IndraLab
Statements
reach
"USP37 was shown to directly interact with MYC at the MBIII region and deubiquitinate MYC.112 Although USP37-mediated deubiquitination and stabilization of MYC is independent of either Fbw7 or the phosphorylation of MYC at T58, overexpression of USP37 can block the Fbw7-mediated degradation of MYC."
USP37 is modified
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"In patients with lung cancer who also experienced OSA, IH induced a decrease in the expression of microRNA-320b, with downstream expression of ubiquitin-specific peptidase 37 (USP37) upregulated secondary to IH and USP37 promoting lung cancer progression by mediating the deubiquitination of Cdc10-dependent transcript 1 (CDT1) (98)."
USP37 affects cell population proliferation
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USP37 activates cell population proliferation.
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USP37 inhibits cell population proliferation.
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USP37 inhibits cell population proliferation. 6 / 8
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"Since concomitant loss of REST and USP37 expression attenuated p27 stabilization and differentiation and rescued cell proliferation, our data strongly suggest that repression of USP37 and consequent p27 degradation, are important for REST dependent maintenance of cell proliferation."
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USP37 activates epithelial to mesenchymal transition.
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USP37 inhibits epithelial to mesenchymal transition.
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USP37 inhibits epithelial to mesenchymal transition. 2 / 2
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"Our results indicated that inhibition of USP37 decreases the migratory potential of cells as compared to control cells and even after 48 hours no significant migration was observed and the scratch was not filled in both PA 1 and IGROV-1 cells in which USP37 was depleted (Fig. 2C and D).3.3
Inhibition of USP37 and its effects on different EMT markers."
reach
"This, in turn, activates the NRF2-ARE signaling pathway, which has been associated with chemotherapy resistance.Our findings suggest that the NRF2-ARE signaling pathway activation, regulated by USP37-mediated NRF2 stabilization, may be responsible for the observed chemotherapy resistance in hepatoma cells."
USP37 affects Snail1
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"We observed increased stabilization of PCNA in cells overexpressing USP37 (Fig. 6B) compared to cells without USP37 overexpression (Fig. 6A), indicating a potential interaction between USP37 and PCNA To test this hypothesis, we treated cells with two cytotoxic agents, HU and cisplatin, and performed immunoprecipitation using anti-USP37 antibody, which was subsequently probed with anti-PCNA antibody."
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"Many recent studies have highlighted the significant role of E3 ubiquitin ligases, deubiquitinases or substrate translocation between cell compartments, leading to substrate stability motivated us to explore the effect of HBx driven exodus of USP37 from the nucleus vis-a-vis its intracellular stability."
reach
"We observed increased stabilization of PCNA in cells overexpressing USP37 (Fig. 6B) compared to cells without USP37 overexpression (Fig. 6A), indicating a potential interaction between USP37 and PCNA To test this hypothesis, we treated cells with two cytotoxic agents, HU and cisplatin, and performed immunoprecipitation using anti-USP37 antibody, which was subsequently probed with anti-PCNA antibody."
USP37 affects Neoplasm Invasiveness
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USP37 activates Neoplasm Invasiveness.
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USP37 inhibits Neoplasm Invasiveness.
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"In the case of K48-linked substrates, binding of the UIMs to the proximal Ub increased catalytic efficiency of USP37 largely through k cat and to a lesser degree through K M . This result was somewhat counter-intuitive since we expected that binding of the UIMs of USP37 to Ub to have a more pronounced effect on K M (a proxy for binding affinity) since others have shown that UIM mutations perturbed the ability to pull down Ub conjugates xref ."
sparser
"In medulloblastomas, REST expression could decrease cyclin-dependent kinase (CDK)NIB/p27 (a CDK inhibitor) by repressing ubiquitin specific peptidase 37 (USP37), which could form a complex with p27 to promote its deubiquitination and stabilization, and resulting in blocked cell proliferation [ xref ]."
