Author Summary Herpesviruses hijack cellular components to enhance viral gene expression. This is particularly important for the efficient nuclear export of herpesvirus intronless mRNAs to allow the production of viral proteins. We have previously demonstrated that Kaposis sarcoma-associated herpesvirus encodes a conserved protein, ORF57, which recruits essential cellular mRNA export proteins onto the viral intronless mRNAs to form an export competent viral ribonucleoprotein particle. Specifically, we have shown that ORF57 interacts directly with the cellular export adaptor protein, Aly, to recruit other cellular mRNA export proteins. Surprisingly however, depletion of Aly has a limited effect on both cellular and viral mRNA nuclear export levels, suggesting a degree of redundancy in the export pathways and the existence of other export adaptor proteins. Here we have identified a novel interaction between ORF57 and a second export adaptor protein, UIF. We show for the first time that the ORF57-UIF

During gene expression, RNA export factors are mainly known for driving nucleo-cytoplasmic transport. While early studies suggested that the exon junction complex (EJC) provides a binding platform for them, subsequent work proposed that they are only recruited by the cap binding complex to the 5 end of RNAs, as part of TREX. Using iCLIP, we show that the export receptor Nxf1 and two TREX subunits, Alyref and Chtop, are recruited to the whole mRNA co-transcriptionally via splicing but before 3 end processing. Consequently, Alyref alters splicing decisions and Chtop regulates alternative polyadenylation. Alyref is recruited to the 5 end of RNAs by CBC, and our data reveal subsequent binding to RNAs near EJCs. We demonstrate that eIF4A3 stimulates Alyref deposition not only on spliced RNAs close to EJC sites but also on single-exon transcripts. Our study reveals mechanistic insights into the co-transcriptional recruitment of mRNA export factors and how this shapes the human transcriptome.

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Influenza A virus nucleoprotein (NP) is a structural component that encapsulates the viral genome into the form of ribonucleoprotein complexes (vRNPs). Efficient assembly of vRNPs is critical for the virus life cycle. The assembly route from RNA-free NP to the NP-RNA polymer in vRNPs has been suggested to require a cellular factor UAP56, but the mechanism is poorly understood. Here, we characterized the interaction between NP and UAP56 using recombinant proteins and showed that UAP56 features two NP binding sites. In addition to the UAP56 core comprised of two RecA domains, we identified the N-terminal extension (NTE) of UAP56 as a previously unknown NP binding site. In particular, UAP56-NTE recognizes the nucleic acid binding region of NP. This corroborates our observation that binding of UAP56-NTE and RNA to NP is mutually exclusive. Collectively, our results reveal the molecular basis for how UAP56 acts on RNA-free NP, and provide new insights into NP-mediated influenza genome packaging ...

A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Plays also a role in the biogenesis

Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. THP1 binds to RNA in vitro.

We describe a novel RNA binding protein, Y14, a predominantly nuclear nucleocytoplasmic shuttling protein. Interestingly, Y14 associates preferentially with mRNAs produced by splicing but not with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Y14 associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs. Splicing of a single intron is sufficient for Y14 association. Y14-containing nuclear complexes are different from general hnRNP complexes. They contain hnRNP proteins and several unique proteins including the mRNA export factor TAP. Thus, Y14 defines novel intermediates in the pathway of gene expression, postsplicing nuclear preexport mRNPs, and newly exported cytoplasmic mRNPs, whose composition is established by splicing. These findings suggest that pre-mRNA splicing imprints mRNA with a unique set of proteins that persists in the cytoplasm and thereby communicates the history of the transcript ...

Many mammalian and viral genes are alternatively spliced and subject to regulation at the post- transcriptional level. However, relatively little is known about the cellular mechanisms for this regulation. We are using retroviruses as model systems to elucidate these mechanisms. Some of our studies focus on HIV Rev, an essential HIV protein. Rev mediates the nucleo-cytoplasmic export of unspliced and incompletely spliced HIV RNAs and provides an important HIV drug target. Another major focus of the laboratory is the function of the constitutive transport element (CTE). The CTE interacts directly with host cell proteins to facilitate export of intron containing RNA. We are currently analyzing the function of cellular proteins that are involved in the CTE mediated export pathway. One is NXF1 (TAP), a protein which has been proposed to play an essential role in cellular mRNA export. A second protein under study is NXT1, an important TAP cofactor. CTE function is also enhanced by SAM68, a major ...

