YME1L1 antigen

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636.35 €

Known as:: YME1L1 antigenic
Catalog number:: 'H00010730-Q01-10
Product Quantity:: 10
Category:: -
Supplier:: ACR
Gene target:: YME1L1 antigen

Related genes to: YME1L1 antigen

Gene:: YME1L1 ^{NIH gene}
Name:: YME1 like 1 ATPase
Previous symbol:: -
Synonyms:: YME1L
Chromosome:: 10p12.1
Locus Type:: gene with protein product
Date approved:: 1999-04-15
Date modifiied:: 2019-04-15

Related products to: YME1L1 antigen

Related articles to: YME1L1 antigen

Exploratory identification of lycorine as a potential inhibitor of the ACP2/YME1L1 prognostic axis in esophageal squamous cell carcinoma: a multi-omics and computational hypothesis.
- Source: PubMed
Publication date: 2026/04/06
Chen FangZhang JunpengXu YingWang YalinCheng Jian
Expression of YME1 Like 1 ATPase Increases With the Stage of Adrenocortical Carcinoma Tissue and Is Associated With Poor Patient Prognosis.
Adrenocortical carcinoma (ACC) is an endocrine tumor arising in the adrenal cortex. Although its incidence is extremely low, it is highly malignant, rapidly proliferating, and infiltrating surrounding organs, resulting in a poor prognosis. YME1 Like 1 ATPase (YME1L1) is an ATP-dependent metalloprotease that regulates mitochondrial proteostasis. Recently, a correlation between expression and the prognosis of several cancers has been reported. However, no studies have examined the expression level of mRNA in ACC tissues or the relationship between expression and the prognosis of ACC patients. Therefore, there is a need to investigate the relationship between expression and the prognosis of ACC patients. - Source: PubMed
Yamashita Shin-NosukeTanaka YoshiatsuIslam ShajedulKitagawa TakaoTokuda KazuhiroPaudel DurgaGiri SaritaOhta TohruHarada FumiyaNagayasu HirokiKuramitsu Yasuhiro
Characterization of Conformational Dynamics and Structural Plasticity of the Catalytic Domain of Human Mitochondrial YME1L Protease.
Mitochondrial proteostasis is essential to maintain cellular function and survival. YME1L is a membrane-anchored AAA+ (TPases ssociated with diverse cellular ctivities) family protease and plays a pivotal role in mitochondrial proteostasis by selectively degrading misfolded and native proteins. The precise mechanisms by which nucleotide binding and hydrolysis influence YME1L's conformational dynamics, proteolytic activity, and stability remain unclear. Here, we characterize the conformational dynamics of the YME1L catalytic domain. Using a hexameric soluble YME1L construct, we employ hydrogen/deuterium exchange mass spectrometry (HDX-MS) and nuclear magnetic resonance (NMR) spectroscopy to demonstrate that nucleotide binding reduces the backbone flexibility and modulates the side-chain dynamics of the AAA+ domain, while Zn binding stabilizes the protease domain. We also reveal long-range functional crosstalk between the AAA+ and protease domains of YME1L. We use functional assays to show the importance of a salt bridge between the AAA+ and protease domains in facilitating ATP-dependent substrate degradation by YME1L. Additionally, we show that ATP binding stabilizes the structure of the catalytic domain of YME1L and protects it from chemical- and heat-induced aggregation. These findings explain the nucleotide-driven regulation of YME1L and provide insights into our understanding of its proteolytic activity and structural stability under stress conditions. - Source: PubMed
Publication date: 2026/02/26
Black Megan KKim AngelinaChen Ching YGoncalves Monica MWaseem SimrahVahidi SiavashHuang Rui
, Rather than , Plays an Essential Role in Modulating the MPP-Induced mtUPR.
Parkinson's disease (PD) is characterized by mitochondrial dysfunction and impaired protein homeostasis, with the mitochondrial unfolded protein response (mtUPR) emerging as a key regulatory pathway in mitigating mitochondrial stress. This study aimed to explore the impact of shRNAs targeting CHCHD2 or FBXO7 on the mitochondrial unfolded protein response (mtUPR) in a Parkinson's disease (PD) cell model, clarify the mitochondrial-nuclear signaling pathways involving CHCHD2 and FBXO7, elucidate the mechanisms underlying mitochondrial dysfunction induced by these genes, and identify new therapeutic targets for early stage PD. An in vitro PD model was established by treating SH-SY5Y cells with MPP; mitochondrial morphology was evaluated using transmission electron microscopy, and qRT-PCR and Western blot were