The FEBS journal最新文献_第2页

The Z isomer of pyridoxilidenerhodanine 5′‐phosphate is an efficient inhibitor of human pyridoxine 5′‐phosphate oxidase, a crucial enzyme in vitamin B6 salvage pathway and a potential chemotherapeutic target 吡哆醇-5′-磷酸的 Z 异构体是人类吡哆醇-5′-磷酸氧化酶的有效抑制剂，而吡哆醇-5′-磷酸氧化酶是维生素 B6 修复途径中的关键酶，也是潜在的化疗靶点

The FEBS journal Pub Date : 2024-09-17 DOI: 10.1111/febs.17274

Claudio Graziani, Anna Barile, Lorenzo Antonelli, Annarita Fiorillo, Andrea Ilari, Fabrizio Vetica, Martino Luigi di Salvo, Alessandro Paiardini, Angela Tramonti, Roberto Contestabile

{"title":"The Z isomer of pyridoxilidenerhodanine 5′‐phosphate is an efficient inhibitor of human pyridoxine 5′‐phosphate oxidase, a crucial enzyme in vitamin B6 salvage pathway and a potential chemotherapeutic target","authors":"Claudio Graziani, Anna Barile, Lorenzo Antonelli, Annarita Fiorillo, Andrea Ilari, Fabrizio Vetica, Martino Luigi di Salvo, Alessandro Paiardini, Angela Tramonti, Roberto Contestabile","doi":"10.1111/febs.17274","DOIUrl":"https://doi.org/10.1111/febs.17274","url":null,"abstract":"Pyridoxal 5′‐phosphate (PLP), the catalytically active form of vitamin B6, acts as a cofactor in many metabolic processes. In humans, PLP is produced in the reactions catalysed by pyridox(am)ine 5′‐phosphate oxidase (PNPO) and pyridoxal kinase (PDXK). Both PNPO and PDXK are involved in cancer progression of many tumours. The silencing of PNPO and PDXK encoding genes determines a strong reduction in tumour size and neoplastic cell invasiveness in models of acute myeloid leukaemia (in the case of PDXK) and ovarian and breast cancer (in the case of PNPO). In the present work, we demonstrate that pyridoxilidenerhodanine 5′‐phosphate (PLP‐R), a PLP analogue that has been tested by other authors on malignant cell lines reporting a reduction in proliferation, inhibits PNPO in vitro following a mixed competitive and allosteric mechanism. We also show that the unphosphorylated precursor of this inhibitor (PL‐R), which has more favourable pharmacokinetic properties according to our predictions, is phosphorylated by PDXK and therefore transformed into PLP‐R. On this ground, we propose the prototype of a novel prodrug‐drug system as a useful starting point for the development of new, potential, antineoplastic agents.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142266976","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

A high cholesterol diet aggravates experimental colitis through SREBP2-modulated endocytosis and degradation of occludin and Zo-1 proteins. 高胆固醇饮食通过 SREBP2 调节的内吞和降解闭塞素和 Zo-1 蛋白，加重实验性结肠炎。

The FEBS journal Pub Date : 2024-09-15 DOI: 10.1111/febs.17269

Qin Yang, Yongjia Li, Xingxing Wang, Qiuying Ding, Yi Tao, Pan Li, Xuemei Lian, Yaxi Chen, Lei Zhao