The various steps of mRNP biogenesis (transcription, processing and export) are interconnected. It has been shown that the transcription machinery plays a pivotal role in mRNP assembly, since several mRNA export factors are recruited during transcription and physically interact with components of the transcription machinery. Although the shuttling DEAD-box protein Dbp5p is concentrated on the cytoplasmic fibrils of the NPC, previous studies demonstrated that it interacts physically and genetically with factors involved in transcription initiation. We investigated the effect of mutations affecting various components of the transcription initiation apparatus on the phenotypes of mRNA export mutant strains. Our results show that growth and mRNA export defects of dbp5 and mex67 mutant strains can be suppressed by mutation of specific transcription initiation components, but suppression was not observed for mutants acting in the very first steps of the pre-initiation complex (PIC) formation. Our results

The results described in this paper indicate that HIV unspliced RNA export and Gag trafficking to the plasma membrane are linked. By simply changing the RNA export element from the RRE to 4 × CTE, we can restore Gag assembly and budding in murine cells (Figures 3 and 5). To explain how a pretranslational event, RNA export, could modulate a post‐translational event, membrane trafficking, we hypothesize that HIV RNA is marked at (or by) nuclear export such that the cytosolic fate of the encoded Gag is predetermined. Based on our findings, both the RRE/Rev/Crm1 and 4 × CTE/NXF1 nuclear export pathways successfully mark unspliced gag‐pol mRNA in human cells and promote proper assembly. However, in murine cells, marking through the action of RRE/Rev/Crm1 is defective and HIV assembly is inhibited. Possibilities for the mark include the structure of the mRNA itself or proteins that comprise the mRNP; these could be added or removed as the export complex is formed, as it transits the NPC, ...

In higher eukaryotes, messenger RNAs (mRNAs) are exported from the nucleus to the cytoplasm via factors deposited near the 5 end of the transcript during splicing. The signal sequence coding region (SSCR) can support an alternative mRNA export (ALREX) pathway that does not require splicing. However …

DDX3 is a DEAD-box protein (Figure 3A). Although DDX3 has been shown to interact with RNA transport factors TAP/NXF1 and REF/Aly, it does not appear to play a role in bulk mRNA export [32-34]. It is interesting to note that Ded1 (yeast DDX3 homolog) modulates translation by controlling the conformation of eIF4F-mRNA complex [35], suggesting a role of Ded1/DDX3 in translation. The function of DDX3 in RNA export was not recognized until DDX3 was found to participate in the Rev-dependent export of unspliced and partially spliced HIV-1 RNAs [3]. Rev is co-immunoprecipitated with DDX3, but a direct interaction between the two proteins has not been experimentally demonstrated. Rather, the purified GST-CRM1 is able to pull down the in vitro translated DDX3. This direct interaction depends on the DDX3 fragment at amino acid positions 260 to 517 that does not include the NES (nuclear export signal) sequence, and is Ran-GTP independent (Figure 3A, 3C), which suggests that instead of a cargo, DDX3 acts as ...

1JN5: Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor.

Deutsch, G.B., Zielonka, E.M., Coutandin, D., Weber, T.A., Schäfer, B., Hannewald, J., Luh, L.M., Durst, F.G., Ibrahim, M., Hoffmann, J., Niesen, F.H., Sentürk, A., Kunkel, H., Brutschy, B., Schleiff, E., Knapp, S., Acker-Palmer, A., Grez, M., McKeon, F. and Dötsch, V. (2011) DNA damage in oocytes induces an irreversible switch of the quality control factor TAp63α from dimer to tetramer. Cell, 144:566-576.. ...

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Ref A: 2D0D1DFD7FF74E9FA87E109E2B54B004 Ref B: AMBEDGE0612 Ref C: 2021-09-21T04:25:31Z. Ref A: 048C0B89731946D4B4A1CADD4D43E752 Ref B: AMBEDGE0717 Ref C: 2021-09-21T04:25:31Z. Ref A: D6C2F2ECBC5B40628A99D98144F6C641 Ref B: AMBEDGE0806 Ref C: 2021-09-21T04:25:31Z ...

