EIF3F Data Analysis

HGNC Gene Name
eukaryotic translation initiation factor 3 subunit F
HGNC Gene Symbol
EIF3F
Identifiers
hgnc:3275 NCBIGene:8665 uniprot:O00303
Orthologs
mgi:1913335 rgd:1306112
INDRA Statements
deubiquitinations all statements
Pathway Commons
Search for EIF3F
Number of Papers
74 retrieved on 2022-05-22

DepMap Analysis

The Dependency Map (DepMap) is a genome-wide pooled CRISPR-Cas9 knockout proliferation screen conducted in more than 700 cancer cell lines spanning many different tumor lineages. Each cell line in the DepMap contains a unique barcode, and each gene knockout is assigned a “dependency score” on a per cell-line basis which quantifies the rate of CRISPR-Cas9 guide drop. It has been found that proteins with similar DepMap scores across cell lines, a phenomenon known as co-dependent genes, have closely related biological functions. This can include activity in the same or parallel pathways or membership in the same protein complex or the same pathway.

We identified the strongest seven co-dependent genes (“Symbol”) for DUBs and ran GO enrichment analysis. We used Biogrid, IntAct, and Pathway Commons PPIDs, and the NURSA protein-protein interaction databases (PPIDs) to determine whether co-dependent genes interact with one another. The “Evidence” column contains the PPIDs in which the interaction appears as well as whether there is support for the association by an INDRA statement. As another approach to identify potential interactors, we looked at proteomics data from the Broad Institute's Cancer Cell Line Encyclopedia (CCLE) for proteins whose expression across ~375 cell lines strongly correlated with the abundance of each DUB; it has previously been observed that proteins in the same complex are frequently significantly co-expressed. The correlations and associated p-values in the CCLE proteomics dataset are provided. And, we determined whether co-dependent genes yield similar transcriptomic signatures in the Broad Institute's Connectivity Map (CMap). A CMap score greater than 90 is considered significantly similar.

DepMap Correlations

Symbol Name DepMap Correlation Evidence CCLE Correlation CCLE Z-score CCLE p-value (adj) CCLE Significant CMAP Score CMAP Type
RPLP2 ribosomal protein lateral stalk subunit P2 0.396 Reactome (7) 0.43 2.27 1.47e-16
RPS13 ribosomal protein S13 0.388 Reactome (11) -0.03 -0.24 7.02e-01
FAU FAU ubiquitin like and ribosomal protein S30 fusion 0.385 Reactome (11) 0.14 0.69 1.82e-02
EIF3H eukaryotic translation initiation factor 3 subunit H 0.369 BioGRID IntAct Pathway Commons INDRA (9) Reactome (11) 0.29 1.49 1.72e-07
EIF3M eukaryotic translation initiation factor 3 subunit M 0.367 BioGRID IntAct INDRA (1) Reactome (11) 0.25 1.28 7.36e-06
EIF3G eukaryotic translation initiation factor 3 subunit G 0.329 BioGRID IntAct Pathway Commons INDRA (4) Reactome (11) 0.61 3.25 1.98e-36
RPS3A ribosomal protein S3A 0.312 Reactome (11) -0.01 -0.16 8.61e-01

Dependency GO Term Enrichment

Gene set enrichment analysis was done on the genes correlated with EIF3Fusing the terms from Gene Ontology and gene sets derived from the Gene Ontology Annotations database via MSigDB.

Using the biological processes and other Gene Ontology terms from well characterized DUBs as a positive control, several gene set enrichment analyses were considered. Threshold-less methods like GSEA had relatively poor results. Over-representation analysis with a threshold of of the top 7 highest absolute value Dependency Map correlations yielded the best results and is reported below.

GO Identifier GO Name GO Type p-value p-value (adj.) q-value
GO:0006413 translational initiation Biological Process 6.15e-10 2.77e-08 1.94e-09
GO:0001732 formation of cytoplasmic translation initiation complex Biological Process 6.39e-09 2.87e-07 7.76e-09
GO:0033290 eukaryotic 48S preinitiation complex Cellular Component 7.98e-09 3.59e-07 7.76e-09
GO:0005852 eukaryotic translation initiation factor 3 complex Cellular Component 9.82e-09 4.42e-07 7.76e-09
GO:0070993 translation preinitiation complex Cellular Component 1.43e-08 6.44e-07 9.04e-09
GO:0002183 cytoplasmic translational initiation Biological Process 7.87e-08 3.54e-06 4.14e-08
GO:0003743 translation initiation factor activity Molecular Function 3.64e-07 1.64e-05 1.64e-07
GO:0071541 eukaryotic translation initiation factor 3 complex, eIF3m Cellular Component 1.75e-06 7.87e-05 6.25e-07
GO:0008135 translation factor activity, RNA binding Molecular Function 1.78e-06 8.01e-05 6.25e-07
GO:0002181 cytoplasmic translation Biological Process 2.41e-06 1.08e-04 7.60e-07
GO:0090079 translation regulator activity, nucleic acid binding Molecular Function 3.74e-06 1.68e-04 1.07e-06
GO:0045182 translation regulator activity Molecular Function 7.74e-06 3.48e-04 2.04e-06
GO:0019080 viral gene expression Biological Process 1.96e-05 8.84e-04 4.77e-06
GO:0005840 ribosome Cellular Component 4.66e-05 2.10e-03 1.05e-05
GO:0071826 ribonucleoprotein complex subunit organization Biological Process 6.62e-05 2.98e-03 1.39e-05
GO:0022613 ribonucleoprotein complex biogenesis Biological Process 3.15e-04 1.42e-02 6.22e-05
GO:0006613 cotranslational protein targeting to membrane Biological Process 4.40e-04 1.98e-02 8.17e-05
GO:0022626 cytosolic ribosome Cellular Component 5.19e-04 2.34e-02 9.11e-05
GO:0072599 establishment of protein localization to endoplasmic reticulum Biological Process 5.56e-04 2.50e-02 9.24e-05
GO:0000184 nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Biological Process 5.85e-04 2.63e-02 9.24e-05
GO:0070972 protein localization to endoplasmic reticulum Biological Process 8.18e-04 3.68e-02 1.23e-04

Literature Mining

INDRA was used to automatically assemble known mechanisms related to EIF3F from literature and knowledge bases. The first section shows only DUB activity and the second shows all other results.

