(Q41848995)

English

DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity

scientific article published on March 1997

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

DAP-kinase is a Ca2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity (English)

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

0 references

1 reference

based on heuristic

inferred from title

author name string

Cohen O

1

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Feinstein E

2

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Kimchi A

3

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

language of work or name

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publication date

1 March 1997

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

The EMBO Journal

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

16

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

5

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

998-1008

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Recent advances in tumor necrosis factor and CD40 signaling

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis

1 reference

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A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain

1 reference

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Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product

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Isolation of DAP3, a novel mediator of interferon-gamma-induced cell death

1 reference

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The death domain: a module shared by proteins with diverse cellular functions.

1 reference

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Tumor necrosis factor can induce both apoptic and necrotic forms of cell lysis.

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Use of DNA sequence and mutant analyses and antisense oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin light chain kinase autoinhibition, calmodulin recognition, and activity

1 reference

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Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members

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1 reference

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inferred from PubMed ID database lookup

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1 reference

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1 reference

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Identifiers

10.1093/EMBOJ/16.5.998

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

ResearchGate publication ID

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