Kosan Biosciences Incorporated presented preclinical data on its proprietary nuclear export inhibitors (NEI) showing potent in vitro and in vivo activity as wel
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Transport of macromolecules into and out of the nucleus is generally effected by targeting signals that are recognized by specific members of the importin/exportin transport receptor family. The latter mediate passage through the nuclear envelope-embedded nuclear pore complexes (NPCs) by conferring interaction with NPC constituents, as well as with other components of the nuclear transport machinery, including the guanine nucleotide-binding protein Ran. Importantly, nuclear transport is regulated at multiple levels via a diverse range of mechanisms, such as the modulation of the accessibility and affinity of target signal recognition by importins/exportins, with phosphorylation/dephosphorylation as a major mechanism. Alteration of the level of the expression of components of the nuclear transport machinery also appears to be a key determinant of transport efficiency, having central importance in development, differentiation and transformation ...
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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 this study, we have shown that (a) although 14-3-3 proteins are predominantly localized in the cytoplasm, a large number of ligands are localized within the nucleus; (b) endogenous 14-3-3, fully competent to bind ligands, can be trapped in the nucleus by inhibiting Crm1-dependent nuclear export with LMB; (c) the leucine-rich putative NES sequence in 14-3-3, despite its structural homology to known NES sequences (Rittinger et al., 1999) and its ability to function as an NES in isolation when fused to GFP (unpublished data), functions primarily in phosphoprotein binding and not as an NES in the context of the intact 14-3-3 molecule; (d) a mutant 14-3-3, which cannot bind to ligands, homes to the nucleus; (e) the nuclear 14-3-3 ligand FKHRL1 is phosphorylated at its major 14-3-3 binding site within the nucleus before its export into the cytoplasm; and (f) at least for FKHRL1, rapid export from the nucleus to the cytoplasm requires both phosphorylation/14-3-3 binding and NES sequences within the ...
Although there appears to be some discrepancy between these new findings and our previous reports that importins are dispensable for the nuclear import of Smads, these observations can be reconciled (Xu et al., 2002, 2003). Our present and previous studies, based on different approaches, may have revealed different nuclear import mechanisms used by basal and activated Smads to enter the nucleus. There are important differences comparing Smads import with or without TGF-β stimulation. Unphosphorylated Smads are monomers, but phosphorylated Smads are assembled into complexes with Smad4 and are thus much larger in size (Wu et al., 2001; Chacko et al., 2004). Moreover, as phospho-Smads accumulate in the nucleus they have to move across the nuclear pore against an ascending concentration gradient of Smads already in the nucleus, whereas unphosphorylated Smads never reach a higher concentration in the nucleus than in the cytoplasm. Thus, importing phospho-Smad complexes and unphosphorylated Smad ...
The nuclear export of Foxo can be inhibited by LMB (Fig. 11), which binds to and thus removes the availability of CRM1 for nuclear export. In the presence of a fully blocking concentration of LMB, any Foxo that enters the nucleus is unable to leave and becomes trapped in the nucleus. Inhibition of nuclear export via LMB thus provides a powerful tool for measuring the rate of unidirectional nuclear influx and for calculating its rate constant of cytoplasmic efflux. The change in the rate constant for unidirectional efflux out of the cytoplasm due to treatment with phosphorylation modulators demonstrates the importance of cytoplasmic phosphorylation/dephosphorylation of Foxo1 in regulation of its rate of cytoplasmic efflux (Figs. 6, 9, and 10). Furthermore, the increase in the rate of nuclear influx that resulted from staurosporine addition in the presence of LMB (Fig. 9A) indicates that the nuclear import machinery is not saturated at the level of expression of Foxo1-GFP employed under our ...
There are two types of protein transport processes evident during nucleocytoplasmic exchange being nuclear import and export. The majority of proteins are synthesised in the cytoplasm, therefore nuclear import is a dominant form of protein transportation into the nucleus. Moreover, nuclear export is equally crucial in nucleocytoplasmic transport during later parts of protein processing to return products into the cytoplasm such as tRNA, rRNA and mRNA. In addition, some proteins may be required to move across the NE several times to be fully developed into a functional subunit. In comparison to the nucleus, after importing proteins into the rough endoplasmic reticulum (rER), they cannot exit due to the absence of specific signals to initiate transportation back across the plasma membrane to the cytoplasm. Nucleus therefore has a unique means of transportation, having equally important import and export process. Most protein carriers involving NPCs are the members karyopherins family. This ...
