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2005 4
2006 5
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83 results

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Page 1
NUB1 and FAT10 Proteins as Potential Novel Biomarkers in Cancer: A Translational Perspective.
Arshad M, Abdul Hamid N, Chan MC, Ismail F, Tan GC, Pezzella F, Tan KL. Arshad M, et al. Cells. 2021 Aug 24;10(9):2176. doi: 10.3390/cells10092176. Cells. 2021. PMID: 34571823 Free PMC article. Review.
The upregulated expression of both NUB1 and FAT10 has been observed in various cancers. NUB1 protein binds to FAT10 non-covalently to promote FAT10 degradation. ...Our knowledge about them is still limited. There is a need to further develop NUB1 and FAT10 as …
The upregulated expression of both NUB1 and FAT10 has been observed in various cancers. NUB1 protein binds to FAT10 non-covale …
Regulation of NUB1 Activity through Non-Proteolytic Mdm2-Mediated Ubiquitination.
Bonacci T, Audebert S, Camoin L, Baudelet E, Iovanna JL, Soubeyran P. Bonacci T, et al. PLoS One. 2017 Jan 18;12(1):e0169988. doi: 10.1371/journal.pone.0169988. eCollection 2017. PLoS One. 2017. PMID: 28099510 Free PMC article.
Here, we report that the oncogenic E3 ubiquitin ligase Mdm2 is a new NUB1 interacting protein which induces its ubiquitination. Interestingly, we found that Mdm2-mediated ubiquitination of NUB1 is not a proteolytic signal. ...We conclude that Mdm2 acts as a positive …
Here, we report that the oncogenic E3 ubiquitin ligase Mdm2 is a new NUB1 interacting protein which induces its ubiquitination. Inter …
NUB1 snubs huntingtin toxicity.
Aron R, Tsvetkov A, Finkbeiner S. Aron R, et al. Nat Neurosci. 2013 May;16(5):523-5. doi: 10.1038/nn.3380. Nat Neurosci. 2013. PMID: 23619755 No abstract available.
Phosphorylated NUB1 distinguishes alpha-synuclein in Lewy bodies from that in glial cytoplasmic inclusions in multiple system atrophy.
Tanji K, Miki Y, Mori F, Kon T, Kakita A, Takahashi H, Wakabayashi K. Tanji K, et al. Brain Pathol. 2019 Nov;29(6):803-812. doi: 10.1111/bpa.12728. Epub 2019 May 17. Brain Pathol. 2019. PMID: 31006160 Free PMC article.
In general, since phosphorylation is strongly related to the alteration of protein propensity, we examined if the fundamental function of NUB1 can be modulated by its phosphorylation. We created a series of phosphomimic mutants of NUB1. Among them, we found that pho …
In general, since phosphorylation is strongly related to the alteration of protein propensity, we examined if the fundamental function of …
Dysregulated NUB1 and neddylation enhances rheumatoid arthritis fibroblast-like synoviocyte inflammatory responses.
Sendo S, Machado CRL, Boyle DL, Benschop RJ, Perumal NB, Choi E, Wang W, Firestein GS. Sendo S, et al. Arthritis Rheumatol. 2024 Apr 2. doi: 10.1002/art.42856. Online ahead of print. Arthritis Rheumatol. 2024. PMID: 38566346
Neddylation is modulated by the negative regulator of ubiquitin-like proteins-1 (NUB1). We determined whether NUB1 and neddylation are aberrant in RA FLS thereby contributing to their aggressive phenotype. ...RESULTS: Enhanced H3K27ac and H3K27me3 peaks were observe …
Neddylation is modulated by the negative regulator of ubiquitin-like proteins-1 (NUB1). We determined whether NUB1 and neddyla …
NUB1 modulation of GSK3beta reduces tau aggregation.
