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1 uclear bodies distinct from those containing promyelocytic leukemia protein.
2 INs abrogated arsenic-induced degradation of 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 se changes are associated with remodeling of promyelocytic leukemia protein nuclear bodies (PML NBs),
20 lear signaling by tethering these kinases at promyelocytic leukemia protein nuclear bodies (PML NBs).
21      Here, we report that Sizn1 localizes to promyelocytic leukemia protein nuclear bodies (PML-NBs).
22  viral protein E4orf3 associates with MRN in promyelocytic leukemia protein nuclear bodies before MRN
23                 These proteins colocalize in promyelocytic leukemia protein nuclear bodies, and this
24                               A component of promyelocytic leukemia protein nuclear bodies, Daxx has
25 e distinct from Cajal bodies, SC-35 domains, promyelocytic leukemia protein nuclear bodies, Polycomb
26 n size and ultimately became juxtaposed with promyelocytic leukemia protein nuclear bodies.
27 s not dependent on interactions with Nbs1 or promyelocytic leukemia protein nuclear bodies.
28 cumulation of RGS14 and its association with promyelocytic leukemia protein nuclear bodies.
29 colocalize with IE1/IE2 proteins adjacent to promyelocytic leukemia protein oncogenic domains.
30 h SUMO-1 and SUMO-2/3 were mislocalized, and promyelocytic leukemia protein PML formed an enlarged ag
31                                          The promyelocytic leukemia protein PML is a tumor and growth
32 mosomal translocation in these patients, the promyelocytic leukemia protein PML is disrupted as are t
33                                          The promyelocytic leukemia protein PML is organized into nuc
34 domain protein PIC1 interacts with the acute promyelocytic leukemia protein PML, and both proteins fo
35 at colocalize with those associated with the promyelocytic leukemia protein PML.
36        We report here an interaction between promyelocytic leukemia protein (PML) and ASC.
37 e significance of its localization with both promyelocytic leukemia protein (PML) and Daxx in a subnu
38 dation during lytic infection, including the promyelocytic leukemia protein (PML) and its small ubiqu
39 e residues and vicinal thiol groups, such as promyelocytic leukemia protein (PML) and PML-retinoic ac
40 P0, via degradation of the ND10 constituents promyelocytic leukemia protein (PML) and Sp100 and the s
41 ontains an E3 ubiquitin ligase that degrades promyelocytic leukemia protein (PML) and Sp100, two majo
42  accumulations of several proteins including promyelocytic leukemia protein (PML) and Sp100.
43 ier (SUMO)-conjugating enzyme, UBC9, and the promyelocytic leukemia protein (PML) and thus was not du
44 f the interferon-inducible repressor protein promyelocytic leukemia protein (PML) and/or Daxx to a vi
45 unctional activities of the tumor suppressor promyelocytic leukemia protein (PML) are mostly associat
46                                We identified promyelocytic leukemia protein (PML) as a Fas-interactin
47 o makes Aire susceptible to interaction with promyelocytic leukemia protein (PML) bodies, sites of ma
48 and it directly targets the tumor-suppressor promyelocytic leukemia protein (PML) for proteasomal deg
49 emonstrate that E4 induces relocation of the promyelocytic leukemia protein (PML) from multiple intra
50                         The tumor suppressor promyelocytic leukemia protein (PML) functions as a stre
51                                          The promyelocytic leukemia protein (PML) gene of acute promy
52                                              Promyelocytic leukemia protein (PML) has been implicated
53 PK2 in nuclear speckles and association with promyelocytic leukemia protein (PML) in response to DNA
54                                          The promyelocytic leukemia protein (PML) is a growth/tumor s
55                                          The promyelocytic leukemia protein (PML) is a mammalian regu
56                                              Promyelocytic leukemia protein (PML) is a multifunctiona
57                                          The promyelocytic leukemia protein (PML) is a nuclear phosph
58                                          The promyelocytic leukemia protein (PML) is a nuclear phosph
59                                              Promyelocytic leukemia protein (PML) is a tumor suppress
60                                          The promyelocytic leukemia protein (PML) is a tumor suppress
61                                              Promyelocytic leukemia protein (PML) is an essential org
62                                              Promyelocytic leukemia protein (PML) is an important reg
63                        The growth suppressor promyelocytic leukemia protein (PML) is disrupted by the
64                                              Promyelocytic leukemia protein (PML) modulates the p53 t
65  infection, the virus genome is localized to promyelocytic leukemia protein (PML) nuclear bodies (NB)
66                                              Promyelocytic leukemia protein (PML) nuclear bodies (NBs
67 moylation pathway, and both proteins disrupt promyelocytic leukemia protein (PML) nuclear bodies (NBs
68                                              Promyelocytic leukemia protein (PML) nuclear bodies (NBs
69 thin the nucleus, Daxx is a component of the promyelocytic leukemia protein (PML) nuclear bodies (NBs
70 BLM-complemented cells, BLM colocalized with promyelocytic leukemia protein (PML) nuclear bodies and
71                             BLM localizes to promyelocytic leukemia protein (PML) nuclear bodies and
72  the human Sir2 homolog, is recruited to the promyelocytic leukemia protein (PML) nuclear bodies of m
73 P0 localizes to cellular structures known as promyelocytic leukemia protein (PML) nuclear bodies or N
74 with cellular nuclear substructures known as promyelocytic leukemia protein (PML) nuclear bodies or N
75                                              Promyelocytic leukemia protein (PML) nuclear bodies or n
76            A fraction of SAP25 is located in promyelocytic leukemia protein (PML) nuclear bodies, and
77 to the nuclear organelles referred to as the promyelocytic leukemia protein (PML) nuclear bodies.
