Готові списки джерел за темами / FBXO24

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Добірка наукової літератури з теми "FBXO24"

Автор: Grafiati

Опубліковано: 11 березня 2023

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Статті в журналах з теми "FBXO24"

Chen, Wei, Sheng Xiong, Jin Li, Xiuying Li, Yuan Liu, Chunbin Zou, and Rama K. Mallampalli. "The Ubiquitin E3 Ligase SCF-FBXO24 Recognizes Deacetylated Nucleoside Diphosphate Kinase A To Enhance Its Degradation." Molecular and Cellular Biology 35, no. 6 (January 12, 2015): 1001–13. http://dx.doi.org/10.1128/mcb.01185-14.

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The Skp-Cul-F box (SCF) ubiquitin E3 ligase machinery recognizes predominantly phosphodegrons or, less commonly, an (I/L)Q molecular signature within substrates to facilitate their recruitment in mediating protein ubiquitination and degradation. Here, we examined the molecular signals that determine the turnover of the multifunctional enzyme nucleoside diphosphate kinase A (NDPK-A) that controls cell proliferation. NDPK-A protein exhibits a half-life of ∼6 h in HeLa cells and is targeted for ubiquitylation through actions of the F-box protein FBXO24. SCF-FBXO24 polyubiquitinates NDPK-A at K85, and two NH 2 -terminal residues, L55 and K56, were identified as important molecular sites for FBXO24 interaction. Importantly, K56 acetylation impairs its interaction with FBXO24, and replacing K56 with Q56, an acetylation mimic, reduces NDPK-A FBXO24 binding capacity. The acetyltransferase GCN5 catalyzes K56 acetylation within NDPK-A, thereby stabilizing NDPK-A, whereas GCN5 depletion in cells accelerates NDPK-A degradation. Cellular expression of an NDPK-A acetylation mimic or FBXO24 silencing increases NDPK-A life span which, in turn, impairs cell migration and wound healing. We propose that lysine acetylation when presented in the appropriate context may be recognized by some F-box proteins as a unique inhibitory molecular signal for their recruitment to restrict substrate degradation.

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Yuan, Lamei, Zhi Song, Xiong Deng, Zhijian Yang, Yan Yang, Yi Guo, Hongwei Lu, and Hao Deng. "Genetic Analysis of FBXO2, FBXO6, FBXO12, and FBXO41 Variants in Han Chinese Patients with Sporadic Parkinson’s Disease." Neuroscience Bulletin 33, no. 5 (March 24, 2017): 510–14. http://dx.doi.org/10.1007/s12264-017-0122-5.

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Chen, Wei, Denghui Gao, Long Xie, Anling Wang, Hui Zhao, Chaowan Guo, Yunqi Sun, Yanfeng Nie, An Hong, and Sheng Xiong. "SCF-FBXO24 regulates cell proliferation by mediating ubiquitination and degradation of PRMT6." Biochemical and Biophysical Research Communications 530, no. 1 (September 2020): 75–81. http://dx.doi.org/10.1016/j.bbrc.2020.06.007.

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Zhang, Yuan-Meng, Ling-Bing Meng, Si-Jun Yu, and Dong-Xing Ma. "Identification of potential crucial genes in monocytes for atherosclerosis using bioinformatics analysis." Journal of International Medical Research 48, no. 4 (April 2020): 030006052090927. http://dx.doi.org/10.1177/0300060520909277.

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Objective To use bioinformatics tools to screen for gene biomarkers from monocytes, which play an important role in the pathogenesis of atherosclerosis. Methods Two expression profiling datasets (GSE27034 and GSE10195) were obtained from the Gene Expression Omnibus dataset and the differentially expressed genes (DEGs) between atherosclerotic human peripheral blood mononuclear cells (PBMC) samples and control subjects were screened using GEO2R. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes pathway enrichment analyses were conducted for the DEGs. STRING and MCODE plug-in of Cytoscape were used for constructing a protein–protein interaction network and analysing hub genes. Results The two datasets had 237 DEGs in common between non-atherosclerotic- and atherosclerotic PBMC samples. Functional annotation demonstrated that these DEGs were mainly enriched in protein binding, positive regulation of transcription from RNA polymerase II promoter, nucleus and viral carcinogenesis. Five hub genes, FBXL4, UBOX5, KBTBD6, FZR1 and FBXO2, were identified. Conclusion This present bioinformatics analysis identified that the FBXL4, UBOX5, KBTBD6 and FBXO21 genes might play vital roles in the pathogenesis of atherosclerosis. These four genes might represent new biomarkers for the diagnosis and treatment of atherosclerosis.

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Angeli, Franca, Russell Wyborski, Bill Chen, Rama Mallampalli, and Michael Lark. "P157 FBXO3-FBXL2 AXIS MODULATORS AS A NOVEL CLASS OF ORAL SMALL MOLECULE COMPOUNDS FOR THE TREATMENT OF CROHN’S DISEASE." Inflammatory Bowel Diseases 26, Supplement_1 (January 2020): S6. http://dx.doi.org/10.1093/ibd/zaa010.014.