Richet E, Pooler AM, Rodriguez T, Novoselov SS, Schmidtke G, Groettrup M, Hanger DP, Cheetham ME, van der Spuy J. Richet E, et al. Hum Mol Genet. 2012 Dec 15;21(24):5254-67. doi: 10.1093/hmg/dds376. Epub 2012 Sep 10. Hum Mol Genet. 2012. PMID: 22965877
Strikingly, NUB1 induced GSK3beta degradation. Deletion of the NUB1 ubiquitin-like (UBL) domain did not impair the interaction with tau and GSK3beta, and the ability to suppress the phosphorylation and aggregation of tau was not affected. However, the UBL motif was …
Strikingly, NUB1 induced GSK3beta degradation. Deletion of the NUB1 ubiquitin-like (UBL) domain did not impair the interaction …
NUB1 suppresses the formation of Lewy body-like inclusions by proteasomal degradation of synphilin-1.
Tanji K, Tanaka T, Mori F, Kito K, Takahashi H, Wakabayashi K, Kamitani T. Tanji K, et al. Am J Pathol. 2006 Aug;169(2):553-65. doi: 10.2353/ajpath.2006.051067. Am J Pathol. 2006. PMID: 16877356 Free PMC article.
From results in this study, we found that NUB1 physically interacts with synphilin-1 through its NEDD8-binding site, implying that NUB1 also targets synphilin-1 to the proteasome for degradation. ...This assay showed that NUB1 suppresses the formation of synp …
From results in this study, we found that NUB1 physically interacts with synphilin-1 through its NEDD8-binding site, implying that …
NUB1-mediated targeting of the ubiquitin precursor UbC1 for its C-terminal hydrolysis.
Tanaka T, Yeh ET, Kamitani T. Tanaka T, et al. Eur J Biochem. 2004 Mar;271(5):972-82. doi: 10.1111/j.1432-1033.2004.03999.x. Eur J Biochem. 2004. PMID: 15009209 Free article.
Interestingly, NUB1 interacted with UbC1 through its UBA domain. Further study revealed that the UBA domain interacted with alpha-peptide bond-linked polyubiquitin, but not with isopeptide bond-linked polyubiquitin, indicating that the UBA domain of NUB1 is a specif …
Interestingly, NUB1 interacted with UbC1 through its UBA domain. Further study revealed that the UBA domain interacted with alpha-pep …
Interaction of NUB1 with the proteasome subunit S5a.
Tanji K, Tanaka T, Kamitani T. Tanji K, et al. Biochem Biophys Res Commun. 2005 Nov 11;337(1):116-20. doi: 10.1016/j.bbrc.2005.09.014. Biochem Biophys Res Commun. 2005. PMID: 16171779
Therefore, NUB1 is thought to be a potent downregulator of NEDD8 conjugation system. ...Although the UBL domain was not an S5a-interacting motif in NUB1, our further studies revealed that the UBL domain is required for the function of NUB1....
Therefore, NUB1 is thought to be a potent downregulator of NEDD8 conjugation system. ...Although the UBL domain was not an S5a-intera …
The role of NUB1 in alpha-synuclein degradation in Lewy body disease model mice.
Tanji K, Miki Y, Maruyama A, Mori F, Mimura J, Itoh K, Kamitani T, Wakabayashi K. Tanji K, et al. Biochem Biophys Res Commun. 2016 Feb 12;470(3):635-642. doi: 10.1016/j.bbrc.2016.01.093. Epub 2016 Jan 18. Biochem Biophys Res Commun. 2016. PMID: 26797281
Immunohistochemical and biochemical studies confirmed that NUB1 was over-expressed in neurons of mice expressing NUB1 (NUB1 Tg), and both NUB1 and abnormal alpha-synuclein (double Tg). NUB1 levels were increased by 4.7-fold in NUB1 Tg mic …
Immunohistochemical and biochemical studies confirmed that NUB1 was over-expressed in neurons of mice expressing NUB1 (NUB1 …
83 results