ライフサイエンスコーパス: death effector domain

1 to Fas-associated death domain (FADD) at the death effector domain.

2 ng through Fas/CD95 and DR5 were also in the death effector domain.

3 nding site to the N-terminal end of the FADD death effector domain.

4 and does not interact with its NH2-terminal death effector domain.

5 in interaction domains: a death domain and a death effector domain.

6 s BAD by direct modification of its BH3 cell death effector domain.

7 n HIPPI and HIP1 was predicted to resemble a death-effector domain.

8 sed of the Fas extracellular domain and FADD death-effector domain.

9 function by recruiting caspase-8 through its death-effector domain.

10 uble, biologically active mutant of the FADD death-effector domain.

11 have no effect when introduced into the FADD death-effector domain.

12 1) by a homophilic interaction involving the death effector domains.

13 SCC-S2 open reading frame contains only one death effector domain and lacks the carboxyl-terminal ca

14 Death-effector domains and homologous protein modules kn

15 The death domain, death effector domain, and caspase recruitment domain (C

16 raction modules that includes death domains, death effector domains, and Caspase activation and recru

17 The death domain and death effector domain are two common motifs that mediate

18 p75(NTR)-induced cell death indicating that death effector domains are involved.

19 uitment domain), DD (death domain), and DED (death effector domain), are believed to exert their effe

20 tant of FADD, lacking the caspase-dimerizing death effector domain, as well as mice overexpressing th

21 proteins such as BIK and BID share a single death effector domain, BH3, with other BCL-2 family prot

22 ted death receptors such as Fas, whereas the death effector domain binds to procaspase 8.

23 her adapters such as TRADD, whereas the FADD death effector domain binds to procaspase 8.

24 ich is important for HIPPI binding, is not a death-effector domain but is a partially opened coiled c

25 e modular proteins consist of death domains, death effector domains, caspase recruitment domains, and

26 We demonstrate that death effector domain containing DNA binding protein (DE

27 in (DEDD), a highly conserved and ubiquitous death effector domain containing protein, exists predomi

28 e caspase-3, caspase-cleaved cytokeratin-18, death-effector-domain containing DNA-binding protein and

29 In this study, we reveal that Death Effector Domain-containing DNA-binding protein (DE

30 s closest in amino acid sequence homology to death effector domain-containing DNA-binding protein, DE

31 PEA-15 is a widely expressed death effector domain-containing phosphoprotein involved

32 PEA-15 is a death effector domain-containing phosphoprotein that bin

33 Here we demonstrate that a small death effector domain-containing protein called PEA-15 b

34 pase-8 but not with FADD/MORT-1, an upstream death effector domain-containing protein of the Fas and

35 coma-associated herpesvirus (KSHV) encodes a death effector domain-containing protein that is homolog

36 A novel Death Effector Domain-containing protein was identified,

37 Interestingly, death effector domain-containing proteins such as MC159,

38 PEA-15 is composed of an N-terminal death effector domain (DED) and a C-terminal tail of irr

39 been solved in solution, revealing that the death effector domain (DED) and death domain (DD) are al

40 , we have reported that E6 binds to the FADD death effector domain (DED) at a novel E6 binding domain

41 ibitor of apoptosis proteins (IAP); however, death effector domain (DED) caspases of the extrinsic pa

42 triggers recruitment of FADD, which via its death effector domain (DED) engages the DEDs of procaspa

43 asymmetric 7:5 oligomer, which promotes FADD death effector domain (DED) filament formation.

44 ASC filaments in turn nucleate procaspase-8 death effector domain (DED) filaments in vitro and in vi

45 The death effector domain (DED) occurs in proteins that regu

46 hrough interaction of its prodomain with the death effector domain (DED) of the receptor-associating

47 prising the death domain (DD) subfamily, the death effector domain (DED) subfamily, the caspase recru

48 One of these domains is the death effector domain (DED) that is predominantly found

49 structurally distinct domains: an N-terminal death effector domain (DED) that promotes activation of

50 Here, we report that PEA-15, a small death effector domain (DED)-containing protein, blocks R

51 ere we report that the expression of a small death effector domain (DED)-containing protein, NDED (NF

52 of AIM2(PYD) with the hydrophobic patches of death effector domain (DED)-containing proteins and conf

53 esistance in COS-7 cells and blocking by the death effector domain (DED)-containing viral protein MC1

54 ns mediated by conserved domains such as the death effector domain (DED).

55 recruitment of adaptor proteins containing a death effector domain (DED).

