Molecular Pharmacology最新文献

{"title":"Discovery of RGS2-FBXO44 interaction inhibitors using a cell-based NanoBit assay.","authors":"Sadikshya Aryal, Cindy Shi Yee Wong, Harrison J McNabb, Ahmad Junaid, Ryan A Altman, Benita Sjögren","doi":"10.1016/j.molpha.2025.100030","DOIUrl":"https://doi.org/10.1016/j.molpha.2025.100030","url":null,"abstract":"<p><p>Regulators of G protein signaling (RGS) proteins negatively regulate signaling through G protein-coupled receptors, and reduced RGS protein function is involved in numerous pathologies. However, therapeutic intervention is challenging, as RGS proteins lack druggable binding pockets and enzymatic activity. Instead, targeting mechanisms that control RGS protein expression show promise as an alternative. Pharmacological stabilization of RGS2 would be a feasible therapeutic strategy in pathologies associated with reduced RGS2 protein levels, such as hypertension, heart failure, and asthma. RGS2 is rapidly degraded through the ubiquitin-proteasomal system, and we recently identified the E3 ligase that recognizes RGS2. F-box Only Protein 44 (FBXO44) acts as the substrate recognition site for RGS2 in this E3 ligase complex, and we hypothesize that inhibiting the RGS2-FBXO44 interaction will lead to enhanced RGS2 levels. Here, we developed a NanoLuc Binary Technology (NanoBiT) assay that detects the interaction between RGS2 and FBXO44. This assay was used to screen 1600 compounds from the Life Chemicals protein-protein interaction fragment library. We identified a promising hit, denoted compound 10, that inhibits the RGS2-FBXO44 interaction with a potency of 19.6 μM, through direct binding to RGS2. The resulting increase in RGS2 protein levels is dependent on FBXO44, as siRNA-mediated FBXO44 knockdown attenuates the effect of compound 10. Altogether, compound 10 represents the first example of a small-molecule inhibitor of the RGS2-FBXO44 interaction and a first step toward the development of molecular probes with a defined mechanism to stabilize RGS2 protein levels. SIGNIFICANCE STATEMENT: This study provides a strategy to identify molecules that selectively inhibit RGS2 protein degradation as well as the first example of a compound with the ability to inhibit RGS2 interaction with the E3 ligase component FBXO44. This study provides proof of concept that a small-molecule RGS2-FBXO44 interaction inhibitor will increase RGS2 protein levels. Future development of compounds with this mechanism of action would be clinically useful in pathologies associated with low RGS2 protein levels, including hypertension, heart failure, and asthma.</p>","PeriodicalId":18767,"journal":{"name":"Molecular Pharmacology","volume":"107 5","pages":"100030"},"PeriodicalIF":3.2,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143811903","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The neuroprotective γ-hydroxybutyrate analog 3-hydroxycyclopent-1-enecarboxylic acid does not directly affect CaMKIIα autophosphorylation at T286 or binding to GluN2B.","authors":"Carolyn Nicole Brown, Rachel E Blaine, Chase Madison Barker, Steven J Coultrap, Karl Ulrich Bayer","doi":"10.1016/j.molpha.2025.100029","DOIUrl":"https://doi.org/10.1016/j.molpha.2025.100029","url":null,"abstract":"<p><p>The Ca²⁺/calmodulin (CaM)-dependent protein kinase II (CaMKII) mediates physiological long-term potentiation (LTP) of synaptic strength and pathological ischemic neuronal cell death. Both functions require CaMKII autophosphorylation at T286 (pT286) and binding to the NMDA-type glutamate receptor subunit GluN2B. The neuroprotection seen with 3-hydroxycyclopent-1-enecarboxylic acid (HOCPCA) was thought to be mediated by impairing binding of the brain-specific CaMKIIα isozyme to GluN2B. However, we show that HOCPCA does not inhibit CaMKIIα enzymatic activity, pT286, cocondensation with GluN2B, or binding to GluN2B. Consistent with no effect on GluN2B binding in vitro or in HEK293 cells, HOCPCA also did not affect the CaMKIIα movement to excitatory synapses in hippocampal neurons in response to LTP stimuli. These findings leave the neuroprotective mechanism of HOCPCA unclear but explain why HOCPCA does not impair LTP. SIGNIFICANCE STATEMENT: This study found that the neuroprotective compound 3-hydroxycyclopent-1-enecarboxylic acid (HOCPCA) does not directly interfere with Ca²⁺/calmodulin (CaM)-dependent protein kinase II (CaMKII) activity or GluN2B binding. Although this leaves the neuroprotective mechanism of HOCPCA unclear, it explains why HOCPCA does not impair long-term potentiation. Overall, this limits the use of HOCPCA as a tool compound to study CaMKII functions, but not its clinical potential.