{"title":"A high cholesterol diet aggravates experimental colitis through SREBP2-modulated endocytosis and degradation of occludin and Zo-1 proteins.","authors":"Qin Yang, Yongjia Li, Xingxing Wang, Qiuying Ding, Yi Tao, Pan Li, Xuemei Lian, Yaxi Chen, Lei Zhao","doi":"10.1111/febs.17269","DOIUrl":"https://doi.org/10.1111/febs.17269","url":null,"abstract":"Disrupted cholesterol homeostasis plays a critical role in the development of multiple diseases, such as cardiovascular disease and cancer. However, the role of cholesterol in inflammatory bowel disease (IBD) remains unclear. In the present study, we investigated whether and how high levels of cholesterol in the diet affect experimental colitis in mice. A normal diet supplemented with 1.25% cholesterol (high cholesterol diet) caused more severe colitis and aggravated the disruption of intestinal tight junction structure, accompanied by higher colonic tissue total cholesterol (TC) levels in a dextran sulfate sodium (DSS)-induced experimental colitis mouse model. Cholesterol aggravated DSS-induced intestinal epithelial barrier impairment and nuclear sterol regulatory element-binding protein 2 (nSREBP2) inhibition both in vivo and in vitro. In addition, nSREBP2 overexpression ameliorated cholesterol-induced intestinal epithelial barrier disruption in Caco2 cells. Interestingly, inhibition of SREBP2 disrupted intestinal epithelial barrier in the absence of cholesterol. Furthermore, SREBP2 regulated the protein expression of tight junction proteins (occludin/Zo-1) via modulating caveolin-1-mediated endocytosis and lysosomal degradation. Analysis of UK Biobank data indicated that, in fully adjusted models, higher serum TC concentrations were an independent protective factor for IBD incidence. The sterol regulatory element-binding factor 2 (SREBF2) gene rs2228313 (G/C) genetic variant was associated with the incidence of IBD and the CC genotype of SREBF2 rs2228313 was associated with higher serum TC levels and decreased the risk of IBD. In summary, a high cholesterol diet aggravates DSS-induced colitis in mice by down-regulating nSREBP2 expression, thereby promoting the endocytic degradation of tight junction proteins. In humans, SREBF2 gene single nucleotide polymorphism rs2228313 and serum TC levels are associated with IBD incidence.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142305290","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

C1ql1 expression in oligodendrocyte progenitor cells promotes oligodendrocyte differentiation 少突胶质祖细胞中 C1ql1 的表达可促进少突胶质细胞的分化

The FEBS journal Pub Date : 2024-09-11 DOI: 10.1111/febs.17256

Zeynep M. Altunay, Joyshree Biswas, Hiu W. Cheung, Robert S. Pijewski, Lucille E. Papile, Yetunde O. Akinlaja, Andrew Tang, Lyndsay C. Kresic, Alexander D. Schouw, Maksym V. Ugrak, Keaven Caro, Perla A. Peña Palomino, Susanne Ressl, Akiko Nishiyama, Stephen J. Crocker, David C. Martinelli

{"title":"C1ql1 expression in oligodendrocyte progenitor cells promotes oligodendrocyte differentiation","authors":"Zeynep M. Altunay, Joyshree Biswas, Hiu W. Cheung, Robert S. Pijewski, Lucille E. Papile, Yetunde O. Akinlaja, Andrew Tang, Lyndsay C. Kresic, Alexander D. Schouw, Maksym V. Ugrak, Keaven Caro, Perla A. Peña Palomino, Susanne Ressl, Akiko Nishiyama, Stephen J. Crocker, David C. Martinelli","doi":"10.1111/febs.17256","DOIUrl":"https://doi.org/10.1111/febs.17256","url":null,"abstract":"Myelinating oligodendrocytes arise from the stepwise differentiation of oligodendrocyte progenitor cells (OPCs). Approximately 5% of all adult brain cells are OPCs. Why would a mature brain need such a large number of OPCs? New myelination is possibly required for higher‐order functions such as cognition and learning. Additionally, this pool of OPCs represents a source of new oligodendrocytes to replace those lost during injury, inflammation, or in diseases such as multiple sclerosis (MS). How OPCs are instructed to differentiate into oligodendrocytes is poorly understood, and for reasons presently unclear, resident pools of OPCs are progressively less utilized in MS. The complement component 1, q subcomponent‐like (C1QL) protein family has been studied for their functions at neuron–neuron synapses, but we show that OPCs express C1ql1. We created OPC‐specific conditional knockout mice and show that C1QL1 deficiency reduces the differentiation of OPCs into oligodendrocytes and reduces myelin production during both development and recovery from cuprizone‐induced demyelination. In vivo over‐expression of C1QL1 causes the opposite phenotype: increased oligodendrocyte density and myelination during recovery from demyelination. We further used primary cultured OPCs to show that C1QL1 levels can bidirectionally regulate the extent of OPC differentiation in vitro. Our results suggest that C1QL1 may initiate a previously unrecognized signaling pathway to promote differentiation of OPCs into oligodendrocytes. This study has relevance for possible novel therapies for demyelinating diseases and may illuminate a previously undescribed mechanism to regulate the function of myelination in cognition and learning.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142189380","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