Deubiquitinase Activity

psp cbn pc bel_lc signor biogrid lincs_drug tas hprd trrust ctd vhn pe drugbank omnipath conib crog dgi | rlimsp isi tees geneways eidos trips medscan sparser reach
EIF3F deubiquitinates NOTCH1 on K1759. 1 / 1
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signor
The activated form of notch needs to be deubiquitinated before being processed by the gamma-secretase activity and entering the nucleus, where it fulfills its transcriptional function. The enzyme accounting for this deubiquitinase activity is eif3f, known so far as a translation initiation factor.
EIF3F deubiquitinates Notch. 1 / 1
1 |

signor
The activated form of notch needs to be deubiquitinated before being processed by the gamma-secretase activity and entering the nucleus, where it fulfills its transcriptional function. The enzyme accounting for this deubiquitinase activity is eif3f, known so far as a translation initiation factor.

Other Statements

psp cbn pc bel_lc signor biogrid lincs_drug tas hprd trrust ctd vhn pe drugbank omnipath conib crog dgi | rlimsp isi tees geneways eidos trips medscan sparser reach
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Interaction of Mss4 with eIF3F prevents the eIF3F mediated apoptosis.

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To investigate whether the phosphor-mimic eIF3f SETE mutant promotes apoptosis, we transfected eIF3f SETE alone or with CDK11 p46 or CDK11 p46M into A375 cells.

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Deregulation of eIF3f expression negatively affects cell viability and induces apoptosis.

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The data also suggest that eIF3f inhibits cancer cell growth and induces apoptosis by blocking the function of sCLU, thereby suppressing the inactivation of p53 and Bax as well as the Akt and ERK pathways.

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The overexpression of eIF3f retarded cancer cell growth and induced apoptosis 51.

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We next defined the relationship among p53, p21, and Bax during eIF3f induced apoptosis.

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Increased eIF3f expression contributes to apoptosis via hnRNP K sequestration and increased rRNA degradation.

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We also showed that restored eIF3f expression in tumor cells causes ribosomal RNA (rRNA) degradation, inhibits translation and cell proliferation, and induces apoptosis XREF_BIBR.

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However, the molecular mechanism by which the increased expression of eIF3f induces apoptosis is poorly understood.

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It has been shown that in melanoma and pancreatic cancer cells eIF3f can induce apoptosis in caspase 3/7 and in a Bcl-2, Bax, or Bcl-XL-independent manner.
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In our current study, we tested the hypothesis that eIF3f coordinates with hnRNP K to regulate rRNA degradation and that decreased eIF3f expression contributes to tumorigenesis by deregulating translation and apoptosis.

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Likewise, eIF3f knockdown in normal human pancreatic epithelial cells has shown an increase in cell proliferation and increased resistance to apoptosis [109].

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These results show that eIF3f silencing affects cell viability and induces apoptosis in A549 cells.

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Loss of eIF3f in pancreatic cancer may contribute to tumor cells ' evading apoptosis via upregulation of protein synthesis.

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Increased expression of eIF3f reduces cellular growth by inducing apoptosis in melanoma and pancreatic cancer cells [XREF_BIBR - XREF_BIBR].

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EIF3f knockdown in A549 cells was shown to inhibit cell proliferation and induce apoptosis.

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The same group found that eIF3f overexpression in cancer cells negatively regulates cell growth by affecting the translation efficiency and the activation of apoptosis (Shi et al., 2006).

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To examine whether eIF3f SATA mutant attenuates apoptosis in CDK11 p46 overexpressing cells, we co-transfected CDK11 p46 with wild type or mutant eIF3f followed by apoptosis assay.

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As predicted, eIF3f SATA mutant did attenuate apoptosis in CDK11 p46 overexpressing cells compared to wild type eIF3f (XREF_FIG).

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Knockdown of endogenous eIF3f by siRNA attenuates apoptosis in melanoma cells after treatment with staurosporine as apoptotic agent [XREF_BIBR].
EIF3F affects translation
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EIF3F inhibits translation.
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A subunit of the eukaryotic initiation factor 3, eIF3f, has also been discovered to modulate host translation inhibitory effects through physical interaction with coronavirus spike protein [132].

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After anti-Fas or staurosporine treatments in human melanoma cells, the caspase processed C-terminal fragment CDK11p46 strongly interacts with eIF3f via its Mov34 domain [XREF_BIBR] and, due to its kinase activity, phosphorylates eIF3f inducing the inhibition of translation.

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Ectopic expression of eIF3f inhibits translation and overall cellular protein synthesis.

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Whether eIF3f inhibits cap-dependent or cap-independent translation is not known.

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We also showed that restored eIF3f expression in tumor cells causes ribosomal RNA (rRNA) degradation, inhibits translation and cell proliferation, and induces apoptosis XREF_BIBR.

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Quantification of luciferase mRNA by qRT-PCR demonstrated that translation of luciferase gene was not influenced by overexpression of Mss4 (XREF_FIG), indicating that Mss4 is indeed able to abolish the eIF3f mediated inhibition of translation.

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XREF_BIBR Overexpression of eIF3f inhibits cell proliferation, induces apoptosis, and inhibits translation and protein expression.

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In our study, silencing of eIF3f increased both cap dependent and IRES dependent translation (up to 2.5-fold increase), indicating a suppressive role of eIF3f on both translation initiation mechanisms (XREF_FIG).

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We also showed that silencing of eIF3f promotes both cap dependent and cap-independent and internal ribosome entry site (IRES)-dependent translation and cytokinesis defects.

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EIF3f inhibits both cap-dependent and IRES-dependent translation.
EIF3F activates translation.
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Thus, we set out to determine whether eIF3f contribute in vivo to cap dependent translation.

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As shown in XREF_FIG, eIF3f wt overexpression led to increase in translation rates in muscle cells.

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Hence any reports describing pathological phenotypes stemming from altered expression of these three subunits should be at least partially regarded as a failure of the dramatically compromised eIF3 complex to ensure productive general translation initiation in sick cells; like underexpression of eIF3f in gastric, melanoma and pancreatic cancers supposedly deregulating apoptosis, eIF3f ubiquitination and proteosomal degradation during muscle atrophy, overexpression of eIF3m in human cancer cell lines and colon cancer patient tissues, as well as overexpression of eIF3c in testicular seminoma cells.