In this study, we have reported a means to specifically prevent p42/p44MAPK nuclear translocation without affecting its activation. Different methods can theoretically be used to achieve the blockage of MAPK nuclear translocation. The one we employed here was to create an artificial anchor for MAPK based on two criteria: a specific interaction with MAPK and a cytoplasmic localization. Several proteins could possibly fulfil the criteria to create a cytoplasmic anchor for MAPK. For instance, the activator of MAPK, MKK1, is a cytoplasmic protein that also binds specifically to MAPK (Bardwell et al., 1996; Fukuda et al., 1997) and has therefore been proposed to play the role of an MAPK anchor in vivo (Fukuda et al., 1997). Moreover expression of MKK1 in Xenopus has been shown to impair MAPK nuclear translocation (Fukuda et al., 1997). However, in our fibroblast CCL39 cell line, the ability of MKK1 expression to prevent MAPK nuclear translocation was much weaker than that of inactive MKP‐3. This ...
We are interested in transport processes and in photosynthesis. Within the realm of photosynthesis we are mainly concerned with dynamic processes that accompany the life cycle of the thylakoid network, including its response to different stresses and its formation and dismantling. Regarding nucleo-cytoplasmic transport, we are particularly interested in its selectivity, the behavior of the ensemble of transporting molecules as it relates to the transport of a single molecule and in applications to gene therapy. In both fields of study, we combine different approaches and methodologies including ensemble and single-molecule biophysical methods, biochemical and molecular biology techniques, statistical mechanical modeling and state-of-the-art electron microscopy.. ...
1JN5: Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor.
Principal nameRanBP9 / Importin-9 antibodyAlternative names for RanBP9 / Importin-9 antibodyIMP9, IPO9, IMP9, KIAA1192, Ran binding protein 9,…
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 ...
The cowpox virus-encoded anti-apoptotic protein cytokine response modifier A (CrmA) is a member of the serpin family that specifically inhibits the cellular proteins caspase 1, caspase 8 and granzyme B. In this study, we have used Flag- and yellow fluorescent protein (YFP)-tagged versions of CrmA to investigate the mechanisms that regulate its subcellular localization. We show that CrmA can actively enter and exit the nucleus and we demonstrate the role of the nuclear export receptor CRM1 in this shuttling process. CrmA contains a novel leucine-rich nuclear export signal (NES) that is functionally conserved in the anti-apoptotic cellular serpin PI-9. Besides this leucine-rich export signal, additional sequences mapping to a 103-amino-acid region flanking the NES contribute to the CRM1-dependent nuclear export of CrmA. Although YFP-tagged CrmA is primarily located in the cytoplasm, shifting its localization to be predominantly nuclear by fusion of a heterologous nuclear localization signal did ...
Recent investigations have elucidated several molecular pathways for the nuclear import and export of proteins (Kau and Silver, 2003; Weis, 2003) across transport passageways or nuclear pore complexes (NPCs) (Dreger, 2003). The NPC is a large (125 MDa) multimeric protein structure that perforates the nuclear envelope and channels proteins greater than 60 kDa into or out of the nucleus. The constituents of the NPC have been described in yeast (Rout et al., 2000) and mammalian cells (Cronshaw et al., 2002). Proteins targeted for receptor-mediated transport across the NPC must either contain a nuclear localization signal (NLS) or a nuclear export signal (NES). Protein NLS are typically short clusters of basic amino acids, often preceded by an acidic amino acid or proline residue. However, a NLS may also consist of bipartite clusters of basic amino acids separated by a spacer region of approximately ten amino acids, often flanked by a neutral or acidic amino acid. Previously described NLSs are ...
The nuclear export receptor Crm1 cooperatively binds its HIV Rev-RRE cargo as a dimer using a species-specific interface that supports viral replication by enhancing nuclear export of HIV RNA.
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
It is an interesting phenomenon that a significant number of signaling molecules including p65 NF-κB, IκBα, Smad proteins and many others contain both nuclear localization and nuclear export sequences that counteract each other (Arenzana-Seisdedos et al., 1997; Gama-Carvalho and Carmo-Fonseca, 2001; Harhaj and Sun, 1999; Huang et al., 2000; Johnson et al., 1999; Reguly and Wrana, 2003). Signaling molecules such as transcription factors, which have roles both in the nucleus and in the cytosol, clearly require nuclear import and nuclear export mechanisms. However, more and more proteins without an obvious nuclear function are being found to shuttle between cytosol and nucleus (Gama-Carvalho and Carmo-Fonseca, 2001). Most of these proteins contain both NLS and NES domains, raising the question of how these opposing localization mechanisms are balanced and dynamically regulated. Several possibilities appear significant for regulating the equilibrium between counteracting localization signals. ...