employed to determine the expression levels of mRNAs and proteins associated with mtUPR, autophagy, CHCHD2, and FBXO7 under oxidative stress. In the MPP-induced PD cell model, we knocked down CHCHD2 and FBXO7 via shRNA and treated the cells with JNK and AKT agonists to observe their effects on mtUPR protein expression. The results showed that mtUPR was activated in MPP-exposed SH-SY5Y cells, and the expression of CHCHD2 and FBXO7 genes was significantly upregulated after MPP intervention; knockdown of CHCHD2 via shRNA resulted in a marked decrease in the expression of mtUPR-related proteins such as HSPA9, HSPD1, YME1L1, and CLPP, while shRNA targeting FBXO7 exerted only a minimal effect on these mtUPR proteins. Furthermore, the administration of JNK or AKT agonists significantly enhanced the expression of MPP-induced mtUPR proteins, including HSPA9, HSPD1, YME1L1, and CLPP. Collectively, these findings indicate that CHCHD2, rather than FBXO7, plays an essential role in modulating the MPP-induced mtUPR and suggest that CHCHD2 may regulate mitochondrial protein homeostasis by activating the mtUPR through the JNK/c-Jun and AKT/ERα pathways. - Source: PubMed
Publication date: 2026/02/05
Wen DongniLi YunjingChen LinaXu HaolingWang YingqingWeng YanhongZhang JingChen XiaochunHuang EnZeng YuqiYe Qinyong
Identification and Experimental Validation of Biomarkers Associated With Mitochondria and Macrophage Polarization in Sepsis.
Sepsis is a common and serious condition, where mitochondria and macrophage polarization play a crucial role. Therefore, this study aimed to identify and validate biomarkers for sepsis associated with mitochondria-related genes (MCRGs) and macrophage polarization-related genes (MPRGs), providing new targets and strategies for therapeutic intervention. This study utilized the GSE95233 and GSE28750 datasets. Initially, intersection genes were identified by overlapping MCRGs and the results from differential expression analysis and weighted gene co-expression network analysis (WGCNA). Biomarkers were identified through machine learning and gene expression analysis. A nomogram was developed and evaluated based on these biomarkers. Finally, functional enrichment, immune infiltration, and reverse transcription quantitative polymerase chain reaction (RT-qPCR) analyses were conducted to further elucidate the biological mechanisms underlying sepsis. The study identified YME1L1, ECHDC3, THEM4, and COQ10A as biomarkers for sepsis. Among them, YME1L1, THEM4, and COQ10A showed significantly lower expression levels in sepsis samples, while ECHDC3 exhibited markedly higher expression. Notably, RT-qPCR analysis confirmed that YME1L1, THEM4, and COQ10A exhibited significantly lower expression levels in sepsis samples. A nomogram based on these biomarkers was developed and validated, effectively predicting sepsis risk. Enrichment analysis indicated that the biomarkers were co-enriched in the oxidative phosphorylation pathway. Additionally, 13 significantly different immune cell types were identified between sepsis and control samples. Biomarker association analysis revealed that CD8 T cells had the strongest positive correlation with YME1L1 (cor = 0.84, < 0.05) and the strongest negative correlation with ECHDC3 (cor = -0.76, < 0.05), suggesting their potential role in the disease mechanism. In this study, YME1L1, ECHDC3, THEM4, and COQ10A were identified as biomarkers for sepsis, with their expression levels validated in clinical samples. These findings provided a promising theoretical foundation for the development of targeted treatments for sepsis. - Source: PubMed
Publication date: 2025/05/19
She LipingDeng XiaojingBian YepingCheng HuiXu Jian

YME1L1 antigen

Related genes to: YME1L1 antigen

Related products to: YME1L1 antigen

Related articles to: YME1L1 antigen

Exploratory identification of lycorine as a potential inhibitor of the ACP2/YME1L1 prognostic axis in esophageal squamous cell carcinoma: a multi-omics and computational hypothesis.

Expression of YME1 Like 1 ATPase Increases With the Stage of Adrenocortical Carcinoma Tissue and Is Associated With Poor Patient Prognosis.

Characterization of Conformational Dynamics and Structural Plasticity of the Catalytic Domain of Human Mitochondrial YME1L Protease.

, Rather than , Plays an Essential Role in Modulating the MPP-Induced mtUPR.

Identification and Experimental Validation of Biomarkers Associated With Mitochondria and Macrophage Polarization in Sepsis.