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On the other hand, genetic activation of eIF3f promoted structural muscle protein synthesis and led to muscle hypertrophy (Csibi et al., 2008).

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Moreover, overexpression of eIF3f K5-10R mutant induces a significant increase in protein synthesis and hypertrophy compared to the wild type protein under normal condition (Csibi et al., 2010, Csibi et al., 2009).

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For instance, eIF3f is an important housekeeping gene and is necessary for initiation of translation.

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Moreover, overexpression of eIF3f K5-10R mutant induces a significant increase in protein synthesis and hypertrophy compared to the wild type protein under normal condition (Csibi et al., 2010 ).

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EIF3f Activates the Cap Dependent Translation in Muscle Cells.
Mutated EIF3F activates translation. 1 / 1
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Interestingly, overexpression of the mutant eIF3f K 5-10 R increased the cap dependent translation in the same order as observed with insulin.

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Recent reports on the biological function of eIF3f in translation and apoptosis in tumor cells demonstrated that eIF3f is down regulated in most human tumors and that overexpression of eIF3f inhibited cell proliferation suggesting a function associated with differentiation XREF_BIBR.

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EIF3f is down-regulated in many human tumours, and over-expression of eIF3f inhibits cell proliferation and induces apoptosis in tumour cells (Shi etal., 2006; 2008a, 2008b).

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Overexpression of eIF3f inhibits cell proliferation and induces apoptosis in melanoma and pancreatic cancer cells.

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Haplotype analyses support a single mutational event on a founder haplotype, while the nascence of the missense variant cannot be determined to a more localized region.As only the identical missense variant in EIF3F has been functionally characterized and shown to result in reduced protein amount/ stability, decreased proliferation rate and reduced translational rate, it remains speculative whether other missense variants might have comparable effects.

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We also showed that restored eIF3f expression in tumor cells causes ribosomal RNA (rRNA) degradation, inhibits translation and cell proliferation, and induces apoptosis XREF_BIBR.

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Conversely, eIF3f expression is suppressed in several cancers, including breast cancer. xref Overexpression of eIF3f inhibits cell proliferation, induces apoptosis, and inhibits translation and protein expression. xref eIF3e binds both to eIF4G and to 40S, thus generating an interaction between the eIF4F complex and the ribosome. xref Several studies support a tumor suppressor role for eIF3e.

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Moreover , overproduction of eIF3F inhibits cap-dependent translation [ 32 ] ( also see Fig. 5 ) , and knockdown of eIF3F increases cell proliferation [ 46 ] .

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Recent reports on the biological function of eIF3f in translation and apoptosis in tumor cells demonstrated that eIF3f is down regulated in most human tumors and that overexpression of eIF3f inhibited cell proliferation suggesting a function associated with differentiation xref .

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Previous studies have demonstrated that overexpression of eIF3f inhibits cell proliferation and induces apoptosis in melanoma and pancreatic cancer cells, suggesting that downregulation of eIF3f is involved in tumorigenesis for many types of cancer [XREF_BIBR, XREF_BIBR, XREF_BIBR].

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XREF_BIBR Overexpression of eIF3f inhibits cell proliferation, induces apoptosis, and inhibits translation and protein expression.

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EIF3f knockdown in A549 cells was shown to inhibit cell proliferation and induce apoptosis.

eidos
These results suggest that eIF3F modulates cell proliferation by repressing translation .

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We confirmed that the loss of eIF3f reduced the proliferation of PCa cells, both in vitro and in vivo.

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These results indicated that eIF3f knockdown caused inhibition of PCa cell proliferation at least partially through the suppression of Akt phosphorylation.

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The proliferation rates of shRNA lentivirus infected PCa cells indicated that eIF3f knockdown markedly decreased the proliferation of PCa cells (XREF_FIG).

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Furthermore, we found that ectopic expression of sheIF3f # 1 resistant wild-type eIF3f rescued the proliferation rate of eIF3f knockdown cells (XREF_FIG).
EIF3F affects cell growth
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EIF3F inhibits cell growth.
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Moreover, increased eIF3f inhibits translation and cell growth and induces apoptosis in melanoma and pancreatic cancer cells [XREF_BIBR].

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The data also suggest that eIF3f inhibits cancer cell growth and induces apoptosis by blocking the function of sCLU, thereby suppressing the inactivation of p53 and Bax as well as the Akt and ERK pathways.

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The same group found that eIF3f overexpression in cancer cells negatively regulates cell growth by affecting the translation efficiency and the activation of apoptosis.

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Therefore, eIF3f inhibits cancer cell growth and induces apoptosis by inhibiting sCLU function.

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The overexpression of eIF3f inhibits cancer cell growth and induces apoptosis.

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The same group found that eIF3f overexpression in cancer cells negatively regulates cell growth by affecting the translation efficiency and the activation of apoptosis (Shi et al., 2006).

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In addition, eIF3f reduces cell growth and increases apoptosis significantly in HeLa and BxPc-3 cells.

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XREF_BIBR, XREF_BIBR, XREF_BIBR Advances in the understanding of the molecular mechanism behind cellular carcinogenesis have shown that ectopic expression of eIF3f by transient gene transfection inhibits translation, cellular growth and proliferation and induces apoptosis.

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Increased expression of eIF3f reduces cellular growth by inducing apoptosis in melanoma and pancreatic cancer cells [XREF_BIBR - XREF_BIBR].

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Endogenous eIF3f silencing by antisense RNA or siRNA inhibits cell growth and induces apoptosis in A549 cancer cells.
EIF3F activates cell growth.
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Modified EIF3F activates cell growth. 2 / 2
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Exogenous expression of shRNA resistant eIF3f in eIF3f knockdown cells restored Akt phosphorylation levels and cell growth.

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Furthermore, ectopic expression of shRNA resistant eIF3f in eIF3f knockdown cells restored Akt phosphorylation levels and cell growth.
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These results confirmed that the inhibition of eIF3f significantly blocked PCa cell growth in vivo.