Our results define a bipartite NLS that is integrated within the DNA-recognition region of IRF3. We mapped the NLS of IRF3 to aa 64-130, partially overlapping with the DBD. Basic amino acids KR77/78 and RK86/87 are required for efficient nuclear import of IRF3. Significantly, we demonstrate that the NLS of IRF3 also plays an important role in the DNA-binding activity.. The IRF family contains nine mammalian members (IRF1, IRF2, IRF3, IRF4, IRF5, IRF6, IRF7, IRF8, and IRF9), which are most conserved in their DBD. IRF1 and IRF2, which are closely related to each other, contain a conserved NLS located immediately C-terminal to the DBD, involving aa 120-138 (33). IRF4, IRF8, and IRF9 are highly conserved with each other and use the homologous NLS (aa 66-85) to direct their accumulation in the nucleus (34). Interestingly, IRF5 contains two monopartite consensus NLSs, a N-terminal NLS and a C-terminal NLS (35). Our study, together with previous reports, demonstrated that the NLSs of IRFs are generally ...
TY - JOUR. T1 - Nuclear import and export signals are essential for proper cellular trafficking and function of ZIC3. AU - Bedard, James E J. AU - Purnell, Jennifer D.. AU - Ware, Stephanie. PY - 2007/1/15. Y1 - 2007/1/15. N2 - Missense, frameshift and nonsense mutations in the zinc finger transcription factor ZIC3 cause heterotaxy as well as isolated congenital heart disease. Previously, we developed transactivation and subcellular localization assays to test the function of ZIC3 point mutations. Aberrant cytoplasmic localization suggested that the pathogenesis of ZIC3 mutations results, at least in part, from failure of appropriate cellular trafficking. To further investigate this hypothesis, the nucleocytoplasmic shuttling properties of ZIC3 have been examined. Subcellular localization assays designed to span the entire open-reading frame of wild-type and mutant ZIC3 proteins identified the presence of nucleocytoplasmic transport signals. ZIC3 domain mapping indicates that a relatively large ...
Combining with a nuclear export signal (NES) to mediate transport of the NES-containing protein through the nuclear pore to the cytoplasm.
In eukaryotic cells, pre-mRNAs undergo extensive processing in the nucleus prior to export. Processing is subject to a quality-control mechanism that retains improperly processed transcripts at or near sites of transcription. A poly(A) tail added by the normal 3′-processing machinery is necessary but not sufficient for export. Retention depends on the exosome. In this study, we identify the poly(A)-binding protein, Pab1, and the poly(A) nuclease, PAN, as important factors that couple 3′ processing to export. Pab1 contains a nonessential leucine-rich nuclear export signal and shuttles between the nucleus and the cytoplasm. It can exit the nucleus either as cargo of exportin 1 or bound to mRNA. Pab1 is essential but several bypass suppressors have been identified. Deletion of PAB1 from these bypass suppressor strains results in exosome-dependent retention at sites of transcription. Retention is also seen in cells lacking PAN, which Pab1 is thought to recruit and which may be responsible for ...
Activation of mitogen-activated protein kinases (MAPKs) and MAPK kinases (MEKs) leads to their translocation from the cytoplasm to the nucleus. Once the transduced signal has abated, the kinases shuttle back to the cytoplasm. However, MAPKs do not appear to have nuclear export signal (NES) motifs coded within their amino acid sequences. Adachi et al. resolve this enigma by showing that MAPK binds to MEK in the nucleus, and both utilize the NES motif found on MEK to relocalize to the cytoplasm. The nuclear export of MAPK was blocked by the specific NES inhibitor leptomycin B. Also, when injected into the nucleus, MAPK relocalized to the cytoplasm with coinjected MEK, but not with a MEK mutant in which the NES was disrupted. Finally, nuclear injection of a protein fragment that includes the MAPK-binding site on MEK decreased MAPK export. Thus, transport of MAPK from the nucleus to the cytoplasm appears to require association of MAPK with MEK.. Adachi, M., Fukuda, M., and Nishida, E. (2000) Nuclear ...