Gene expression requires proper messenger RNA (mRNA) export and translation. However, the functional links between these consecutive steps have not been fully defined. Gle1 is an essential, conserved mRNA export factor whose export function is dependent on the small molecule inositol hexakisphosphat …

The coordination and coupling of the several steps in mRNA biogenesis helps to ensure proper regulation of gene expression. The DEAD-box helicase Dbp5/Rat8 is an essential mRNA export factor that has also been implicated in other steps of mRNA ...

The coordination and coupling of the several steps in mRNA biogenesis helps to ensure proper regulation of gene expression. The DEAD-box helicase Dbp5/Rat8 is an essential mRNA export factor that has also been implicated in other steps of mRNA ...

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p,The PIWI-interacting RNA (piRNA) pathway protects genome integrity in part through establishing repressive heterochromatin at transposon loci. Silencing requires piRNA-guided targeting of nuclear PIWI proteins to nascent transposon transcripts, yet the subsequent molecular events are not understood. Here, we identify SFiNX (silencing factor interacting nuclear export variant), an interdependent protein complex required for Piwi-mediated cotranscriptional silencing in Drosophila. SFiNX consists of Nxf2-Nxt1, a gonad-specific variant of the heterodimeric messenger RNA export receptor Nxf1-Nxt1 and the Piwi-associated protein Panoramix. SFiNX mutant flies are sterile and exhibit transposon derepression because piRNA-loaded Piwi is unable to establish heterochromatin. Within SFiNX, Panoramix recruits heterochromatin effectors, while the RNA binding protein Nxf2 licenses cotranscriptional silencing. Our data reveal how Nxf2 might have evolved from an RNA transport receptor into a cotranscriptional ...

TY - JOUR. T1 - Influenza A virus NS1 protein promotes efficient nuclear export of unspliced viral M1 mRNA. AU - Pereira, Carina F.. AU - Read, Eliot K. C.. AU - Wise, Helen M.. AU - Amorim, Maria J.. AU - Digard, Paul. PY - 2017/8. Y1 - 2017/8. N2 - Influenza A virus mRNAs are transcribed by the viral RNA-dependent RNA polymerase in the cell nucleus before being exported to the cytoplasm for translation. Segment 7 produces two major transcripts: an unspliced mRNA that encodes the M1 matrix protein and a spliced transcript that encodes the M2 ion channel. Export of both mRNAs is dependent on the cellular NXF1/TAP pathway, but it is unclear how they are recruited to the export machinery or how the introncontaining but unspliced M1 mRNA bypasses the normal quality-control checkpoints. Using fluorescent in situ hybridization to monitor segment 7 mRNA localization, we found that cytoplasmic accumulation of unspliced M1 mRNA was inefficient in the absence of NS1, both in the context of segment 7 RNPs ...

IFN-γ induces the expression of a wide variety of genes, many of which are involved in antiviral response (23). To determine whether induction of Nup98 and Nup96 was sufficient to reverse the M protein export block, we tested whether transfection with Nup98 and Nup96 cDNA would substitute for IFN-γ and relieve the inhibition of mRNA export. Using a luciferase reporter gene assay (24), cells were co-transfected with a mixture of plasmids coding for the M protein alone, for Nup98 and Nup96 alone, or for both. M protein expression clearly inhibited luciferase expression, and this inhibition was partially relieved by Nup98 and Nup96 expression (Fig. 4C). Thus, Nup98 and Nup96 expression is capable of reversing M protein-mediated inhibition of nuclear mRNA export.. The mechanism by which increased expression of Nup98 and of Nup96 reverses M protein-mediated inhibition of mRNA export remains to be elucidated. The inhibitory region of the M protein has been mapped (12, 25) and shown to target the ...

mRNA export factor is a protein that in humans is encoded by the RAE1 gene. Mutations in the Schizosaccharomyces pombe Rae1 and Saccharomyces cerevisiae Gle2 genes have been shown to result in accumulation of poly(A)-containing mRNA in the nucleus, suggesting that the encoded proteins are involved in RNA export. The protein encoded by this gene is a homolog of yeast Rae1. It contains four WD40 motifs, and has been shown to localize to distinct foci in the nucleoplasm, to the nuclear rim, and to meshwork-like structures throughout the cytoplasm. This gene is thought to be involved in nucleocytoplasmic transport, and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton. Alternatively spliced transcript variants encoding the same protein have been found for this gene. RAE1 has been shown to interact with NUP98. GRCh38: Ensembl release 89: ENSG00000101146 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000027509 - Ensembl, May 2017 Human PubMed Reference:. Mouse ...