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Endogenous eIF3f silencing by antisense RNA or siRNA inhibits cell growth and induces apoptosis in A549 cancer cells.
FBXO32 affects EIF3F
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FBXO32 inhibits EIF3F.
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Genetic repression of eIF3f in differentiated skeletal muscle is sufficient to induce atrophy XREF_BIBR and degradation of eIF3f by MAFbx suppresses S6K1 activation by mTOR.

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The silencing of MAFbx expression by small hairpin RNA interference prevents eIF3f degradation in myotubes undergoing atrophy [XREF_BIBR].

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In addition, recent studies indicate that under atrophic conditions, atrogin-1 can directly regulate mTORC1 signalling and protein synthesis via the ubiquitination and subsequent degradation of eIF3f.

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Furthermore, berberine, an inhibitor of mitochondrial respiration, induces atrophy through MAFbx/atrogin-1-mediated degradation of eIF3f in a mice model of type 2 diabetes (Wang et al., 2010).

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Proteasomal degradation of eIF3f mediated by the overexpressed MAFbx/atrogin-1 under starvation and diseases is leading to decreased protein synthesis and muscle wasting.

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Evidences indicate that increase of MAFbx in response to food deprivation causes eIF3f loss, leading to marked decrease on phosphorylation of p70 S6K, without alterations in mTOR activity, indicating the association of mTOR downstream targets [XREF_BIBR].

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Furthermore, berberine, an inhibitor of mitochondrial respiration, induces atrophy through MAFbx and atrogin-1-mediated degradation of eIF3f in a mice model of type 2 diabetes.

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Our data are consistent with a model whereby alcohol increases proteolysis via FOXO independent increase in atrogin-1, which degrades eIF3f and therefore impairs formation of a functional preinitiation complex and protein synthesis.

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Degradation of eIF3f by MAFbx Suppresses S6K1 Activation by mTOR.

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In addition, expression of a protein Fbxo32, which degrades MyoD and eIF3-f in skeletal muscle, was also increased in muscle of CTG550 mice.
FBXO32 activates EIF3F.
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FBXO32 activates EIF3F. 7 / 7
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MAFbx has been shown to target and degrade MyoD, myogenin, and Eif3f (Csibi et al., 2009; Jogo et al., 2009; Lagirand-Cantaloube et al., 2008; Tintignac et al., 2005), and degradation of any of these [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]

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Of note, a subset of microRNAs (miRNAs) in the delta like homolog 1 and the type III iodothyronine deiodinase (Dlk1-Dio3) cluster showed an anti-atrophic effect, probably by limiting the degradation of eIF3f by MAFbx and atrogin -1 [XREF_BIBR].
| PMC

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MAFbx has been shown to target and degrade MyoD, myogenin, and Eif3f, and degradation of any of these proteins reduces myotube diameters.

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Ectopic expression of MAFbx in myotubes induces atrophy and degradation of eIF3-f.

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Muscles undergoing atrophy accumulates the inactive form of S6K1 suggesting that degradation of eIF3f mediated by MAFbx participates to S6K1 inactivation during atrophy and raises the question whether MAFbx interacts with free eIF3f molecules or bound to hypophosphorylated S6K1.

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It was found that the E3 ubiquitin ligase MAFbx and atrogin -1 targets the Mov34 motif of eIF3f during atrophy for polyubiquitination and subsequent degradation by the proteasome [XREF_BIBR, XREF_BIBR, XREF_BIBR].
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Atrogin-1 also targets myogenic differentiastion1 (MyoD) and eukaryotic initiation factor 3 subunit 5 (eIF3-f), which play key roles in the control of protein synthesis XREF_BIBR.
FBXO32 increases the amount of EIF3F.
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FBXO32 increases the amount of EIF3F. 2 / 2
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Importantly, the knockdown of MAFbx/atrogin-1 attenuated these berberine-induced effects on skeletal muscle, particularly on alterations in eIF3f expression and mTORC1 activity (Wang et al., 2010).

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Importantly, knockdown of atrogin-1 prevented the berberine induced decrease in eIF3f levels, protein synthesis and atrophy [XREF_BIBR].
EIF3F affects TP53
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EIF3F activates TP53.
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EIF3F activates TP53. 4 / 8
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qRT-PCR revealed that eIF3f did not stimulate the upregulation of p53 mRNA, suggesting that eIF3f does not inhibit p53 levels.

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EIF3f increases the stability of p53.

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EIF3f overexpression activates p53 and Bax and inhibits Akt and ERK signaling.

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These results suggest that eIF3f promotes the tumor suppressor function of p53 by increasing the stability of p53 protein.
EIF3F increases the amount of TP53.
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EIF3F increases the amount of TP53. 2 / 3
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A previous result revealed that eIF3f increases p53 protein levels.

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As shown in Figure XREF_FIG, eIF3f transfection in HeLa cells upregulated the expression of the apoptotic proteins p53, p21, and Bax.
EIF3F decreases the amount of TP53.
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EIF3F decreases the amount of TP53. 2 / 2
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Therefore, we assessed how eIF3f inhibits p53 expression using qRT-PCR and cycloheximide (CHX) assays.

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qRT-PCR revealed that eIF3f did not stimulate the upregulation of p53 mRNA, suggesting that eIF3f does not inhibit p53 levels.
Modified EIF3F decreases the amount of TP53. 1 / 1
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Overexpression of eIF3f was recently shown to suppress Akt and ERK signaling, increase p53 protein levels and inhibit clusterin protein expression, which promotes cancer cell proliferation and reduces chemosensitivity [XREF_BIBR].
EIF3F affects CLU
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EIF3F inhibits CLU.
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EIF3F inhibits CLU. 4 / 7
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To assess whether the overexpression of eIF3f inhibits the function of CLU, we next measured the expression of several proteins that induce apoptosis.

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Correction : eIF3f reduces tumor growth by directly interrupting clusterin with anti-apoptotic property in cancer cells.

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EIF3f reduces tumor growth by directly interrupting clusterin with anti-apoptotic property in cancer cells.

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To assess how eIF3f inhibits CLU activity, we generated several deletion constructs and analyzed the specific sites responsible for the binding between eIF3f and CLU.
EIF3F decreases the amount of CLU.
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Modified EIF3F decreases the amount of CLU. 2 / 2
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Consequently, the overexpression of eIF3f suppressed Akt and ERK signaling and subsequently depleted CLU expression.

