(Q24323139)

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

The biochemical mechanism of caspase-2 activation

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Mechanisms of caspase activation

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Requirement for p53 and p21 to sustain G2 arrest after DNA damage

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

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.ONC.1209569

7 January 2021

Essential role for caspase-8 in transcription-independent apoptosis triggered by p53

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

The protein structures that shape caspase activity, specificity, activation and inhibition

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

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.ONC.1209569

7 January 2021

Caspase-2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase-7.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

PIDD mediates NF-kappaB activation in response to DNA damage

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

C-Abl as a modulator of p53.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Bcl-2 rescues ceramide- and etoposide-induced mitochondrial apoptosis through blockage of caspase-2 activation.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Bcl-2-regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Tumor suppressor p53 is a direct transcriptional activator of the human bax gene

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

PUMA, a novel proapoptotic gene, is induced by p53

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Caspases: killer proteases

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

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.ONC.1209569

7 January 2021

Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

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.ONC.1209569

7 January 2021

The Birc6 (Bruce) gene regulates p53 and the mitochondrial pathway of apoptosis and is essential for mouse embryonic development

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

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.ONC.1209569

7 January 2021

Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

AlphaII-spectrin is an in vitro target for caspase-2, and its cleavage is regulated by calmodulin binding.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Arsenic trioxide triggers a regulated form of caspase-independent necrotic cell death via the mitochondrial death pathway

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

p53 induces apoptosis by caspase activation through mitochondrial cytochrome c release.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Transcription, apoptosis and p53: catch-22.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

p53-dependent caspase-2 activation in mitochondrial release of apoptosis-inducing factor and its role in renal tubular epithelial cell injury

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Comprehensive studies on subcellular localizations and cell death-inducing activities of eight GFP-tagged apoptosis-related caspases

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Association of caspase-2 with the promyelocytic leukemia protein nuclear bodies

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

LRDD, a novel leucine rich repeat and death domain containing protein

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

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.ONC.1209569

7 January 2021

Death in the balance: alternative participation of the caspase-2 and -9 pathways in neuronal death induced by nerve growth factor deprivation.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

RAIDD is required for apoptosis of PC12 cells and sympathetic neurons induced by trophic factor withdrawal

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021

Activation of caspase-8 in drug-induced apoptosis of B-lymphoid cells is independent of CD95/Fas receptor-ligand interaction and occurs downstream of caspase-3.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1209569

7 January 2021