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"Constitutive expression of USP37 promotes p27 deubiquitination in medulloblastoma cells, whereas a catalytically dead USP37 mutant is unable to stabilize p27.Dobson et al. further explored the molecular basis of REST-induced USP37 downregulation and found that USP37 supresses medulloblastoma tumor growth in an orthotopic mouse model by modulating its downstream targets [87]."
| PMC
"Ectopically expressed wild-type <span class="match term0">USP37</span> formed a complex with <span class="match term1">p27</span>, promoted its deubiquitination and stabilization and blocked cell proliferation."
reach
"Since concomitant loss of REST and USP37 expression attenuated p27 stabilization and differentiation and rescued cell proliferation, our data strongly suggest that repression of USP37 and consequent p27 degradation, are important for REST dependent maintenance of cell proliferation."
reach
"Addition of USP37 to a reaction mix containing HA-ubiquitin and Myc-p27 caused a substantial increase in the 27kD form of p27 and a corresponding decrease in the slower migrating forms of the protein relative to reactions containing USP37 and a protease inhibitor N-ethyl maleimide (NEM) or USP37 C350-S or USP1 (XREF_FIG)."
MiR-320b affects USP37
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MiR-320b activates USP37.
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"The results revealed that 6IH treatment could decrease the expression of miR-320b yet increase that of USP37 and CDT1, and the overexpression of miR-320b could downregulate the expressions of USP37 and CDT1, while the effect of miR-320b mimic on the expressions of miR-320b, USP37, and CDT1 could be counteracted by overexpressed CDT1 (oe-CDT1)."
MiR-320b inhibits USP37.
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MiR-320b decreases the amount of USP37.
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"The results revealed that 6IH treatment could decrease the expression of miR-320b yet increase that of USP37 and CDT1, and the overexpression of miR-320b could downregulate the expressions of USP37 and CDT1, while the effect of miR-320b mimic on the expressions of miR-320b, USP37, and CDT1 could be counteracted by overexpressed CDT1 (oe-CDT1)."
reach
"Based on these observations, we propose that when converging forks stall, USP37 prevents CMG unloading by TRAIP (Fig. 6), and we speculate that a similar phenomenon occurs when mammalian cells are treated with topoisomerase inhibitors.We also found that TRAIP promotes CMG unloading in USP37-depleted extracts even when forks were stalled ~1 kb apart."
reach
"These data thus indicated that USP37 suppresses replisome ubiquitylation and disassembly by TRAIP when CMGs stall at close range for an extended time.To explore the distance-dependence of CMG ubiquitylation, we generated a panel of meDPC substrates in which DPCs were separated by 56, 305, and 1033 bp (Extended Data Fig. 6b, top)."
Snail1 affects USP37
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"Constitutive expression of USP37 promotes p27 deubiquitination in medulloblastoma cells, whereas a catalytically dead USP37 mutant is unable to stabilize p27.Dobson et al. further explored the molecular basis of REST-induced USP37 downregulation and found that USP37 supresses medulloblastoma tumor growth in an orthotopic mouse model by modulating its downstream targets [87]."
| PMC
reach
"In medulloblastomas, REST expression could decrease cyclin dependent kinase (CDK) NIB and p27 (a CDK inhibitor) by repressing ubiquitin specific peptidase 37 (USP37), which could form a complex with p27 to promote its deubiquitination and stabilization, and resulting in blocked cell proliferation [XREF_BIBR]."
sparser
"In the case of K48-linked substrates, binding of the UIMs to the proximal Ub increased catalytic efficiency of USP37 largely through k cat and to a lesser degree through K M . This result was somewhat counter-intuitive since we expected that binding of the UIMs of USP37 to Ub to have a more pronounced effect on K M (a proxy for binding affinity) since others have shown that UIM mutations perturbed the ability to pull down Ub conjugates xref ."
USP37 activates USP37.
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"Ambiguously, the transcription of USP37 is suppressed in medulloblastoma cells through the activity of RE1 silencing transcription factor to prevent the USP37 mediated stabilization of the cyclin dependent kinase inhibitor p27, which is known to act as a negative regulator of cell cycle XREF_BIBR."
USP37 increases the amount of USP37.
