EIF3H Data Analysis

HGNC Gene Name
eukaryotic translation initiation factor 3 subunit H
HGNC Gene Symbol
EIF3H
Identifiers
hgnc:3273 NCBIGene:8667 uniprot:O15372
Orthologs
mgi:1915385 rgd:735178
INDRA Statements
deubiquitinations all statements
Pathway Commons
Search for EIF3H
Number of Papers
69 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
EIF3F eukaryotic translation initiation factor 3 subunit F 0.369 BioGRID IntAct INDRA (9) Reactome (11) 0.29 1.49 1.72e-07
EIF3M eukaryotic translation initiation factor 3 subunit M 0.367 BioGRID IntAct INDRA (2) Reactome (11) 0.82 4.43 2.74e-89
EIF3E eukaryotic translation initiation factor 3 subunit E 0.347 BioGRID IntAct INDRA (7) Reactome (11) 0.89 4.80 5.65e-124
UTP23 UTP23 small subunit processome component 0.289 0.07 0.32 2.51e-01
RAD21 RAD21 cohesin complex component 0.262 Reactome (1) -0.18 -1.08 1.82e-03
MED30 mediator complex subunit 30 0.234 -0.26 -1.53 2.92e-06
RPS3 ribosomal protein S3 0.234 Reactome (11) 0.71 3.84 2.18e-56

Dependency GO Term Enrichment

Gene set enrichment analysis was done on the genes correlated with EIF3Husing 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:0001732 formation of cytoplasmic translation initiation complex Biological Process 1.12e-08 3.09e-06 8.14e-07
GO:0033290 eukaryotic 48S preinitiation complex Cellular Component 1.40e-08 3.87e-06 8.14e-07
GO:0005852 eukaryotic translation initiation factor 3 complex Cellular Component 1.72e-08 4.76e-06 8.14e-07
GO:0070993 translation preinitiation complex Cellular Component 2.50e-08 6.93e-06 8.89e-07
GO:0002183 cytoplasmic translational initiation Biological Process 1.38e-07 3.81e-05 3.91e-06
GO:0006413 translational initiation Biological Process 3.55e-07 9.82e-05 8.40e-06
GO:0003743 translation initiation factor activity Molecular Function 6.35e-07 1.76e-04 1.29e-05
GO:0071541 eukaryotic translation initiation factor 3 complex, eIF3m Cellular Component 2.45e-06 6.78e-04 4.35e-05
GO:0008135 translation factor activity, RNA binding Molecular Function 3.11e-06 8.60e-04 4.90e-05
GO:0002181 cytoplasmic translation Biological Process 4.19e-06 1.16e-03 5.96e-05
GO:0070181 small ribosomal subunit rRNA binding Molecular Function 6.41e-06 1.77e-03 7.73e-05
GO:0090079 translation regulator activity, nucleic acid binding Molecular Function 6.52e-06 1.81e-03 7.73e-05
GO:0045182 translation regulator activity Molecular Function 1.35e-05 3.73e-03 1.42e-04
GO:0022613 ribonucleoprotein complex biogenesis Biological Process 1.40e-05 3.88e-03 1.42e-04
GO:0031369 translation initiation factor binding Molecular Function 5.40e-05 1.50e-02 5.11e-04
GO:0071826 ribonucleoprotein complex subunit organization Biological Process 1.15e-04 3.17e-02 1.02e-03

Literature Mining

INDRA was used to automatically assemble known mechanisms related to EIF3H 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
EIF3H deubiquitinates SNAI1. 3 / 3
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We observed overexpression of EIF3H deubiquitinated endogenous Snail, but knockdown of EIF3H facilitated ubiquitination of endogenous Snail.

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Furthermore, we demonstrated Snail, as the novel identified substrate of EIF3H, could be deubiquitinated and stabilized by EIF3H.

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EIF3H interacts with and deubiquitinates Snail to prolong its half-life.
Modified EIF3H leads to the deubiquitination of SNAI1. 1 / 1
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When co-expressed Snail-Flag with EIF3H in HEK293T cells, we found that Snail ubiquitination could be abolished by EIF3H overexpression.

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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The proliferation of colorectal cancer cells is suppressed by silencing of EIF3H.

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Our results suggest that eIF3h content is near a threshold in Hap1 cells, since overexpression of SNAP-eIF3H appears to diminish wild-type eIF3h protein levels and fails to increase the proliferation rate of wild-type cells.