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Abstract Background Ubiquitination is a common post-translational modification, tagging proteins for degradation. The ubiquitin proteasome system is activated in Crohn’s Disease (CD), and modulation of its components might be a novel strategy for therapeutic intervention to control inflammation. The conjugation of ubiquitin to a target protein is orchestrated by a series of enzymatic reactions, the last step being catalyzed by a selective ubiquitin E3 ligase. Among ubiquitin E3 ligases, Fbxl2 serves as a sentinel gatekeeper to limit inflammation by targeting and enhancing the degradation of tumor necrosis factor receptor associated factors (TRAF) proteins, which link cell surface signals (through NFkB signaling) to cytokine secretion. In addition, Fbxl2 controls the ubiquitination of the inflammasome, NOD-like receptor protein 3 (NLRP3), which mediates the release of interleukin (IL)1β and IL18 (Fig.1). Fbxl2 protein itself is ubiquitinated and degraded by another protein, called Fbxo3. Inhibition of Fbxo3 results in increased Fbxl2 levels and decreased TRAF and NLRP3. Individuals with a natural occurring polymorphism within Fbxo3V221Ihave decreased lipopolysaccharide(LPS)-induced cytokine (TNFα, IL1β & IL6) production, Fbxo3 and TRAF levels and increased Fbxl2, providing human genetic target validation for Fbxo3-Fbxl2 axis modulation in inflammatory conditions. BC1261 is a first-in-class, selective, orally available Fbxo3 inhibitor in clinical development for the treatment of CD. Methods and Results In vitro data demonstrated that BC1261 binds to Fbxo3, prevents Fbxo3/Fbxl2 association and produces a concentration-dependent inhibition of LPS-induced release of TNFα and IL1β from human peripheral blood mononuclear cells. In an acute DSS-mouse model, administration of BC-1261 via drinking water ad libitum (30 μg/ml) or by daily intraperitoneal (IP) injection (150 μg) for 5 days resulted in the attenuation of the shortening of colonic length, tissue damage (Fig2.A), and TNFα and IL6 tissue levels (Fig.2B). In a repeated DSS-mouse model, BC-1261 (10 mg/kg bid) given orally for 19 days was comparable to the positive control (anti-p40) in the DAI composite (Fig2.C), stool consistency (Fig2.D), and histopathology score in the proximal colon (Fig2.E). BC-1261 also lead to clinically relevant reductions on endoscopy score (Fig2.F). Conclusion BC1261, a Fbxo3 inhibitor, was efficacious in both acute and chronic preclinical models of colitis. Taken together, these results suggest the potential utility of selective Fbxo3-Fbxl2 modulation in the treatment of CD.

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Masle-Farquhar, Etienne, Amanda Russell, Yangguang Li, Fen Zhu, Lixin Rui, Robert Brink, and Christopher C. Goodnow. "Loss-of-function of Fbxo10, encoding a post-translational regulator of BCL2 in lymphomas, has no discernible effect on BCL2 or B lymphocyte accumulation in mice." PLOS ONE 16, no. 4 (April 29, 2021): e0237830. http://dx.doi.org/10.1371/journal.pone.0237830.

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Regulation of the anti-apoptotic BCL2 protein determines cell survival and is frequently abnormal in B cell lymphomas. An evolutionarily conserved post-translational mechanism for over-expression of BCL2 in human B cell lymphomas and the BCL2 paralogue CED-9 in Caenorhabditis elegans results from loss-of-function mutations in human FBXO10 and its C.elegans paralogue DRE-1, a BCL2/CED-9-binding subunit of the SKP-CULLIN-FBOX (SCF) ubiquitin ligase. Here, we tested the role of FBXO10 in BCL2 regulation by producing mice with two different CRISPR/Cas9-engineered Fbxo10 mutations: an Asp54Lys (E54K) missense mutation in the FBOX domain and a Cys55SerfsTer55 frameshift (fs) truncating mutation. Mice homozygous for either mutant allele were born at the expected Mendelian frequency and appeared normal in body weight and appearance as adults. Spleen B cells from homozygous mutant mice did not have increased BCL2 protein, nor were the numbers of mature B cells or germinal centre B cells increased as would be expected if BCL2 was increased. Other lymphocyte subsets that are also regulated by BCL2 levels also displayed no difference in frequency in homozygous Fbxo10 mutant mice. These results support one of two conclusions: either FBXO10 does not regulate BCL2 in mice, or it does so redundantly with other ubiquitin ligase complexes. Possible candidates for the latter include FBXO11 or ARTS-XIAP. The difference between the role of FBXO10 in regulating BCL2 protein levels in C. elegans and in human DLBCL, relative to single-gene deficient mouse leukocytes, should be further investigated.

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Manfiolli, Adriana O., Ana Leticia G. C. Maragno, Munira M. A. Baqui, Sami Yokoo, Felipe R. Teixeira, Eduardo B. Oliveira, and Marcelo D. Gomes. "FBXO25-associated Nuclear Domains: A Novel Subnuclear Structure." Molecular Biology of the Cell 19, no. 5 (May 2008): 1848–61. http://dx.doi.org/10.1091/mbc.e07-08-0815.

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Skp1, Cul1, Rbx1, and the FBXO25 protein form a functional ubiquitin ligase complex. Here, we investigate the cellular distribution of FBXO25 and its colocalization with some nuclear proteins by using immunochemical and biochemical approaches. FBXO25 was monitored with affinity-purified antibodies raised against the recombinant fragment spanning residues 2-62 of the FBXO25 sequence. FBXO25 protein was expressed in all mouse tissues tested except striated muscle, as indicated by immunoblot analysis. Confocal analysis revealed that the endogenous FBXO25 was partially concentrated in a novel dot-like nuclear domain that is distinct from clastosomes and other well-characterized structures. These nuclear compartments contain a high concentration of ubiquitin conjugates and at least two other components of the ubiquitin-proteasome system: 20S proteasome and Skp1. We propose to name these compartments FBXO25-associated nuclear domains. Interestingly, inhibition of transcription by actinomycin D or heat-shock treatment drastically affected the nuclear organization of FBXO25-containing structures, indicating that they are dynamic compartments influenced by the transcriptional activity of the cell. Also, we present evidences that an FBXO25-dependent ubiquitin ligase activity prevents aggregation of recombinant polyglutamine-containing huntingtin protein in the nucleus of human embryonic kidney 293 cells, suggesting that this protein can be a target for the nuclear FBXO25 mediated ubiquitination.

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Guo, Fengjie, Xiaoyu Jiang, Domenico Roberti, Lixin Rui, and Izidore S. Lossos. "FBXO10 Targets HGAL for Degradation." Blood 126, no. 23 (December 3, 2015): 3904. http://dx.doi.org/10.1182/blood.v126.23.3904.3904.

