IndraLab
Statements
USP4 is modified
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USP4 is phosphorylated.
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USP4 is ubiquitinated.
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USP4 is methylated.
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USP4 is dephosphorylated.
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USP4 is produced.
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"In addition, the relationship between hsa_circ_0001326 and hsa-miR-136-5p, or between hsa-miR-136-5p and USP4 are also need further verify.In brief, we found luteolin promoted M2 polarization and inhibited M1 polarization by upregulating the expression of hsa_circ_0001326, which then mediated the expression of hsa-miR-136-5p and USP4."
USP4 affects cell population proliferation
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USP4 activates cell population proliferation.
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USP4 activates cell population proliferation. 10 / 48
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"TbetaRI stabilized downstream from TGF-beta signaling causes the phosphorylation of Smad2 and 3, the transcription factors responsible for target gene induction [XREF_BIBR], as verified by our result that USP4 fortified Smad2 phosphorylation and promoted migration and proliferation of hepatoma cell."
USP4 inhibits cell population proliferation.
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"In view of the data presented here and previous reports, we propose a working model ( xref ), in which that TNFα rapidly induces Lys63-linked TAK1 polyubiquitnation and binding of USP4 to TAK1, Lys63-linked TAK1 would be rapidly deubiquitinated by USP4 to attenuate the magnitude of TNFα-induced Lys63-linked TAK1 polyubiquitination and TAK1-mediated IKK/NF-κB activation."
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"Although it has been reported that USP4 deubiquitinates TAK1 and negatively regulates TNF- and IL-1-induced activation of NF-kappaB, how TAK1 ubiquitination is regulated in adaptive immune cells such as T cells and whether such a regulation regulates T cell mediated immune response remain unknown."
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"The protein expression of USP4 in liver tissue samples from patients with NAFLD was significantly lower than that of healthy controls, and mechanistically, USP4 inhibits TAK1 degradation by removing the K48-linked ubiquitinated chain, leading to inhibition of signaling activation of the downstream NF-κB and JNK cascades, which in turn reverses the disruption of IRS-AKT-GSK3β signaling, inhibits IR, and thus attenuates hepatic steatosis and inflammation (35)."
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"Molecular analysis revealed that USP4 deficiency augmented the activation of the transforming growth factor beta activated kinase 1 (TAK1)-(JNK1/2)/P38 signaling in response to hypertrophic stress, and blockage of TAK1 activation abolished the pathological effects of USP4 deficiency in vivo."
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"In addition to these newly identified nuclear functions, both USP4 and USP15 are well known to function in the cytosol, i.e. USP4 modulates the Wnt and beta-catenin, NF-kappaB, p53 and TGF-beta signaling pathways while USP15 performs functions in the TGF-beta receptor and NF-kappaB signaling pathways."
sparser
"However, when ALAL-1 was depleted, the SART3-mediated nuclear translocation of USP4 was partially impaired ( xref ), while the interaction between SART3 and USP4 was not affected by depletion of ALAL-1 ( xref ), indicating that ALAL-1 is involved in USP4 relocalization without impairing SART3-USP4 interaction in bulk."
sparser
"Interestingly, the pathways found to be affected by either ALAL-1 or SART3 depletion were previously reported in different studies to be modulated by SART3 directly or indirectly through its interacting partner USP4 ( xref ; xref ; xref ; xref ), suggesting that the interaction of ALAL-1 with SART3 could be regulating the SART3–USP4 complex."
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"In order to verify the importance of the beta-hairpin linker between the DUSP and UBL domains as seen in the crystal structure of SART3 and USP4 complex, we generated a series of mutants, e.g. the linkers of USP4 (124 HGLFVKHC 131) and USP15 (124 QGMFVKHC 131) replaced by the USP11 linker (186 LPNIQ 190) and vice versa, denoted as USP4 L11 and USP15 L11, USP11 L4 and USP11 L15."
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"The complex structure of the NLS on Tip110 and importin 2α is involved a bipartite binding, and removal of Tip110 NLS prevents the entry of USP4 or USP15 in the nucleus and abrogates their subsequent deubiquitinase activity (12, 55), which may explain the detection of a higher ubiquitinated form of cytoplasmic expressed Tip110ΔNLS mutant (
Figures 2D
,
4C, E
)."
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"While it has been reported that overexpressed SART3 causes nuclear localization of exogenously expressed USP4, we found that SART3 depletion from U2OS cells did not detectably affect the nuclear and cytoplasmic distribution of endogenous USP4 (data not shown), suggesting that USP4 nuclear targeting might be mediated by multiple mechanisms."
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"However, in breast cancer, USP4 was also recognized as a tumour suppressor for its up-regulatory effect on programmed cell death 4 (PDCD4) to restrain tumour growth.20 Moreover, USP4 was able to target TRAF2 and TRAF6 for deubiquitination and thereafter inhibited TNFalpha induced cancer cell migration.34 In the present study, we proved that USP4 expression was drastically increased in melanoma."
sparser
"However, when ALAL-1 was depleted, the SART3-mediated nuclear translocation of USP4 was partially impaired ( xref ), while the interaction between SART3 and USP4 was not affected by depletion of ALAL-1 ( xref ), indicating that ALAL-1 is involved in USP4 relocalization without impairing SART3-USP4 interaction in bulk."
sparser
"Interestingly, the pathways found to be affected by either ALAL-1 or SART3 depletion were previously reported in different studies to be modulated by SART3 directly or indirectly through its interacting partner USP4 ( xref ; xref ; xref ; xref ), suggesting that the interaction of ALAL-1 with SART3 could be regulating the SART3–USP4 complex."
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"In order to verify the importance of the beta-hairpin linker between the DUSP and UBL domains as seen in the crystal structure of SART3 and USP4 complex, we generated a series of mutants, e.g. the linkers of USP4 (124 HGLFVKHC 131) and USP15 (124 QGMFVKHC 131) replaced by the USP11 linker (186 LPNIQ 190) and vice versa, denoted as USP4 L11 and USP15 L11, USP11 L4 and USP11 L15."