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Finally, reduction of eIF3h levels in breast and prostate cancer cell lines by short interfering RNA methods reduces their rates of proliferation and anchorage independent growth in soft agar.

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The higher polyp number associated with the C allele of rs16892766 could be explained by the location of this SNP in the EIF3H gene, which increases cell proliferation, growth, and survival when overexpressed.

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Reduction of eIF3h levels in breast and prostate cancer cell lines by shRNA methods has previously been shown to reduce cell proliferation and anchorage independent growth in soft agar XREF_BIBR.

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XREF_BIBR At the cellular level, EIF3H overexpression increases proliferation, growth and survival.

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Reduction of EIF3H has previously been shown to reduce cell proliferation and anchorage independent growth in soft agar [XREF_BIBR].

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EIF3h potentiates the cell proliferation and inhibits the cell apoptosis of gastric cancer cells 13.

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We observed that EIF3H overexpression in both KYSE150 and KYSE510 cells increased cell proliferation in vitro ( Fig. 2e and f ) , whereas depletion of EIF3H significantly reduced cell proliferation ( Fig. 2g and h ) .

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Knockdown of EIF3H inhibited cell proliferation and colony formation .

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The in vitro results indicated that silencing EIF3H in MM cells could significantly suppress cell proliferation, promote cell apoptosis and induce cell cycle arrest.

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Knockdown of the translation initiation factor EIF3H, which scored as essential in 8 BrCa, 5 PDAC, and 3 HGS-OvCa cell lines, by any of three independent shRNAs significantly reduced cell proliferation in the HGS-OvCa cell lines tested (OVCAR5, OVCAR8 and A2780) (XREF_FIG).

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We observed that EIF3H overexpression in both KYSE150 and KYSE510 cells increased cell proliferation in vitro, whereas depletion of EIF3H significantly reduced cell proliferation.

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Knockdown of EIF3H significantly inhibited the proliferation and colony formation of OS cells in vitro, and tumour growth in nude mice in vivo.

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EIF3H depletion in ESCC cells significantly decreased the ability of cell proliferation and mobility, examined by CCK8 assay, colony formation assay and transwell assay in vitro and xenograft and tail-vein lung metastatic mouse models in vivo.
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Thus, functional knockdown of EIF3H expression inhibits HCC growth and metastasis in vitro and in vivo.

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Besides, it also takes part in EMT process and the knockdown of EIF3H suppressed tumor metastasis in vivo.

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Taken together, these results indicate that EIF3H knockdown inhibits cell mobility and tumor metastasis in ESCC.

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To find out whether EIF3H enhances cancer metastasis ability in vivo, we then performed lung metastatic model assay.

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To find out whether EIF3H enhances cancer metastasis ability in vivo , we then performed lung metastatic model assay .

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Taken together , these results indicate that EIF3H knockdown inhibits cell mobility and tumor metastasis in ESCC .

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Our results exhibited that ectopic expression of EIF3H promoted ESCC metastasis with the increase of Snail, N-Cadherin and Vimentin, and decrease of E-cadherin, while knockdown of EIF3H exerted an opposite effect.

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Other than the translation initiation function of EIF3H, in the present study, our finding that EIF3H promotes metastasis through stabilizing YAP addresses a knowledge gap for YAP turnover regulation.

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In the spontaneous lung metastasis model, we observed that loss of EIF3H significantly decreased lung metastasis nodules.

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Functional analyses showed that EIF3H overexpression promoted LUAD cell migration and invasion in vitro as well as metastasis in nude mice by activating epithelial-mesenchymal transition (EMT) signaling.
EIF3H bound to PDCD4 activates Neoplasm Metastasis. 1 / 1
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EIF3H interacts with PDCD4 enhancing lung adenocarcinoma cell metastasis.
Mutated EIF3H activates Neoplasm Metastasis. 1 / 1
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To our surprise, we observed, while only overexpression of the wild-type EIF3H fully recapitulates lung metastasis, the expression of mutant EIF3H fails to restore lung metastasis, indicating that EIF3H-YAP axis is critical for EIF3H driven tumor invasion and metastasis (XREF_FIG and XREF_SUPPLEMENTARY).
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Overexpression of eIF3h has recently been shown to inhibit Myc dependent induction of apoptosis of primary prostate cells and EIF3H and MYC and may cooperate in enhanced protein translation either in a general way or for a specific subset of mRNAs XREF_BIBR.

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EIF3h potentiates the cell proliferation and inhibits the cell apoptosis of gastric cancer cells 13.