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Abstract Expression of the Human Germinal center Associated Lymphoma (HGAL) gene is restricted to germinal center (GC) B-lymphocytes and GC-derived lymphomas. HGAL expression identifies lymphomas characterized by a better prognosis. We previously showed that HGAL is a unique adaptor protein that regulates both cell motility and B-cell receptor (BCR) signaling, processes that are central for successful completion of the GC reaction. In our previous studies we demonstrated that upon BCR activation HGAL binds to and increases Syk kinase activity, resulting in enhanced BCR signaling. Syk induces HGAL phosphorylation, leading to its redistribution from lipid rafts to the bulk membrane and cytoplasm, followed by its rapid degradation. The mechanism of HGAL degradation is currently unknown. To elucidate the mechanism of HGAL degradation, we hypothesized that HGAL is degraded by a SKP1-CUL1-F-box protein (SCF) ubiquitin ligase complex. Consequently, we examined the ability of HGAL to be recruited to the SCF by screening a panel of F-box proteins transfected into HEK293T cells by reciprocal coimmunoprecipitations (Co-IPs). These studies revealed that HGAL specifically bound only FBXO10. Concordantly, HGAL Co-IPed with endogenous SKP1 and CUL1 in the presence of FBXO10. Furthermore, a dose dependent reduction of HGAL levels was observed in Raji cells transfected with increasing quantities of FBXO10 expressing plasmid. In contrast, none of the other FBXO11 tested F-box proteins affected HGAL levels. The reduction in HGAL protein level by FBXO10 was due to enhanced proteolysis, as demonstrated by the decrease in HGAL protein half-life and the rescue of its levels by either addition of proteasome inhibitor MG132 or expression of a dominant-negative CUL1 mutant (CUL1 (1-242)). Furthermore, depletion of FBXO10 by two short hairpin RNA (shRNA) constructs in Raji cells increased HGAL stability and half-life. SCF complexes mediates protein degradation by polyubiquitination. We therefore examined if HGAL protein can be ubiquinated. To this end we cotransfected 293T cells with HGAL-V5, FBXO10-FLAG, HA-ubiquitin with or without CUL1 (1-242) and blotted immunoprecipitated HGAL for ubiquitin. FBXO10 expression markedly increased HGAL ubiquitination and this was significantly decreased in cells coexpressing CUL1 (1-242). Similarly, HGAL ubiquitination was markedly decreased in cells expressing FBXO10 (FBXO10- ΔF-box), in which the F-box motif, necessary for linking the target protein to the SCF ubiquitin ligase moieties, is deleted. These results support the function of FBXO10 in binding HGAL and facilitating its ubiquitination by the SCF complex prior to its degradation. We next analyzed the functional significance of HGAL degradation by FBXO10 on BCR activation, as measured by intracellular and transmembrane Ca2+ mobilization. Overexpression of FBXO10 in Raji cells expressing endogenous HGAL led to decreased levels of HGAL and in Ca2+ mobilization. In contrast, FBXO10 did not affect BCR-induced Ca2+ mobilization in Raji cells in which HGAL was deleted by crispr/Cas9 targeting. These results suggest that FBXO10 affects BCR signaling via regulating HGAL levels. While FBXO10 mediates HGAL degradation post BCR-induced HGAL phosphorylation, FBXO10 also bound HGAL in the absence of BCR activation. The binding of FBXO10 to HGAL was unaffected in Raji cells incubated with anti-IgM antibodies. Treatment of cellular lysates with l-phosphatase did not affect FBXO10 binding to HGAL. These findings indicate that FBXO10-dependent degradation of HGAL is phosphorylation independent. In contrast, HGAL degradation by FBXO10 was dependent on HGAL lipid raft localization, since HGAL myristoylation and palmitoylation mutants (G2A, C43A/C45A, and G2A/C43A/C45A) exhibited decreased Co-IP with the FBXO10 protein. To further map FBXO10 binding motifs of HGAL, we generated HGAL deletion and mutant constructs and examined their ability to Co-IP with FBXO10. These studies revealed that HGAL amino acids 91-95(HRVLC) mediate HGAL binding to FBXO10. In summary, our results demonstrate that SCFFBXO10 is the ubiquitin ligase for HGAL and regulates BCR signaling via controlling HGAL expression. Some diffuse large cell lymphomas expressing HGAL harbor inactivating mutations or express low levels of FBXO10, thus predisposing to enhanced BCR signaling- a phenomenon implicated in lymphomagenesis. Disclosures No relevant conflicts of interest to declare.

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Qie, Shuo. "The E3 Ubiquitin Ligase Fbxo4 Functions as a Tumor Suppressor: Its Biological Importance and Therapeutic Perspectives." Cancers 14, no. 9 (April 25, 2022): 2133. http://dx.doi.org/10.3390/cancers14092133.

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Fbxo4, also known as Fbx4, belongs to the F-box protein family with a conserved F-box domain. Fbxo4 can form a complex with S-phase kinase-associated protein 1 and Cullin1 to perform its biological functions. Several proteins are identified as Fbxo4 substrates, including cyclin D1, Trf1/Pin2, p53, Fxr1, Mcl-1, ICAM-1, and PPARγ. Those factors can regulate cell cycle progression, cell proliferation, survival/apoptosis, and migration/invasion, highlighting their oncogenic or oncogene-like activities. Therefore, Fbxo4 is defined as a tumor suppressor. The biological functions of Fbxo4 make it a potential candidate for developing new targeted therapies. This review summarizes the gene and protein structure of Fbxo4, the mechanisms of how its expression and activity are regulated, and its substrates, biological functions, and clinicopathological importance in human cancers.

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Дисертації з теми "FBXO24"

Medeiros, Ana Carla. "Caracterização parcial do complexo SCF1 contendo a proteína FBXO25 fosforilada." Universidade de São Paulo, 2015. http://www.teses.usp.br/teses/disponiveis/17/17131/tde-09092015-110529/.