USP4 affects TA
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"In particular, the genes like TaMKP1, TaECS, TaGGT, TaYqgF, TaGBF1, TaCML11, TaEXPB23, TaWRKY2, SR3WRSI5, TaMYB19, TdSHN1, TaTPS1, TaNHX2, TaWNK1, TaRSL4 A-homeolog, TaAPX7, TaAQP8, TaBIERF3, TaAOX1a, TaPP2C1, PI4K, TaAPXb, TaHsfA7, TaCIPK29, TaMYB30-B, TaHAP2E, TaWRKY19, TaC3H50, TaCLC-1, TaSAMDC, TaSRG, TaSnRK2.7, TaERF4, TaCRT1, TaSOS1, TaHBP1b, TaTPC1, TaSOS2, TaST, TaPUB15, TaAIDFa, TaSIP, TaDi19A, TaRab7, TaCML8, TaMYB3R1, TaSNAC2, TaBADH1, TaMyb3R-2, TaSnRK2.4, TaP5CR, TaCBSX4, TaCIPK14, W69, TaWRKY44, TaMAPK44, TaSDIR1, TaSOD2, TNHXS1, TaNAC, TaRINO1, TaPEX11-1, TaCIPK15, TaSnRK2.8, TaNAC2, TaCML5, TaPOP5, TaSC, TaglyII, TaNAC5, Ta-sro1, TaACA6, TabZIP71, TaSK5, TaNAC47, TaWRKY93, TaABL1, TaSRZ1, Tamyb4, TaMGD, TaNOA1, TaRacB, TaMSRMK3, TaiSAP8, TaDSM1, TaSKIPa, TaAOC1, TaSRWD3, TaCIPK25, TaMIOX, TVP1, TaERF1, Ta-UnP, TaSRWD2, TaABP, TaMSRB, TaWRKY79, TaNIP and TaMAPK1 were expressed in most of the tissues and in all ten developmental stages, as well (Figs. xref , xref )."
| PMC
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"However, Tip110 was found to interact with and promote nuclear translocation of USP4 and USP15 but not USP11, and this is due to β-hairpin of the linker region of the DUSP and UBL domains of both USP4 and USP15 proteins that were associated with the HAT domain of Tip110 ( xref , xref , xref , xref ) In addition, the binding of USP15 to Tip110 is 20-fold stronger than USP4 ( xref )."
sparser
"However, Tip110 was found to interact with and promote nuclear translocation of USP4 and USP15 but not USP11, and this is due to β-hairpin of the linker region of the DUSP and UBL domains of both USP4 and USP15 proteins that were associated with the HAT domain of Tip110 ( xref , xref , xref , xref ) In addition, the binding of USP15 to Tip110 is 20-fold stronger than USP4 ( xref )."
USP4 affects Neoplasm Invasiveness
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USP4 activates Neoplasm Invasiveness.
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USP4 activates Neoplasm Invasiveness. 10 / 41
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"Decreased level of USP4 protein leads to increased ubiquitination of ELAV-like RNA-binding protein 1 (ELAVL1), which in turn increases Rho GDP dissociation inhibitor alpha (ARHGDIA) expression, ultimately promoting migration and invasion of PCa cell.23 METTL3 was also found to affect lymphoid enhancer-binding factor 1 (LEF1) protein levels by affecting m A methylation of LEF1 mRNA, thereby downregulating the activity of wingless/integrated (Wnt) signaling to affect PCa progression."
USP4 inhibits Neoplasm Invasiveness.
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"According to a previous study by Iyengar [XREF_BIBR], Akt promotes USP4 to enter the cell membrane and cytoplasm to phosphorylate USP4 and regulate its subcellular localization, and Akt phosphorylation of USP4 occurs by combining with other de-ubiquitinating enzymes (DUBs) to de-ubiquitinate the TGF-beta receptor [XREF_BIBR]."
sparser
"USP4 inhibits p53- and p53-mediated apoptosis, regulates NF-κB signaling pathway and modulates TGFβ signaling, xref , xref , xref , xref promoting breast cancer xref and lung adenocarcinoma invasiveness. xref We demonstrate here that both USP17 and USP4 are expressed at higher levels in breast and lung cancer cell lines compared to normal cells."
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"Recently, it has been reported that USP4 could antagonize p53 signalling through its deubiquitinating activity.15, 18 Given that Bax and Bcl2 are 2 canonical downstream regulators of p53 in mediating cell apoptosis and were regulated by USP4 in response to cisplatin treatment, we speculated that pro survival effect of USP4 in response to cisplatin treatment may be associated with p53 signalling pathway."
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"In addition to these newly identified nuclear functions, both USP4 and USP15 are well known to function in the cytosol, i.e. USP4 modulates the Wnt and beta-catenin, NF-kappaB, p53 and TGF-beta signaling pathways while USP15 performs functions in the TGF-beta receptor and NF-kappaB signaling pathways."
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"USP4, for example, interacts directly with end resection factors CtIP and MRN [172], USP21 deubiquitinates and stabilizes BRCA2 to promote RAD51 binding and successful HR [173], and USP10 deubiquitinates and stabilizes p53 to promote its nuclear localization and apoptosis in response to DSBs [174]."
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"Studies focused on the other USPs demonstrated that USP14 overexpression regulates IkappaB polyubiquitination to stimulate its degradation 26, and ectopic expression of USP4 inhibits the TRAF2- and TRAF6 stimulated NF-kappaB reporter gene and negatively regulates the TNF-alpha-induced IkappaB-alpha degradation and NF-kappaB activation 27."
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"Indeed, ectopic expression of USP4 WT, but not the C311A mutant, which is still capable of interacting with BRCA1, reduced both endogenous BRCA1 ubiquitylation (Fig. 3a, mostly polyubiquitinated BRCA1 species at high MW) and exogenous-overexpressed BRCA1 ubiquitylation in cells (Fig. 3b), suggesting that the DUB catalytic activity of USP4 is critical for USP4-dependent deubiquitylation of BRCA1."
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"Importantly, we further demonstrate that USP4 mutants (L301R, S315C and R559W) that are defective either in DUB activity or in interacting with BRCA1 can cause significant decrease in BRCA1 protein level and hence confer increased sensitivity to IR or anticancer drugs such as DOX, ETO or PARPi."
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"For instance, USP4 is reported to participate in the control of p53-related signaling through deubiquitinating ARF-BP1 , the suppression of canonical Wnt signaling pathway through deubiquitinating TCF4 , the activation of TGF-β signaling through deubiquitinating substrates like TβR-I and SMAD4 and the inhibition of NF-κB pathway through deubiquitinating mediators like TRAF2, TRAF6 and TAK1 ."