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As shown in XREF_FIG, EIF3H knockdown also increased the rate of apoptosis in the two OS cell lines based on flow cytometry using Annexin V and 7-AAD double staining at both the early and late phases of apoptosis (Saos2 cells : 14.13 and 3.83% vs. 4.97 and 0.67% in controls, respectively, P < 0.05; U2OS cells : 7.96 and 12.53% vs. 6.89 and 7.14% in controls, respectively, P < 0.01).

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XREF_BIBR Coamplification of EIF3H may also reduce MYC dependent apoptosis in prostate epithelial cells.

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EIF3H knockdown inhibited cell growth, migration, colony formation, and promoted apoptosis, and this was confirmed with GFP expressing infected cells that were counted daily for 5 days.

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The knockdown of EIF3H, TPPP3, or DOCK2 promoted apoptosis of stem cells.

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Mahmood et al demonstrated that EIF3H knockdown with specific small interfering RNA induced cell cycle arrest and apoptosis in breast tumour cells.

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Furthermore, overexpressed eIF3h inhibits Myc dependent induction of apoptosis of primary prostate cells.
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Knockdown of EIF3H led to cell cycle arrest and promoted apoptosis in OS cells.

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The in vitro results indicated that silencing EIF3H in MM cells could significantly suppress cell proliferation, promote cell apoptosis and induce cell cycle arrest.

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In addition, we showed that EIF3H knock-down led to cell apoptosis.
EIF3H affects translation
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EIF3H activates translation.
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These risk variants, conferring an approximate 10%-18% increase in risk per allele, are located either inside or near protein coding genes that include TFEB (lysosome biogenesis and autophagy), EIF3H (initiation of translation), CYP17A1 (steroidogenesis), SPSB2 (proteasome degradation), and RPS21 (ribosome biogenesis).

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In agreement with this, our data show that, as CCT is required for the correct folding of eIF3h and eIF3i subunits, it indirectly influences gene expression with eIF3i overexpression enhancing both cap- and IRES (internal ribosome entry segment)-dependent translation initiation, whereas eIF3h overexpression selectively increases IRES dependent translation initiation.

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Our results are in agreement with these ideas and suggest an eIF3H mediated control of HIF-1alpha translation that could explain in part its oncogenic properties.

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Together with the study which suggests that eIF3h may play an important regulatory role in translation of specific mRNAs [75] as discussed above, these findings suggest that aberrant over-expression o[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]

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In any case, polysomal microarray analysis clearly demonstrated that eIF3h is a general stimulator of efficient translation of short uORF (s)-containing mRNAs throughout the transcriptome.

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This is an important TOR effect, since the S6K pathway not only stimulates overall protein synthesis but also eIF3h mediated translation reinitiation after an upstream open reading frame (uORF), a frequent feature found in plant mRNAs.

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Interestingly, the oncogenic function of METTL3 in NSCLC is complicated, where METTL3 could methylate YAP mRNA and recruit YTHDF1/3 and eIF3b to promote translation of YAP mRNA, or could interact with eIF3h to promote translation of target mRNAs (e.g., BRD4) independent of its enzymatic activity.

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Translation assays revealed that eIF3h supports the efficient translation of the mRNAs for CLV1 and the leaf transcription factor, AS1, which contain uORFs in their 5 ' UTR.
EIF3H inhibits translation.
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We next tested the functional interaction between METTL3 and eIF3h, and found depletion of eIF3h abrogated the enhanced translation by METTL3 (XREF_FIG and XREF_FIG).
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Increased expression of EIF3H gene increases CRC growth and invasiveness thereby providing a biological mechanism for the 8q23.3 association XREF_BIBR.

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We found that EIF3H overexpression significantly increased the abilities of migration and invasion in KYSE150 and KYSE510 cells.

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We found that EIF3H is significantly upregulated in esophageal cancer and ectopic expression of EIF3H in ESCC cell lines promotes cell proliferation, colony formation, migration and invasion.

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Functional analyses showed that EIF3H overexpression promoted LUAD cell migration and invasion in vitro as well as metastasis in nude mice by activating epithelial-mesenchymal transition (EMT) signaling.

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We observed, while the elevation of EIF3H drastically increases the tumor invasion in various breast cancer cell lines, including MDA-MB-231, 4T1, depletion of EIF3H by RNA interference largely attenuates tumor invasion (XREF_FIG - XREF_FIG & XREF_SUPPLEMENTARY - XREF_SUPPLEMENTARY).

