Caspase-dependent cleavage of the retinoblastoma protein is an early step in neuronal apoptosis. (Q54050681)

24 May 2018

title

Caspase-dependent cleavage of the retinoblastoma protein is an early step in neuronal apoptosis. (English)

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24 May 2018

1 reference

Boutillier AL

1

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24 May 2018

Trinh E

series ordinal

2

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24 May 2018

Loeffler JP

series ordinal

3

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24 May 2018

language of work or name

English

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publication date

1 April 2000

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24 May 2018

published in

Oncogene

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24 May 2018

volume

19

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24 May 2018

issue

18

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24 May 2018

page(s)

2171-2178

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24 May 2018

https://scigraph.springernature.com/pub.10.1038/sj.onc.1203532

exact match

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cites work

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Depolarization regulates cyclin D1 degradation and neuronal apoptosis: a hypothesis about the role of the ubiquitin/proteasome signalling pathway.

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mdm-2 inhibits the G1 arrest and apoptosis functions of the p53 tumor suppressor protein

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Proteolytic cleavage of the mdm2 oncoprotein during apoptosis

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Requirement for a functional Rb-1 gene in murine development

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Induction of apoptosis in cerebellar granule neurons by low potassium: inhibition of death by insulin-like growth factor I and cAMP.

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Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells

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ICE, neuronal apoptosis and neurodegeneration

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Degradation of E2F by the ubiquitin-proteasome pathway: regulation by retinoblastoma family proteins and adenovirus transforming proteins

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Cell death and the cell cycle: a relationship between transformation and neurodegeneration?

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Loss of the retinoblastoma protein-related p130 protein in small cell lung carcinoma

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ICE family proteases: mediators of all apoptotic cell death?

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Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis

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Proteolytic activities that mediate apoptosis

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21 January 2018

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7 January 2021

A DEVD-inhibited caspase other than CPP32 is involved in the commitment of cerebellar granule neurons to apoptosis induced by K+ deprivation.

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7 January 2021

The role of CED-3-related cysteine proteases in apoptosis of cerebellar granule cells.

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7 January 2021

Identification of the MDM2 oncoprotein as a substrate for CPP32-like apoptotic proteases

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7 January 2021

E2F-1 functions in mice to promote apoptosis and suppress proliferation

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7 January 2021

The role of depolarization in the survival and differentiation of cerebellar granule cells in culture.

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https://api.crossref.org/works/10.1038%2FSJ.ONC.1203532

7 January 2021

Inhibition of apoptosis by the retinoblastoma gene product.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1203532

7 January 2021

Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1203532

7 January 2021

SV40 large T antigen binds preferentially to an underphosphorylated member of the retinoblastoma susceptibility gene product family

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https://api.crossref.org/works/10.1038%2FSJ.ONC.1203532

7 January 2021

Inhibition of the interleukin-1 beta converting enzyme family rescues neurons from apoptotic death

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https://api.crossref.org/works/10.1038%2FSJ.ONC.1203532

7 January 2021

Effects of ICE-like protease and calpain inhibitors on neuronal apoptosis.

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https://api.crossref.org/works/10.1038%2FSJ.ONC.1203532

7 January 2021

Signaling to p53: breaking the MDM2-p53 circuit

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7 January 2021

Potassium deprivation-induced apoptosis of cerebellar granule neurons: a sequential requirement for new mRNA and protein synthesis, ICE-like protease activity, and reactive oxygen species.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.ONC.1203532

7 January 2021

The retinoblastoma susceptibility gene product/Sp1 signalling pathway is modulated by Ca2+/calmodulin kinases II and IV activity

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7 January 2021

Identifiers

DOI

10.1038/SJ.ONC.1203532

1 reference

24 May 2018

PubMed ID

10822366

1 reference

24 May 2018