MOF‐mediated acetylation of CDK9 promotes global transcription by modulating P‐TEFb complex formation MOF 介导的 CDK9 乙酰化通过调节 P-TEFb 复合物的形成促进全局转录

The FEBS journal Pub Date : 2024-09-09 DOI: 10.1111/febs.17264

Wenqi Chen, Jinmeng Chu, Yujuan Miao, Wenwen Jiang, Fei Wang, Na Zhang, Jingji Jin, Yong Cai

{"title":"MOF‐mediated acetylation of CDK9 promotes global transcription by modulating P‐TEFb complex formation","authors":"Wenqi Chen, Jinmeng Chu, Yujuan Miao, Wenwen Jiang, Fei Wang, Na Zhang, Jingji Jin, Yong Cai","doi":"10.1111/febs.17264","DOIUrl":"https://doi.org/10.1111/febs.17264","url":null,"abstract":"Cyclin‐dependent kinase 9 (CDK9), a catalytic subunit of the positive transcription elongation factor b (P‐TEFb) complex, is a global transcriptional elongation factor associated with cell proliferation. CDK9 activity is regulated by certain histone acetyltransferases, such as p300, GCN5 and P/CAF. However, the impact of males absent on the first (MOF) (also known as KAT8 or MYST1) on CDK9 activity has not been reported. Therefore, the present study aimed to elucidate the regulatory role of MOF on CDK9. We present evidence from systematic biochemical assays and molecular biology approaches arguing that MOF interacts with and acetylates CDK9 at the lysine 35 (i.e. K35) site, and that this acetyl‐group can be removed by histone deacetylase HDAC1. Notably, MOF‐mediated acetylation of CDK9 at K35 promotes the formation of the P‐TEFb complex through stabilizing CDK9 protein and enhancing its association with cyclin T1, which further increases RNA polymerase II serine 2 residues levels and global transcription. Our study reveals for the first time that MOF promotes global transcription by acetylating CDK9, providing a new strategy for exploring the comprehensive mechanism of the MOF–CDK9 axis in cellular processes.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142189381","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Biochemical analyses reveal new insights into RCAN1/Rcn1 inhibition of calcineurin. 生化分析揭示了 RCAN1/Rcn1 对钙调素抑制作用的新见解。

The FEBS journal Pub Date : 2024-09-06 DOI: 10.1111/febs.17266

Yan Ren, Hui Chen, Shan-Yue Zhao, Lei Ma, Qing-Xia He, Wei-Bin Gong, Jia-Wei Wu, Hong-Wei Yao, Zhi-Xin Wang

{"title":"Biochemical analyses reveal new insights into RCAN1/Rcn1 inhibition of calcineurin.","authors":"Yan Ren, Hui Chen, Shan-Yue Zhao, Lei Ma, Qing-Xia He, Wei-Bin Gong, Jia-Wei Wu, Hong-Wei Yao, Zhi-Xin Wang","doi":"10.1111/febs.17266","DOIUrl":"https://doi.org/10.1111/febs.17266","url":null,"abstract":"Calcineurin is a serine/threonine protein phosphatase that is highly conserved from yeast to human and plays a critical role in many physiological processes. Regulators of calcineurin (RCANs) are a family of endogenous calcineurin regulators, which are capable of inhibiting the catalytic activity of calcineurin in vivo and in vitro. In this study, we first characterized the biochemical properties of yeast calcineurin and its endogenous regulator Rcn1, a yeast homolog of RCAN1. Our data show that Rcn1 inhibits yeast calcineurin toward pNPP substrate with a noncompetitive mode; and Rcn1 binds cooperatively to yeast calcineurin through multiple low-affinity interactions at several docking regions. Next, we reinvestigated the mechanism underlying the inhibition of mammalian calcineurin by RCAN1 using a combination of biochemical, biophysical, and computational methods. In contrast to previous observations, RCAN1 noncompetitively inhibits calcineurin phosphatase activity toward both pNPP and phospho-RII peptide substrates by targeting the enzyme active site in part. Re-analysis of previously reported kinetic data reveals that the RCAN1 concentrations used were too low to distinguish between the inhibition mechanisms [Chan B et al. (2005) Proc Natl Acad Sci USA 102, 13075]. The results presented in this study provide new insights into the interaction between calcineurin and RCAN1/Rcn1.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142143513","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Phosphorylation of cytosolic hPGK1 affects protein stability and ligand binding: implications for its subcellular targeting in cancer. 细胞质 hPGK1 的磷酸化影响蛋白质的稳定性和配体结合：对其在癌症中的亚细胞靶向的影响。