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As shown in XREF_FIG - XREF_FIG and XREF_SUPPLEMENTARY - XREF_SUPPLEMENTARY, knockdown of either the YAP and CTGF expression abrogated EIF3H driven tumor cell invasion.

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We show that increased expression of EIF3H gene increases CRC growth and invasiveness thereby providing a biological mechanism for the 8q23.3 association.

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To further determine whether YAP is a physiologically relevant substrate for EIF3H that mediates EIF3H promoted tumor cell invasion, we have characterized catalytic function for EIF3H in regulating YAP abundance, YAP turnover rate and YAP ubiquitylation.

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We observed, while the elevation of EIF3H drastically increases the tumor invasion in various breast cancer cell lines, including MDA-MB-231, 4T1, depletion of EIF3H by RNA interference largely attenuates tumor invasion (XREF_FIG - XREF_FIG & XREF_SUPPLEMENTARY - XREF_SUPPLEMENTARY).
EIF3H affects SNAI1
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EIF3H activates SNAI1.
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EIF3H activates SNAI1. 3 / 3
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EIF3H promotes aggressiveness of esophageal squamous cell carcinoma by modulating Snail stability.

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Results showed that EIF3H obviously upregulated the Snail protein, but did not affect the mRNA level of Snail.

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We further validated whether EIF3H modulates Snail stability through deubiquitination.
EIF3H increases the amount of SNAI1.
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Modified EIF3H increases the amount of SNAI1. 1 / 1
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XREF_FIG a, EIF3H expression increased Snail protein level.
EIF3H increases the amount of SNAI1. 1 / 1
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The results exhibited that knockdown of EIF3H inhibited Snail protein level, and upregulated E-cadherin protein, whereas downregulated expression of N-Cadherin and Vimentin.
EIF3H decreases the amount of SNAI1.
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EIF3H decreases the amount of ubiquitinated SNAI1. 1 / 1
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EIF3H significantly decreased the poly-ubiquitin level of ubiquitinated Snail in an in vitro ubiquitination assay.
EIF3H affects cell growth
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Overexpression of EIF3H promotes cancer cell growth [XREF_BIBR], results in a malignant phenotype [XREF_BIBR], and serves as a prognostic marker of recurrence and metastasis [XREF_BIBR, XREF_BIBR].

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EIF3H knockdown inhibited cell growth, migration, colony formation, and promoted apoptosis, and this was confirmed with GFP expressing infected cells that were counted daily for 5 days.

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50 Recent studies have shown that EIF3H promoted cancer cell growth by stimulating protein synthesis.

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Besides, the mechanism of EIF3H mediated cell growth and migration also needs further study.

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Overexpression of EIF3S3 promotes cancer cell growth.

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We observed that disruption of EIF3H by RNA interference results in attenuation of EMT as indicated by upregulation of E-cadherin and suppression of vimentin as well as fibronectin, while elevation of EIF3H significantly enhances EMT phenotypes in breast cancer cells with dramatic alteration of morphology, loss of E-cadherin and accumulation of vimentin as well as fibronectin (XREF_SUPPLEMENTARY - XREF_SUPPLEMENTARY).

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A recent publication in lung adenocarcinoma demonstrated that EIF3H overexpression could also induce EMT signaling pathway [XREF_BIBR].

eidos
We observed that disruption of EIF3H by RNA interference results in attenuation of EMT as indicated by upregulation of E-cadherin and suppression of vimentin as well as fibronectin , while elevation of EIF3H significantly enhances EMT phenotypes in breast cancer cells with dramatic alteration of morphology , loss of E-cadherin and accumulation of vimentin as well as fibronectin ( Fig. S1G-J ) .

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Knockdown of EIF3H inhibits the EMT process and cell mobility induced by Snail.
EIF3H affects MYC
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EIF3H inhibits MYC. 3 / 3
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XREF_BIBR Coamplification of EIF3H may also reduce MYC dependent apoptosis in prostate epithelial cells.

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Overexpression of eIF3h has recently been shown to inhibit Myc dependent induction of apoptosis of primary prostate cells and EIF3H and MYC and may cooperate in enhanced protein translation either in a general way or for a specific subset of mRNAs XREF_BIBR.

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Furthermore, overexpressed eIF3h inhibits Myc dependent induction of apoptosis of primary prostate cells.
PDCD4 affects EIF3H
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PDCD4 inhibits EIF3H.
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PDCD4 inhibits EIF3H. 2 / 2
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Furthermore, we discovered that introduction of PDCD4 to EIF3H overexpressing LUAD cells abrogated the function of EIF3H, reducing migration and invasion of LUAD cells by downregulating EMT signaling.