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Overexpression of eIF3f was recently shown to suppress Akt and ERK signaling, increase p53 protein levels and inhibit clusterin protein expression, which promotes cancer cell proliferation and reduces chemosensitivity [XREF_BIBR].
EIF3F decreases the amount of CLU. 2 / 2
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The previous figures show that eIF3f inhibited CLU expression and induced apoptotic signal.

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EIF3f transfection was observed to significantly decrease the psCLU and alpha/beta CLU expression and inhibit Akt and ERK phosphorylation.
EIF3F increases the amount of CLU.
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EIF3F increases the amount of CLU. 1 / 1
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Knockdown of eIF3f in the HEK293a cells increased the CLU expression at 72h post transfection.
Modified EIF3F increases the amount of CLU. 1 / 1
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Overexpression of eIF3f was recently shown to suppress Akt and ERK signaling, increase p53 protein levels and inhibit clusterin protein expression, which promotes cancer cell proliferation and reduces chemosensitivity [XREF_BIBR].
EIF3F affects RPS6KB1
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Degradation of eIF3f by MAFbx Suppresses S6K1 Activation by mTOR.

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The degradation of eIF3f suppresses S6K1 activation by mTOR in a MAFbx / atrogin-1-induced atrophy model ( Csibi et al ., 2010 ) .

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The degradation of eIF3f suppresses S6K1 activation by mTOR in a MAFbx/atrogin-1-induced atrophy model (Csibi et al., 2010).

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Here we present evidence that in MAFbx induced atrophy the degradation of eIF3f suppresses S6K1 activation by mTOR, whereas an eIF3f mutant insensitive to MAFbx polyubiquitination maintained persistent phosphorylation of S6K1 and rpS6.

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Moreover inhibition of eIF3f degradation (mutant eIF3f K 5-10 R) in MAFbx induced atrophy maintained S6K1 activation by mTOR (XREF_FIG) and electroporation of eIF3f K 5-10 R expression vector in mice not only protects against muscle atrophy but also induces hypertrophy XREF_BIBR.

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The degradation of eIF3f suppresses S6K1 activation by mTOR in a MAFbx and atrogin-1-induced atrophy model.

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Only eIF3f with an intact TOS motif coimmunoprecipitates with mTOR-raptor (XREF_FIG) and activates mTOR-raptor and S6K1 pathway (XREF_FIG).

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In contrast, eIF3f knockdown was sufficient to induce the repression of S6K1 activity and the lack of myogenic differentiation (XREF_FIG).

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Genetic repression of eIF3f in differentiated skeletal muscle is sufficient to induce atrophy XREF_BIBR and degradation of eIF3f by MAFbx suppresses S6K1 activation by mTOR.

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To further confirm that eIF3f mediates activation of S6K1 by mTOR, an eIF3f mutant deleted of the C-terminal domain was transfected in mouse primary muscle cells and the phosphorylation of downstream targets of mTOR was assessed.

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We confirmed that the loss of eIF3f reduced the proliferation of PCa cells, both in vitro and in vivo.

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EIF3f silencing significantly suppressed the growth of PCa cells, both in vitro and in vivo.

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These results suggested that eIF3f has an oncogenic role in PCa, mediated at least partially through the regulation of Akt signaling, and that eIF3f represents a potential target for the inhibition of PCa growth and progression.

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The results indicated that silencing of eIF3f expression by lentiviral transfection significantly repressed tumor growth of PCa cells, both in vitro and in vivo.

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These results confirmed that the inhibition of eIF3f significantly blocked PCa cell growth in vivo.

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These results indicated that eIF3f knockdown caused inhibition of PCa cell proliferation at least partially through the suppression of Akt phosphorylation.

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In silico analyses suggested that eIF3f may promote the progression of PCa.

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The proliferation rates of shRNA lentivirus infected PCa cells indicated that eIF3f knockdown markedly decreased the proliferation of PCa cells (XREF_FIG).

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EIF3f Knockdown Suppressed the Growth of PCa Tumor Xenografts.
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Figure XREF_FIG shows that the presence of eIF3f promotes adrenoceptor activation.

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In this study, we found a novel physical interaction between human eIF3f and the alpha 1B-adrenergic receptor (alpha 1B-ADR) and that eIF3f stimulates adrenoceptor activity.

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In the present work, we report that eIF3f physically and stably interacts with the alpha 1B-ADR, and that eIF3f stimulates adrenoceptor activity.

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In the presence of catecholamine, eIF3f stimulates adrenoceptor activity.

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Upon catecholamine stimulation, eIF3f promotes adrenoceptor activity in vitro, independently of the eIF3f proline- and alanine rich N-terminal region.

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EIF3f promotes adrenoceptor activity upon catecholamine stimulation.

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The eukaryotic translation initiation factor 3f (eIF3f) interacts physically with the alpha 1B-adrenergic receptor and stimulates adrenoceptor activity.
EIF3F affects AKT
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EIF3F inhibits AKT.
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EIF3F inhibits AKT. 2 / 4
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EIF3f overexpression activates p53 and Bax and inhibits Akt and ERK signaling.

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Targeting eIF3f Suppresses the Growth of Prostate Cancer Cells by Inhibiting Akt Signaling.
EIF3F increases the amount of AKT.
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Modified EIF3F increases the amount of AKT. 2 / 2
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Exogenous expression of shRNA resistant eIF3f in eIF3f knockdown cells restored Akt phosphorylation levels and cell growth.

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Furthermore, ectopic expression of shRNA resistant eIF3f in eIF3f knockdown cells restored Akt phosphorylation levels and cell growth.
EIF3F decreases the amount of AKT.
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Modified EIF3F decreases the amount of AKT. 1 / 1
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Overexpression of eIF3f was recently shown to suppress Akt and ERK signaling, increase p53 protein levels and inhibit clusterin protein expression, which promotes cancer cell proliferation and reduces chemosensitivity [XREF_BIBR].
EIF3F affects EIF3F
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EIF3F decreases the amount of EIF3F.
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EIF3F decreases the amount of EIF3F. 2 / 3
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These findings suggest that eIF3f functions as a negative regulator of cell growth due to the naturally reduced levels of eIF3f contributing to cancer development and overexpression resulting in apoptosis [XREF_BIBR].