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A FBXO25 é parte de uma E3 ligase do tipo RING, (Really Interesting New Gene), oligomérica do tipo SCF, responsável pelo reconhecimento específico do substrato a ser degradado via Sistema Ubiquitina-Proteassoma (SUP). O SUP é o principal mecanismo proteolítico intracelular, responsável pela degradação de 80-90% das proteínas citosólicas e nucleares. A FBXO25 é capaz de formar um complexo SCF1 ativo (formado pela interação das proteínas Skp1, Cul1, Roc1 e uma proteína do tipo F-box), capaz de ubiquitinar seus substratos. Essa proteína se acumula no núcleo celular formando uma nova estrutura subnuclear denominada FANDs (FBXO25 Associated Nuclear Domains) que estão envolvidos na ubiquitinação nuclear. Nesse trabalho, purificamos complexos SCF1 (WT ou sem o domínio de interação com Skp1 (F)), tratados ou não com PMA, pela técnica de imunoprecipitação. Identificamos por espectrometria de massas um sítio de fosforilação essencial para FBXO25, quando células transfectadas são tratadas com o mitógeno PMA. Buscamos também por substratos diferencialmente ubiquitinados por esses complexos, por meio de ensaios em ProtoArrays®, identificando substratos envolvidos na via de sinalização ERK1/2.
The FBXO25 is an E3 ligase RING type (Really Interesting New Gene), SCF oligomeric type, responsible for the specific recognition of the substrate to be degraded via the ubiquitin-proteasome system (SUP). SUP is the main intracellular proteolytic mechanism responsible for 80-90% degradation of cytosolic and nuclear proteins. The FBXO25 is capable of forming a complex SCF1 (formed by the interaction of proteins Skp1, Cul1, Roc1 protein and a type F-box), resulting in an active SCF complex which is able to ubiquitinate their substrates. This protein accumulates in the nucleus forming a subnuclear structure called FANDs (FBXO25 Associated Nuclear Domains) that are involved in nuclear ubiquitination. In this work, we purify complex SCF1 (WT or F- box, which is not able to interact with Skp1), treated or not with PMA, by immunoprecipitation technique. We identified by mass spectrometry, an essential phosphorylation site for FBXO25, when it is phosphorylated under the action of the mitogenic reagent PMA. We also search for differentially ubiquitinated substrates for these complexes, by testing in ProtoArrays® identifying substrates involved in the signaling pathway ERK1 / 2.

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Vieira, Nichelle Antunes. "Caracterização de células humanas Hap1 nocaute para FBXO25: via de sinalização da ERK quinase e proliferação celular." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/17/17131/tde-25042018-143544/.

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A proteína FBXO25 é uma E3-ligase do tipo SCF, responsável pela seletividade da ligação da Ub à proteína substrato e pelo direcionamento da proteína marcada para o barril proteassomal 26s. Sabe-se que FBXO25 é capaz de interagir e ubiquitinar a proteína Elk-1 em células HEK293T e, assim, inibir a expressão de genes importantes na regulação da proliferação celular, como C-FOS e EGR-1, após estímulo com o mitógeno PMA. Aqui mostramos que FBXO25 atua em um outro ponto da via das MAPKs, modulando os níveis de fosforilação de ERK1/2. Por meio da utilização de células nocaute para FBXO25 (FBXO25KO) foi possível observar que o tratamento com PMA promoveu aumento dos níveis de fosforilação de ERK1/2 nestas células quando comparadas com sua linhagem parental. Observouse também que o estímulo com os mitógenos PMA ou ATP levou a um aumento da proliferação celular não relacionada à modulação direta do ciclo celular nas células nocautes, sendo que estas apresentaram uma redução significativa dos seus níveis de apoptose. Tomando esses resultados em conjunto, mostramos que FBXO25 atua sobre a sinalização de MAPK por meio de redução da ativação ERK1/2 e, dessa forma, promove uma resposta secundária sobre o fenótipo de proliferação celular
The FBXO25 protein is an SCF-type E3-ligase responsible for the selectivity of Ub binding to the protein and the targeting of the labeled protein to the 26s proteasome barrel. FBXO25 has been long known to be able to interact and ubiquitinate the Elk-1 protein in HEK293T cells, thereby inducing a decrease in the expression of important genes in the regulation of cell proliferation such as CFOS and EGR-1 after stimulation with the mitogen PMA. Here we show that FBXO25 acts at another point in the MAPK pathway by modulating the ERK1/2 phosphorylation levels. We observed that the treatment with PMA rised the phosphorylated levels of ERK1/2 in knockout cells for FBXO25 (FBXO25KO) when compared to its parental lineage. Stimulation with the mitogens PMA or ATP also led to an increase in cell proliferation unrelated to a direct modulation of the cell cycle in knockout cells, with a significant weight of apoptosis levels being observed. Taking these results together, we show that FBXO25 acts on MAPK signaling by reducing ERK1/2 activation and thus promotes a secondary response on the cell proliferation phenotype.

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Tsui, Hoyee. "The role of p21-activated kinase 1 (Pak1) in the heart." Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/the-role-of-p21activated-kinase-1-pak1-in-the-heart(8c34d7bc-a2aa-4ae0-a197-91ed905212f5).html.