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Overexpression of PDCD4 in LUAD cells reduced EIF3H mRNA and protein levels by suppressing c-Jun-induced EIF3H transcription.
PDCD4 activates EIF3H.
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PDCD4 activates EIF3H. 1 / 1
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Overexpression of PDCD4 in LUAD cells reduced EIF3H mRNA and protein levels by suppressing c-Jun-induced EIF3H transcription.
EIF3H affects competence
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EIF3H activates competence.
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It was proposed that, by analogy with the function of yeast eIF3a and Tif32 discussed above, eIF3h (specifically its N-terminal part) might support efficient REI by preserving the competence of a fraction of uORF translating ribosomes to resume traversing downstream.

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In plants, eIF3 non core subunit h (eIF3h) greatly elevates the reinitiation competence of mRNAs coding for the Arabidopsis basic zipper transcription factors (bZIPs) and several ARFs; while the 60S ribosomal protein L24B (RPL24B), which is encoded by SHORT VALVE1, lifts translation of uORF containing mRNAs that encode ARF3 (ETTIN) and ARF5.
EIF3H increases the amount of competence.
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EIF3H increases the amount of competence. 1 / 1
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Besides, in plants, the eIF3h subunit helps to prevent the permanent loss of reinitiation competence, suggesting that this subunit might also be involved in tethering 40S to eIF4G.
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Hsa-miR-939-3p decreases the amount of EIF3H. 2 / 2
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biopax:mirtarbase
No evidence text available

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Hsa-miR-873-3p decreases the amount of EIF3H. 2 / 2
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Hsa-miR-6888-3p decreases the amount of EIF3H. 2 / 2
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No evidence text available

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Hsa-miR-6864-3p decreases the amount of EIF3H. 2 / 2
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Hsa-miR-6860 decreases the amount of EIF3H. 2 / 2
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Hsa-miR-6849-3p decreases the amount of EIF3H. 2 / 2
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No evidence text available

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Hsa-miR-661 affects EIF3H
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Hsa-miR-661 decreases the amount of EIF3H. 2 / 2
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No evidence text available

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No evidence text available
Hsa-miR-612 affects EIF3H
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Hsa-miR-612 decreases the amount of EIF3H. 2 / 2
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No evidence text available

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Hsa-miR-548ah-5p decreases the amount of EIF3H. 2 / 2
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Hsa-miR-520h decreases the amount of EIF3H. 2 / 2
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Hsa-miR-520g-3p decreases the amount of EIF3H. 2 / 2
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No evidence text available

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Hsa-miR-5189-5p decreases the amount of EIF3H. 2 / 2
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Hsa-miR-4522 decreases the amount of EIF3H. 2 / 2
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Hsa-miR-3672 decreases the amount of EIF3H. 2 / 2
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Hsa-miR-3664-5p decreases the amount of EIF3H. 2 / 2
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Hsa-miR-3609 decreases the amount of EIF3H. 2 / 2
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No evidence text available

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Hsa-miR-3187-5p decreases the amount of EIF3H. 2 / 2
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No evidence text available

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Hsa-miR-3120-5p decreases the amount of EIF3H. 2 / 2
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Hsa-miR-3065-5p decreases the amount of EIF3H. 2 / 2
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Hsa-miR-196a-3p decreases the amount of EIF3H. 2 / 2
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Hsa-miR-1285-3p decreases the amount of EIF3H. 2 / 2
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No evidence text available

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Bisphenol A affects EIF3H
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Bisphenol A increases the amount of EIF3H. 2 / 2
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ctd
No evidence text available

ctd
No evidence text available
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Benzo[a]pyrene increases the amount of EIF3H. 2 / 2
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ctd
No evidence text available

ctd
No evidence text available
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We observed that disruption of EIF3H by RNA interference results in attenuation of EMT as indicated by upregulation of E-cadherin and suppression of vimentin as well as fibronectin , while elevation of EIF3H significantly enhances EMT phenotypes in breast cancer cells with dramatic alteration of morphology , loss of E-cadherin and accumulation of vimentin as well as fibronectin ( Fig. S1G-J ) .

eidos
We observed , while the elevation of EIF3H drastically increases the tumor invasion in various breast cancer cell lines , including MDA-MB-231 , 4T1 , depletion of EIF3H by RNA interference largely attenuates tumor invasion ( Fig. 1B-F & Fig. S1A-C ) .
EIF3H affects MAPK
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EIF3H activates MAPK. 2 / 2
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Zhu and colleagues identified that the transforming growth factor-beta and mitogen activated protein kinase pathways are potentially targeted by EIF3H using microarray analysis.

