The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1
about
Cullin-RING ubiquitin ligases: global regulation and activation cyclesCOP9 signalosome subunit Csn8 is involved in maintaining proper duration of the G1 phaseStructural variability of the ubiquitin specific protease DUSP-UBL double domainsThe deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2CSN controls NF-kappaB by deubiquitinylation of IkappaBalphaK63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activationCOP9 signalosome controls the Carma1-Bcl10-Malt1 complex upon T-cell stimulationCharacterization of the human COP9 signalosome complex using affinity purification and mass spectrometryThe U4/U6 recycling factor SART3 has histone chaperone activity and associates with USP15 to regulate H2B deubiquitinationThe Role of the COP9 Signalosome and Neddylation in DNA Damage Signaling and RepairCrystal structure and versatile functional roles of the COP9 signalosome subunit 1Dual function of Rpn5 in two PCI complexes, the 26S proteasome and COP9 signalosome.Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasomeSolution structure of the human ubiquitin-specific protease 15 DUSP domainNeurospora COP9 signalosome integrity plays major roles for hyphal growth, conidial development, and circadian functionThe minimal deneddylase core of the COP9 signalosome excludes the Csn6 MPN- domainIdentification of cancer genes using a statistical framework for multiexperiment analysis of nondiscretized array CGH data.Downregulation of COP9 signalosome subunits differentially affects the CSN complex and target protein stabilityUSP15 stabilizes MDM2 to mediate cancer-cell survival and inhibit antitumor T cell responsesDeubiquitylation of deubiquitylasesControl of multicellular development by the physically interacting deneddylases DEN1/DenA and COP9 signalosome.Subunit 6 of the COP9 signalosome promotes tumorigenesis in mice through stabilization of MDM2 and is upregulated in human cancers.Revisiting the COP9 signalosome as a transcriptional regulator.Characterization of the role of COP9 signalosome in regulating cullin E3 ubiquitin ligase activityEmerging regulatory mechanisms in ubiquitin-dependent cell cycle control.CIF-1, a shared subunit of the COP9/signalosome and eukaryotic initiation factor 3 complexes, regulates MEL-26 levels in the Caenorhabditis elegans embryo.Mapping the protein interaction network of the human COP9 signalosome complex using a label-free QTAX strategy.Structural aspects of recently discovered viral deubiquitinating activities.Enhanced protein expression in the baculovirus/insect cell system using engineered SUMO fusions.The COP9 signalosome negatively regulates proteasome proteolytic function and is essential to transcription.The deubiquitylase USP15 stabilizes newly synthesized REST and rescues its expression at mitotic exitProtein partners of deubiquitinating enzymes.The ubiquitin-specific peptidase USP15 regulates human papillomavirus type 16 E6 protein stability.COP9 signalosome interacts ATP-dependently with p97/valosin-containing protein (VCP) and controls the ubiquitination status of proteins bound to p97/VCP.Deubiquitylation of hepatitis B virus X protein (HBx) by ubiquitin-specific peptidase 15 (USP15) increases HBx stability and its transactivation activity.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.COP9 signalosome function in the DDR.Roles of COP9 signalosome in cancer.
P2860
Q21203558-C816265B-F242-49FF-9B52-4423ECCB928FQ24293399-EC7D7EA6-15BF-49BB-A195-AE09125BE739Q24293418-42457B2B-D4D8-4AA2-A5BC-32F39BB474B4Q24296502-486E1DCC-9AF6-4F1E-B66B-447D04AB27DCQ24298155-C73F759F-2470-4CA5-BE72-FF5B0CAC89F4Q24310641-573D497D-14BA-4BA3-9303-F71DA106F681Q24310748-810E5094-822A-4729-8A11-0047743C2048Q24311222-905FECE8-DC30-46CB-85EB-2A81F3986BD0Q24321869-D6B53523-BB92-4F75-97E2-0E55B12F6B70Q24337279-08E7DED3-3796-4E20-B30E-7236680D758EQ26782011-3A35C5C5-25EE-47CB-AFB5-DF52E991E9BCQ27678871-8404D975-90F3-441C-B7F5-2FA0FE30BC3AQ27937368-4DADF283-3FF4-49E5-9E51-08A28A92D50FQ28259286-A60FD301-24C5-4393-9950-8E5D03BACE86Q28282716-90FE8891-A633-4370-B7CB-309794E143FEQ28483644-B0036C9C-F138-4F4F-8AAA-9244E5C4A054Q31089679-39F2CB6B-9392-49E5-B52C-EC94C153BD1DQ31142505-34B8F1A6-56BF-4E68-A2C0-3829A325276CQ33311403-EBBB56CD-1223-42D3-B04B-87C5106D0150Q33655162-EB7FFB92-328D-4062-A5F4-24CE7EFCDEB4Q33861462-544F6AA2-A672-4A4D-90C4-854FEC566118Q34585770-DF450F18-DEA5-40D0-8C32-D9A6EFD6F623Q34627210-C91BB1D9-2292-4FF3-B883-073E33EB7C90Q34967074-C0AA20D8-A540-45D3-B8B9-29C581171E5DQ35612223-2B74353B-7F96-4692-926E-F20E16E98F11Q35770195-D4BBEC21-43C1-4E7C-AA60-C5A4B629B73BQ35857063-267BB74A-1CFC-4DB3-B584-6FEEF3ABAFA0Q36163496-F55D2A91-2550-4AFB-8BEE-A6165E63673BQ36567780-65F83444-5B0E-4A02-9388-F9730A0F68D9Q36978961-61A8C7E1-FFFC-4D6E-8989-6008F2AC1A9AQ37066433-A3E4E5E9-66B7-4FB9-BFD0-841B14E91973Q37075932-734BB8E2-22F6-4E2C-92A6-28BBEE833E68Q37237774-04350217-5E3A-4361-8317-AD00C641FF2BQ37333809-028E19C1-87F1-4BCE-A038-233A5343897BQ37454309-46D91B1A-BECE-4D17-9474-642C3FDE9BAEQ37578928-8532E9D3-29C4-405D-B340-46696214A21CQ37690395-55279059-D752-4DA6-B2EE-3271C79C4E57Q37728992-E819E7FE-C38A-4776-95BF-FF9A71F995ECQ37867729-F3DF1556-79DB-4272-9EF6-5B66A65F1AF7Q37923711-E0FC5D33-78FA-4B29-B549-21881AF6BE1A
P2860
The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
name
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@ast
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@en
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@en-gb
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@nl
type
label
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@ast
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@en
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@en-gb
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@nl
prefLabel
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@ast
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@en
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@en-gb
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@nl
P2093
P1433
P1476
The zinc finger of the CSN-ass ...... l to rescue the E3 ligase Rbx1
@en
P2093
Adi Guterman
Annett Helfrich
Barbara Kapelari
Bettina K J Hetfeld
Hartmut Scheel
Kay Hofmann
Peter-Michael Kloetzel
Rüdiger Schade
P304
P356
10.1016/J.CUB.2005.05.059
P407
P577
2005-07-01T00:00:00Z