ライフサイエンスコーパス: promyelocytic leukemia protein

1 INs abrogated arsenic-induced degradation of promyelocytic leukemia protein.

2 uclear bodies distinct from those containing promyelocytic leukemia protein.

3 isruption and colocalize with Mdm2, p53, and promyelocytic leukemia protein.

4 fraction of cells expressing E1 and E2, the promyelocytic leukemia protein, a component of nuclear d

5 ar regulatory proteins such as p53, IkappaB, promyelocytic leukemia protein and c-Jun.

6 UMO-1 with the target proteins p53, E1B, and promyelocytic leukemia protein and define a substrate bi

7 eduction of 5' mRNA cap affinity of eIF4E by promyelocytic leukemia protein and Z, and E3 ubiquitin c

8 a characterized intrinsic antiviral factor, promyelocytic leukemia protein, and are antagonized by I

9 in this review include alpha-synuclein, the promyelocytic leukemia protein, and glyceraldehyde 3-pho

10 mutations of which lead to BS, localizes to promyelocytic leukemia protein bodies and to the nucleol

11 nuclear compartments identified as speckles, promyelocytic leukemia protein bodies, and nucleoli.

12 e nucleus and subsequently to the subnuclear promyelocytic leukemia protein bodies, suggesting that t

13 zed by multitelomere clusters and associated promyelocytic leukemia protein bodies.

14 Such structures were distinct from PML (promyelocytic leukemia protein) bodies, and it appeared

15 Apoptosis by nuclear TRADD-DD is promyelocytic leukemia protein dependent, involves p53,

16 by translocating to the nucleus, increasing promyelocytic leukemia protein expression and decreasing

17 The promyelocytic leukemia protein is a well known tumor sup

18 f functionally unrelated proteins, including promyelocytic leukemia protein, KAP-1TIF1beta, Z, Mel18,

19 lear signaling by tethering these kinases at promyelocytic leukemia protein nuclear bodies (PML NBs).

20 Here, we report that Sizn1 localizes to promyelocytic leukemia protein nuclear bodies (PML-NBs).

21 viral protein E4orf3 associates with MRN in promyelocytic leukemia protein nuclear bodies before MRN

22 These proteins colocalize in promyelocytic leukemia protein nuclear bodies, and this

23 A component of promyelocytic leukemia protein nuclear bodies, Daxx has

24 e distinct from Cajal bodies, SC-35 domains, promyelocytic leukemia protein nuclear bodies, Polycomb

25 n size and ultimately became juxtaposed with promyelocytic leukemia protein nuclear bodies.

26 s not dependent on interactions with Nbs1 or promyelocytic leukemia protein nuclear bodies.

27 cumulation of RGS14 and its association with promyelocytic leukemia protein nuclear bodies.

28 colocalize with IE1/IE2 proteins adjacent to promyelocytic leukemia protein oncogenic domains.

29 h SUMO-1 and SUMO-2/3 were mislocalized, and promyelocytic leukemia protein PML formed an enlarged ag

30 The promyelocytic leukemia protein PML is a tumor and growth

31 mosomal translocation in these patients, the promyelocytic leukemia protein PML is disrupted as are t

32 The promyelocytic leukemia protein PML is organized into nuc

33 domain protein PIC1 interacts with the acute promyelocytic leukemia protein PML, and both proteins fo

34 at colocalize with those associated with the promyelocytic leukemia protein PML.

35 We report here an interaction between promyelocytic leukemia protein (PML) and ASC.

36 e significance of its localization with both promyelocytic leukemia protein (PML) and Daxx in a subnu

37 dation during lytic infection, including the promyelocytic leukemia protein (PML) and its small ubiqu

38 e residues and vicinal thiol groups, such as promyelocytic leukemia protein (PML) and PML-retinoic ac

39 P0, via degradation of the ND10 constituents promyelocytic leukemia protein (PML) and Sp100 and the s

40 ontains an E3 ubiquitin ligase that degrades promyelocytic leukemia protein (PML) and Sp100, two majo

41 accumulations of several proteins including promyelocytic leukemia protein (PML) and Sp100.

42 f the interferon-inducible repressor protein promyelocytic leukemia protein (PML) and/or Daxx to a vi

43 unctional activities of the tumor suppressor promyelocytic leukemia protein (PML) are mostly associat

44 We identified promyelocytic leukemia protein (PML) as a Fas-interactin

45 and it directly targets the tumor-suppressor promyelocytic leukemia protein (PML) for proteasomal deg

46 emonstrate that E4 induces relocation of the promyelocytic leukemia protein (PML) from multiple intra