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TGF-betaand MAPK pathways are potentially targeted by EIF3H.
EIF3H affects FN1
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EIF3H activates FN1. 2 / 2
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eidos
We observed that disruption of EIF3H by RNA interference results in attenuation of EMT as indicated by upregulation of E-cadherin and suppression of vimentin as well as fibronectin , while elevation of EIF3H significantly enhances EMT phenotypes in breast cancer cells with dramatic alteration of morphology , loss of E-cadherin and accumulation of vimentin as well as fibronectin ( Fig. S1G-J ) .

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We observed that disruption of EIF3H by RNA interference results in attenuation of EMT as indicated by upregulation of E-cadherin and suppression of vimentin as well as fibronectin, while elevation of EIF3H significantly enhances EMT phenotypes in breast cancer cells with dramatic alteration of morphology, loss of E-cadherin and accumulation of vimentin as well as fibronectin (XREF_SUPPLEMENTARY - XREF_SUPPLEMENTARY).
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This structure appears to be an inhibitory state wherein the subunit H inhibits the ATPase activity by stabilizing ADP binding to the catalytic site.

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Together with biochemical data, the structure supports a mechanistic model wherein subunit H inhibits ATPase activity by stabilizing an open catalytic site that results in tight binding of inhibitory ADP at another site.
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5-fluorouracil increases the amount of EIF3H. 2 / 2
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ctd
No evidence text available