P19 embryonal carcinoma cells differentiate into neuron-like cells in the presence of retinoic acid. We conducted a quantitative proteomic analysis of changes in protein expression accompanying the differentiation process using isobaric tag technology coupled with LC-MS/MS. Replicate quantitative data were obtained for 182 proteins in total cell lysates. This comparison between rapidly dividing undifferentiated cells and neuron-like cells revealed protein changes reflecting withdrawal from the cell cycle accompanied by a dynamic reorganization of the cytoskeleton and an up-regulation of mitochondrial biogenesis. Mitochondria isolated from P19 and neuron-like cells provided replicate quantitative information on the relative abundance of 60 mitochondrial proteins. P160 myb-binding protein, Mybbp1a, was one of the proteins most markedly down-regulated during neuronal differentiation. Mybbp1a may repress the transcription coactivator PGC-1 and thus inhibit transcription of nuclear genes encoding ...

1KOH: The crystal structure and mutational analysis of a novel RNA-binding domain found in the human Tap nuclear mRNA export factor.

This project will explore the effect of CRISPR/Cas9 mediated mutations in the NXF1 gene on the outgrowth and function of primary hippocampal and cortical neurons in culture systems.Marie-Louise HammarskjoldSchool of MedicineGeorge S. BloomCollege and Graduate School of Arts & SciencesDavid RekoshSchool of MedicineFind out more: https://3c.virginia.edu/projects/121

Although several SR proteins were reported to shuttle poorly in HeLa cells (Cáceres et al., 1998; Lin et al., 2005; Sapra et al., 2009), we have recently shown that all SR proteins act as NXF1 adapters in pluripotent P19 cells (Müller-McNicoll et al., 2016). To investigate this discrepancy, we developed a quantitative shuttling assay to measure the nucleocytoplasmic shuttling of seven canonical family members. Key technical advances were the use of stable clonal cell lines expressing similar and near-endogenous levels of GFP-tagged proteins (donor) and a membrane-bound marker protein (recipient). Quantification of total nuclear fluorescence in a large number of donor and recipient cells allowed for the first time the determination of mean shuttling capacities of individual SR proteins. We could show that all seven SR proteins shuttle in P19 cells; however, they shuttle to different extents, suggesting a differential participation in nuclear export and retention of mRNAs. SR proteins were ...

The large majority of genes encoded by humans and other metazoans contain introns. In general, mRNAs containing introns give rise to a higher level of the encoded protein than do the equivalent intronless, cDNA-derived mRNAs. The mechanisms underlying this difference are complex because splicing can strongly influence not only the efficiency of mRNA 3′ end formation but also mRNA stability and even translation (Ryu and Mertz, 1989; Niwa et al., 1990; Matsumoto et al., 1998). Nevertheless, for most human genes, splicing is not essential for detectable mRNA and protein synthesis. In fact, a recent survey of 15 genes showed that the presence of an excisable intron enhanced gene expression in human cells by an average of 6.3±4.7 fold with a range of from 1.5- to over 20-fold (S. Lu and B. R. Cullen, unpublished).. The first evidence suggesting that splicing also enhances the efficiency of mRNA export came from the demonstration that several intron-containing mRNAs are exported more efficiently ...