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"Conversely, whereas USP4 and USP15 target p53 inhibiting ligases ARF-BP1 [XREF_BIBR] and MDM2 [XREF_BIBR], respectively, USP11 stabilizes p53 [XREF_BIBR] as well as several other tumor suppressors including PML [XREF_BIBR], BRCA2 [XREF_BIBR] and Mre11 complex members MRE11 & RAD50 [XREF_BIBR]."
sparser
"In view of the data presented here and previous reports, we propose a working model ( xref ), in which that TNFα rapidly induces Lys63-linked TAK1 polyubiquitnation and binding of USP4 to TAK1, Lys63-linked TAK1 would be rapidly deubiquitinated by USP4 to attenuate the magnitude of TNFα-induced Lys63-linked TAK1 polyubiquitination and TAK1-mediated IKK/NF-κB activation."
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"Molecular analysis revealed that USP4 deficiency augmented the activation of the transforming growth factor beta activated kinase 1 (TAK1)-(JNK1/2)/P38 signaling in response to hypertrophic stress, and blockage of TAK1 activation abolished the pathological effects of USP4 deficiency in vivo."
reach
"In addition to these newly identified nuclear functions, both USP4 and USP15 are well known to function in the cytosol, i.e. USP4 modulates the Wnt and beta-catenin, NF-kappaB, p53 and TGF-beta signaling pathways while USP15 performs functions in the TGF-beta receptor and NF-kappaB signaling pathways."
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"Collectively, our results support the concept that dysregulation of miR-148a is associated with the poor prognosis of HCC and may account for the tumor progression to advanced stages, and that, of the newly identified targets, USP4 overexpression may contribute to HCC progression towards more aggressive feature presumably by facilitating TGF-beta signaling pathways, growth advantage and migrating capability."
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"USP4 can serve as a double-edged sword in tumor progression because it functions as a tumor suppressor in lung cancer by indirectly circumventing stemness [56], while USP4 promotes TNBC metastasis by enhancing TGF-β signaling and inducing the suppressive activity of Tregs [87, 119]."
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"In this context, to achieve a certain biological outcome, the same DUB can regulate the pathway at different levels (e.g., USP15 and USP4 promote signaling by targeting the TGF-beta receptor and the effector SMADs) or multiple DUBs can act on the same target (e.g., USP15 and OTUB1 promote signaling through stabilizing R-SMADs)."
sparser
"The proteasome has both ubiquitin ligases and DUBs that associate with it (Crosas et al., 2006) , and several DUB-ligase pairs interact directly, including BRCC36-BRCA1, BAP1-BRCA1, USP4-Ro52, USP7-MDM2, USP8-GRAIL, USP20-pVHL, USP33-pVHL and USP44-APC (Kee and Huibregtse, 2007; Marfany and Denuc, 2008; Ventii and Wilkinson, 2008) ."
USP4 affects apoptotic process
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USP4 activates apoptotic process.
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USP4 activates apoptotic process. 10 / 16
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"The silencing of USP4 can inhibit the apoptosis of cancer cells and increase the persistent survival rate of HNSCC, as immunosuppressive diseases, UXP9X, CYLD1, and BPLF1 accelerate the development of HNSCC through the escape inhibition mechanism of immune cells or promoting the spread of virus infection."
USP4 inhibits apoptotic process.
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USP4 affects Neoplasm Metastasis
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USP4 activates Neoplasm Metastasis.
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USP4 activates Neoplasm Metastasis. 10 / 22
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"Studies have shown that USP4 plays an important role in rectal cancer bladder cancer melanoma The high expression of USP4 in liver cancer and cervical squamous cell carcinoma implies that USP4 may be a potential oncogene, and it has been confirmed that the abnormal expression of USP4 promotes the occurrence, development, invasion and metastasis of rectal cancer ."
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"Hematoxylin-eosin (H&E) staining was carried out to assess lung nodules in mice based on the tissue structure and nuclei, and the staining results also showed that USP4 knockdown inhibited the lung metastasis of KYSE150 cells, while USP4 overexpression in KYSE180 cells promoted lung metastasis in vivo (Fig. 3G, H)."
USP4 inhibits Neoplasm Metastasis.
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"Since our data showed that Rheb ubiquitination was inhibited by EGF treatment (Fig. xref ), we examined whether the interaction between USP4 and Rheb was affected by EGF treatment and found that EGF treatment promoted their interaction at both endogenous and exogenous level (Fig. xref and Supplementary information, Fig. xref )."
USP4 affects cell migration
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USP4 activates cell migration.
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USP4 inhibits cell migration.
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USP4 inhibits cell migration. 8 / 8
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"However, in breast cancer, USP4 was also recognized as a tumour suppressor for its up-regulatory effect on programmed cell death 4 (PDCD4) to restrain tumour growth.20 Moreover, USP4 was able to target TRAF2 and TRAF6 for deubiquitination and thereafter inhibited TNFalpha induced cancer cell migration.34 In the present study, we proved that USP4 expression was drastically increased in melanoma."
USP4 activates USP4.
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"Furthermore, gastrodin significantly upregulated the expression of USP4 and increased the binding of USP4 to the insulin receptor.Considering the importance of the PI3K-Akt pathway in the pathogenesis of T2DM, we detected the effects of gastrodin on the PI3K-Akt pathway to further explore the underlying mechanism of gastrodin in ameliorating insulin resistance."
USP4 increases the amount of USP4.
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USP4 phosphorylates USP4.
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USP4 inhibits USP4.
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USP4 decreases the amount of USP4.
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"However, in breast cancer, USP4 was also recognized as a tumour suppressor for its up-regulatory effect on programmed cell death 4 (PDCD4) to restrain tumour growth.20 Moreover, USP4 was able to target TRAF2 and TRAF6 for deubiquitination and thereafter inhibited TNFalpha induced cancer cell migration.34 In the present study, we proved that USP4 expression was drastically increased in melanoma."
sparser
"Second, the role of the CENPF-USP4 axis in CRC metastasis has been identified, but the specific downstream molecular mechanisms remain unclear and require further investigation, In particular, the role of autophagy activation in mediating CRC metastasis through CENPF requires more in-depth exploration."
sparser
"In summary, our groundbreaking research, for the first time, has unveiled CENPF as a novel promoter of CRC metastasis and elucidate the molecular mechanism of the interaction between CENPF and USP4 in inducing migration and invasion of colorectal cancer cells, evidenced from molecular, cellular, animal models, and clinical specimens."