56 a physical protein complex with Src via its death effector domains (DED) and maintains the complex i

57 Proteins with death effector domains (DED) are key signal transducers

58 domains (CARD); (3) Death Domains (DD); (4) Death Effector Domains (DED); (5) BIR domains of Inhibit

59 PEA-15 is a small, death effector-domain (DED)-containing protein that was

60 enriched in astrocytes, 15 kDa (PEA-15) is a death-effector domain (DED) containing protein involved

61 The death-effector domain (DED) is a critical protein intera

62 ein consisting of only the N-terminal tandem death effector domains (DEDs) (N protein) was dramatical

63 Homophilic interactions of death effector domains (DEDs) are crucial for the signal

64 Death effector domains (DEDs) are protein interaction mo

65 Death Effector Domains (DEDs) have been known to mediate

66 The prodomains death effector domains (DEDs) of caspase 8 were sufficie

67 th domains (DDs) of Fas and FADD and between death effector domains (DEDs) of FADD and caspase-8/10.

68 Unexpectedly, the two tandem death effector domains (DEDs) of MC159 rigidly associate

69 protein both show sequence similarity to the death effector domains (DEDs) of the Fas/TNFR1 signaling

70 teraction modules known as death domains and death effector domains (DEDs) to assemble receptor signa

71 drophobic patch 1 and alpha2 regions of both death effector domains (DEDs) within MC159 resulted in l

72 10 contain long pro-domains with duplicated death effector domains (DEDs), as well as their correspo

73 as- and TNFR1-induced apoptosis and contains death effector domains (DEDs).

74 rization of FADD and caspase-8 through their death effector domains (DEDs).

75 nal prodomain, which contains two homologous death effector domains (DEDs).

76 ses a prodomain consisting of two homologous death effector domains (DEDs).

77 iral FLIP and, as such, possesses two tandem death effector domains (DEDs).

78 inhibitory proteins (cFLIP) assemble through death-effector domains (DEDs), directing death receptor

79 ark of this family is the presence of tandem death-effector domains (DEDs).

80 cting site on PEA-15 consists of part of the death effector domain domain plus additional C-terminal

81 ed version of FADD that lacks the N-terminal death effector domain (FADD(DN)) increases the sensitivi

82 that human CLARP contains two amino-terminal death effector domains fused to a carboxyl-terminal casp

83 novel human protein that contains FADD/Mort1 death effector domain homology regions, designated FLAME

84 resembles a similar surface involved in the death effector domain homotypic interactions.

85 erminus that shows a significant homology to death effector domain II of cell death regulatory protei

86 nd TNF-dependent signaling, whereas the FADD death effector domain mutants rescued only TNF signaling

87 The FADD-MBD4 interaction involved the death effector domain of FADD and a region of MBD4 adjac

88 FLICE binds to the death effector domain of FADD and upon overexpression in

89 ependently of the death effector domain, the death effector domain of FADD comes into direct contact

90 cate that in contrast to current models, the death effector domain of FADD is involved in interaction

91 em we previously identified mutations in the death effector domain of FADD that prevented binding to

92 to demonstrate that E6 binds directly to the death effector domain of Fas-associated death domain (FA

93 ace identified in Drosophila Tube DD and the death effector domain of hamster PEA-15, two physiologic

94 man TRAF6, which directly interacts with the death effector domain of pro-caspase 8, and the N-termin

95 The presence of two death effector domains of c-FLIP and S-nitrosylation of

96 of caspase-8 and -10 both interact with the death-effector domain of FADD.

97 energy transfer analysis indicates that the death-effector domains of caspase-8 and -10 both interac

98 or MACH) through an interaction between the death-effector domains of FADD and caspase 8.

99 Mutations in either the death effector domain or C-terminal tail of PEA-15 that

100 among the four families (death domain or DD, death effector domain or DED, caspase recruitment domain

101 protein E8 share substantial homology to the death effector domain present in the adaptor molecule Fa

102 The scaffolding protein PEA-15 is a death effector domain protein that directly interacts wi

103 ysteine-containing glutathione peroxidase, a death effector domain protein, a chemokine, a major hist

104 Surprisingly, these mutations were in the death effector domain rather than the death domain.

105 Also, their N termini contain FADD-like death effector domains, suggesting possible interaction

106 is now reveals how the FADD-nucleated tandem death effector domain (tDED) helical filament is require

107 re through the oligomerization of its tandem death effector domain (tDED), resulting in caspase activ

108 h ASC at the inflammasome through its tandem death effector domain (tDED), which is regulated by the

109 he pro-domain of FLICE2 encodes a functional death effector domain that binds to the corresponding do

110 haracterized a phosphoprotein protein with a death effector domain that has a novel bifunctional role

111 Instead, a hydrophobic region of the FADD death-effector domain that is not present in the death d

112 omain of FADD functions independently of the death effector domain, the death effector domain of FADD

113 Bap31 complex is dependent on the variant of death effector domain (vDED) in Bap31 and is required fo