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Nuclear mRNA export is a highly complex and regulated process in cells. Cellular transcripts must undergo successful maturation processes, including splicing, 5-, and 3-end processing, which are essential for assembly of an export competent ribonucleoprotein particle. Many viruses replicate in the nucleus of the host cell and require cellular mRNA export factors to efficiently export viral transcripts. However, some viral mRNAs undergo aberrant mRNA processing, thus prompting the viruses to express their own specific mRNA export proteins to facilitate efficient export of viral transcripts and allowing translation in the cytoplasm. This review will focus on the Kaposis sarcoma-associated herpesvirus ORF57 protein, a multifunctional protein involved in all stages of viral mRNA processing and that is essential for virus replication. Using the example of ORF57, we will describe cellular bulk mRNA export pathways and highlight their distinct features, before exploring how the virus has evolved to exploit

Essential messenger RNA (mRNA) export factors execute critical steps to mediate directional transport through nuclear pore complexes (NPCs). At cytoplasmic NPC filaments, the ATPase activity of DEAD-box protein Dbp5 is activated by inositol hexakisphosphate (IP(6))-bound Gle1 to mediate remodeling of mRNA-protein (mRNP) complexes. Whether a single Dbp5 executes multiple remodeling events and how Dbp5 is recycled are unknown. Evidence suggests that Dbp5 binding to Nup159 is required for controlling interactions with Gle1 and the mRNP. Using in vitro reconstitution assays, we found here that Nup159 is specifically required for ADP release from Dbp5. Moreover, Gle1-IP(6) stimulates ATP binding, thus priming Dbp5 for RNA loading. In vivo, a dbp5-R256D/R259D mutant with reduced ADP binding bypasses the need for Nup159 interaction. However, NPC spatial control is important, as a dbp5-R256D/R259D nup42Δ double mutant is temperature-sensitive for mRNA export. Further analysis reveals that remodeling ...

Nuclear export of mRNA is mediated by interactions between soluble factors and nuclear pore complex (NPC) proteins. In Saccharomyces cerevisiae, Nab2 is an essential RNA-binding protein that shuttles between the nucleus and cytoplasm. The mechanism for trafficking of Nab2-bound mRNA through the NPC has not been defined. Gle1 is also required for mRNA export, and Gle1 interactions with NPC proteins, the RNA helicase Dbp5, and Gfd1 have been reported. Here we report that Nab2, Gfd1, and Gle1 associate in a complex. By using immobilized recombinant Gfd1, Nab2 was isolated from total yeast lysate. A similar biochemical assay with immobilized recombinant Nab2 resulted in coisolation of Gfd1 and Gle1. A Nab2-Gfd1 complex was also identified by coimmunoprecipitation from yeast lysates. In vitro binding assays with recombinant proteins revealed a direct association between Nab2 and Gfd1, and two-hybrid assays delineated Gfd1 binding to the N-terminal Nab2 domain. This N-terminal Nab2 domain is distinct ...

In this study, we used multiple functional assays to characterize NXT1, a protein that we identified based on its sequence relatedness to NTF2. The similarities of NXT1 and NTF2 include their amino acid identity (26% within a species), low molecular sizes (NTF2, 127 amino acids; NXT1, 140 amino acids), acidic isoelectric points (NTF2, 5.1; NXT1, 5.0), steady-state nuclear localization (45), interaction with the NPC (6, 31, 36), and direct binding to Ran (31, 34). However, NXT1 and NTF2 also have distinct properties that provide insights into their respective functions. NTF2 binds to Ran-GDP and mediates its import into the nucleus (38, 43,45), thereby functioning as a nuclear import factor. In contrast, NXT1 binds to Ran-GTP. The precise function of this interaction is unknown, but it clearly suggests a role in nuclear export. Indeed, using a permeabilized cell assay (16), we have shown here that NXT1 stimulates nuclear export of PKI. The logical interpretation of this result is that NXT1 ...

Nuclear pore-associated protein; required for biogenesis of the small ribosomal subunit; component of TREX-2 complex (Sac3p-Thp1p-Sus1p-Cdc31p) involved in transcription elongation and mRNA export from the nucleus; involved in post-transcriptional tethering of active genes to the nuclear periphery and to non-nascent mRNP; similar to the human germinal center-associated nuclear protein (GANP) ...