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"Furthermore, knockdown of FBXO3-induced down-regulation of USP4 could not be rescued by either lysosome inhibitor (chloroquine) or proteasome inhibitor (MG132) (Fig 4A and 4B), suggesting that knockdown of FBXO3-induced down-regulation of USP4 is unlikely to be at the transcriptional levels or at the levels of the proteasome-/lysosome-mediated protein stability.It has been reported that aspartyl aminopeptidase (DNPEP) can bind to and degrade USP4 [38]."
sparser
"Second, the role of the CENPF-USP4 axis in CRC metastasis has been identified, but the specific downstream molecular mechanisms remain unclear and require further investigation, In particular, the role of autophagy activation in mediating CRC metastasis through CENPF requires more in-depth exploration."
sparser
"In summary, our groundbreaking research, for the first time, has unveiled CENPF as a novel promoter of CRC metastasis and elucidate the molecular mechanism of the interaction between CENPF and USP4 in inducing migration and invasion of colorectal cancer cells, evidenced from molecular, cellular, animal models, and clinical specimens."
sparser
"The proteasome has both ubiquitin ligases and DUBs that associate with it (Crosas et al., 2006) , and several DUB-ligase pairs interact directly, including BRCC36-BRCA1, BAP1-BRCA1, USP4-Ro52, USP7-MDM2, USP8-GRAIL, USP20-pVHL, USP33-pVHL and USP44-APC (Kee and Huibregtse, 2007; Marfany and Denuc, 2008; Ventii and Wilkinson, 2008) ."
reach
"In addition to these newly identified nuclear functions, both USP4 and USP15 are well known to function in the cytosol, i.e. USP4 modulates the Wnt and beta-catenin, NF-kappaB, p53 and TGF-beta signaling pathways while USP15 performs functions in the TGF-beta receptor and NF-kappaB signaling pathways."
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"These results indicate that FBXO3 increases Twist1 and USP4 protein expression in an E3 ligase activity-independent manner, in which the FBXO3-ApaG domain is indispensable.To investigate the causal effects of USP4 on FBXO3-induced Twist1 expression and cell migration, we performed rescuing experiments."
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"Specifically, up-regulated USP4 potentiated the growth and invasion of colorectal cancer though deubiquitination and stabilization of PRL-3.19 In addition, USP4 transduced Akt activation to TGF-beta signalling by deubiquitinating and stabilizing TGF-beta type I receptor, thus augmented breast cancer cell invasion and migration.33 These studies demonstrate USP4 as a powerful tumour promoter and an important determinant for canonical oncogenic signalling."
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"USP4, for example, interacts directly with end resection factors CtIP and MRN [172], USP21 deubiquitinates and stabilizes BRCA2 to promote RAD51 binding and successful HR [173], and USP10 deubiquitinates and stabilizes p53 to promote its nuclear localization and apoptosis in response to DSBs [174]."
sparser
"Since our data showed that Rheb ubiquitination was inhibited by EGF treatment (Fig. xref ), we examined whether the interaction between USP4 and Rheb was affected by EGF treatment and found that EGF treatment promoted their interaction at both endogenous and exogenous level (Fig. xref and Supplementary information, Fig. xref )."
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"USP4, for example, interacts directly with end resection factors CtIP and MRN [172], USP21 deubiquitinates and stabilizes BRCA2 to promote RAD51 binding and successful HR [173], and USP10 deubiquitinates and stabilizes p53 to promote its nuclear localization and apoptosis in response to DSBs [174]."
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"Interestingly, these speculations have been confirmed that HECW1 can promote the proliferation, migration and invasion of cancer cells by inducing the ubiquitination and degradation of SMAD4 (34), while USP4 can mediate the deubiquitination of SMAD4, leading to the expression of apoptotic proteins (35)."
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"Furthermore, knockdown of FBXO3-induced down-regulation of USP4 could not be rescued by either lysosome inhibitor (chloroquine) or proteasome inhibitor (MG132) (Fig 4A and 4B), suggesting that knockdown of FBXO3-induced down-regulation of USP4 is unlikely to be at the transcriptional levels or at the levels of the proteasome-/lysosome-mediated protein stability.It has been reported that aspartyl aminopeptidase (DNPEP) can bind to and degrade USP4 [38]."
USP4 affects signal transduction
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USP4 activates signal transduction.
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USP4 inhibits signal transduction.
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USP4 inhibits signal transduction. 3 / 3
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"This study demonstrates that inhibition of USP4 to activate Keap1-Nrf2-ARE signaling pathway may represent a mechanism by which vialinin A conferred protection against cerebral ischaemia‒reperfusion injury and sheds light on its promising prospects as a therapeutic intervention for ischaemic stroke."
USP4 affects inflammatory response
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USP4 inhibits inflammatory response.
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USP4 inhibits inflammatory response. 7 / 7
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"Notably, this study found that reactivating the TRAF6 pathway negated the effects of USP4 on microglial inflammation and subsequent neuron injuries.Collectively, this study highlighted that the USP4 elevation suppressed microglia activation-evoked inflammation and neuron injury by inhibiting the TRAF6-NF-κB pathway."
USP4 activates inflammatory response.
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USP4 activates epithelial to mesenchymal transition.
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USP4 activates epithelial to mesenchymal transition. 10 / 10
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"Our study showed that after interfering with USP4 expression, lung adenocarcinoma cells changed from a long spindle shape to round, the migration and invasion abilities of cells decreased, N-cadherin expression decreased, and E-cadherin expression increased, indicating that USP4 promoted the invasion and migration of lung adenocarcinoma cells by promoting the EMT of cancer cells."
USP4 inhibits epithelial to mesenchymal transition.
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"Mechanistically, EVO directly interacts with USP4, thereby disrupting the protein stability of SOX9.In this study, we demonstrated that evodiamine inhibits colorectal cancer (CRC) stemness by disrupting USP4-mediated SOX9 stabilization, providing novel insights into the molecular mechanisms of CRC progression."
