MAP2K7 (Phospho-Thr275) Antibody
- Known as:
- MAP2K7 (Phospho-Thr275) Antibody
- Catalog number:
- 11743
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- MAP2K7 (Phospho-Thr275) Antibody
Ask about this productRelated genes to: MAP2K7 (Phospho-Thr275) Antibody
- Gene:
- MAP2K7 NIH gene
- Name:
- mitogen-activated protein kinase kinase 7
- Previous symbol:
- PRKMK7
- Synonyms:
- MKK7, Jnkk2
- Chromosome:
- 19p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-04-28
- Date modifiied:
- 2016-10-05
Related products to: MAP2K7 (Phospho-Thr275) Antibody
Related articles to: MAP2K7 (Phospho-Thr275) Antibody
- Pancreatic ductal adenocarcinoma (PDAC) is highly lethal and remains largely refractory to targeted therapy despite its near-universal dependence on oncogenic KRAS. Single-agent KRAS inhibitors often fail due to adaptive resistance mechanisms that emerge under pharmacologic pressure. Previous studies combining MAP2K4 inhibition with KRASG12C-targeted therapy determined that partial JNK suppression can enhance anticancer responses. Here, we extend this concept to PDAC, which is predominantly driven by KRASG12D mutations, and demonstrate that full JNK pathway inactivation restores sensitivity to KRAS inhibition in resistant cells. Using selective MAP2K4, MAP2K7, or combined inhibitors, we show that more extensive JNK suppression disables the feedback loop that reactivates KRAS signaling. In contrast, KRASG12D inhibitor-sensitive cells derive no benefit from JNK pathway inhibition, revealing a resistance-specific vulnerability amenable to therapeutic exploitation. - Source: PubMed
Publication date: 2026/09/07
Connors Gina MPham Thao DBecker Jeffrey HArgus Aria ABaba KenkichiKinoshita TakayoshiMunshi Hidayatullah GScheidt Karl A - Nephrotic syndrome (NS) is a glomerular disorder, with significant morbidity globally. Given the challenge of glucocorticoid resistance, this study aimed to evaluate actionable genetic and epigenetic biomarkers to enable early prediction of therapeutic response. - Source: PubMed
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Almeshary Majid AHussein Dalia TRefaat ManarEl-Refaey Ahmed MEl-Khawaga Omali Y - West Nile virus (WNV) is a mosquito-borne pathogen of escalating epidemiological importance and a growing global health concern, driven by the climate-associated expansion of its mosquito vectors. Although WNV is an extensively studied flavivirus, most host-pathogen interaction studies focus on static and structural aspects rather than dynamic and functional ones. Delineating phosphorylation-mediated interactions between WNV proteins and human kinases bridges a critical gap by providing important insight into the molecular mechanisms underlying infection. In this study, we investigated potential phosphorylation-mediated interactions between WNV proteins and human kinases using an integrative computational framework combining motif prediction, phosphoproteomic data analysis and structural docking. Key interactions were predicted between viral proteins and regulatory kinases within the AKT-ERK pathway and the AMPK-mediated autophagy, including major network kinases such as RAF1, IKBKB, and ULK1. In addition, experimentally validated phosphorylation sites in viral proteins were found to be associated with multiple candidate host kinases, including MAP2K7 and MAP2K9, suggesting complex regulatory networks. Integration with phosphoproteomic datasets supported the relevance of multiple predicted kinases, including those associated with antiviral responses and translational regulation. Protein-protein docking demonstrated stable, energetically favorable interactions between selected host kinases and viral proteins, particularly the viral polymerase (NS5), helicase (NS3), and NS1. The findings of this study establish a framework for future research on the development of host-directed antiviral strategies. - Source: PubMed
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