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To further confirm that eIF3f could affect hMSH4 stability, the levels of eIF3f in 293T/eIF3f-hMSH 4 cells were reduced by eIF3f RNAi, and the levels of hMSH4 were examined by immunoblotting.
EIF3F activates EIF3F.
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EIF3F activates EIF3F. 2 / 2
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Furthermore, we found that ectopic expression of sheIF3f # 1 resistant wild-type eIF3f rescued the proliferation rate of eIF3f knockdown cells (XREF_FIG).

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Phosphorylation of eIF3f enhances the association of eIF3f with the core eIF3 subunits during apoptosis.
EIF3F increases the amount of EIF3F.
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EIF3F increases the amount of EIF3F. 1 / 1
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The function of eIF3f in inhibition of translation was also supported by our observation that starvation caused an increase in the eIF3f level, in both primary fibroblast cells and pancreatic epithelial cells (XREF_FIG).
MSH4 affects EIF3F
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MSH4 activates EIF3F. 2 / 5
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Furthermore, the interplay between hMSH4 and eIF3f inhibits IR induced AKT activation, and hMSH4 promotes eIF3f mediated bypass of S phase arrest, and ultimately enhancing an early G2/M arrest in response to IR treatment.

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Conversely, eIF3f significantly increased the sensitivity of cells treated with 2Gy IR and hMSH4 substantially promoted this effect.
EIF3F affects Hypertrophy
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Moreover, overexpression of eIF3f K5-10R mutant induces a significant increase in protein synthesis and hypertrophy compared to the wild type protein under normal condition (Csibi et al., 2010, Csibi et al., 2009).

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Genetic activation of eIF3f induces hypertrophy associated with an increase in phosphorylation of mTORC1 substrates S6K1 and 4E-BP1, and limits atrophy by increasing expression of muscle structural proteins during starvation (Csibi et al., 2010).

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Under basal conditions, overexpression of eIF3f in differentiated muscle cells is sufficient to induce hypertrophy via increased activity of mTORC1.

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Moreover, overexpression of eIF3f K5-10R mutant induces a significant increase in protein synthesis and hypertrophy compared to the wild type protein under normal condition (Csibi et al., 2010 ).
EIF3F affects Atrophy
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Genetic blockade of eIF3f expression induced atrophy.

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Genetic activation of eIF3f induces hypertrophy associated with an increase in phosphorylation of mTORC1 substrates S6K1 and 4E-BP1, and limits atrophy by increasing expression of muscle structural proteins during starvation (Csibi et al., 2010).

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In contrast, genetic blockade of eIF3f induces myotubes atrophy associated with a decrease in the phosphorylation of mTORC1 substrates (Csibi et al., 2010).
Berberine affects EIF3F
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Berberine inhibits EIF3F.
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In mast cells, the GeneChip® microarray showed that antigen increased the expression of EIF3F and MALT1, inhibited by berberine.

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Berberine decreases eIF3-f and protein synthesis by an atrogin-1-dependent mechanism.
Berberine decreases the amount of EIF3F.
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Berberine decreases the amount of EIF3F. 2 / 2
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We proposed that this response could be linked to changes in the protein synthesis mediator, eIF3-f, because berberine also decreased the level of eIF3-f in muscles of wild-type and db/db mice (XREF_FIG A and B and XREF_FIG A).

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In mast cells, the GeneChip (R) microarray showed that antigen increased the expression of EIF3F and MALT1, inhibited by berberine.
EIF3F affects Notch
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EIF3F activates Notch.
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EIF3F activates Notch. 3 / 3
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These results suggest that eIF3f is specifically involved in an ubiquitination and deubiquitination process targeting activated Notch.

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The translation initiation factor 3f (EIF3F) is recruited to activate Notch on endocytic vesicles by the Deltex1 serving as a bridging factor.

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The activated form of notch needs to be deubiquitinated before being processed by the gamma-secretase activity and entering the nucleus, where it fulfills its transcriptional function. The enzyme accounting for this deubiquitinase activity is eif3f, known so far as a translation initiation factor.
EIF3F inhibits Notch.
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EIF3F inhibits Notch. 1 / 1
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Finally, catalytically inactive forms of eIF3f as well as shRNAs targeting eIF3f repress Notch activation in a coculture assay, showing that eIF3f is a new positive regulator of the Notch pathway.
EIF3F affects MSH4
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EIF3F activates MSH4. 1 / 3
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To understand the function of the eIF3f-hMSH4 interaction, we examined whether eIF3f promoted the stabilization of hMSH4.
EIF3F bound to MSH4 activates MSH4. 1 / 1
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The results presented in Figure XREF_FIG A clearly indicated that the interaction between hMSH4 and eIF3f was mediated through the N-terminal region of hMSH4 - most likely involving the first 150 amino acids of hMSH4.
EIF3F affects BAX
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EIF3F activates BAX.
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EIF3F activates BAX. 1 / 2
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EIF3f overexpression activates p53 and Bax and inhibits Akt and ERK signaling.
EIF3F increases the amount of BAX.
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EIF3F increases the amount of BAX. 1 / 1
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As shown in Figure XREF_FIG, eIF3f transfection in HeLa cells upregulated the expression of the apoptotic proteins p53, p21, and Bax.
Modified EIF3F increases the amount of BAX. 1 / 1
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Consistent with previous reports, the current study demonstrated that the overexpression of eIF3f enhanced p53, p21, and activated Bax levels in a time dependent manner in HeLa cervical cancer cells.
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The staining patterns of the two proteins are well overlapped ( Fig. 1c , panel E ) , suggesting that the S protein may sequester the eIF3f to the cytoplasm .

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The staining patterns of the two proteins are well overlapped (Fig. 1c, panel E), suggesting that the S protein may sequester the eIF3f to the cytoplasm.The interaction between SARS-CoV S protein and eIF3f was further investigated by checking if the two proteins could form complexes in vitro.

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The staining patterns of the two proteins are well overlapped (XREF_FIG, panel E), suggesting that the S protein may sequester the eIF3f to the cytoplasm.
EIF3F affects cell death
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MD 11 -mediated delivery of recombinant eIF3f induces melanoma and colorectal carcinoma cell death.

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To determine whether exogenously administered eIF3f proteins were able to compensate the loss of endogenous eIF3f and induce cancer cell death, we analyzed the therapeutic action of MD 11 -eIF3f in several tumor cells.