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"In androgen treatment-sensitive prostate cancer, METTL3 mediates m6A modification of USP4 mRNA at A2696, and m6A reader protein YTHDF2 binds to and induces degradation of USP4 mRNA, increasing the expression of Rho GDP dissociation inhibitor alpha (ARHGDIA) protein and promoting migration and invasion [182]."
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"Given the key role of m 6 A mRNA methylation in affecting mRNA stability, it was reasonable to speculate that METTL3 knockdown reduces the m 6 A modification levels in USP4 mRNA and thus increase USP4 mRNA levels by atenuating the inhibitory effect of m 6 A modification on USP4 mRNA stability."
sparser
"This study reveals a non-canonical function of the E3 ubiquitin ligase FBXO3 in PI3K-induced breast cancer metastasis, showing that FBXO3 binds to and protects USP4 from aspartyl aminopeptidase (DNPEP)-mediated degradation, resulting in Twist1 protein stabilization and increased tumor metastasis."
sparser
"We carried out ubiquitination assays by co-transfecting HEK293T cells with a Myc-HDAC2 expression plasmid plus His and Flag empty vectors, His-Ubiquitin and Flag empty vectors, His-Ubiquitin, Flag-USP4 and Flag empty vectors,or His-Ubiquitin, Flag-USP4 and Flag-TRPS1 vectors and compared them with cells transfected with Myc plus His vector and Flag-empty vectors."
sparser
"This study reveals a non-canonical function of the E3 ubiquitin ligase FBXO3 in PI3K-induced breast cancer metastasis, showing that FBXO3 binds to and protects USP4 from aspartyl aminopeptidase (DNPEP)-mediated degradation, resulting in Twist1 protein stabilization and increased tumor metastasis."
USP4 affects homologous recombination
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USP4 activates homologous recombination.
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USP4 activates homologous recombination. 4 / 4
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USP4 activates homologous recombination. 3 / 3
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"USP4 was found to enhance DNA double-strand breaks repairment , DNA-end resection and homologous recombination via a conversed and specific domain to form a complex with CtIP and the MRE11-RAD50-NBS1 complex which can be abrogated by USP4 auto-deubiquitination on several specific cysteine residues ."
USP4 bound to RBBP8 activates homologous recombination. 1 / 1
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USP4 phosphorylates homologous recombination.
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USP4 affects cell differentiation
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USP4 inhibits cell differentiation.
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USP4 inhibits cell differentiation. 5 / 5
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"The role of USP4 in many pathological and physiological processes has been reported; USP4 promotes breast cancer invasive migration through the relaxin2-mediated TGF-β1/Smad2/MMP-9 pathway [31]; USP4 inhibits myogenic cell differentiation by catalyzing MyoD activity [32]; The H19/miR-148a/USP4 axis promotes hepatic stellate cells by enhancing and TGF-β signaling in hepatocytes to promote liver fibrosis [33]."
USP4 activates cell differentiation.
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"In conclusion, these findings highlight the interaction between USP4 and RAB7A as a promising target for therapeutic intervention in managing periodontal diseases.Abbreviation: 3-MA: 3-methyladenine; Baf A1:bafilomycin A 1 ; BECN1: beclin 1, autophagy related; CEJ-ABC: cementoenamel junctionto alveolar bone crest; IL1B/IL-1beta: interleukin 1 beta; KD:knockdown; LPS: lipopolysaccharide; MOI: multiplicity of infection;OE: overexpression; P.g."
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"In summary, our findings collectively suggest that reduced USP4 levels mediate RAB7A ubiquitination, disrupting lysosomal trafficking and autophagosome-lysosome fusion, which contributes to the development and progression of periodontitis.As evidenced by numerous studies, autophagy plays a dual and complex role in the preservation of periodontal homeostasis [46–48]."
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"In this study, our investigation revealed that the ubiquitination of RAB7A, mediated by reduced levels of the deubiquitinating enzyme USP4 (ubiquitin specific peptidase 4), disrupts normal lysosomal trafficking and autophagosome-lysosome fusion, thereby contributing significantly to periodontitis progression."
USP4 affects cell growth
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USP4 inhibits cell growth.
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USP4 inhibits cell growth. 5 / 5
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"Previous studies have shown that USP4 expression was significantly decreased in breast cancer tissue and that USP4 inhibited breast cancer cell growth through inhibiting PDCD4 degradation. xref USP4 was downregulated in lung adenocarcinoma and served as an independent predictor. xref Some other studies claimed that USP4 might have oncogenic properties."
USP4 activates cell growth.
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"To confirm complex formation of endogenous components, proximity ligation assay (PLA) was performed using the breast cancer cell line MDA-231-BM, known to produce high levels of hyaluronan. xref Using antibodies against HAS2 and USP4 or USP17, reactive signals in the form of red dots indicating interactions between endogenous HAS2 and USP17, and HAS2 and USP4, were observed; only a low background level of dots was seen when each antibody was used alone, or in the fixation control without antibody ( xref )."
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"Furthermore, gastrodin significantly upregulated the expression of USP4 and increased the binding of USP4 to the insulin receptor.Considering the importance of the PI3K-Akt pathway in the pathogenesis of T2DM, we detected the effects of gastrodin on the PI3K-Akt pathway to further explore the underlying mechanism of gastrodin in ameliorating insulin resistance."
sparser
"In mpkCCD14 cells, USP4 could be immunoprecipitated with an anti-AQP2 antibody, and prior treatment with dDAVP had no clear effect on the interaction, as shown in xref A. Similar results were obtained in MDCK-hAQP2 cells, as shown in xref B, with an interaction between AQP2 and USP4 observed under control conditions, or after treatment of cells with the adenylate cyclase activator forskolin (MDCK-hAQP2 cells have limited response to VP)."
sparser
"USP4 and AQP2 were detected in samples immunoprecipitated using either anti-AQP2 or anti-USP4, confirming that a USP4 and AQP2 interaction occurs in vivo, as shown in xref C. Similar to the cultured cell experiments, prior stimulation of the tubule suspensions with dDAVP had no clear effect on the USP4-AQP2 interaction, as shown in xref C."