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Heart failure is associated with a high mortality rate and is one of the most prevalent diseases worldwide whereby susceptibility increases with age. The development of heart failure occurs over an extensive period of time in which arrhythmias and hypertrophy are both very prevalent manifestations throughout this progression. Arrhythmias are defined as an irregular rhythm originating from intracellular calcium dysregulation, which can be fatal. Cardiac hypertrophy is a compensatory condition induced by increased workload involving augmented cardiomyocyte growth accompanied by myocardial remodelling. However, under prolonged periods of increased stress this compensatory mechanism can lead to cardiac dysfunction. The current treatments for heart failure are mainly aimed at relieving symptoms or itself possess proarrhythmic ability. Therefore it is fundamental to elucidate the pathways involved in arrhythmias and hypertrophy for the development of more effective treatment. p21 activated protein kinase (Pak1) is a novel gene involved in the regulation of cardiac function, however, the mechanisms involved remain inconclusive. This study has demonstrated Pak1 to be both antiarrhythmic and antihypertrophic, emphasizing Pak1 as a credible therapeutic target for simultaneously treating both manifestations. The antiarrhythmic properties of Pak1 were demonstrated through cardiomyocyte-specific Pak1 knockout (Pak1cko) mouse model which underwent Isoproterenol (ISO) stimulation for 2 weeks. Compared with ISO treated control group, the Pak1cko group had increased calcium irregularities and particularly a prolongation in sarcoplasmic reticulum (SR) calcium refill. The absence of Pak1 abrogated the transcriptional up-regulation of sarcoplasmic reticulum calcium ATPase 2a (SERCA2a) under stressed conditions. Further analysis in neonatal rat cardiomyocytes (NRCMs) revealed this regulation to be through activation of the transcription factor, SRF. The antihypertrophic effects of Pak1 were further illustrated through cardiomyocyte-specific overexpressed constitutively-active Pak1 (Pak1cTG) mice which were subjected to transverse aortic constriction (TAC) for 3 weeks. Compared to TAC control group, Pak1cTG mice had improved cardiac performance accompanied with diminished fibrosis. Further analysis led to the discovery of a novel antihypertrophic pathway of Pak1 involving positive regulation of the E3ligase, Fbxo32 through activation of Smad3. This pathway is vital in the prevention of calcineurin (PP2B) accretion. Berberine administration in TAC treated mice corroborated that Fbxo32 up-regulation is sufficient in the prevention of hypertrophy. In conclusion, my study has demonstrated that Pak1 conveys antiarrhythmic influence through the up-regulation of SERCA2a. In the prevention of pathological hypertrophy, Pak1 inhibits PP2B through positive regulation of Fbxo32. Overall, my thesis has advanced the knowledge about cardioprotective pathways initiated by Pak1 under stressed conditions, presenting Pak1 as a promising therapeutic target.

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Stavropoulou, Alexandra Vassiliki. "Histone deacetylase (HDAC) inhibitors and FBXL20 in breast cancer." Thesis, Imperial College London, 2008. http://hdl.handle.net/10044/1/7389.

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Research performed over the last decade has highlighted the role of HDAC inhibitors (HDACis) as modulators of transcriptional activity and as a potential new class of therapeutic agents against many types of malignacies including breast cancer. These drugs inhibit histone deacetylases, leading to derepression of transcription of various genes that are important for cell cycle arrest and cell death. Trichostatin A (TSA) is one of the best established HDAC inhibitors and has been shown to exhibit potent differentiating and anti-proliferative properties. My data demonstrated that treatment of the MCF-7 breast cancer cell line with TSA causes G2/M phase cell cycle arrest. I characterised the novel F-Box protein called FBXL20 and identified it as a direct target of TSA. This protein is part of a novel E3 ligase complex as it binds Skpl, CUL-I and ROC-I and forms a classical SCF complex that is responsible for ubiquitination and targeting proteins for degradation by the 26S proteasome. I further studied the differences between FBXL20 in human cells and its isoform in rat cells. My data showed that FBXL20 is localised in the cytoplasm, concentrated around the nucleus and plays a role in the TSA-induced effects in MCF-7 cells, through regulating the pro-apoptotic protein Bim. Silencing FBXL20 abolished the G2/M arrest caused by TSA treatment. Although FBXL20 is a similar protein to Skp2 they are regulated by different proteins and exert different functions. These findings provide novel data to demonstrate that known and novel HDACis induce G2/M arrest followed by cell death and that this arrest is dependent on the novel FBXL20 protein in breast cancer cells. Using these newly defined properties of HDACis, I screened a panel of potential HDACis and identified at least one to be more potent than SAHA, which is currently used in the clinical setting and showed that it is able to inhibit proliferation, cause cell cycle arrest and cell death of breast cancer cells.

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Patel, Shachi. "Fbxo7 in T cell development and oncogenesis." Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.709293.

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Rowicka, Paulina Aiko. "The role of FBXO7 in mitochondrial biology and Parkinson's disease." Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/282989.

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Parkinson's disease is a progressive neurodegenerative disorder of the central nervous system, manifesting with both motor and non-motor symptoms. Autosomal recessive mutations in the FBXO7 gene have been identified to cause a rapidly progressing early-onset form of PD. Canonically, FBXO7 functions as a substrate-recruiting subunit of the SCF-type E3 ubiquitin ligase. However, it also has a variety of other atypical functions, such as cell cycle regulation, proteasome regulation, and mitophagy. The overall aim of this research was to characterise the functional role of FBXO7 in various in vitro and in vivo PD models. The models examined included FBXO7 shRNA knockdown SH-SY5Y cell lines, FBXO7 CRISPR knockout SH-SY5Y cell lines, primary patient fibroblasts with a FBXO7 mutation, and MEFs and tissues from a Fbxo7 KO mouse. My analysis of fibroblasts from a patient without FBXO7 expression revealed several interesting phenotypes. Briefly, the patient fibroblasts proliferated slower due to increased apoptosis and lower CDK6 and cyclin D1 expression, which led to fewer cells progressing through the G1 phase of the cell cycle. My experiments showed that these cells also had mitochondrial respiration defects, exhibiting lower basal respiration, ATP production, maximal respiration and spare capacity, in addition to complex I, III and IV deficiencies. Patient fibroblasts also had significantly lower levels of 12S and 16S ribosomal mRNA transcripts, which are necessary for the translation of mitochondrially encoded subunits of complexes I, III, and IV. Similar phenotypes were also observed in MEFs from a Fbxo7 KO mouse model, indicating conservation between human and mouse FBXO7 in regulating mitochondria, cell death and proliferation. In a tissue-specific KO mouse model of PD, where FBXO7 expression was ablated in the dopaminergic neurons, I analysed proteins regulated by FBXO7 which might be responsible for cell loss in the substantia nigra. I discovered that RPL23, a regulator of MDM2, was ubiquitinated by SCFFbxo7 using K48 chain linkages, promoting its degradation by the proteasome. This suggests that misregulation of the MDM2:p53 axis may underlie the cell loss observed in this conditional Fbxo7 KO mouse model. In conclusion, these results elaborate on the role of FBXO7 in mitochondrial biology, and identify a new ubiquitination substrate of FBXO7 in a mouse model of PD. It is hoped that by elucidating the potential pathogenic mechanisms of FBXO7 in rare familial forms of the disease, it will be possible to translate findings to the more prevalent sporadic forms of Parkinson's disease as well.

