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1 AT comprises two essential subunits, SET and pp32.
2 t also contains the tumor suppressor protein pp32.
3 djacent benign prostate continues to express pp32.
4 e cloning of cDNAs encoding human and murine pp32.
9 truncation analysis define a region spanning pp32 amino acids 150-174 as absolutely required for inhi
11 tain long, acidic COOH-terminal tails, while pp32 and APRIL share a second motif: rev-like leucine-ri
12 ptomycin B leads to the nuclear retention of pp32 and APRIL, their increased association with HuR, an
13 he other involves two protein ligands of HuR-pp32 and APRIL-which contain leucine-rich nuclear export
17 x also contains the tumor suppressor protein pp32 and the granzyme A-activated DNase NM23-H1, which i
20 e assembly protein SET, the tumor suppressor pp32, and the base excision repair enzyme APE can induce
21 andscape of the leucine-rich repeat protein, pp32 (Anp32), obtained by combining pressure-dependent s
27 In this study, we identify the region of pp32 associated with the ability to inhibit oncogene-med
29 t that hyperphosphorylated Rb interacts with pp32 but not with the closely related proteins pp32r1 an
31 n in expression of SET, which complexes with pp32, by a marked change in acetylation status of histon
32 at the histone binding and INHAT activity of pp32 can be regulated by its physical association with o
34 antibodies with higher affinity for phospho-pp32 demonstrate that pp32 is indeed phosphorylated in v
35 p32 is suggestive of a transcription factor, pp32 did not significantly modulate transcription of a r
36 This family includes the tumor suppressor pp32, expressed in normal tissue, and the pro-oncogenic
38 ervations, we hypothesized that reduction of pp32 expression might be an important differentiation si
39 ernative use of genes of the closely-related pp32 family is a common occurrence in human prostate can
41 2r1 and pp32r2, the oncogenic members of the pp32 family, are expressed in prostatic adenocarcinoma,
45 We demonstrate that antisense inhibition of pp32 in NIH3T3 cells leads to a variety of phenotypic ch
50 alization and transfection studies show that pp32 INHAT domains are responsible for histone binding,
51 In contrast, in cotransfection experiments, pp32 inhibited the ability of a broad assortment of onco
63 r affinity for phospho-pp32 demonstrate that pp32 is indeed phosphorylated in vivo at these two sites
65 onstrate that the main barrier to folding of pp32 is quite broad and lies near the unfolded state, wi
72 fication of the pp32 kinase and the sites of pp32 phosphorylation as well as the generation of antibo
75 tic role for the mammalian Set/TAF-Ibeta and pp32 proteins as transducers of chromatin signaling by i
80 antibodies with higher affinity for phospho-pp32 should now provide key information and tools for fu
81 er by comparing the sequence and function of pp32 species from paired benign prostate tissue and adja
82 late-activating factor-Ibeta (TAF-Ibeta) and pp32, specifically bind to unacetylated, hypoacetylated,
83 containing the Set/TAF-Ibeta oncoprotein and pp32 strongly inhibits the HAT activity of p300/CBP and
86 5K interacting factors, importin-alpha 1 and pp32, that may also participate in the functions previou
89 ing corresponds to the most stable region of PP32, we monitored amide hydrogen exchange by NMR spectr
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