sparser
"The characteristic pattern [ xref ] of ubiquitylated AQP2 was observed in the immunoprecipitated samples, as shown in xref A. Incubation of immunoprecipitated AQP2 with enzymatically active USP4, but not active USP30, significantly decreased the levels of ubiquitylated AQP2 compared to the control condition, as shown in xref B. This data indicates that a direct and functional interaction between USP4 and AQP2 can occur in vitro to modulate AQP2 ubiquitylation."
reach
"Furthermore, gastrodin significantly upregulated the expression of USP4 and increased the binding of USP4 to the insulin receptor.Considering the importance of the PI3K-Akt pathway in the pathogenesis of T2DM, we detected the effects of gastrodin on the PI3K-Akt pathway to further explore the underlying mechanism of gastrodin in ameliorating insulin resistance."
reach
"Our results indicate that gastrodin promotes the phosphorylation of GATA1 via the PI3K/AKT pathway, enhances the transcriptional activity of GATA1, and then increases the expression level of USP4, thereby reducing the ubiquitination and degradation of insulin receptors and ultimately improving insulin resistance."
reach
"The results of the study showed that gastrodin promotes the phosphorylation of GATA1 via the PI3K/AKT pathway, increases the transcriptional activity of GATA1, and subsequently increases the expression level of USP4, thereby reducing the ubiquitination and degradation of insulin receptors, and ultimately improving insulin resistance."
sparser
"In mpkCCD14 cells, USP4 could be immunoprecipitated with an anti-AQP2 antibody, and prior treatment with dDAVP had no clear effect on the interaction, as shown in xref A. Similar results were obtained in MDCK-hAQP2 cells, as shown in xref B, with an interaction between AQP2 and USP4 observed under control conditions, or after treatment of cells with the adenylate cyclase activator forskolin (MDCK-hAQP2 cells have limited response to VP)."
sparser
"USP4 and AQP2 were detected in samples immunoprecipitated using either anti-AQP2 or anti-USP4, confirming that a USP4 and AQP2 interaction occurs in vivo, as shown in xref C. Similar to the cultured cell experiments, prior stimulation of the tubule suspensions with dDAVP had no clear effect on the USP4-AQP2 interaction, as shown in xref C."
sparser
"The characteristic pattern [ xref ] of ubiquitylated AQP2 was observed in the immunoprecipitated samples, as shown in xref A. Incubation of immunoprecipitated AQP2 with enzymatically active USP4, but not active USP30, significantly decreased the levels of ubiquitylated AQP2 compared to the control condition, as shown in xref B. This data indicates that a direct and functional interaction between USP4 and AQP2 can occur in vitro to modulate AQP2 ubiquitylation."
USP4 affects activation
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7
USP4 affects E3_Ub_ligase
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6
1
USP4 deubiquitinates E3_Ub_ligase.
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4
USP4 binds E3_Ub_ligase.
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2
1
USP4 affects P-Inter
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6
sparser
"Lastly, a comparison of F-Block-Unp ABB (effectively an overshadowing treatment) with P-Inter-Unp ABB (effectively an overshadowing control condition) detected no appreciable difference, which indicates that with the present parameters no appreciable overshadowing of X by Y occurred when testing occurred in Context B, F (1, 72) = 1.72, p = ."
USP4 affects Interferon
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6
USP4 inhibits Interferon.
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4
USP4 activates Interferon.
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2
P-Inter affects USP4
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6
sparser
"Lastly, a comparison of F-Block-Unp ABB (effectively an overshadowing treatment) with P-Inter-Unp ABB (effectively an overshadowing control condition) detected no appreciable difference, which indicates that with the present parameters no appreciable overshadowing of X by Y occurred when testing occurred in Context B, F (1, 72) = 1.72, p = ."
sparser
"To confirm complex formation of endogenous components, proximity ligation assay (PLA) was performed using the breast cancer cell line MDA-231-BM, known to produce high levels of hyaluronan. xref Using antibodies against HAS2 and USP4 or USP17, reactive signals in the form of red dots indicating interactions between endogenous HAS2 and USP17, and HAS2 and USP4, were observed; only a low background level of dots was seen when each antibody was used alone, or in the fixation control without antibody ( xref )."
Vialinin A affects USP4
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5
reach
"During the course of our studies, we observed that mutating theUSP4 catalytic cysteine to alanine (C311A) to render USP4 enzymatically inactive (" catalytic-dead " [CD]), almost totally abrogated its interactions with CtIP and MRN (XREF_FIG A; note that binding of USP4 to CtIP and RAD50 was not abrogated by the DNA intercalating agent ethidium bromide (EtBr), suggesting that interaction was not mediated by DNA bridging."
USP4 affects CS
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5
USP4 affects Adenocarcinoma of Lung
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5
USP4 activates Adenocarcinoma of Lung. 5 / 5
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5
reach
"Our study showed that after interfering with USP4 expression, lung adenocarcinoma cells changed from a long spindle shape to round, the migration and invasion abilities of cells decreased, N-cadherin expression decreased, and E-cadherin expression increased, indicating that USP4 promoted the invasion and migration of lung adenocarcinoma cells by promoting the EMT of cancer cells."
reach
"During the course of our studies, we observed that mutating theUSP4 catalytic cysteine to alanine (C311A) to render USP4 enzymatically inactive (" catalytic-dead " [CD]), almost totally abrogated its interactions with CtIP and MRN (XREF_FIG A; note that binding of USP4 to CtIP and RAD50 was not abrogated by the DNA intercalating agent ethidium bromide (EtBr), suggesting that interaction was not mediated by DNA bridging."
reach
"In conclusion, these findings highlight the interaction between USP4 and RAB7A as a promising target for therapeutic intervention in managing periodontal diseases.Abbreviation: 3-MA: 3-methyladenine; Baf A1:bafilomycin A 1 ; BECN1: beclin 1, autophagy related; CEJ-ABC: cementoenamel junctionto alveolar bone crest; IL1B/IL-1beta: interleukin 1 beta; KD:knockdown; LPS: lipopolysaccharide; MOI: multiplicity of infection;OE: overexpression; P.g."
CS affects USP4
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5
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4
USP4 inhibits skeletal muscle tissue development.
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2
USP4 activates skeletal muscle tissue development.
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2
USP4 affects myoblast differentiation
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4
USP4 affects insulin receptors
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4
USP4 affects innate immune response
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4
USP4 inhibits innate immune response.