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While the lacking of literature does not allow formulate any hypothesis on glioblastoma cells and eIF3f correlation, our result on C2C12 confirms that overexpression of eIF3f does not induce cell death but it acts as " cell growth enhancer " instead of " death executer. "
EIF3F affects HNRNPK
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EIF3F inhibits HNRNPK. 2 / 3
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Our data support a model (XREF_FIG) in which eIF3f sequesters hnRNP K to inhibit it 's binding to rRNA, which leads to increased rRNA degradation and attenuated translation.

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Indeed, silencing of eIF3f increased the binding of hnRNP K to 28S rRNA by more than 9-fold (XREF_FIG).

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Mechanistically, the authors found that eIF3f inhibits both cap-dependent and cap-independent translation and that eIF3f promotes rRNA degradation through direct interaction with heterogeneous nuclear ribonucleoprotein K (Wen et al., 2012).

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Furthermore, one mechanism of translation inhibition likely involves eIF3f-mediated rRNA degradation by a direct eIF3f-hnRNP K (RNA-binding protein) interaction [109].
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In cancer cells, the loss of eIF3f results in an increased binding of hnRNP K to rRNA, reducing rRNA degradation, and possibly favoring oncogenesis through increased translation [109].
EIF3F affects HACD1
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EIF3F inhibits HACD1.
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EIF3F inhibits HACD1. 2 / 2
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By utilizing a bicistronic luciferase report system, it was shown that eIF3f normally inhibits both cap-dependent and cap-independent (i.e., IRES) mechanisms of translation initiation.

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Mechanistically, the authors found that eIF3f inhibits both cap-dependent and cap-independent translation and that eIF3f promotes rRNA degradation through direct interaction with heterogeneous nuclear ribonucleoprotein K (Wen et al., 2012).
EIF3F activates HACD1.
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EIF3F activates HACD1. 1 / 1
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EIF3f Activates the Cap Dependent Translation in Muscle Cells.
Cadmium dichloride increases the amount of EIF3F. 2 / 2
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RABIF affects EIF3F
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RABIF inhibits EIF3F. 1 / 2
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XREF_BIBR, XREF_BIBR, XREF_BIBR To study whether Mss4 is capable to abolish this specific property of eIF3f protein, A7 melanoma cells were transfected with pCS2+ MT empty vector, pCS2+ MT-Mss4 and pCS2+ MT-eIF3f or both plasmids together in addition to pRL-CMV vector in which the luciferase reporter gene is controlled by the CMV promoter.
Proteasome affects EIF3F
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MAFbx/atrogin-1 interacts with the Mov34 domain of eIF3f and promotes its ubiquitination resulting in proteasome-mediated degradation of eIF3f during muscle wasting (Lagirand-Cantaloube et al., 2008) (Fig. 1).

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MAFbx and atrogin -1 interacts with the Mov34 domain of eIF3f and promotes its ubiquitination resulting in proteasome mediated degradation of eIF3f during muscle wasting (XREF_FIG).
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Mechanistically , the authors found that eIF3f inhibits both cap-dependent and cap-independent translation and that eIF3f promotes rRNA degradation through direct interaction with heterogeneous nuclear ribonucleoprotein K ( Wen et al ., 2012 ) .

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Notably , the eIF3f level was reportedly reduced in pancreatic cancer , and overexpression of eIF3f in pancreatic cancer cells resulted in apoptosis ; 33moreover , eIF3f promoted rRNA degradation and inhibited translation.34eIF3f has been shown to act as a tumor suppressor in melanoma.35 ,36 In patients with gastric cancer , reduced expression of eIF3f was associated with poor prognosis , and eIF3f presumably plays an important role in gastric cancer recurrence.37-39However , it remains controversial whether eIF3f acts as an oncogene or a suppressor .
EIF3F affects cytokinesis
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We also showed that silencing of eIF3f promotes both cap dependent and cap-independent and internal ribosome entry site (IRES)-dependent translation and cytokinesis defects.

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In our current study, we found evidence that stable knockdown of eIF3f in normal human pancreatic ductal epithelial cells increased cell size, nuclear pleomorphism, cytokinesis defects, cell proliferation, clonogenicity, apoptotic resistance, migration, and formation of 3-dimensional irregular masses.
EIF3F affects NOTCH1
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EIF3F activates NOTCH1. 1 / 2
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The activated form of notch needs to be deubiquitinated before being processed by the gamma-secretase activity and entering the nucleus, where it fulfills its transcriptional function. The enzyme accounting for this deubiquitinase activity is eif3f, known so far as a translation initiation factor.
EIF3F affects Death
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EIF3F activates Death. 2 / 2
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For instance, one hour treatment of MD 11 -wt eIF3f induced 30% death in Colo857 and HCT116 p53 -/- and 50% in B16 and HCT116 p53 +/+, while MD 11 -K510R killed as expected 50% of Colo857 cells and 100% of the others.

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The same effect was reached in colorectal carcinoma cells lacking of p53 (HCT116 p53 -/-) in about 1 hour for MD 11 -K510R, 1.5 hours for MD 11 -NF and 3 hours for MD 11 -wt eIF3f, confirming that this cell line is more resistant than wild-type to the death stimulus and that p53 may play a role in eIF3f induced death (XREF_FIG).
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Previous studies have demonstrated that overexpression of eIF3f inhibits cell proliferation and induces apoptosis in melanoma and pancreatic cancer cells, suggesting that downregulation of eIF3f is involved in tumorigenesis for many types of cancer [11, 16, 19] .

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Together , these previous findings suggest that eIF3f may be involved in the regulation of cell growth and proliferation and contributes to tumorigenesis ; however , its role in GC remains unclear .
AKT affects EIF3F
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AKT increases the amount of EIF3F. 2 / 2
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Additional work is required to establish if Akt signaling activates eIF3f expression in prostate cancer.