</p>","PeriodicalId":18767,"journal":{"name":"Molecular Pharmacology","volume":"107 4","pages":"100029"},"PeriodicalIF":3.2,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143788587","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural similarity-based search for glinides exhibiting cis- and trans-inhibitory activity toward uric acid transporter 1.","authors":"Misa Sayama, Takaaki Suzuki, Yoshie Reien, Seiji Miyauchi, Naohiko Anzai, Itsuko Ishii","doi":"10.1016/j.molpha.2025.100028","DOIUrl":"https://doi.org/10.1016/j.molpha.2025.100028","url":null,"abstract":"<p><p>Various types of drugs can affect serum urate levels as side effects. Although these drugs are used to treat different diseases, they might share a structural component that acts on a common target to affect urate levels. Human urate transporter 1 (URAT1) plays an essential role in urate reabsorption at the renal proximal tubule and thus might be a common target for drugs that can affect serum urate levels. Our aim was to elucidate the structural requirements for a compound to show activity toward URAT1 and to identify clinically used drugs that can affect URAT1 activity. Our search was based on structural similarities in the compounds. [¹⁴C]Urate uptake by URAT1-expressing human embryonic kidney 293 (HEK-hURAT1) cells in the presence of an analog of a small molecule with known URAT1 activity suggested that structural moieties of salicylic acid can increase URAT1 cis-inhibitory activity. Therefore, we searched a database for drugs with substructures similar to salicylic acid. We were able to predict some types of loop diuretics, statins, and angiotensin receptor blockers as drug candidates that might affect URAT1. In addition, we found that glinides inhibit urate uptake by HEK-hURAT1 cells. Three glinides (nateglinide, mitiglinide, and repaglinide) all inhibited urate uptake by HEK-hURAT1 cells concentration-dependently (IC₅₀: nateglinide, 39 μM; mitiglinide, 63 μM; repaglinide, 3.9 μM). Furthermore, glinides also showed trans-inhibition activity in URAT1-expressing Xenopus oocytes pretreated with the glinides. These findings suggest that glinides sharing a salicylic acid-like substructure might affect serum urate level by acting on URAT1. SIGNIFICANCE STATEMENT: Some types of loop diuretics, statins, angiotensin receptor blockers, and glinides were predicted to affect URAT1, based on their chemical structural similarity to salicylic acid, the structure of which allows it to interact with URAT1. Glinides in particular showed cis- and trans-inhibitory activity toward URAT1.</p>","PeriodicalId":18767,"journal":{"name":"Molecular Pharmacology","volume":"107 4","pages":"100028"},"PeriodicalIF":3.2,"publicationDate":"2025-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143788584","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification and molecular characterization of missense mutations in orphan G protein-coupled receptor GPR61 occurring in severe obesity.","authors":"Choi Har Tsang, Alexander De Rosa, Paweł Kozielewicz","doi":"10.1016/j.molpha.2025.100026","DOIUrl":"https://doi.org/10.1016/j.molpha.2025.100026","url":null,"abstract":"<p><p>Severe obesity is a complex chronic metabolic condition with a body mass index over 40 and can be caused, for example, by dysregulated G protein-coupled receptors (GPCRs) signaling. The orphan GPCR GPR61 had been linked to the regulation of metabolism and, here, we identify 34 mutations in the GPR61 gene which are present with much higher frequency in severe obesity samples from the UK10K obesity screen compared to the normal population. Furthermore, the cumulative sum of GPR61 mutations was found to be higher compared to the highly mutated and well-established target, melanocortin 4 receptor. Some GPR61 mutations presented an impact on ligand-independent GPR61-induced cAMP production. Specifically, R236C^5.66 compromised G_s protein activation and altered the pattern of cellular expression. Our data warrant further studies to assess the role of this orphan GPCR in metabolism in greater detail. SIGNIFICANCE STATEMENT: This study identified missense mutations, including previously unknown variants, of the GPR61 gene in severely obese patients. This occurrence was higher than for the well-established obesity target melanocortin 4 receptor. In the in vitro assays, 3 mutations of GPR61, in particular R236C^5.66, were loss of function because they reduced the constitutive activity of the receptor. The data support the notion that GPR61 can act as a promising target in obesity and its functions should be explored in future studies.