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"The results showed reduced survival of U2OS cells in colony formation assays after USP37 inhibition and exposure to HU-mediated replication stress, while overexpression of USP37 led to enhanced survival in response to HU (Fig. 4A), suggesting that USP37 plays a crucial role in aiding the survival of osteosarcoma cells under replication stress.Exposure to replication stress has been shown to affect the spatial localization and levels of USP37 and its associated interacting partners."
USP37 decreases the amount of USP37.
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USP37 deubiquitinates USP37.
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"Given that we have previously demonstrated USP37's interaction with CHK1 its ability to enhance CHK1 activity [ xref ], both of which are closely associated with replication fork movement, and that USP37 is also known to play a crucial role in the Homologous Recombination pathway [ xref ], we conducted a DNA fiber assay to evaluate replication fork movement at the single molecule level."
reach
"We did observe deubiquitination of CHK1 in the same assay, consistent with earlier reports.Given that we have previously demonstrated USP37's interaction with CHK1 its ability to enhance CHK1 activity [23], both of which are closely associated with replication fork movement, and that USP37 is also known to play a crucial role in the Homologous Recombination pathway [55], we conducted a DNA fiber assay to evaluate replication fork movement at the single molecule level."
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USP37 binds.
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USP37 is active.
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USP37 translocates.
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"A recent study demonstrated that HBx, an oncoprotein of the hepatitis B virus and a regulator of hepatocarcinogenesis, promoted the translocation of USP37 from the nucleoplasm to the cytoplasm and that the degradation of USP37 seemed to be prevented by the E3 ligases, APC/CDH1 and SCF/β-TrCP [ xref ]."
reach
"Our study has found that USP37 interacts with PCNA, a central replication factor, and has a higher affinity for PCNA-DNA complex than for PCNA alone.We propose a model where USP37 is recruited to the replication fork by interacting with PCNA at high or physiological levels of USP37."
USP37 affects apoptotic process
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USP37 inhibits apoptotic process.
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USP37 activates apoptotic process.
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"The inactivation of APC and C-CDH 1 is reinforced through the ubiquitin dependent degradation of CDH1 in S phase by the SKP1-Cullin-F-box (SCF) family ubiquitin ligase, SCF-cyclin F, as well as through deubiquitination of the critical APC and C-CDH 1 target cyclin A2 in late G1 and S phases by the E2F induced deubiquitinase USP37."
USP37 affects homologous recombination
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USP37 activates homologous recombination.
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USP37 inhibits homologous recombination.
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USP37 affects cell migration
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USP37 activates cell migration.
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USP37 inhibits cell migration.
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USP37 affects 14-3-3gamma
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USP37 affects Neoplasm Metastasis
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USP37 activates Neoplasm Metastasis.
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USP37 inhibits Neoplasm Metastasis.
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USP37 inhibits Neoplasm Metastasis. 1 / 1
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"In medulloblastomas, REST expression could decrease cyclin-dependent kinase (CDK)NIB/p27 (a CDK inhibitor) by repressing ubiquitin specific peptidase 37 (USP37), which could form a complex with p27 to promote its deubiquitination and stabilization, and resulting in blocked cell proliferation [ xref ]."
USP37 affects stemness
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USP37 affects cell invasion
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USP37 affects cell cycle
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USP37 activates cell cycle.
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USP37 inhibits cell cycle.
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USP37 inhibits cell cycle. 2 / 2
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"Established PLK1-dependent degradation substrates include EMI1 (Hansen et al. 2004; Moshe et al. 2004) and USP37 (Burrows et al. 2012), both of which antagonize the cell cycle E3 APC/C; WEE1 (Watanabe et al. 2004), which controls cyclin dependent kinase activity; and Claspin (Peschiaroli et al. 2006; Mailand et al. 2006; Mamely et al. 2006), which promotes DNA damage checkpoint signaling in S-phase."
USP37 affects 14-3-3γ
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E3_Ub_ligase affects USP37
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E3_Ub_ligase binds USP37.
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E3_Ub_ligase activates USP37.
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E3_Ub_ligase ubiquitinates USP37.
