(Q28506614)

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DNA fragmentation factor 45-deficient cells are more resistant to apoptosis and exhibit different dying morphology than wild-type control cells

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scholarly article

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PubMed publication ID

24 January 2017

DNA fragmentation factor 45-deficient cells are more resistant to apoptosis and exhibit different dying morphology than wild-type control cells (English)

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PubMed publication ID

24 January 2017

apoptotic process

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DNA fragmentation factor, alpha subunit

1 reference

GOA release 2020-03-11

author name string

J. Zhang

1

1 reference

PubMed publication ID

24 January 2017

X. Wang

2

1 reference

PubMed publication ID

24 January 2017

K. E. Bove

3

1 reference

PubMed publication ID

24 January 2017

M. Xu

4

1 reference

PubMed publication ID

24 January 2017

language of work or name

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publication date

24 December 1999

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PubMed publication ID

24 January 2017

Journal of Biological Chemistry

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PubMed publication ID

24 January 2017

274

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PubMed publication ID

24 January 2017

52

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PubMed publication ID

24 January 2017

37450–37454

1 reference

PubMed publication ID

24 January 2017

Social controls on cell survival and cell death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Life, death, and the pursuit of apoptosis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Programmed cell death in animal development

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Apoptosis in the pathogenesis and treatment of disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Genetic control of programmed cell death in the nematode C. elegans.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Caenorhabditis elegans gene ced-9 protects cells from programmed cell death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

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/10.1074%2FJBC.274.52.37450

21 January 2018

Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Regulation of lymphocyte survival by the bcl-2 gene family

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Bcl-2 gene family in the nervous system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

The Bcl-2 protein family: arbiters of cell survival

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Bcl-xL regulates the membrane potential and volume homeostasis of mitochondria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Apoptosis by death factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Death receptors: signaling and modulation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Cytochrome c: can't live with it--can't live without it.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Mitochondria and apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Protease activation during apoptosis: death by a thousand cuts?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Caspases: killer proteases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Caspases: enemies within

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Activation of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease). Oligomerization and direct interaction with histone H1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Resistance to DNA fragmentation and chromatin condensation in mice lacking the DNA fragmentation factor 45

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Cell death throes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Cell nucleus and DNA fragmentation are not required for apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Studies of the lamin proteinase reveal multiple parallel biochemical pathways during apoptotic execution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Functional differences of two forms of the inhibitor of caspase-activated DNase, ICAD-L, and ICAD-S.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Transition from caspase-dependent to caspase-independent mechanisms at the onset of apoptotic execution.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Native recombinant cyclophilins A, B, and C degrade DNA independently of peptidylprolyl cis-trans-isomerase activity. Potential roles of cyclophilins in apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Apoptotic nuclear morphological change without DNA fragmentation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

The apoptosis endonucleases: cleaning up after cell death?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

A matter of life and cell death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

CPP32/apopain is a key interleukin 1 beta converting enzyme-like protease involved in Fas-mediated apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Proteases to die for

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

The role of DNA fragmentation in apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Sphingosine 1-phosphate inhibits activation of caspases that cleave poly(ADP-ribose) polymerase and lamins during Fas- and ceramide-mediated apoptosis in Jurkat T lymphocytes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.52.37450

21 January 2018

Identifiers

10.1074/JBC.274.52.37450

0 references

PubMed publication ID

1 reference

PubMed publication ID

24 January 2017

ResearchGate publication ID

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