</p>","PeriodicalId":18767,"journal":{"name":"Molecular Pharmacology","volume":"107 4","pages":"100026"},"PeriodicalIF":3.2,"publicationDate":"2025-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143710736","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ion channels and G protein-coupled receptors: Cannabidiol actions on disorders of excitability and synaptic excitatory-inhibitory ratio.","authors":"Richard W Tsien, Evan C Rosenberg","doi":"10.1016/j.molpha.2025.100017","DOIUrl":"10.1016/j.molpha.2025.100017","url":null,"abstract":"<p><p>Brain excitability is dysfunctional in epilepsy and overlapping neuropsychiatric conditions including autism spectrum disorder (ASD). Epilepsy and ASD are often attributed to malfunctioning coordination between synaptic excitation and inhibition. Dravet syndrome (DS) is a severe form of epilepsy arising from haploinsufficiency of the SCN1A gene that encodes the voltage-gated sodium channel Nav1.1. A DS mouse model (Scn1a^+/-) recapitulated essential features of DS and revealed that sodium current density was profoundly reduced in GABAergic inhibitory interneurons while pyramidal cells were spared, suggesting that DS is an \"interneuronopathy.\" Further studies from the Catterall group and others have expanded this picture: DS symptoms, which include recurrent seizures, ataxia, cognitive impairment, ASD, and premature death, could be assigned in part to brain region-specific effects; the Nav1.1 mutations cause dysfunction in some subtypes of interneurons, not others, and are temporally restricted; DS-causing sodium channel mutations were found throughout SCN1A as well as in SCN1B, encoding the β1 subunit. Interest in therapeutic approaches was sparked by preclinical studies of cannabidiol (CBD) that led to the 2018 US Food and Drug Administration approval for treatment of seizures in patients with DS. Independent evidence showed that CBD antagonized GPR55, a G protein-coupled receptor activated by the lipid signaling molecule lysophosphatidylinositol (LPI). We summarized evidence from our group and others that CBD has a dual mechanism of action, targeting both ion channels and GPR55. CBD quells an epileptogenic vicious cycle: seizures strengthen LPI-GPR55 signaling while LPI-GPR55 signaling elevates the synaptic excitatory-inhibitory ratio, thereby promoting further seizures. SIGNIFICANCE STATEMENT: Modern medicine relies on ion channels and G protein-coupled receptors (GPCRs) as key targets. In studies of Dravet syndrome, a devastating genetic disorder with features of epilepsy and autism, William Catterall connected NaV1.1 mutations to deficient excitability of inhibitory neurons. He and his colleagues explored preclinical interventions using cannabidiol (CBD) and clobazam, opening the way to a current understanding of CBD's therapeutic mechanism. CBD affects both ion channels and GPR55, a GPCR activated by lysophosphatidylinositol, an activity-dependent lipid messenger, readjusting the synaptic excitatory-inhibitory ratio.</p>","PeriodicalId":18767,"journal":{"name":"Molecular Pharmacology","volume":"107 3","pages":"100017"},"PeriodicalIF":3.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143573406","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Expression of concern: \"Caveolin-1 and Lipid Microdomains Regulate G_s Trafficking and Attenuate G_s/Adenylyl Cyclase Signaling\" [Molecular Pharmacology, Volume 76, Issue 5, November 2009, Pages 1082-1093].","authors":"","doi":"10.1016/j.molpha.2025.100023","DOIUrl":"https://doi.org/10.1016/j.molpha.2025.100023","url":null,"abstract":"","PeriodicalId":18767,"journal":{"name":"Molecular Pharmacology","volume":"107 3","pages":"100023"},"PeriodicalIF":3.