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E3_Ub_ligase ubiquitinates USP37. 1 / 1
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"Given that we have previously demonstrated USP37's interaction with CHK1 its ability to enhance CHK1 activity [ xref ], both of which are closely associated with replication fork movement, and that USP37 is also known to play a crucial role in the Homologous Recombination pathway [ xref ], we conducted a DNA fiber assay to evaluate replication fork movement at the single molecule level."
reach
"We did observe deubiquitination of CHK1 in the same assay, consistent with earlier reports.Given that we have previously demonstrated USP37's interaction with CHK1 its ability to enhance CHK1 activity [23], both of which are closely associated with replication fork movement, and that USP37 is also known to play a crucial role in the Homologous Recombination pathway [55], we conducted a DNA fiber assay to evaluate replication fork movement at the single molecule level."
USP37 affects Snail1 protein
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USP37 affects RAP80-BRCA1
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USP37 affects Carcinogenesis
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USP37 activates Carcinogenesis. 4 / 4
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"207 In addition to Fbw7 , other E3 ligases , such as beta-TrCP1 , CHIP and FBXO32 , can also ubiquitinate c-Myc , mediate its subsequent degradation and inhibit tumorigenesis.208-210 Moreover , the USP37 and USP36 can promote tumorigenesis by stabilizing c-Myc.211 ,212 By mass spectrometry , SUMO ligase protein inhibitor of activated STAT ( PIAS ) and Sentrin-specific protease 7 ( SENP7 ) were also found to control the SUMOylation of c-Myc at K326 and regulate its ubiquitination and degradation ( Fig. 2c ) .213 Ubiquitination regulates p53 p53 , one of the most important tumor suppressors , works in multiple cellular processes , such as cell cycle regulation , DNA repair and apoptosis ."
"Flow cytometry analysis of the HBx-expressing cells showed deregulation of cell cycle apparently due to the enhanced gene expression and stabilization of <span class="match term0">USP37</span> protein and deubiquitination of <span class="match term1">Cyclin A</span> by <span class="match term0">USP37</span>"
14-3-3γ affects USP37
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Valproic acid affects USP37
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Hsa-miR-19b-3p affects USP37
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USP37 affects polyubiquitin chains
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USP37 activates polyubiquitin chains.
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USP37 inhibits polyubiquitin chains.
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"Interestingly, RAP80 's access to polyubiquitin chains assembled by RNF8 and RNF168 is regulated by HR promoting factors such as RNF169, which competes with RAP80 for binding sites on polyubiquitin [XREF_BIBR], and the DUBs USP26 and USP37, which degrade polyubiquitin chains to reduce RAP80 accumulation [XREF_BIBR]."
USP37 affects migration
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"Accumulating evidence has demonstrated that USP37 promotes lung cancer cell proliferation , migration , and invasion16 but inhibits lung cancer cell apoptosis in a deubiquitination-dependent manner.19 Therefore , it is possible that IH-mediated miR-320b reduction in lung cancer cells resulted in the upregulation of USP37 , which further promoted cancer cell proliferation , invasion , and survival ."
USP37 affects E3_Ub_ligase
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USP37 binds E3_Ub_ligase.
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USP37 inhibits E3_Ub_ligase.
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USP37 inhibits E3_Ub_ligase. 1 / 1
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USP37 affects Deubiquitinase
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USP37 affects DNA Breaks, Double-Stranded
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USP37 activates DNA Breaks, Double-Stranded.
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USP37 inhibits DNA Breaks, Double-Stranded.
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USP37 inhibits DNA Breaks, Double-Stranded. 1 / 1
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USP37 affects Cell Survival
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USP37 activates Cell Survival.
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USP37 inhibits Cell Survival.
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USP37 inhibits Cell Survival. 1 / 1
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CDK1/2i affects USP37
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CDK1/2i decreases the amount of USP37.
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"As shown in Fig. 6 C and Fig. S3 D, overexpression of USP37 resulted in an evident decrease in polyubiquitination of ERK1/2, while CDK1/2 inhibitors reversed this function.Intriguingly, we found that CDK1/2i treatment also markedly decreased USP37 protein levels but led to a significant increase in USP37 polyubiquitination (Fig. 6, A and B; and Fig. S3, A–C and E)."