78 cellular nuclear structures known as ND10 or promyelocytic leukemia protein (PML) nuclear bodies.
79 y distributed in the nucleus or localized to promyelocytic leukemia protein (PML) nuclear bodies.
80  nuclear structures that are associated with promyelocytic leukemia protein (PML) nuclear bodies.
81                          The latter enforces promyelocytic leukemia protein (PML) nuclear body (NB) f
82 tion of nuclear protein complexes, including promyelocytic leukemia protein (PML) nuclear domains and
83  Daxx normally resides within the nucleus in promyelocytic leukemia protein (PML) oncogenic domains (
84 ed to HSV-1 genomes but had no effect on the promyelocytic leukemia protein (PML) or Sp100.
85                                          The promyelocytic leukemia protein (PML) plays an essential
86 nd interferon and through the degradation of promyelocytic leukemia protein (PML) since interferon ha
87 3 ubiquitin ligase E6AP in the regulation of promyelocytic leukemia protein (PML) stability and forma
88                                              Promyelocytic leukemia protein (PML) sumoylation has bee
89                                              Promyelocytic leukemia protein (PML) was originally iden
90 feron, as they fail to direct degradation of promyelocytic leukemia protein (PML), a component of hos
91 ization with ICP0 are distinct from those of promyelocytic leukemia protein (PML), a well-characteriz
92 nd it interacts with the death receptor Fas, promyelocytic leukemia protein (PML), and several transc
93 olve direct interactions between ATO and the promyelocytic leukemia protein (PML), as well as acceler
94 y dispersal of ND10 constituents such as the promyelocytic leukemia protein (PML), CREB-binding prote
95 r structures containing both constant [e.g., promyelocytic leukemia protein (PML), SP100, death domai
96 lear structures contain both constant [e.g., promyelocytic leukemia protein (PML), Sp100, death-domai
97  only known inhibitor of FV replication, the promyelocytic leukemia protein (PML), which binds the FV
98            The most common fusion partner is promyelocytic leukemia protein (PML), which is fused to
99 sent are its transient targeting to punctate promyelocytic leukemia protein (PML)-associated nuclear
100 galovirus (HCMV) infection, the periphery of promyelocytic leukemia protein (PML)-associated nuclear
101 i are equivalent to the previously described promyelocytic leukemia protein (PML)-associated prerepli
102 nctate distribution and localized to ND10 in promyelocytic leukemia protein (PML)-expressing cells, w
103                                          The promyelocytic leukemia protein (PML)-nuclear body is a c
104 used to an N-terminal partner, most commonly promyelocytic leukemia protein (PML).
105 lear structures and disperses its organizing promyelocytic leukemia protein (PML).
106 t nuclear dots that stain positively for the promyelocytic leukemia protein (PML).
107 retinoic acid receptor alpha (RARalpha) with promyelocytic leukemia protein (PML-RARalpha) or with pr
108                        In APL, expression of promyelocytic leukemia protein retinoic acid receptor-al
109  leukemia (APL) cases, translocons produce a promyelocytic leukemia protein-retinoic acid receptor al
110                  The aberrant association of promyelocytic leukemia protein-retinoic acid receptor-al
111                                 Furthermore, promyelocytic leukemia protein, RNA polymerase II (Pol I
112 bination with the intrinsic antiviral factor promyelocytic leukemia protein, significantly impairs th
113                            Specifically, the promyelocytic leukemia protein (TRIM19; also called PML)

 
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