146 related articles for article (PubMed ID: 8995226)
1. DUB-2 is a member of a novel family of cytokine-inducible deubiquitinating enzymes.
Zhu Y; Lambert K; Corless C; Copeland NG; Gilbert DJ; Jenkins NA; D'Andrea AD
J Biol Chem; 1997 Jan; 272(1):51-7. PubMed ID: 8995226
[TBL] [Abstract][Full Text] [Related]
2. DUB-1, a deubiquitinating enzyme with growth-suppressing activity.
Zhu Y; Carroll M; Papa FR; Hochstrasser M; D'Andrea AD
Proc Natl Acad Sci U S A; 1996 Apr; 93(8):3275-9. PubMed ID: 8622927
[TBL] [Abstract][Full Text] [Related]
3. DUB-2A, a new member of the DUB subfamily of hematopoietic deubiquitinating enzymes.
Baek KH; Mondoux MA; Jaster R; Fire-Levin E; D'Andrea AD
Blood; 2001 Aug; 98(3):636-42. PubMed ID: 11468161
[TBL] [Abstract][Full Text] [Related]
4. Essential regions of deubiquitinating enzyme activity and enhancer function for DUB-2A expressed in T-lymphocytes.
Baek KH; Kim YS; Lee HJ; Kang I
Arch Biochem Biophys; 2004 Oct; 430(2):191-7. PubMed ID: 15369818
[TBL] [Abstract][Full Text] [Related]
5. The murine DUB-1 gene is specifically induced by the betac subunit of interleukin-3 receptor.
Zhu Y; Pless M; Inhorn R; Mathey-Prevot B; D'Andrea AD
Mol Cell Biol; 1996 Sep; 16(9):4808-17. PubMed ID: 8756639
[TBL] [Abstract][Full Text] [Related]
6. The deubiquitinating enzyme DUB-2 prolongs cytokine-induced signal transducers and activators of transcription activation and suppresses apoptosis following cytokine withdrawal.
Migone TS; Humbert M; Rascle A; Sanden D; D'Andrea A; Johnston JA
Blood; 2001 Sep; 98(6):1935-41. PubMed ID: 11535532
[TBL] [Abstract][Full Text] [Related]
7. The DUB/USP17 deubiquitinating enzymes, a multigene family within a tandemly repeated sequence.
Burrows JF; McGrattan MJ; Johnston JA
Genomics; 2005 Apr; 85(4):524-9. PubMed ID: 15780755
[TBL] [Abstract][Full Text] [Related]
8. DUB-1A, a novel deubiquitinating enzyme subfamily member, is polyubiquitinated and cytokine-inducible in B-lymphocytes.
Baek KH; Kim MS; Kim YS; Shin JM; Choi HK
J Biol Chem; 2004 Jan; 279(4):2368-76. PubMed ID: 14583620
[TBL] [Abstract][Full Text] [Related]
9. Critical regions for deubiquitinating activity of DUB-2 expressed in T-lymphocytes.
Lee JH; Kim YS; Kim M; Baek KH
Am J Hematol; 2001 Aug; 67(4):270-2. PubMed ID: 11443643
[TBL] [Abstract][Full Text] [Related]
10. Cytokine-regulated protein degradation by the ubiquitination system.
Baek KH
Curr Protein Pept Sci; 2006 Apr; 7(2):171-7. PubMed ID: 16611142
[TBL] [Abstract][Full Text] [Related]
11. DUB-3, a cytokine-inducible deubiquitinating enzyme that blocks proliferation.
Burrows JF; McGrattan MJ; Rascle A; Humbert M; Baek KH; Johnston JA
J Biol Chem; 2004 Apr; 279(14):13993-4000. PubMed ID: 14699124
[TBL] [Abstract][Full Text] [Related]
12. The DUB/USP17 deubiquitinating enzymes: a gene family within a tandemly repeated sequence, is also embedded within the copy number variable beta-defensin cluster.
Burrows JF; Scott CJ; Johnston JA
BMC Genomics; 2010 Apr; 11():250. PubMed ID: 20403174
[TBL] [Abstract][Full Text] [Related]
13. Lymphocyte-specific murine deubiquitinating enzymes induced by cytokines.
Baek KH
Am J Hematol; 2002 Dec; 71(4):340-5. PubMed ID: 12447969
[TBL] [Abstract][Full Text] [Related]
14. DUB-1, a fate determinant of dynein heavy chain in B-lymphocytes, is regulated by the ubiquitin-proteasome pathway.
Lee MY; Ajjappala BS; Kim MS; Oh YK; Baek KH
J Cell Biochem; 2008 Dec; 105(6):1420-9. PubMed ID: 18980247
[TBL] [Abstract][Full Text] [Related]
15. Embryonic demise caused by targeted disruption of a cysteine protease Dub-2.
Baek KH; Lee H; Yang S; Lim SB; Lee W; Lee JE; Lim JJ; Jun K; Lee DR; Chung Y
PLoS One; 2012; 7(9):e44223. PubMed ID: 22984479
[TBL] [Abstract][Full Text] [Related]
16. Analysis of cis-acting sequences and trans-acting factors regulating the interleukin-3 response element of the DUB-1 gene.
Jaster R; Baek KH; D'Andrea AD
Biochim Biophys Acta; 1999 Sep; 1446(3):308-16. PubMed ID: 10524205
[TBL] [Abstract][Full Text] [Related]
17. The deubiquitinating enzyme DUB2A enhances CSF3 signalling by attenuating lysosomal routing of the CSF3 receptor.
Meenhuis A; Verwijmeren C; Roovers O; Touw IP
Biochem J; 2011 Mar; 434(2):343-51. PubMed ID: 21155715
[TBL] [Abstract][Full Text] [Related]
18. Segmental duplications containing tandem repeated genes encoding putative deubiquitinating enzymes.
Liu H; Li L; Zilberstein A; Hahn CS
Proc IEEE Comput Syst Bioinform Conf; 2004; ():31-9. PubMed ID: 16447997
[TBL] [Abstract][Full Text] [Related]
19. Conjugation and deconjugation of ubiquitin regulating the destiny of proteins.
Baek KH
Exp Mol Med; 2003 Feb; 35(1):1-7. PubMed ID: 12642897
[TBL] [Abstract][Full Text] [Related]
20. Decoupling deISGylating and deubiquitinating activities of the MERS virus papain-like protease.
Clasman JR; Everett RK; Srinivasan K; Mesecar AD
Antiviral Res; 2020 Feb; 174():104661. PubMed ID: 31765674
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