CDK1/2i deubiquitinates USP37.
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"As shown in Fig. 6 C and Fig. S3 D, overexpression of USP37 resulted in an evident decrease in polyubiquitination of ERK1/2, while CDK1/2 inhibitors reversed this function.Intriguingly, we found that CDK1/2i treatment also markedly decreased USP37 protein levels but led to a significant increase in USP37 polyubiquitination (Fig. 6, A and B; and Fig. S3, A–C and E)."
14-3-3gamma affects USP37
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Sodium arsenate affects USP37
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Hsa-miR-30c-5p affects USP37
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Hsa-miR-19a-3p affects USP37
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Bisphenol A affects USP37
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USP37 affects tumorigenicity
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USP37 affects tumor growth MCF-7 ADR cells
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USP37 affects smoothened signaling pathway
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USP37 inhibits smoothened signaling pathway.
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USP37 inhibits smoothened signaling pathway. 1 / 1
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USP37 activates smoothened signaling pathway.
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USP37 activates smoothened signaling pathway. 1 / 1
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USP37 affects signal transduction
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USP37 affects purmorphamine
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USP37 affects glycolytic process
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USP37 activates glycolytic process. 2 / 2
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"However, whether USP37 influences keloid formation through regulating SALL4 deubiquitination is unknown.Here, we hypothesized and demonstrated that USP37 deubiquitinated and stabilized SALL4 to activate PI3K/AKT pathway, thereby promoting proliferation, invasion, migration, extracellular matrix (ECM) accumulation and glycolysis in keloid fibroblasts."
USP37 affects doxorubicin
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USP37 activates doxorubicin. 2 / 2
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USP37 affects SIVmac239 WT
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USP37 affects Osteosarcoma
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USP37 affects LINE1
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USP37 affects LINE-1 elements
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USP37 affects E3 APC/C
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reach
"Established PLK1-dependent degradation substrates include EMI1 (Hansen et al. 2004; Moshe et al. 2004) and USP37 (Burrows et al. 2012), both of which antagonize the cell cycle E3 APC/C; WEE1 (Watanabe et al. 2004), which controls cyclin dependent kinase activity; and Claspin (Peschiaroli et al. 2006; Mailand et al. 2006; Mamely et al. 2006), which promotes DNA damage checkpoint signaling in S-phase."
USP37 affects Breast Neoplasms
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USP37 affects APC CDH1
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UIM3 affects USP37
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"Therefore, the difference in the ability of the UIMs to bind ubiquitin plays a differential role on the kinetic parameters of USP37 depending on the type of ubiquitin chain, shedding light on the mechanism of substrate selection by USP37.When individual UIM mutants were tested, the authors found that UIM2 and UIM3 modulate the ability of USP37 to cleave all ubiquitin chain types, in contrast with that of UIM1."
| PMC
UIM2 affects USP37
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"Therefore, the difference in the ability of the UIMs to bind ubiquitin plays a differential role on the kinetic parameters of USP37 depending on the type of ubiquitin chain, shedding light on the mechanism of substrate selection by USP37.When individual UIM mutants were tested, the authors found that UIM2 and UIM3 modulate the ability of USP37 to cleave all ubiquitin chain types, in contrast with that of UIM1."
| PMC
Vinclozolin affects USP37
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Various affects USP37
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Targeting KEN box degron affects USP37
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eidos
"B In the late G2 / M phase , USP37 acts as a substrate of the APC / C complex via phosphorylation by PLK1 and is further ubiquitinated by betaTrCP for the biphasic degradation , resulting in the downregulation of USP37 , necessary for the G2 / M phase transition Interestingly , the APC-CDH1 complex degrades USP37 in late mitosis by targeting its KEN box degron ."
