Solution structure of the human ubiquitin-specific protease 15 DUSP domain
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Structural variability of the ubiquitin specific protease DUSP-UBL double domainsIsoform-specific localization of the deubiquitinase USP33 to the Golgi apparatusStructure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like DomainsComparative Genomics of Mycoplasma bovis Strains Reveals That Decreased Virulence with Increasing Passages Might Correlate with Potential Virulence-Related Factors.Enhanced protein expression in the baculovirus/insect cell system using engineered SUMO fusions.Alternative exon skipping biases substrate preference of the deubiquitylase USP15 for mysterin/RNF213, the moyamoya disease susceptibility factorThe Regulations of Deubiquitinase USP15 and Its Pathophysiological Mechanisms in Diseases.Direct and indirect control of mitogen-activated protein kinase pathway-associated components, BRAP/IMP E3 ubiquitin ligase and CRAF/RAF1 kinase, by the deubiquitylating enzyme USP15.Structural basis for recruiting and shuttling of the spliceosomal deubiquitinase USP4 by SART3.Ubiquitin Specific Peptidase 15 (USP15) suppresses glioblastoma cell growth via stabilization of HECTD1 E3 ligase attenuating WNT pathway activity.USP15 regulates type I interferon response and is required for pathogenesis of neuroinflammation.Gli1-induced deubiquitinase USP48 aids glioblastoma tumorigenesis by stabilizing Gli1.Plant Deubiquitinases and Their Role in the Control of Gene Expression Through Modification of Histones.
P2860
Q24293418-3EA215C3-B0BF-4FA9-A7F0-10E0BD9E185EQ24317741-3E3AB1E8-5767-4AB5-B8FD-8228EB4F3CD1Q27683231-5EFB5181-0464-430D-89BE-94E7ABFB7C20Q33660689-BAB7EECC-AAB7-44DC-AD3F-11EF04E1D88CQ36978961-21EAFE7A-97BE-4EA6-9C5C-AE457E8356F6Q37690395-845FE590-FC8A-4714-A71A-45AF22A438EFQ37728992-69F70C0C-0E0B-4F05-A81A-8E1DA27F0BD9Q39252412-FF9DA5D1-9FFE-4B35-8171-8C4F147DCD6DQ42598430-5462788F-9168-458E-9395-9FA0BC291F9EQ47104172-A2436B11-10A4-415E-B364-F131C7453BA8Q47974546-41426FB0-DCD4-4AB1-9259-D636DDA2F0FEQ48264617-D011AEEB-2963-468B-8D88-61C379655F84Q49539596-A102E264-10A6-49D9-B0B5-3C25B433D724
P2860
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
@ast
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
@en
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
@nl
type
label
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
@ast
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
@en
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
@nl
prefLabel
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
@ast
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
@en
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
@nl
P2093
P2860
P50
P3181
P356
P1476
Solution structure of the human ubiquitin-specific protease 15 DUSP domain
@en
P2093
Gert E Folkers
Mark Daniëls
Robert Kaptein
P2860
P304
P3181
P356
10.1074/JBC.M510993200
P407
P577
2006-02-24T00:00:00Z