The FEBS journal Pub Date : 2024-09-06 DOI: 10.1111/febs.17262

Juan Luis Pacheco-García, Mario Cano-Muñoz, Dmitry S Loginov, Pavla Vankova, Petr Man, Angel L Pey

{"title":"Phosphorylation of cytosolic hPGK1 affects protein stability and ligand binding: implications for its subcellular targeting in cancer.","authors":"Juan Luis Pacheco-García, Mario Cano-Muñoz, Dmitry S Loginov, Pavla Vankova, Petr Man, Angel L Pey","doi":"10.1111/febs.17262","DOIUrl":"https://doi.org/10.1111/febs.17262","url":null,"abstract":"Human phosphoglycerate kinase 1(hPGK1) is a key glycolytic enzyme that regulates the balance between ADP and ATP concentrations inside the cell. Phosphorylation of hPGK1 at S203 and S256 has been associated with enzyme import from the cytosol to the mitochondria and the nucleus respectively. These changes in subcellular locations drive tumorigenesis and are likely associated with site-specific changes in protein stability. In this work, we investigate the effects of site-specific phosphorylation on thermal and kinetic stability and protein structural dynamics by hydrogen-deuterium exchange (HDX) and molecular dynamics (MD) simulations. We also investigate the binding of 3-phosphoglycerate and Mg-ADP using these approaches. We show that the phosphomimetic mutation S256D reduces hPGK1 kinetic stability by 50-fold, with no effect of the mutation S203D. Calorimetric studies of ligand binding show a large decrease in affinity for Mg-ADP in the S256D variant, whereas Mg-ADP binding to the WT and S203D can be accurately investigated using protein kinetic stability and binding thermodynamic models. HDX and MD simulations confirmed the destabilization caused by the mutation S256D (with some long-range effects on stability) and its reduced affinity for Mg-ADP due to the strong destabilization of its binding site (particularly in the apo-state). Our research provides evidence suggesting that modifications in protein stability could potentially enhance the translocation of hPGK1 to the nucleus in cancer. While the structural and energetic basis of its mitochondrial import remain unknown.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142142259","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

SMAR1 and p53-regulated lncRNA RP11-431M3.1 enhances HIF1A translation via miR-138 in colorectal cancer cells under oxidative stress. SMAR1和p53调控的lncRNA RP11-431M3.1通过miR-138增强氧化应激下结直肠癌细胞中HIF1A的翻译。

The FEBS journal Pub Date : 2024-09-06 DOI: 10.1111/febs.17253

Ganesh Suraj Bose, Shruti Jindal, Kiran Gautam Landage, Aarzoo Jindal, Monali Prakash Mahale, Abhijeet P Kulkarni, Smriti Mittal

{"title":"SMAR1 and p53-regulated lncRNA RP11-431M3.1 enhances HIF1A translation via miR-138 in colorectal cancer cells under oxidative stress.","authors":"Ganesh Suraj Bose, Shruti Jindal, Kiran Gautam Landage, Aarzoo Jindal, Monali Prakash Mahale, Abhijeet P Kulkarni, Smriti Mittal","doi":"10.1111/febs.17253","DOIUrl":"https://doi.org/10.1111/febs.17253","url":null,"abstract":"Eukaryotic cells respond to stress by altering coding and non-coding gene expression programs. Alongside many approaches and regulatory mechanisms, long non-coding RNAs (lncRNA) are finding a significant place in gene regulation, suggesting an involvement in various cellular processes and pathophysiology. LncRNAs are regulated by many transcription factors, including SMAR1 and p53, which are tumor suppressor genes. SMAR1 inhibits cancer cell metastasis and invasion and is also known to inhibit apoptosis during low-dose stress in coordination with p53. Data mining analysis suggested that these tumor suppressor genes might coregulate the lncRNA RP11-431M3.1 in colon cancer cells. Importantly, RP11-431M3.1 expression was found to be negatively correlated with patient survival rates in a number of cancers. Oxidative stress occurs when an imbalance in the body is caused by reactive oxygen species (ROS). This imbalance is known to be important in the development/pathogenesis of colon cancer. We are researching the role and control of this lncRNA in HCT116 cells under conditions of oxidative stress. We observed a dose-dependent differential expression of lncRNA upon H2O2 treatment and found that p53 and SMAR1 bind differentially to the promoter in response to the dose of stress inducer used. RP11-431M3.1 was observed to sponge miR-138 which has an important target gene, hypoxia-inducible factor (HIF1A). miR-138 was observed to bind differentially to RP11-431M3.1 and HIF1A RNA depending on the dose of oxidative stress. Furthermore, the knockdown of RP11-431M3.1 decreased the migration and proliferation of colon cancer cells. Our results suggest a previously undescribed regulatory mechanism through which RP11-431M3.1 is transcriptionally regulated by SMAR1 and p53, target HIF1A through miR-138, and highlight its potential as a therapeutic and diagnostic marker for cancer.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142142260","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