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This results indicated that Akt signaling might upregulate the expression level of eIF3f in PCa cells.
EIF3F affects MKI67
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EIF3F increases the amount of MKI67.
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EIF3F increases the amount of MKI67. 1 / 1
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The IHC analysis of the xenograft tissues exhibited that inhibiting eIF3f reduced Ki67 expression, indicating decreased proliferation of tumor cells (XREF_FIG - XREF_FIG).
EIF3F activates MKI67.
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EIF3F activates MKI67. 1 / 1
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The IHC analysis of the xenograft tissues exhibited that inhibiting eIF3f reduced Ki67 expression , indicating decreased proliferation of tumor cells ( Figure 3D-F ) .
EIF3F affects ERK
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EIF3F inhibits ERK.
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EIF3F inhibits ERK. 1 / 1
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EIF3f overexpression activates p53 and Bax and inhibits Akt and ERK signaling.
EIF3F decreases the amount of ERK.
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Modified EIF3F decreases the amount of ERK. 1 / 1
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Overexpression of eIF3f was recently shown to suppress Akt and ERK signaling, increase p53 protein levels and inhibit clusterin protein expression, which promotes cancer cell proliferation and reduces chemosensitivity [XREF_BIBR].
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E3_Ub_ligase inhibits EIF3F.
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The reduced Akt1 kinase activity observed upon statins treatment, resulted in an increase in dephosphorylation on FoxO3 and FoxO1 transcription factors, their translocation into the nucleus, and activation of the Atrogin1 and MAFbx gene encoding ubiquitin ligase E3, which eliminates MyoD, calcineurin, eIF3-F translation initiator, and FoxO1 [XREF_BIBR].
E3_Ub_ligase activates EIF3F.
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It was found that the E3 ubiquitin ligase MAFbx and atrogin -1 targets the Mov34 motif of eIF3f during atrophy for polyubiquitination and subsequent degradation by the proteasome [XREF_BIBR, XREF_BIBR, XREF_BIBR].
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Valproic acid increases the amount of EIF3F. 1 / 1
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Triphenyl phosphate increases the amount of EIF3F. 1 / 1
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Titanium dioxide decreases the amount of EIF3F. 1 / 1
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Thimerosal affects EIF3F
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Thimerosal decreases the amount of EIF3F. 1 / 1
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Sodium fluoride decreases the amount of EIF3F. 1 / 1
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Sodium arsenite increases the amount of EIF3F. 1 / 1
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Sodium arsenate increases the amount of EIF3F. 1 / 1
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Progesterone increases the amount of EIF3F. 1 / 1
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Potassium chromate increases the amount of EIF3F. 1 / 1
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Paracetamol affects EIF3F
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Paracetamol increases the amount of EIF3F. 1 / 1
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Nickel acetate increases the amount of EIF3F. 1 / 1
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Methylmercury chloride decreases the amount of EIF3F. 1 / 1
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Methyl methanesulfonate increases the amount of EIF3F. 1 / 1
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Mercury(0) affects EIF3F
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Mercury(0) decreases the amount of EIF3F. 1 / 1
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MTORC1 affects EIF3F
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MTORC1 increases the amount of EIF3F. 1 / 1
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Interestingly, the translation of eIF3f is regulated via a rapamycin sensitive mechanism which raises the possibility that mTORC1 activation could induce eIF3f expression and protein synthesis in a feed-forward manner [XREF_BIBR].
Ketone body affects EIF3F
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Ketone body increases the amount of EIF3F. 1 / 1
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Indometacin affects EIF3F
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Indometacin increases the amount of EIF3F. 1 / 1
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Hsa-miR-6889-3p decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-6807-5p decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-661 affects EIF3F
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Hsa-miR-661 decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-550b-2-5p decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-550a-5p decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-550a-3-5p decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-4436b-5p decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-4252 decreases the amount of EIF3F. 1 / 1
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Hsa-miR-320a decreases the amount of EIF3F. 1 / 1
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Hsa-miR-3116 decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-16-5p decreases the amount of EIF3F. 1 / 1
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Hsa-miR-155-5p decreases the amount of EIF3F. 1 / 1
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Hsa-miR-149-5p decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-1271-3p decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-1254 decreases the amount of EIF3F. 1 / 1
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biopax:mirtarbase
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Hsa-miR-106b-5p decreases the amount of EIF3F. 1 / 1
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Gentamycin affects EIF3F
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Gentamycin increases the amount of EIF3F. 1 / 1
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Estrogen affects EIF3F
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Estrogen bound to ESR1 decreases the amount of EIF3F. 1 / 1
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Specifically, estrogen bound ERalpha represses transcription of the EIF3F gene, while promoting eIF3f mRNA translation.
Diarsenic trioxide increases the amount of EIF3F. 1 / 1
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Cupric oxide decreases the amount of EIF3F. 1 / 1
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Copper(II) sulfate decreases the amount of EIF3F. 1 / 1
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Cobalt dichloride increases the amount of EIF3F. 1 / 1
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Clothianidin decreases the amount of EIF3F. 1 / 1
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Chloropicrin decreases the amount of EIF3F. 1 / 1
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Benzo[a]pyrene increases the amount of EIF3F. 1 / 1
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Ubiquitin affects EIF3F
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The reduced Akt1 kinase activity observed upon statins treatment, resulted in an increase in dephosphorylation on FoxO3 and FoxO1 transcription factors, their translocation into the nucleus, and activation of the Atrogin1 and MAFbx gene encoding ubiquitin ligase E3, which eliminates MyoD, calcineurin, eIF3-F translation initiator, and FoxO1 [XREF_BIBR].
Quercetin affects EIF3F
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Niclosamide affects EIF3F
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Niclosamide decreases the amount of EIF3F. 1 / 1
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ICG 001 affects EIF3F
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ICG 001 decreases the amount of EIF3F. 1 / 1
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HR affects EIF3F
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HR inhibits EIF3F. 1 / 1
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(c) L929 fibroblasts were infected with MHV-Gluc (MOI = 0.05, n = 3) for 12 hr upon a 48 hr knockdown of eIF3e, eIF3f and eIF3i using single target-specific siRNAs.
GSK-J4 affects EIF3F
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GSK-J4 increases the amount of EIF3F. 1 / 1
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FMN1 affects EIF3F
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FMN1 inhibits EIF3F. 1 / 1
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Within the LD block of EIF3F, five of seven common SNPs (rs79714374, rs12421289, rs12278319, rs7941782, rs4758267, rs12420464, rs56392532) were identified to be tagging SNPs for six different haplotypes with frequencies between 3.5 and 53.4%.