whether factor-deprived or drug-treated cells die

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Differential inhibitory effects of CrmA, P35, IAP and three mammalian IAP homologues on apoptosis in NIH3T3 cells following various death stimuli

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4401492

7 January 2021

Identifiers

DOI

10.1038/SJ.CDD.4401492

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Dimensions Publication ID

21 September 2017

1024432855

0 references

1 reference