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2
USP4 activates innate immune response.
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2
USP4 affects activity
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4
USP4 affects UBL
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4
USP4 affects Proteasome
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2
reach
"The role of USP4 in many pathological and physiological processes has been reported; USP4 promotes breast cancer invasive migration through the relaxin2-mediated TGF-β1/Smad2/MMP-9 pathway [31]; USP4 inhibits myogenic cell differentiation by catalyzing MyoD activity [32]; The H19/miR-148a/USP4 axis promotes hepatic stellate cells by enhancing and TGF-β signaling in hepatocytes to promote liver fibrosis [33]."
USP4 affects IKK_complex
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4
Modified USP4 leads to the dephosphorylation of IKK_complex. 2 / 2
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2
USP4 leads to the dephosphorylation of IKK_complex. 2 / 2
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2
reach
"Furthermore, we point out, for the first time, that KLF2 modulates cell growth, apoptosis, and sensitivity to BTZ through HMGA2.Our study further elucidates the intricate regulatory network in BTZ-resistant MM cells by revealing that USP4 modulates HMGA2 expression via KLF2, establishing a previously uncharacterized USP4/KLF2/HMGA2 cascade in MM resistance to BTZ."
reach
"Future work will be warranted to uncover the downstream effectors underlying the activity of HMGA2.In summary, our study demonstrates a novel regulatory network where USP4 stabilizes KLF2 protein via deubiquitination and thus enhances HMGA2 expression, with the ability to modulate BTZ sensitivity, growth, and apoptosis of BTZ-resistant MM cells (Fig. 7C)."
USP4 affects DNA repair
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2
UBL affects USP4
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4
Proteasome affects USP4
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2
sparser
"Osteocytes are the main cells in mature bone tissue, accounting for about 95% of the total bone cells. xref Osteocytes can secrete paracrine factors, such as OPG, RANKL and sclerostin (Sost), which can participate in the regulation of osteoblast and osteoclast differentiation and activity and play a key role in bone remodelling. xref , xref Sost binds to LPR5/6 on osteoblast cell membranes to interfere with WNT binding to WNT receptor Frizzled, which acts as an antagonist of WNT/β‐catenin signalling to inhibit osteogenesis and bone formation. xref Sirtuin 1 (SIRT1) inhibits the expression of Sost by modifying the acetylation of H3K9 at the Sost promoter. xref , xref The phosphorylation of USP4 by casein kinase 2 (Ck2) inhibits the ubiquitination degradation of SIRT1, thus inhibiting the transcription of Sost and reducing the RANKL/OPG ratio in osteocytes, thereby reducing osteoclastogenesis and increasing osteoblastogenesis. xref Overall, Sost expression regulated by CK2–USP4–SIRT1 pathway is essential for osteocytes to maintain bone homeostasis."
Vialinin A affects USP4
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1
2
Vi-A affects USP4
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3
USP4 affects immune response
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3
USP4 affects glucose import
|
3
USP4 affects degradation
|
3
|
3
reach
"The Adenosine A2 receptor is deubiquitinated by USP4; the ubiquitination status and trafficking of the EGFR growth factor receptor is regulated by the USP8 and STAM complex; the beta2-AR undergoes increased agonist stimulated ubiquitination, lysosomal trafficking, and degradation after knockdown of USPs 20 and 33."
USP4 binds adenosine.
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1
USP4 affects Vi-A
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3
USP4 affects Ubiquitination
|
3
sparser
"To confirm complex formation of endogenous components, proximity ligation assay (PLA) was performed using the breast cancer cell line MDA-231-BM, known to produce high levels of hyaluronan. xref Using antibodies against HAS2 and USP4 or USP17, reactive signals in the form of red dots indicating interactions between endogenous HAS2 and USP17, and HAS2 and USP4, were observed; only a low background level of dots was seen when each antibody was used alone, or in the fixation control without antibody ( xref )."
USP4 affects Th17
|
3
reach
"By isolating T cells from patients with RHD as well as healthy volunteers and detecting the mRNA level of USP4 in CD4 T cells, the researchers found that the mRNA level of USP4 was related to the mRNA level of IL-17 and the function of Th17, indicating that USP4 may mediate the function of Th17 under inflammatory stimulation."
sparser
"To investigate if Snail1 can indeed bind and regulate the USP4 promoter, luciferase reporter constructs were generated in which luciferase expression was controlled by the wild type USP4 promoter or promoters with the E-box sequence mutations shown in xref and co-transfected with Snail1 into HEK293 cells."
USP4 affects RGR
|
3
USP4 affects EV71
|
3
USP4 affects Carcinoma, Hepatocellular
|
3
USP4 activates Carcinoma, Hepatocellular. 3 / 3
|
3
reach
"The USPs family is the largest and most important DUB family, and many of these elements are involved in the occurrence and development of multiple cancers, such as USP1, USP4, USP7, USP22, and USP28, which promote or inhibit the development and progression of colorectal, breast, and hepatocellular carcinomas via deubiquitining the hub genes of cancer-related signaling pathways [10, 11]."
USP4 affects Carcinogenesis
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1
1
USP4 affects BRAP
|
3
sparser
"To confirm complex formation of endogenous components, proximity ligation assay (PLA) was performed using the breast cancer cell line MDA-231-BM, known to produce high levels of hyaluronan. xref Using antibodies against HAS2 and USP4 or USP17, reactive signals in the form of red dots indicating interactions between endogenous HAS2 and USP17, and HAS2 and USP4, were observed; only a low background level of dots was seen when each antibody was used alone, or in the fixation control without antibody ( xref )."
USP15 affects BRAP
|
3
sparser
"To investigate if Snail1 can indeed bind and regulate the USP4 promoter, luciferase reporter constructs were generated in which luciferase expression was controlled by the wild type USP4 promoter or promoters with the E-box sequence mutations shown in xref and co-transfected with Snail1 into HEK293 cells."
RGR affects USP4
|
3
sparser
"To confirm complex formation of endogenous components, proximity ligation assay (PLA) was performed using the breast cancer cell line MDA-231-BM, known to produce high levels of hyaluronan. xref Using antibodies against HAS2 and USP4 or USP17, reactive signals in the form of red dots indicating interactions between endogenous HAS2 and USP17, and HAS2 and USP4, were observed; only a low background level of dots was seen when each antibody was used alone, or in the fixation control without antibody ( xref )."