Pakistan Exports Stats", NationMaster. Retrieved from http://www.nationmaster.com/country-info/profiles/Pakistan/Economy/Exports. "Pakistan Exports Stats, NationMaster." 2009-2013. ,http://www.nationmaster.com/country-info/profiles/Pakistan/Economy/Exports,.. Pakistan Exports Stats, NationMaster, ,http://www.nationmaster.com/country-info/profiles/Pakistan/Economy/Exports, [assessed 2009-2013]. "Pakistan Exports Stats", NationMaster [Internet]. 2009-2013. Avaliable from: ,http://www.nationmaster.com/country-info/profiles/Pakistan/Economy/Exports,.. "Pakistan Exports Stats", NationMaster. Avaliable at: nationmaster.com. Assessed 2009-2013.. "Pakistan Exports Stats, NationMaster," http://www.nationmaster.com/country-info/profiles/Pakistan/Economy/Exports (assessed 2009-2013). "Pakistan Exports Stats", NationMaster, http://www.nationmaster.com/country-info/profiles/Pakistan/Economy/Exports (last visited 2009-2013). "Pakistan Exports Stats", NationMaster, ...
Required for pre-mRNA splicing. Can also modulate alternative splicing in vitro. Represses the splicing of MAPT/Tau exon 10. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-sequence specific.
View Notes - BIO 320 Lecture10slides_2009 from BIO 50160 at University of Texas. BIO320 - Lecture 10 02/19/2009 NUCLEAR TRANSPORT Optional Reading on Blackboard Science (2006) 314: 766-767 The
Analysis of TNF-α-induced p65 nuclear entry, phosphorylation (Ser 536), promoter activity and IκBα degradation during DMF treatment. a Nuclear p65 translocat
According to Statistics Netherlands, the volume of exports of goods was 6.4 percent up in September 2014 from September 2013. In the preceding month, exports grew by more than 1 percent. Higher exports of Dutch products and higher re-exports contributed to the growth.
The nucleo-cytoplasmic localization of KLF6 alongside one another with the presence of a purposeful NLS supported the idea that KLF6 could also harbor a
Types of Export   The Service offers data export of three types: as general statistics link Download statistics in  section
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View and download the latest detailed of HS code 32050000 Export data with product, price, date, quantity, major Indian export ports, exporting countries.
Akoumianaki T, Kardassis D, Polioudaki H, Georgatos SD, Theodoropoulos PA. (2009) Nucleocytoplasmic shuttling of soluble tubulin in mammalian cells. J...
Hyperornithinemia-hyperammonemia-homocitrullinuria 증후군을 유발하는 SLC25A15 유전자의 새로운 변이 - HHH syndrome;Urea cycle disorders;SLC25A15;Genetics
Recent studies have established that glucose deprivation causes inhibition of the nuclear tRNA export process in S. cerevisiae (30, 46). While the mechanism responsible for regulating nuclear tRNA export in response to the glucose level is not understood, findings from this study strongly suggest that it is most likely due to the function of the nuclear tRNA export receptors and the intranuclear tRNA chaperone Utp8p being controlled by glucose availability (Fig. 4). How the glucose level influences Utp8p function in nuclear tRNA export is not known, but evidence obtained suggests that the ability of the tRNA export receptors to function in nuclear tRNA export in response to glucose availability is most likely related to regulation of nuclear reimport of the tRNA export receptors after a round of tRNA export to the cytoplasm (Fig. 3). This conclusion is in accordance with previous studies showing cytoplasmic accumulation of several nuclear export receptors, including the nuclear tRNA export ...
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
The RS1 protein (gene RSC1A1) participates in regulation of Na+-D-glucose cotransporter SGLT1 and some other solute carriers. In subconfluent LLC-PK1 cells, RS1 inhibits release of SGLT1 from the trans-Golgi network and transcription of SGLT1. In subconfluent cells, RS1 is localized in the nucleus and the cytoplasm whereas confluent cells contain predominantly cytoplasmic RS1. In the present study, the mechanism and regulation of confluence-dependent nuclear location of RS1 was investigated. Confluence dependent nuclear location of RS1 was shown to be regulated by the cell cycle. A nuclear shuttling signal (NS) in pRS1 was identified that ensures confluence-dependent distribution of pRS1 and comprises nuclear localization signal (NLS) and nuclear export signal (NES). The NLS and NES of RS1 mediate translocation into and out of the nucleus via importin ß1 and CRM1, respectively, and the nuclear/cytoplasmic distribution of the RS1 protein is determined by the nuclear export activity. The adjacent ...