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Sammler, Esther. "Signalling pathway of FBXO7 and its role in hereditary Parkinsonism." Thesis, University of Dundee, 2014. https://discovery.dundee.ac.uk/en/studentTheses/2a2889b3-20b5-4353-af11-72782c07ef3a.

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Parkinson’s Disease (PD) is the second most common neurodegenerative disorder after Alzheimer’s and old age is the strongest risk factor for developing PD. PD has traditionally been seen as a motor disorder, but its non-motor symptoms such as dysautonomia, sensory dysfunction, sleeping problems and neuropsychiatric features equally add to the disease burden. There is no cure for PD and this is probably a reflection of our poor understanding of the disease pathogenesis. One way of tackling this is to focus on the small, but significant number of PD patients with a family history compatible with Mendelian autosomal inheritance (10-15%). Hereditary and sporadic PD share important clinical and neuropathological features, and there is reasonable hope that dissecting molecular pathways of PD gene products will have more general implications for the pathophysiology of PD associated neurodegeneration and help device new treatment strategies. Mutations in the FBXO7 gene have recently been shown to cause an autosomal recessive early onset Parkinsonian-pyramidal syndrome and FBXO7 has been designated as PARK 15 (Di Fonzo et al., 2009). FBXO7 is a member of the F-box protein family, which functions as the variable subunit of Skp1-Cullin1-F-box protein (SCF) E3 ubiquitin ligase complexes and as such dictate substrate specificity. The canonical outcome of ubiquitylation is proteasomal degradation and my working hypothesis is that FBXO7 may be involved in protein quality control in the brain. A perturbation thereof may be a first step towards FBXO7 dependent disease. At the time of starting with my PhD project, little was known about the molecular function of FBXO7 and how mutations in FBXO7 result in neurodegeneration. In order to learn more and dissect the signalling pathway of FBXO7 I have used tagged stable overexpression cell lines of the FBXO7 wildtype as well as human disease mutant proteins for tag-pulldowns followed by mass-spectrometry to identify interacting partners and possible substrates. With this approach I have been able to confirm the interaction between FBXO7 and its core SCF E3 ligase partners as well as some of the previously reported interacting partners. I have been able to show that not only the FBXO7 wildytpe protein, but also all of the so far reported human disease mutants are able to assemble into an SCF complex. Hence, my fist conclusion is that the human disease mutants do not exert their pathogenicity by SCF complex disruption. Next, a knock-in (KI) mouse model of one of the pathogenic FBXO7 mutations (R378G) was generated and evaluated by molecular and biochemical approaches as well as motor and behaviour phenotyping. In particular, I have used the Fbxo7 mouse model for extensive proteomic screens to identify wildtype (wt) and KI Fbxo7 interactors: endogenous Fbxo7 immunoprecipitations from mouse brain lysates and subsequent fingerprint mass-spectrometry; differential whole proteome: ex vivo differential dimethyl labelling of wt and KI brain samples, and Fbxo7-dependent ubiquitinome analysis: quantitative di-GLY capture proteomics combining in vivo SILAC labelling with antibody-based affinity enrichment of “di-GLY remnant motifs”- containing peptides prior to proteomic profiling of the wild-type in comparison to the homozygous R379G Fbxo7 KI ubiquitinome in MEF lysates. The di-GLY remnant motif is the signature peptide of ubiquitinylated protein sites at peptide level after tryptic digestions. Some of my findings are: • For the first time I show that endogenous Fbxo7 actually assembles into an Skp1-Cullin1-Fbxo7 complex and that the pathogenic R378G does not disrupt SCFFbxo7-KI complex formation in vivo. This is true for the Fbxo7 KI mouse model, but also for patient derived immortalized cell lines carrying the R378G FBXO7 mutation.• Endogenous Fbxo7 interacts with the Sumo E3 ligase complex RanBP2/ RanGAP1*Sumo1/Ubc9 complex. • In the differential enrichment of ubiquitylated protein species in SILAC labelled wild-type and homozygous R379G Fbxo7 KI MEFs, I have clearly identifies 2 highly conserved lysine residues, which are conserved amongst VDAC 1, 2, and 3 in mouse as well as human homologous, to be preferentially ubiquitinylated in a Fbxo7 wild-type background (in collaboration with Dr. Patrick Pedrioli, MRC Programme leader).• There is a significant difference in motor performance between wildtype and homozygous R379G KI Fbxo7 mice at 10 months of age (in collaboration with Dr. Steve Martin, Neuroscience Division, Dundee). • Furthermore, I have successfully set up an in vitro FBXO7 dependent ubiquitinylation assays.

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Liu, Jia, and 劉佳. "Role of FBXO31 in regulating MAPK-mediated genotoxic stress response and cancer cell survival." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2013. http://hdl.handle.net/10722/205657.

