PubMed for id: 126119

Year	Number of Results
1996	1
2002	1
2004	2
2006	1
2007	1
2009	1
2010	1
2011	3
2013	1
2015	1
2017	2
2018	4
2019	2
2020	3
2021	4
2022	3
2023	2
2024	1

1

Josephin domain containing 2 (JOSD2) promotes lung cancer by inhibiting LKB1 (Liver kinase B1) activity.

Yuan T, Zeng C, Liu J, Zhao C, Ge F, Li Y, Qian M, Du J, Wang W, Li Y, Liu Y, Dai X, Zhou J, Chen X, Ma S, Zhu H, He Q, Yang B. Yuan T, et al. Signal Transduct Target Ther. 2024 Jan 5;9(1):11. doi: 10.1038/s41392-023-01706-y. Signal Transduct Target Ther. 2024. PMID: 38177135 Free PMC article.

2

Deubiquitinating enzyme JOSD2 affects susceptibility of non-small cell lung carcinoma cells to anti-cancer drugs through DNA damage repair.

Ge F, Liu X, Zhang H, Yuan T, Zhu H, Yang B, He Q. Ge F, et al. Zhejiang Da Xue Xue Bao Yi Xue Ban. 2023 Oct 3;52(5):533-543. doi: 10.3724/zdxbyxb-2023-0256. Zhejiang Da Xue Xue Bao Yi Xue Ban. 2023. PMID: 37899394 Free PMC article. Chinese, English.

3

Deubiquitinating enzyme Josephin-2 stabilizes PHGDH to promote a cancer stem cell phenotype in hepatocellular carcinoma.

Wang Y, Li ZX, Wang JG, Li LH, Shen WL, Dang XW. Wang Y, et al. Genes Genomics. 2023 Feb;45(2):215-224. doi: 10.1007/s13258-022-01356-4. Epub 2022 Dec 30. Genes Genomics. 2023. PMID: 36583817

4

Deubiquitinating enzyme JOSD2 promotes hepatocellular carcinoma progression through interacting with and inhibiting CTNNB1 degradation.

Huang Y, Zeng J, Liu T, Xu Q, Song X, Zeng J. Huang Y, et al. Cell Biol Int. 2022 Jul;46(7):1089-1097. doi: 10.1002/cbin.11812. Epub 2022 May 14. Cell Biol Int. 2022. PMID: 35568970

5

Deubiquitinase JOSD2 stabilizes YAP/TAZ to promote cholangiocarcinoma progression.

Qian M, Yan F, Wang W, Du J, Yuan T, Wu R, Zhao C, Wang J, Lu J, Zhang B, Lin N, Dong X, Dai X, Dong X, Yang B, Zhu H, He Q. Qian M, et al. Acta Pharm Sin B. 2021 Dec;11(12):4008-4019. doi: 10.1016/j.apsb.2021.04.003. Epub 2021 Jun 25. Acta Pharm Sin B. 2021. PMID: 35024322 Free PMC article.

6

Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes.

Tzvetkov N, Breuer P. Tzvetkov N, et al. Biol Chem. 2007 Sep;388(9):973-8. doi: 10.1515/BC.2007.107. Biol Chem. 2007. PMID: 17696782

7

The deubiquitinase JOSD2 is a positive regulator of glucose metabolism.

Krassikova L, Zhang B, Nagarajan D, Queiroz AL, Kacal M, Samakidis E, Vakifahmetoglu-Norberg H, Norberg E. Krassikova L, et al. Cell Death Differ. 2021 Mar;28(3):1091-1109. doi: 10.1038/s41418-020-00639-1. Epub 2020 Oct 20. Cell Death Differ. 2021. PMID: 33082514 Free PMC article.

8

USP13 promotes deubiquitination of ZHX2 and tumorigenesis in kidney cancer.

Xie H, Zhou J, Liu X, Xu Y, Hepperla AJ, Simon JM, Wang T, Yao H, Liao C, Baldwin AS, Gong K, Zhang Q. Xie H, et al. Proc Natl Acad Sci U S A. 2022 Sep 6;119(36):e2119854119. doi: 10.1073/pnas.2119854119. Epub 2022 Aug 29. Proc Natl Acad Sci U S A. 2022. PMID: 36037364 Free PMC article.

9

JosD1, a membrane-targeted deubiquitinating enzyme, is activated by ubiquitination and regulates membrane dynamics, cell motility, and endocytosis.

Seki T, Gong L, Williams AJ, Sakai N, Todi SV, Paulson HL. Seki T, et al. J Biol Chem. 2013 Jun 14;288(24):17145-55. doi: 10.1074/jbc.M113.463406. Epub 2013 Apr 26. J Biol Chem. 2013. PMID: 23625928 Free PMC article.

10

Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity.

Weeks SD, Grasty KC, Hernandez-Cuebas L, Loll PJ. Weeks SD, et al. J Biol Chem. 2011 Feb 11;286(6):4555-65. doi: 10.1074/jbc.M110.177360. Epub 2010 Nov 30. J Biol Chem. 2011. PMID: 21118805 Free PMC article.

Save citations to file

Email citations

Send citations to clipboard

Add to Collections

Add to My Bibliography

Create a file for external citation management software

Your saved search

Your RSS Feed

My NCBI Filters

Results by year

Text availability

Article attribute

Article type

Publication date

29 results

Results by year