47 The tumor suppressor promyelocytic leukemia protein (PML) functions as a stre

48 The promyelocytic leukemia protein (PML) gene of acute promy

49 Promyelocytic leukemia protein (PML) has been implicated

50 PK2 in nuclear speckles and association with promyelocytic leukemia protein (PML) in response to DNA

51 The promyelocytic leukemia protein (PML) is a growth/tumor s

52 The promyelocytic leukemia protein (PML) is a mammalian regu

53 Promyelocytic leukemia protein (PML) is a multifunctiona

54 The promyelocytic leukemia protein (PML) is a nuclear phosph

55 The promyelocytic leukemia protein (PML) is a nuclear phosph

56 Promyelocytic leukemia protein (PML) is a tumor suppress

57 The promyelocytic leukemia protein (PML) is a tumor suppress

58 Promyelocytic leukemia protein (PML) is an essential org

59 Promyelocytic leukemia protein (PML) is an important reg

60 The growth suppressor promyelocytic leukemia protein (PML) is disrupted by the

61 Promyelocytic leukemia protein (PML) modulates the p53 t

62 infection, the virus genome is localized to promyelocytic leukemia protein (PML) nuclear bodies (NB)

63 moylation pathway, and both proteins disrupt promyelocytic leukemia protein (PML) nuclear bodies (NBs

64 Promyelocytic leukemia protein (PML) nuclear bodies (NBs

65 thin the nucleus, Daxx is a component of the promyelocytic leukemia protein (PML) nuclear bodies (NBs

66 Promyelocytic leukemia protein (PML) nuclear bodies (NBs

67 BLM-complemented cells, BLM colocalized with promyelocytic leukemia protein (PML) nuclear bodies and

68 BLM localizes to promyelocytic leukemia protein (PML) nuclear bodies and

69 the human Sir2 homolog, is recruited to the promyelocytic leukemia protein (PML) nuclear bodies of m

70 P0 localizes to cellular structures known as promyelocytic leukemia protein (PML) nuclear bodies or N

71 with cellular nuclear substructures known as promyelocytic leukemia protein (PML) nuclear bodies or N

72 Promyelocytic leukemia protein (PML) nuclear bodies or n

73 A fraction of SAP25 is located in promyelocytic leukemia protein (PML) nuclear bodies, and

74 cellular nuclear structures known as ND10 or promyelocytic leukemia protein (PML) nuclear bodies.

75 y distributed in the nucleus or localized to promyelocytic leukemia protein (PML) nuclear bodies.

76 nuclear structures that are associated with promyelocytic leukemia protein (PML) nuclear bodies.

77 to the nuclear organelles referred to as the promyelocytic leukemia protein (PML) nuclear bodies.

78 The latter enforces promyelocytic leukemia protein (PML) nuclear body (NB) f

79 tion of nuclear protein complexes, including promyelocytic leukemia protein (PML) nuclear domains and

80 Daxx normally resides within the nucleus in promyelocytic leukemia protein (PML) oncogenic domains (

81 ed to HSV-1 genomes but had no effect on the promyelocytic leukemia protein (PML) or Sp100.

82 The promyelocytic leukemia protein (PML) plays an essential

83 nd interferon and through the degradation of promyelocytic leukemia protein (PML) since interferon ha

84 3 ubiquitin ligase E6AP in the regulation of promyelocytic leukemia protein (PML) stability and forma

85 Promyelocytic leukemia protein (PML) sumoylation has bee

86 Promyelocytic leukemia protein (PML) was originally iden

87 feron, as they fail to direct degradation of promyelocytic leukemia protein (PML), a component of hos

88 ization with ICP0 are distinct from those of promyelocytic leukemia protein (PML), a well-characteriz

89 nd it interacts with the death receptor Fas, promyelocytic leukemia protein (PML), and several transc

90 olve direct interactions between ATO and the promyelocytic leukemia protein (PML), as well as acceler

91 y dispersal of ND10 constituents such as the promyelocytic leukemia protein (PML), CREB-binding prote

92 r structures containing both constant [e.g., promyelocytic leukemia protein (PML), SP100, death domai

93 lear structures contain both constant [e.g., promyelocytic leukemia protein (PML), Sp100, death-domai

94 only known inhibitor of FV replication, the promyelocytic leukemia protein (PML), which binds the FV

95 The most common fusion partner is promyelocytic leukemia protein (PML), which is fused to

96 galovirus (HCMV) infection, the periphery of promyelocytic leukemia protein (PML)-associated nuclear

97 sent are its transient targeting to punctate promyelocytic leukemia protein (PML)-associated nuclear

98 i are equivalent to the previously described promyelocytic leukemia protein (PML)-associated prerepli

99 nctate distribution and localized to ND10 in promyelocytic leukemia protein (PML)-expressing cells, w

100 The promyelocytic leukemia protein (PML)-nuclear body is a c

101 used to an N-terminal partner, most commonly promyelocytic leukemia protein (PML).

102 lear structures and disperses its organizing promyelocytic leukemia protein (PML).

103 t nuclear dots that stain positively for the promyelocytic leukemia protein (PML).

104 retinoic acid receptor alpha (RARalpha) with promyelocytic leukemia protein (PML-RARalpha) or with pr

105 In APL, expression of promyelocytic leukemia protein retinoic acid receptor-al

106 leukemia (APL) cases, translocons produce a promyelocytic leukemia protein-retinoic acid receptor al

107 The aberrant association of promyelocytic leukemia protein-retinoic acid receptor-al

108 Furthermore, promyelocytic leukemia protein, RNA polymerase II (Pol I

109 bination with the intrinsic antiviral factor promyelocytic leukemia protein, significantly impairs th

110 Specifically, the promyelocytic leukemia protein (TRIM19; also called PML)