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Esophageal cancer is the third most common digestive tract malignancy. Along with surgery, genotoxic drugs (e.g. cisplatin) and radiotherapy are the mainstays of treatment for this disease. Environmental factors and environmental stress-induced responses contribute to esophageal tumorigenesis and chemoresistance. Studying key molecules in stress-induced signal pathway can help unravel the underlying mechanisms and discover rational therapeutic targets. Cyclin D1 is DNA damage response protein. Genotoxic stress induces rapid cyclin D1 degradation and the molecules mediating this response are cell-type dependent. The first part of this study investigated the changes of cyclin D1 expression in response to genotoxic stress in immortalized esophageal epithelial cells, which are experimental models commonly used to study the early events of cancer development. The results showed that cyclin D1 underwent rapid proteasomal degradation before p53-induced p21 accumulation, which substantiates that cyclin D1 plays a role in eliciting cell cycle arrest very early in the DNA damage response. FBXO31 and FBX4, two F-box proteins previously reported to mediate cyclin D1 degradation, were found to be accumulated and unchanged, respectively, after ionizing irradiation in immortalized esophageal epithelial cells and esophageal squamous cell carcinoma (ESCC) cell lines. Yet, knockdown of FBXO31 did not rescue rapid cyclin D1 degradation upon UV or ionizing irradiation. This led to the hypothesis that accumulation of FBXO31 may have novel functions beyond mediating cyclin D1 degradation in cells responding to genotoxic stress. The second part of this study explored the function of FBXO31 in genotoxic stress response. The accumulation of FBXO31 in cancer cells after exposure to various genotoxic stresses was found to coincide with p38 deactivation, giving the clue that FBXO31 may negatively regulate this important pathway. Further studies revealed that knockdown of FBXO31 resulted in sustained activation of stress-activated MAPKs (SAPKs) p38 and JNK, as well as increase in UV-induced cell apoptosis, whereas overexpression of FBXO31 had opposite effects. The inhibitory role of FBXO31 on SAPK activation and apoptosis was confirmed by shRNA rescue experiments. Consistent with the observed anti-apoptotic effect, soft agar, colony formation and in vivo xenograft experiments showed that FBXO31 had oncogenic function in ESCC. Moreover, in vitro and in vivo results showed that knockdown of FBXO31 could sensitize ESCC cells to cisplatin treatment. The mechanism underlying the inhibition of SAPKs by FBXO31 was investigated in the third part of this study. Co-immunoprecipitation results showed that FBXO31 could interact with MKK6 (a p38 activator), but not p38, JNK1, or other MAP2Ks. FBXO31 was found to be co-localized with MKK6 in the cytoplasm. Mapping of interaction domains of FBXO31 revealed that aa 115-240 and aa 351-475 were responsible for binding to MKK6. Further study found that binding of FBXO31 to MKK6 could facilitate the K48-linked polyubiquitination and degradation of MKK6. Taken together, the results of this study showed that FBXO31 accumulation upon genotoxic stress can promote the degradation of MKK6 via K48-linked ubiquitination, thereby inhibiting SAPK activation and protecting cancer cells from genotoxic stress-induced apoptosis. FBXO31 may be a potentially useful therapeutic target to overcome chemoresistance in cancer therapy.
published_or_final_version
Anatomy
Doctoral
Doctor of Philosophy

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Kleppa, Marc-Jens [Verfasser]. "Charakterisierung des Gens Fbxl22 und seiner Funktion während der Muskelentwicklung der Maus / Marc-Jens Kleppa." Hannover : Technische Informationsbibliothek und Universitätsbibliothek Hannover (TIB), 2011. http://d-nb.info/1019235071/34.

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Shang, Jinsai. "STRUCTURAL AND FUNCTIONAL STUDIES OF F-BOX-ONLY PROTEIN FBXO7 AND ITS INTERACTIONS WITH PROTEASOME INHIBITOR PI31." OpenSIUC, 2015. https://opensiuc.lib.siu.edu/dissertations/1053.

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F-box only protein 7 (Fbxo7), a member of the F-box-only subfamily of FBPs, is a biologically and pathophysiologically important human protein that assumes many critical functions. The different functions of Fbxo7 depend on the formation of various multi-protein complexes. Possible interplay between different Fbxo7 functions further complicate the protein-protein interaction networks involved in Fbxo7 biology. Although significant progresses have been made to understand the functions, regulation, specificity, and protein interaction network of Fbxo7, a myriad of questions remain to be answered. The objectives of the work presented in this dissertation are to elucidate the molecular structures underlying the functions of Fbxo7 and the interaction with its protein partners, such as proteasome inhibitor PI31. The best known biological function of Fbxo7 is its role as the substrate-recognition subunit of the SCFFbxo7 (Skp1-Cul1-F-box protein) E3 ubiquitin ligase that catalyzes the ubiquitination of hepatoma up-regulated protein (HURP) and inhibitor of apoptosis protein (IAP). Fbxo7 also assumes various SCF-independent functions through interact with its protein partners that are not the substrates of the ubiquitin proteasome system, such as PI31, Cdk6, p27, PINK1 (PTEN-induced kinase 1), and Parkin. PI31 is a known proteasome regulator which was initially characterized as a proteasome inhibitor in vitro. The binding affinity between Fbxo7 and PI31 is very strong, and The Fbxo7-PI31 interaction is mediated by heterodimerization of the FP domains of the two proteins. This work is focus on study the protein structure of the two FP domains in Fbxo7 and PI3. Chapter 1 reviewed the F-box-only protein Fbxo7 biology including the function of Fbxo7 protein in ubiquitination proteasome pathway and some SCF-independent functions which are relate to human disease. Chapter 2 discussed the function of proteasome inhibitor PI31. With the many important biological functions, Fbxo7 is clearly an extraordinary important protein, but the lack of structural knowledge has hampered efforts to achieve a better understanding of Fbxo7 biology. In this work, we have determined the crystal structure of Fbxo7 FP domain (residues 181-335) and the crystal structure of the PI31 FP domain (residues 1-161) using a longer protein construct both at 2.0Å resolution. The Fbxo7 FP domain adopts an α/β-fold similar to that of the PI31 FP domain and the secondary structure elements of the two FP domains are comparable including the C-terminal helix, indicating that the two FP domains share the same overall global fold. However, an α helix and three β strands in the Fbxo7 are longer than their counterparts in the PI31 FP domain. The two FP domains also differ substantially in the length and conformation of the longest connecting loop. More importantly, structural differences between the two FP domains lead to drastically different modes of inter-domain protein–protein interaction: the PI31 FP domain utilizes either an α interface or β interface for homodimeric interaction, whereas the Fbxo7 FP domain utilizes an αβ interface. We have note that the inter-domain interaction of the Fbxo7 FP domain is much more extensive, featuring a larger contact surface area, better shape complementarity and more hydrophobic and hydrogen-bonding interactions. The results of this structural study provide critical insights into how Fbxo7 may dimerize (or multimerize) and interact with PI31 via the FP domain. Chapter 4 and Chapter 5 discussed the structure determinations, structure features and detail of protein-protein interactions of Fbxo7 and PI31 FP domains. Chapter 2 reviewed the corresponding fundamental biochemical techniques that been used in this study. Chapter 3 discussed protein structure determination by X-ray crystallography in structural biology studies. It was believed that the FP domains of Fbxo7 and PI31 mediate homodimerization and heterodimerization of the proteins and the FP domain is not present in other human proteins. In order to study the Fbxo7-PI31 heterodimerization protein-protein interactions, we performed modeling studies. Chapter 6 discussed the model building and binding studies. Based on the result of model building studies, we propose that an interaction between the two FP domains of Fbxo7 and PI31 should be mediated by a αβ interface using the α-helical surface of the Fbxo7 FP domain and the β-sheet surface of the PI31 FP domain. According to the result of pull down assay, the PI31 FP domain may complete with Skp1 for the binding with Fbxo7. It is possible that the formation of heterodimer between the Fbxo7 and PI31 mediate by FP domains may lead to the Fbxo7 dissociation from SCFFbxo7 complex which might reveal a new regulation mechanism.