| PMC
Resveratrol affects USP37
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Protein deubiquitinase affects USP37
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Methyl methanesulfonate affects USP37
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Mechanisms include affects USP37
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Hsa-mir-4775 affects USP37
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Hsa-mir-4501 affects USP37
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Hsa-mir-4280 affects USP37
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Hsa-mir-4264 affects USP37
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Hsa-mir-3164 affects USP37
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Hsa-miR-8060 affects USP37
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Hsa-miR-6828-5p affects USP37
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Hsa-miR-6809-3p affects USP37
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Hsa-miR-5580-5p affects USP37
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Hsa-miR-548av-3p affects USP37
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Hsa-miR-5003-3p affects USP37
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Hsa-miR-4753-3p affects USP37
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Hsa-miR-3591-5p affects USP37
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Hsa-miR-3118 affects USP37
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Hsa-miR-30b-5p affects USP37
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Hsa-miR-302d-5p affects USP37
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Hsa-miR-302b-5p affects USP37
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Hsa-miR-1910-5p affects USP37
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Hsa-miR-191-5p affects USP37
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Hsa-miR-185-3p affects USP37
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Hexabromocyclododecane affects USP37
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Haloperidol affects USP37
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Ethyl methanesulfonate affects USP37
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Dorsomorphin affects USP37
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Dexamethasone affects USP37
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Aristolochic acid A affects USP37
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Amosite asbestos affects USP37
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Aflatoxin B1 affects USP37
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WP1130 affects USP37
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Ub-binding site affects USP37
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USP37 affects tumorigenicity MCF-7
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USP37 affects tumorigenesis lung cancer
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USP37 affects tumor growth
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USP37 affects tumor MCF-7 ADR cells
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USP37 affects stemness cell invasion EMT breast cancer
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USP37 affects spindle assembly
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USP37 inhibits spindle assembly. 1 / 1
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USP37 affects spheroids
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USP37 affects spheroid
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USP37 affects sensitivity cisplatin
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USP37 affects retrotransposition
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USP37 inhibits retrotransposition. 1 / 1
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USP37 affects response to xenobiotic stimulus
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USP37 activates response to xenobiotic stimulus. 1 / 1
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USP37 affects resistance breast cancer cells adriamycin
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USP37 affects replication fork protection
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USP37 activates replication fork protection. 1 / 1
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USP37 inhibits protein-containing complex assembly. 1 / 1
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USP37 affects protein folding
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USP37 activates protein folding. 1 / 1
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USP37 affects polyubiquitination protein
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USP37 affects oncogenic fusion PLZF-RARA
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USP37 affects metabolic process
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USP37 activates metabolic process. 1 / 1
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USP37 affects lung cancer cell
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eidos
"Accumulating evidence has demonstrated that USP37 promotes lung cancer cell proliferation , migration , and invasion16 but inhibits lung cancer cell apoptosis in a deubiquitination-dependent manner.19 Therefore , it is possible that IH-mediated miR-320b reduction in lung cancer cells resulted in the upregulation of USP37 , which further promoted cancer cell proliferation , invasion , and survival ."
USP37 affects invasion migration breast cancer cells
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USP37 affects invading capacity MCF-7 MDA-MB-231 cells
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USP37 affects intrinsic apoptosis including Bcl-2
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USP37 affects hedgehog Hh pathway components Smo
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USP37 affects growth experimental MB
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USP37 affects entry
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USP37 affects drug sensitivity cisplatin
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USP37 affects deubiquitination HIF2alpha kidney cancer
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USP37 affects chromosome segregation
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USP37 activates chromosome segregation. 1 / 1
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USP37 affects cellular
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USP37 affects cellular breast cancer cells
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USP37 affects cell migration capacity
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USP37 affects cell growth
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USP37 inhibits cell growth. 1 / 1
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USP37 affects breast cancer stem-like properties
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USP37 affects bioriented kinetochore-microtubule attachment
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USP37 affects aphidicolin
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USP37 activates aphidicolin. 1 / 1
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USP37 affects adriamycin resistance breast cancer cells
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USP37 affects activation Hh pathway
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USP37 affects Ub-binding site
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USP37 affects Snail1 N-cadherin Vimentin
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reach
"In patients with lung cancer who also experienced OSA, IH induced a decrease in the expression of microRNA-320b, with downstream expression of ubiquitin-specific peptidase 37 (USP37) upregulated secondary to IH and USP37 promoting lung cancer progression by mediating the deubiquitination of Cdc10-dependent transcript 1 (CDT1) (98)."