We have characterized the nuclear localization signal (NLS) of XRCC1 structurally using X-ray crystallography and functionally using fluorescence imaging. Crystallography and binding studies confirm the bipartite nature of the XRCC1 NLS interaction with Importin α (Impα) in which the major and minor binding motifs are separated by ,20 residues, and resolve previous inconsistent determinations. Binding studies of peptides corresponding to the bipartite NLS, as well as its major and minor binding motifs, to both wild-type and mutated forms of Impα reveal pronounced cooperative binding behavior that is generated by the proximity effect of the tethered major and minor motifs of the NLS. The cooperativity stems from the increased local concentration of the second motif near its cognate binding site that is a consequence of the stepwise binding behavior of the bipartite NLS. We predict that the stepwise dissociation of the NLS from Impα facilitates unloading by providing a partially complexed ...
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 factor B (NF-B) represents a family group of dimeric DNA binding proteins, the pleotropic type of which really is a heterodimer made up of RelA and p50 subunits. of heterologous protein. Furthermore, the cytoplasmic distribution of RelA can be delicate to a nuclear export inhibitor, leptomycin B, recommending that RelA Bortezomib cost goes through constant nuclear export. Oddly enough, manifestation of p50 prevents the cytoplasmic manifestation of RelA, resulting in the nuclear build up of both RelA and p50. Collectively, these results claim that the nuclear and cytoplasmic shuttling of RelA can be controlled by both an intrinsic NES-like series as well as the p50 subunit of NF-B. Nuclear element B (NF-B) signifies a family group of eukaryotic transcription elements taking part in the rules of Bortezomib cost various mobile genes mixed up in immediate early procedures of immune system, acute-phase, and inflammatory reactions aswell as Bortezomib cost genes involved with cell success (for ...
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 ...
Efficient Nuclear Delivery of Antisense Oligonucleotides or siRNA In Vitro and In Vivo by Nano-Transforming Polymersomes - diagram, schematic, and image 02 ...
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 …
Protein crystallization is an attractive method for protein processing and formulation. Anti-idiotype RNAs that mimic the leucine-rich nuclear export signal and specifically bind to CRM1/exportin 1. A questionnaire eliciting responses on characteristics, post-exposure practices, and impacts was sent to 2500 operating ...
Azar WJ, Zivkovic S, Werther GA, Russo VC. IGFBP-2 nuclear translocation is mediated by a functional NLS sequence and is essential for its pro-tumorigenic actions in cancer cells. Oncogene (2013) PubMed ...
Tertiary folding of the Rev-response element (RRE) in HIV RNA ensures the rapid formation of the Rev-RRE viral ribonucleoprotein particle via a two-step process.
The nuclear translocation of ERKs is normally regulated by the phosphorylation status of MEK1 (Whitmarsh and Davis, 1999). MEK1 binds to ERKs and prevents nuclear translocation of ERKs by its nucleus export signal. Phosphorylation of MEK1 leads to the activation of ERKs and the dissociation of MEK1-ERK complexes, which results in the subsequent nuclear translocation of activated ERKs. In several Gq-coupled GPCR systems, the G protein-dependent pathway activates ERKs through PKC, and the activated ERKs translocate into the nucleus, whereas the β-arrestin functions as a scaffold for both MEK1 and ERKs, thereby preventing the nuclear translocation of β-arrestin-activated ERKs (Tohgo et al., 2002; Shenoy and Lefkowitz, 2005). In addition, the prevention of the nuclear translocation of β-arrestin-activated ERKs is related to the interaction between receptor and β-arrestin. With the reduction in receptor-β-arrestin interaction allowing the recycling of the internalized receptor, a certain amount ...
Export Data And Price Of Protein , www.eximpulse.com Eximpulse Services is the place where you can find the recent and updated Trade intelligence report of Protein Export Data. Whole information is based on updated Export shipment data of Indian Customs. All the compilation is done on the basis of All India ports data and has been done on daily basis. This helps you to get all India Protein Export data. You can find previous two days Protein Export data on Eximpulse Services. Protein Export data can be useful in different kind of analysis such as: Export price, Quantity, market scenarios, Price trends, Duty optimization and many more. Some Sample Shipment records for Protein Export Data of India are mentioned above. Further for Free sample and pricing of detailed reports contact on [email protected] Data post 2012 as per Notification No.18/2012 - Customs(N.T.) and does not have names of Indian companies and Foreign Companies.. ...