USP19 exerts a tumor-promoting role in diffuse large B cell lymphoma through stabilizing PARK7. USP19 通过稳定 PARK7 在弥漫大 B 细胞淋巴瘤中发挥肿瘤促进作用。

The FEBS journal Pub Date : 2024-09-06 DOI: 10.1111/febs.17259

Yaqing Li, Xiyang Liu, Yulai Li, Jieting Wang, Mengqian Zhang, Weili Xue, Mingzhi Zhang

{"title":"USP19 exerts a tumor-promoting role in diffuse large B cell lymphoma through stabilizing PARK7.","authors":"Yaqing Li, Xiyang Liu, Yulai Li, Jieting Wang, Mengqian Zhang, Weili Xue, Mingzhi Zhang","doi":"10.1111/febs.17259","DOIUrl":"https://doi.org/10.1111/febs.17259","url":null,"abstract":"Diffuse large B-cell lymphoma (DLBCL) is the most common subtype of non-Hodgkin lymphoma and is associated with a poor prognosis. Data from the Gene Expression Profiling Interactive Analysis (GEPIA) database revealed dysregulated expression of several ubiquitin-specific proteases (USPs) in DLBCL tissues (DLBCL vs. non-DLBCL = 47 vs. 337), including USP19 (log2fold change = 1.17, P < 0.05). USP19 is closely linked to tumorigenesis, but its role in DLBCL progression remains largely unknown. Here, we investigated the role of USP19 in DLBCL development. Genetic manipulation of USP19 using adenovirus-based vectors was performed in two DLBCL cell lines, SUDHL4 and DB cells. The results showed that USP19 knockdown suppressed the proliferation, anchorage-independent growth and xenograft tumor formation of DLBCL cells and arrested the cell cycle at the G1 stage. In parallel, DLBCL cells overexpressing USP19 acquired a more malignant phenotype. Next, to explore USP19 interactors, we performed co-immunoprecipitation/liquid chromatography-mass spectrometry and identified potential interacting proteins. Among them, Parkinson disease protein 7 (PARK7), a member of the peptidase C56 family known to be involved in carcinogenesis, was further validated to bind with and be stabilized by USP19. Additionally, we found that USP19 induced PARK7 deubiquitylation in both DLBCL cell lines, and PARK7 acted as a downstream effector of USP19 in regulating the growth of DLBCL cells. Collectively, USP19 exerts a tumor-promoting role in DLBCL through interacting with and stabilizing PARK7.","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2024-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142142261","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

PELO regulates erythroid differentiation through interaction with MYC to upregulate KLF10. PELO 通过与 MYC 相互作用上调 KLF10 来调节红细胞分化。

The FEBS journal Pub Date : 2024-08-29 DOI: 10.1111/febs.17254

Jinglan Hao, Guiqin Han, Xin Liang, Yongtong Ruan, Chen Huang, Naer Sa, Hang Hu, Bixi Hu, Zhongqi Li, Kai Zhang, Ping Gao, Xiaoming Dong

引用次数: 0

Further diversity in the origins of fish antifreeze proteins 鱼类抗冻蛋白起源的进一步多样性。

The FEBS journal Pub Date : 2024-08-29 DOI: 10.1111/febs.17260

Kathryn Vanya Ewart

引用次数: 0