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143743311","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Role of HNF4A-AS1/HNRNPC-mediated HNF4A ubiquitination protection against ritonavir-induced hepatotoxicity.","authors":"Xiaofei Wang, Zijing Wang, Jingya Wang, Yihang Yu, Yiting Wang, Zaihuan Xiong, Shengna Han, Xiao-Bo Zhong, Pei Wang, Lirong Zhang","doi":"10.1016/j.molpha.2025.100021","DOIUrl":"10.1016/j.molpha.2025.100021","url":null,"abstract":"<p><p>Ritonavir (RTV) is an important drug for anti-human immunodeficiency virus treatment and is mainly metabolized by cytochrome P450 (CYP) 3A4. Clinically, the most common side effect of RTV treatment is hepatoxicity. We previously showed that the long noncoding RNA hepatocyte nuclear factor 4 alpha (HNF4A) antisense 1 (HNF4A-AS1) negatively regulated CYP3A4 expression and participated in RTV-induced hepatotoxicity in vitro, but the mechanism has not been well understood. In this study, similar results were observed in the mouse, where liver-specific knockdown of Hnf4aos (homolog of human HNF4A-AS1) led to increased serum aspartate (∼1.8-fold) and alanine transaminase (∼2.4-fold) levels and enlarged and degenerated hepatocytes 24 hours after RTV administration. Meanwhile, endoplasmic reticulum stress markers GRP78, PDI, and XBP-1 increased about 2.4-fold, 2.1-fold, and 2.7-fold, respectively. The aggravated liver injury correlated with Hnf4aos knockdown, attributable to heightened Cyp3a11 (homolog of human CYP3A4) expression (mRNA and protein levels were 1.8-fold and 2.5-fold, respectively). Importantly, in vitro studies revealed the underlying mechanism that HNF4A-AS1 mediated the interaction between heterogeneous nuclear ribonucleoprotein C and HNF4A, whereas heterogeneous nuclear ribonucleoprotein C promoted HNF4A degradation through the ubiquitination pathway, thereby decreasing CYP3A4 expression and alleviating RTV-induced liver injury. Overall, our findings unveil a novel mechanism by which HNF4A-AS1 regulates CYP3A4 expression to influence RTV-induced liver injury. SIGNIFICANCE STATEMENT: HNF4A-AS1 negatively regulates the expression of CYP3A4, whose overexpression is highly correlated with ritonavir (RTV)-induced liver injury. In this study, the role of Hnf4aos (homolog of human HNF4A-AS1) in RTV-induced hepatotoxicity was confirmed in mice. We found that HNF4A-AS1 and HNRNPC form a complex and facilitate the ubiquitination and degradation of HNF4A protein, thereby decreasing CYP3A4 expression and alleviating RTV hepatotoxicity.</p>","PeriodicalId":18767,"journal":{"name":"Molecular Pharmacology","volume":"107 3","pages":"100021"},"PeriodicalIF":3.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143557309","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"6,7-Dichloro-1H-indole-2,3-dione-3-oxime functions as a superagonist for the intermediate-conductance Ca²⁺-activated K⁺ channel K_Ca3.1.","authors":"Joshua A Nasburg, Kyle C Rouen, Connor J Dietrich, Heesung Shim, Miao Zhang, Igor Vorobyov, Heike Wulff","doi":"10.1016/j.molpha.2025.100018","DOIUrl":"10.1016/j.molpha.2025.100018","url":null,"abstract":"<p><p>NS309 (6,7-dichloro-1H-indole-2,3-dione-3-oxime) is widely used as a pharmacological tool to increase the activity of small- and intermediate-conductance calcium-activated potassium channels. NS309 is assumed to function as a positive allosteric gating modulator. However, its binding site and the molecular details of its action remain unknown. Here, we show that NS309 has a profound effect on the calcium-dependent gating of the intermediate-conductance Ca²⁺-activated K⁺ channel K_Ca3.1. In inside-out experiments, 10 μM NS309 shifted the calcium EC₅₀ from 430 to 31 nM. In whole-cell experiments, changing free intracellular calcium from 250 nM to 3 μM decreased the EC₅₀ of NS309 from 74 to 8.6 nM. We further observed that NS309 could elicit greater responses than saturating calcium, making it a \"superagonist.