EV71 affects USP4
|
3
E3_Ub_ligase affects USP4
|
2
1
BRAP affects USP4
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3
Short hairpin RNA affects USP4
|
2
Foci affects USP4
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2
USP4 affects response to xenobiotic stimulus
|
2
USP4 affects osteoblast differentiation
|
2
USP4 inhibits osteoblast differentiation. 2 / 2
|
2
USP4 affects hyaluronic acid
|
2
USP4 affects foci
|
2
USP4 affects cytokine production
|
2
reach
"In the present study, we found that the USP4 and beta-catenin axis was involved in metastatic potential through USP4 mediated stabilization of beta-catenin and that knockdown of USP4 and beta-catenin suppressed the metastatic potential including clonogenicity, migration, and invasion, and induced MET by downregulating ZEB1 expression."
USP4 affects U4 snRNP
|
2
USP4 affects Pancreatic Neoplasms
|
2
USP4 affects NF-kappaB luciferase
|
2
reach
"For example, USP4 has been shown to interact with and deubiquitinate RORγt, promoting its function and IL-17A transcription in rheumatic heart disease (Yang et al. 2015); similarly, USP7 has been found to promote lupus nephritis by regulating NF-κB p65 signaling via JMJD3 stabilization (Zhang et al. 2021)."
USP4 affects Hypertrophy
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2
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2
USP4 activates Esophageal Squamous Cell Carcinoma. 2 / 2
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2
USP4 affects ERK1/2-MAPK
|
2
USP4 affects DSB repair
|
2
USP4 affects DNA Damage
|
2
USP4 affects DNA Breaks, Double-Stranded
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2
USP4 affects CrkII
|
2
reach
"The Cell Counting Kit-8 (CCK-8) assay results showed that the proliferation of hypertrophic scar fibroblasts transfected with siUSP4 was significantly inhibited on the fifth and seventh day, indicating that down-regulation of USP4 could suppress the proliferation of hypertrophic scar fibroblasts."
USP4 affects Cell Survival
|
1
1
USP4 affects Angiotensin-2
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2
USP4 affects ADP-ribosylatibon factor-binding protein 1
|
2
reach
"USP4, for example, interacts directly with end resection factors CtIP and MRN [172], USP21 deubiquitinates and stabilizes BRCA2 to promote RAD51 binding and successful HR [173], and USP10 deubiquitinates and stabilizes p53 to promote its nuclear localization and apoptosis in response to DSBs [174]."
Rho52 affects USP4
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2
RBBP8 affects foci
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2
LncRNA affects USP4
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2
EVO affects USP4
|
2
reach
"[49, 50, 51, 52, 53] To illustrate, phosphorylation of USP4 by protein kinase B (PKB, also known as AKT) results in its redistribution from the nucleus to the cytoplasm, which enables USP4 to reach the cell membrane and deubiquitinate the transforming growth factor-beta (TGF-beta) receptor I (TbetaR-I)."
Peptidase activity affects Ubiquitin
|
1
Natural small molecule product U4-I05 affects USP4
|
1
reach
"A natural small molecule product U4-I05 diminished the stem-like features of CSCs and enhanced their sensitivity to oxaliplatin and 5-fluorouracil by targeting inhibition of its deubiquitinating enzyme activity through binding the catalytic domain of USP4 (311 cysteine site) at nanomolar concentrations, triggering proteasome-mediated degradation of beta-catenin and Twist1."
MiR-553 affects USP4
|
1
Lipopolysaccharide affects USP4
|
1
Lipopolysaccharide decreases the amount of USP4. 1 / 1
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1
Catalytic affects USP4
|
1
Adenosine affects USP4
|
1
Adenosine receptor affects USP4
|
1
USP4 binds adenosine receptor-A2A. 1 / 1
|
1
VLX1570 affects USP4
|
1
Ubiquitin affects peptidase activity
|
1
USP4 affects siUSP4-2
|
1
USP4 affects several inflammatory cytokines T cells
|
1
USP4 affects peptidase activity
|
1
USP4 affects pathological cardiac hypertrophy
|
1
USP4 affects p-CrkII
|
1
USP4 affects nitric oxide
|
1
USP4 decreases the amount of nitric oxide. 1 / 1
|
1
USP4 affects fibrosis progress autoimmune hepatitis
|
1
USP4 affects catalytic activity
|
1
USP4 affects breast cancer cell migration
|
1
USP4 affects adenosine receptor
|
1
USP4 binds adenosine receptor-A2A. 1 / 1
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1
USP4 affects Ubiquitin, and peptidase activity
|
1
USP4 affects UBL domain
|
1
USP4 affects U6-snRNA
|
1
USP4 affects Tumor Growth
|
1
USP4 affects TGFbeta receptor
|
1
USP4 affects Smad433
|
1
USP4 affects SMAD2/3/4 reporter
|
1
USP4 affects Rhabdomyosarcoma
|
1
USP4 activates Rhabdomyosarcoma. 1 / 1
|
1
USP4 affects Periodontitis
|
1
USP4 inhibits Periodontitis. 1 / 1
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1
USP4 affects PI3K Akt pathway
|
1
USP4 affects NPs
|
1
USP4 affects LvBr4
|
1
USP4 affects IGF-I-Myr-AKT-induced migration MDA-MB-231 breast cancer cells
|
1
USP4 affects GW3965
|
1
USP4 affects EMT process liver cancer
|
1
USP4 affects DUSP domain
|
1
USP4 affects DNA-templated transcription
|
1
USP4 inhibits DNA-templated transcription. 1 / 1
|
1
USP4 affects 1,4-diphenylbenzene
|
1
1,4-diphenylbenzene binds USP4. 1 / 1
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1
UBL domain affects USP4
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1
RIGI affects DUSP domain
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1
NPs affects USP4
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1
Evodiamine affects USP4
|
1
Evodiamine decreases the amount of USP4. 1 / 1
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1
EDX pattern affects USP4
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1
DUSP domain affects USP4
|
1
Angiotensin-2 affects USP4
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1
Angiotensin-2 inhibits USP4. 1 / 1
|
1
1,4-diphenylbenzene affects USP4
|
1
1,4-diphenylbenzene binds USP4. 1 / 1
|
1