In eukaryotic cells, most mRNAs are exported from the nucleus by the transcription export (TREX) complex, which is loaded onto mRNAs after their splicing and capping. We have studied in mammalian cells the nuclear export of mRNAs that code for secretory proteins, which are targeted to the endoplasmic reticulum membrane by hydrophobic signal sequences. The mRNAs were injected into the nucleus or synthesized from injected or transfected DNA, and their export was followed by fluorescent in situ hybridization. We made the surprising observation that the signal sequence coding region (SSCR) can serve as a nuclear export signal of an mRNA that lacks an intron or functional cap. Even the export of an intron-containing natural mRNA was enhanced by its SSCR. Like conventional export, the SSCR-dependent pathway required the factor TAP, but depletion of the TREX components had only moderate effects. The SSCR export signal appears to be characterized in vertebrates by a low content of adenines, as ...

The THO/TREX complex is the transcription- and export-related complex associated with spliceosomes that preferentially deal with spliced mRNAs as opposed to unspliced mRNAs. Thoc2 plays a role in RNA polymerase II (RNA pol II)-dependent transcription and is required for the stability of DNA repeats [1]. In humans, the TRE complex is comprised of the exon-junction-associated proteins Aly/REF and UAP56 together with the THO proteins THOC1 (hHpr1/p84), Thoc2 (hRlr1), THOC3 (hTex1), THOC5 (fSAP79), THOC6 (fSAP35), and THOC7 (fSAP24). Although much evidence indicates that the function of the TREX complex as an adaptor between the mRNA and components of the export machinery is conserved among eukaryotes, in Drosophila the majority of mRNAs can be exported from the nucleus independently of the THO complex [2]. ...

In previous studies, we established a genetic interaction between the NC2-component Bur6 and mRNA export. More specifically, mutations in BUR6 were observed to be synthetic lethal with dbp5-2, yra1-1 or sub2-85 mutant alleles (Estruch and Cole 2003; F. Estruch, L. Peiró-Chova and C. Cole, unpublished results). To gain more information about the causes of the genetic relationships between BUR6 and genes encoding mRNA export factors, we selected for genes that, upon overexpression, could bypass the synthetic lethality of the bur6-1 and dbp5-2 mutations. This genetic screen identified a truncated version of Rpb2 (Rpb2t) as a multicopy suppressor of both the bur6-1 dbp5-2 and the mot1-301 dbp5-2 double-mutant strain (F. Estruch, L. Peiró-Chova and C. Cole, unpublished results). Interestingly, overexpression of different truncated forms of Rpb2 acted as a suppressor of the growth defect caused by a limiting amount of NC2 or Mot1, like that provided by the expression of the PGAL10-BUR6, PGAL10-YDR1, ...

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NIH3T3 cells showing the localization of nuclear transport factor RanBP1 and F-actin in interphase cells. Cells were fixed in formaldehyde and labele...

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As Jim Kelly predicted, the NXT looks to be a hot holiday item. The trade publication Toy Wishes Magazine, after a review of thousands of holiday toys, has the NXT on its Hot Dozen list for Christmas 2006. Read about ...

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Nitin: I sent you guys at Mindsensors a mail for 14-15 hours ago, have you gotten/read/answered it yet? Thanks. If not, drop me a mail at [email protected] and Ill send you the e-mail back to that address (I sent it to the support e-mail address). Thanks ...

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ASP.NET GridView to Excel conversion.; Author: pramod.hegde; Updated: 15 Apr 2012; Section: Office Development; Chapter: Enterprise Systems; Updated: 15 Apr 2012

繼承對種族主義的批判. 印度種姓制度以血緣世襲的方式區分人的貴賤，達利特人（賤民）最低等被視為不可接觸，至今仍存。另一邊廂，美國上幾個世紀的黑奴制度以膚色區劃奴隸階級，即使後來黑奴解放，深膚色人種仍然受著嚴重的經濟和文化歧視。. 人為地建構身份階層，對特定族群作出有違人性的區分，是鞏固權力和維持優勢地位的一貫做法。但這做法也反向操作，用來挑戰某些價值和社會規範。例如，應用於性傾向，可得出異性戀中心主義：異性戀是一種由人建構出來的階級體制，令社會裡不是異性戀的人受到排拒，剝削了同性戀的人性和尊嚴……藉由建構同性戀和被壓迫的身份，他們聚集了群眾和得到某種道德力量。在建構出假想敵後，同性戀政治份子批判異性戀中心主義的社會，製作仇恨名單（The Export of ...

This file exports the most commonly used modules within HLearn-distributions. Most likely this is the only file you will have to import. ...

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