\" Molecular modeling suggested 2 possible binding sites for NS309 in K_Ca3.1, which we probed by mutagenesis and determined that NS309 is binding in the interface between the S₄₅A segment of the intracellular S4-S5 linker and the N-lobe of the channel-associated calmodulin. Molecular dynamic simulations revealed that NS309 pushes several water molecules out of the interface pocket, establishes stable contacts with S181 and L185 in the S₄₅A segment of K_Ca3.1 and E54 in calmodulin, and promotes longer sustained widening of the inner gate of K_Ca3.1 at V282 in the S6 segment. Polar substitutions of the hydrophobic-gating residues V282 and A279 resulted in constitutively open channels that could not be further potentiated by NS309, suggesting that NS309 produces its agonistic effects by increasing the open probability of the inner gate of K_Ca3.1. SIGNIFICANCE STATEMENT: The publication of the full-length cryo-electron microscopy structure of the intermediate-conductance Ca²⁺-activated K⁺ channel K_Ca3.1 suggested that the previously reported binding site of NS309 (6,7-dichloro-1H-indole-2,3-dione-3-oxime) was a crystallization artifact because this structure only included the C-terminus and the channel-associated calmodulin. This study demonstrates that the true binding site of NS309 is located between the S4 and S5 linker of K_Ca3.1 and the N-lobe of calmodulin. NS309 acts as a stabilizing force within the gating interface and increases the open probability of the inner hydrophobic gate.</p>","PeriodicalId":18767,"journal":{"name":"Molecular Pharmacology","volume":"107 3","pages":"100018"},"PeriodicalIF":3.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143605375","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"LIM and SH3 protein 2 (Lasp2) is a novel pregnane X receptor target gene in mouse liver.","authors":"Anja Konzack, Mikko Karpale, Tomas Smutny, Mohamed Hassanen, Piia Lassila, Maria H Ahonen, Mahmoud-Sobhy Elkhwanky, Outi Kummu, Petr Pavek, Jukka Hakkola","doi":"10.1016/j.molpha.2025.100019","DOIUrl":"10.1016/j.molpha.2025.100019","url":null,"abstract":"<p><p>LIM and Src homology 3 (SH3) protein 2 (LASP2) is a small focal adhesion protein first identified as a splice variant of the nebulette gene (Nebl). As the newest member of the nebulin protein family, the regulation and function of LASP2 remain largely unknown. Our previous RNA-sequencing results identified Nebl as one of the most highly induced genes in the mouse liver in response to the activation of pregnane X receptor (PXR). In this study, we investigated this phenomenon further and show that PXR induces Lasp2 instead of Nebl, which partially use the same exons. Lasp2 was found to be induced in response to PXR ligand pregnenolone 16α-carbonitrile (PCN) treatment in mouse liver in vivo both after 4-day treatment and after long-term, 28-day treatment and in both male and female mice. Interestingly, the Lasp2 induction was more efficient in high-fat diet-fed mice (103-fold after 4-day PCN treatment) than in the normal chow-fed mice (32-fold after 4-day PCN treatment). Lasp2 induction was abolished in PXR knockout mice but could be rescued by re-expression of PXR, indicating that Lasp2 induction is PXR mediated. In mouse primary hepatocytes cycloheximide did not inhibit Lasp2 induction by PCN and a PXR binding site could be recognized upstream of the mouse Lasp2 gene suggesting direct regulation of Lasp2 by PXR. In human 3D hepatocytes, rifampicin induced only a modest increase in LASP2 expression. This study shows for the first time that PXR activation strongly induces Lasp2 expression in mouse liver and establishes Lasp2 as a novel PXR target gene. SIGNIFICANCE STATEMENT: RNA-sequencing results have previously identified nebulette (Nebl) to be efficiently induced by pregnane X receptor activating compounds. This study shows that instead of Nebl, LIM and Src homology 3 (SH3) protein 2 (Lasp2) coding for a small focal adhesion protein and partly sharing exons with the Nebl gene is a novel target of pregnane X receptor in mouse liver.</p>","PeriodicalId":18767,"journal":{"name":"Molecular Pharmacology","volume":"107 3","pages":"100019"},"PeriodicalIF":3.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11964950/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143537357","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to \"Antitumor Effects of Dehydroxymethylepoxyquinomicin, a Novel Nuclear Factor-κB Inhibitor, in Human Liver Cancer Cells Are Mediated through a Reactive Oxygen Species-Dependent Mechanism\".","authors":"","doi":"10.1016/j.molpha.2025.100022","DOIUrl":"10.1016/j.molpha.2025.100022","url":null,"abstract":"","PeriodicalId":18767,"journal":{"name":"Molecular Pharmacology","volume":"107 3","pages":"100022"},"PeriodicalIF":3.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143476759","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}