USP37 affects S/G2/M
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USP37 affects RNF8/168
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USP37 affects Pan et al., 2015
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USP37 affects PM EMT markers
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USP37 affects MCF-7 ADR cancer cells
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USP37 affects K48
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USP37 affects K11
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USP37 affects Infections
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USP37 inhibits Infections. 1 / 1
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USP37 affects Hh targets Smo Gli-1 cell marker Ki-67 tumor tissues
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USP37 affects Hemagglutinins
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USP37 affects HIF2alpha protein stability
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USP37 affects HIF2alpha ccRCC
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USP37 affects HA-14-3-3gamma
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USP37 affects G1
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USP37 affects Drug Resistance
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USP37 activates Drug Resistance. 1 / 1
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USP37 affects DSB repair
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USP37 affects Chemical Sensitivity Human Breast Cancer Cells
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USP37 affects CDT1 protein
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USP37 affects CDT1 deubiquitination miR-320b IH-mediated lung cancer
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eidos
"USP37 promotes the expression of CDT1 by deubiquitination miR-320b impaired IH-mediated lung cancer progression by inhibiting CDT1 expression through targeting USP37 To understand whether the regulation of CDT1 expression by USP37 plays a role in lung cancer cell growth and invasion , the expressions of miR-320b and / or CDT1 in lung cancer cells ( A549 and H1650 ) were altered ."
USP37 affects C-Cdh1
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USP37 affects BC
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USP37 affects APC/C Cdh1
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USP37 affects ADR cells
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eidos
"Knockdown of USP37 reduces the chemoresistance of MCF-7 and MCF-7 / ADR cells against adriamycin and activates the mechanism of apoptosis USP37 gene expression in both MCF-7 and MCF-7 / ADR cells was markedly upregulated by the exposure to adriamycin in a dose-dependent manner ( Figure 5A-D ) ."
USP37 affects ADR cells adriamycin
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S/G2/M affects USP37
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Particulate Matter affects USP37
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Overexpression miR-320b affects USP37
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Osteosarcoma affects USP37
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Osteosarcoma activates USP37. 1 / 1
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reach
"(Additional file 1: Figure S2C, D) as we have recently shown that USP37 regulates tolerance of replication stress by enhancing CHK1 activity so in order to gain insight into genes that correlated with knock down or overexpression of USP37, we proceeded with exome sequencing analysis in osteosarcoma cells overexpressing USP37 or in cells in which USP37 was depleted."
MYC affects Hemagglutinins
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K48 affects USP37
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1
K11 affects USP37
|
1
Hemagglutinins affects USP37
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1
HA-14-3-3gamma affects USP37
|
1
G9a pharmacological affects USP37
|
1
G1 affects USP37
|
1
|
1
EC 3.5.1.98 (histone deacetylase) inhibitor decreases the amount of USP37. 1 / 1
|
1
D-aspartic acid affects USP37
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1
D-aspartic acid increases the amount of USP37. 1 / 1
|
1
Carcinogenesis affects USP37
|
1
Carcinogenesis activates USP37. 1 / 1
|
1
CDK2 inhibitor affects USP37
|
1
C-Cdh1 affects USP37
|
1
APC/C Cdh1 affects USP37
|
1
APC-CDH1 complex affects USP37
|
1
eidos
"B In the late G2 / M phase , USP37 acts as a substrate of the APC / C complex via phosphorylation by PLK1 and is further ubiquitinated by betaTrCP for the biphasic degradation , resulting in the downregulation of USP37 , necessary for the G2 / M phase transition Interestingly , the APC-CDH1 complex degrades USP37 in late mitosis by targeting its KEN box degron ."
| PMC
APC CDH1 affects USP37
|
1
4-hydroxynon-2-enal affects USP37
1
|
2-palmitoylglycerol affects USP37
1
|
1
|
17alpha-ethynylestradiol affects USP37
1
|
14-3-3γ affects MYC
|
1
(R)-pantothenic acid affects USP37
1
|
2,3',4,4',5-pentachlorobiphenyl affects USP37
1
|