ctd
No evidence text available
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EIF3H decreases the amount of poly-ubiquitin.
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EIF3H decreases the amount of poly-ubiquitin. 1 / 1
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EIF3H significantly decreased the poly-ubiquitin level of ubiquitinated Snail in an in vitro ubiquitination assay.
EIF3H activates poly-ubiquitin.
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Thus, Trp119 and Tyr140 on EIF3H are critical to ensuring the EIF3H mediated removal of YAP poly-ubiquitin conjugates.
EIF3H affects cell cycle
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EIF3H inhibits cell cycle.
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Mahmood et al demonstrated that EIF3H knockdown with specific small interfering RNA induced cell cycle arrest and apoptosis in breast tumour cells.
EIF3H activates cell cycle.
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The in vitro results indicated that silencing EIF3H in MM cells could significantly suppress cell proliferation, promote cell apoptosis and induce cell cycle arrest.
EIF3H affects HIF1A
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EIF3H decreases the amount of HIF1A.
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EIF3H decreases the amount of HIF1A. 1 / 1
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Indeed, we demonstrate in Fig. 5E -F that not only does inhibition of eIF3H via RNAi decrease CPEB2B mediated HIF1alpha expression, but that this mechanism is likely due to translation as demonstrated in Fig. 5F, S4.
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EIF3H activates HIF1A.
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EIF3H activates HIF1A. 1 / 1
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Our results are in agreement with these ideas and suggest an eIF3H mediated control of HIF-1alpha translation that could explain in part its oncogenic properties.
EIF3H affects EIF3H
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EIF3H inhibits EIF3H.
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EIF3H inhibits EIF3H. 1 / 1
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Overexpression of eIF3h has recently been shown to inhibit Myc dependent induction of apoptosis of primary prostate cells and EIF3H and MYC and may cooperate in enhanced protein translation either in a general way or for a specific subset of mRNAs XREF_BIBR.
EIF3H activates EIF3H.
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EIF3H activates EIF3H. 1 / 1
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The expression of EIF3H is upregulated in HCC tissues compared with paired non tumor tissues from the same donor, thus linking upregulation of EIF3H to pathological hepatic changes.
2,3,7,8-tetrachlorodibenzodioxine increases the amount of EIF3H.
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ctd
No evidence text available
2,3,7,8-tetrachlorodibenzodioxine decreases the amount of EIF3H.
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ctd
No evidence text available
17alpha-ethynylestradiol increases the amount of EIF3H.
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17alpha-ethynylestradiol increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
17alpha-ethynylestradiol decreases the amount of EIF3H.
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17alpha-ethynylestradiol decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Vorinostat affects EIF3H
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Moreover, when eIF3H silenced cells were treated with SAHA, we observed a further reduction in HIF-1alpha expression relative to that seen with either treatment alone (XREF_FIG), suggesting that SAHA and sieIF3H target HIF-1alpha via parallel pathways.
Vinclozolin affects EIF3H
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Vinclozolin decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Sunitinib affects EIF3H
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Sunitinib increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Serpentine asbestos increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
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ctd
No evidence text available
Polyphenol affects EIF3H
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Polyphenol decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Perfluorooctanoic acid increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
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Nickel subsulfide decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Methyltestosterone decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
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Methylparaben decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Methylmercury compound decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Methylmercury chloride decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Ketone body affects EIF3H
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Ketone body increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
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Hsa-miR-6830-3p decreases the amount of EIF3H. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-5582-5p decreases the amount of EIF3H. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-5571-5p decreases the amount of EIF3H. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-511-5p decreases the amount of EIF3H. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-4423-3p decreases the amount of EIF3H. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-3622a-5p decreases the amount of EIF3H. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-3613-3p decreases the amount of EIF3H. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-302d-5p decreases the amount of EIF3H. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-302b-5p decreases the amount of EIF3H. 1 / 1
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biopax:mirtarbase
No evidence text available
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Hsa-miR-16-5p decreases the amount of EIF3H. 1 / 1
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biopax:mirtarbase
No evidence text available
Hexabromocyclododecane decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Gentamycin affects EIF3H
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Gentamycin increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Gefitinib affects EIF3H
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Based on these premises, we evaluated MYC and EIF3H gene status in patients with NSCLC treated with the EGFR-TKI gefitinib.
Doxorubicin affects EIF3H
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Doxorubicin increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
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Disodium selenite increases the amount of EIF3H. 1 / 1
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No evidence text available
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Dibutyl phthalate increases the amount of EIF3H. 1 / 1
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No evidence text available
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Cyclosporin A increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
Cas9 affects EIF3H
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Cas9 activates EIF3H. 1 / 1
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Hap1 cells were genetically modified with a construct encoding S. pyogenes Cas9 protein and guide strand construct targeting exon 1 of eIF3H.
Cadmium dichloride increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
SNAI1 affects EIF3H
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SNAI1 decreases the amount of EIF3H. 1 / 1
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Knockdown of Snail strikingly reversed the promoting effects of ectopic expression of EIF3H.
N-nitrosomorpholine increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
N-methyl-4-phenylpyridinium decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
HNRNPA2B1 affects EIF3H
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HNRNPA2B1 increases the amount of EIF3H. 1 / 1
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These data indicated that hnRNP A2B1 promoted the expressions of EIF3H, TPPP3, and DOCK2 and inhibited the expressions of DAPK1, SYT7, and RNF128 in melanoma stem cells.
GABPB2 affects EIF3H
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GABPB2 decreases the amount of EIF3H. 1 / 1
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biopax:msigdb
No evidence text available
GABPA affects EIF3H
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GABPA decreases the amount of EIF3H. 1 / 1
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biopax:msigdb
No evidence text available
Eif3a affects EIF3H
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Eif3a increases the amount of EIF3H. 1 / 1
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Thus, it would be essential to investigate if EIF3H overexpression might go along and is driven by an additional overexpression of an EIF3 member of module I.
ELK1 affects EIF3H
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ELK1 decreases the amount of EIF3H. 1 / 1
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biopax:msigdb
No evidence text available
EIF3H affects zinc(2+)
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The above result suggests that the complexation of EIF3H with EIF3F further supports the binding of the zinc ion to the same site (XREF_FIG).

reach
Translation assays revealed that eIF3h supports the efficient translation of the mRNAs for CLV1 and the leaf transcription factor, AS1, which contain uORFs in their 5 ' UTR.
EIF3H affects start
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Mutated EIF3H activates start. 1 / 1
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One might hypothesize that the rpl24b or eif3h mutations cause a relaxation of start codon recognition specifically for reinitiating ribosomes.
EIF3H affects mTORC1
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EIF3H bound to MTOR inhibits mTORC1. 1 / 1
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Although the role of Eif3h in ASD is not clearly understood, a recent study has shown that Eif3h can directly interact with the mammalian target of rapamycin (mTOR) and collybistin (a neuron specific Rho-GEF) to downregulate the mTORC1 signaling cascade which is highly implicated in ASD 92.