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Книги з теми "FBXO24"

Haydu, Julie Erika M. The Roles of F-box and Leucine-Rich Repeat Protein 4 (FBXL4) in Mitochondrial Encephalopathy and T-cell Acute Lymphoblastic Leukemia. [New York, N.Y.?]: [publisher not identified], 2015.

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Morton, Sarah U., Edward G. Neilan, Roy W. A. Peake, Jiahai Shi, Klaus Schmitz-Abe, Meghan Towne, Kyriacos Markianos, Sanjay P. Prabhu, and Pankaj B. Agrawal. "Hyperammonemia as a Presenting Feature in Two Siblings with FBXL4 Variants." In JIMD Reports, 7–15. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/8904_2016_17.

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Antoun, Ghadi, Skye McBride, Jason R. Vanstone, Turaya Naas, Jean Michaud, Stephanie Redpath, Hugh J. McMillan, et al. "Detailed Biochemical and Bioenergetic Characterization of FBXL4-Related Encephalomyopathic Mitochondrial DNA Depletion." In JIMD Reports, 1–9. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/8904_2015_491.

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Guo, Jianping, Brian J. North, Adriana E. Tron, Hiroyuki Inuzuka, and Wenyi Wei. "The Role of FBXO Subfamily of F-box Proteins in Tumorigenesis." In SCF and APC E3 Ubiquitin Ligases in Tumorigenesis, 73–87. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-05026-3_4.

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Ravindranath, Abhilash K., Swayamjot Kaur, and Lorna Rodriguez. "Abstract 4226: CD44 increases drug resistance by protecting FBXO21 mediated ubiquitination of P-glycoprotein." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4226.

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Tsai, M. J., W. Osman, A. Elhance, J. Adair, L. Chafin, J. D. Londino, and R. K. Mallampalli. "FBXO45 Targets IFNLR1 to Impair IFN-lambda Signaling During Influenza Infection." In American Thoracic Society 2022 International Conference, May 13-18, 2022 - San Francisco, CA. American Thoracic Society, 2022. http://dx.doi.org/10.1164/ajrccm-conference.2022.205.1_meetingabstracts.a3622.

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Nelson, David E., and Heike Laman. "Abstract 2961: Spatiotemporal regulation of the SCF ubiquitin ligase component, Fbxo7." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2961.

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Katayama, Kazuhiro, Kohji Noguchi, Junko Mitsuhashi, and Yoshikazu Sugimoto. "Abstract 810: FBXO15 is an F-box protein in E3 ligase complex for P-glycoprotein." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-810.

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Lu, Jianrong, Yue Jin, Anitha K. Shenoy, Hao Chen, Huacheng Luo, Lizi Wu, and Kamal A. Mohammed. "Abstract 1425: FBXO11 suppresses epithelial plasticity and proliferation by ubiquitinating the Snail family of transcription factors." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1425.

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Yan, Ying, Lepakshe Madduri, Nichole Brandquist, Chitra Palanivel, Sumin Zhou, Charles Enke та Michel Ouellette. "Abstract 1986: p53/FBXL20 axis negatively regulates the protein stability of PR55α, a PP2A regulatory subunit". У Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1986.

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Randle, Suzanne J., El Kahina Meziane, Mikhail Lomonosov, and Heike Laman. "Abstract LB-189: Fbxo7 functions in the proliferation and maturation of hematopoietic cells." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-lb-189.

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Xu, F., M. Ceng, and W. Ouyang. "FBXO6 Regulates Antiviral Immunity Through Inhibition of ER-Stress Induced Apoptosis of Alveolar Macrophages." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a3977.

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Stankiewicz, Elzbieta, Xueying Mao, D. Chas Mangham, Lei Xu, Gabrielle Fisher, Bernard North, Henrik Moller, et al. "Abstract 1614: Identification of FBXL4 as a bone metastasis-associated gene in prostate cancer." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1614.

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Valverde, Alfonso García, Jordi Rosell, Daniel Pilco Janeta, Sergi Sayols, Claudia Valverde, Anna Esteve, Marta Gut, et al. "Abstract 3767: FBXO32 ubiquitin ligase mediates apoptosis evasion and adaptation to KIT inhibition in gastrointestinal stromal tumor - GIST." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-3767.

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