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The striking formation of an enlarged meristematic dome (XREF_FIG) or of a pinformed stem in the eif3h mutant XREF_BIBR suggests that Arabidopsis eIF3h supports stem cell homeostasis, organ initiation, and morphogenesis.

reach
Underexpression of eIF3h causes defects in zebrafish embryo development, suggesting that eIF3h could be directly involved in translation initiation of specific transcripts during embryogenesis.
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Functional analyses showed that EIF3H overexpression promoted LUAD cell migration and invasion in vitro as well as metastasis in nude mice by activating epithelial-mesenchymal transition (EMT) signaling.
EIF3H affects YAP1
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EIF3H activates YAP1. 1 / 1
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eidos
EIF3H catalyzed YAP for deubiquitylation , resulting in its stabilization .
EIF3H affects WUS
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EIF3H activates WUS. 1 / 1
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Together, these results are consistent with the notion that translational defects in the eif3h mutant cause activation of WUS , which in turn contributes to the meristem expansion observed in the eif3h mutant.
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eidos
EIF3H knockdown leads to decrease of YAP protein expression and increases ubiquitination , especially the K48-linkage specific polyubiquitination ( Fig. 4I and Fig. S6A ) .
EIF3H affects TOR
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EIF3H activates TOR. 1 / 1
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Upregulated TOR is recruited to polysomes where it phosphorylates S6K1, which shortly before its release from polysomes phosphorylates eIF3h.
EIF3H affects TGFB
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EIF3H activates TGFB. 1 / 1
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Zhu and colleagues identified that the transforming growth factor-beta and mitogen activated protein kinase pathways are potentially targeted by EIF3H using microarray analysis.
EIF3H affects SXL
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EIF3H activates SXL. 1 / 1
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Depletion of eIF3d, but not eIF3e or eIF3h, reduced the inhibitory effect of SXL, suggesting that eIF3d is a potential target of the repressor complex within the translational machinery.
EIF3H affects RPS6KB1
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EIF3H activates RPS6KB1. 1 / 1
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Because plant eIF3h physically interacts with S6K1, it was further suggested that eIF3h might be the downstream target of activated S6K1.
EIF3H affects Melanoma
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EIF3H Knockdown Inhibits Malignant Melanoma through Regulating Cell Proliferation , Apoptosis and Cell Cycle .
EIF3H affects METTL3
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EIF3H inhibits METTL3. 1 / 1
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Knockdown of eIF3h suppressed the ability of METTL3 to promote cellular invasion (XREF_FIG and XREF_FIG).
EIF3H affects Eif3a
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EIF3H activates Eif3a. 1 / 1
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Overexpression of EIF3H does not lead to elevated EIF3, but protein synthesis is enhanced, as is translation of oncogenic mRNAs.
EIF3H affects ENO2
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Modified EIF3H decreases the amount of ENO2. 1 / 1
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We observed that loss of EIF3H in 4T1 cells led to decreased YAP and ENO2 expression.
EIF3H affects EIF3D
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EIF3H inhibits EIF3D. 1 / 1
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Depletion of eIF3d, but not eIF3e or eIF3h, reduced the inhibitory effect of SXL, suggesting that eIF3d is a potential target of the repressor complex within the translational machinery.
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Knockdown of EIF3H could decrease cell viability through both cell cycle arrest and apoptosis induction and inhibited the formation of colonies in anchorage independent conditions in breast cancer cells.
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D-glucopyranose decreases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
COPS5 affects EIF3H
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COPS5 inhibits EIF3H. 1 / 1
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Reducing the copy number of eIF3f or eIF3h reduced the growth inhibitory phenotype of DTrc8 over-expression, much like reduction of the COP9 signalosome subunits, CSN5 and 6.
CCT_complex affects EIF3H
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In the present study, we show that the eukaryotic cytosolic chaperonin CCT [chaperonin containing TCP-1 (tailless complex polypeptide 1)] binds to newly synthesized eIF3b and promotes the correct folding of eIF3h and eIF3i.
CCN2 affects EIF3H
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CCN2 activates EIF3H. 1 / 1
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As shown in XREF_FIG - XREF_FIG and XREF_SUPPLEMENTARY - XREF_SUPPLEMENTARY, knockdown of either the YAP and CTGF expression abrogated EIF3H driven tumor cell invasion.
Antirheumatic Agents increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
3-methylcholanthrene increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available
4,4'-diaminodiphenylmethane increases the amount of EIF3H. 1 / 1
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ctd
No evidence text available