about
Evidence for OTUD-6B participation in B lymphocytes cell cycle after cytokine stimulationHuman HERC5 restricts an early stage of HIV-1 assembly by a mechanism correlating with the ISGylation of GagDomain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitinUSP13 enzyme regulates Siah2 ligase stability and activity via noncatalytic ubiquitin-binding domainsUSP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondriaRegulation and cellular roles of ubiquitin-specific deubiquitinating enzymesOptimising methods for the preservation, capture and identification of ubiquitin chains and ubiquitylated proteins by immunoblottingUSP2-45 Is a Circadian Clock Output Effector Regulating Calcium Absorption at the Post-Translational LevelInterferon-inducible antiviral effectorsPolyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21Molecular characterization of ubiquitin-specific protease 18 reveals substrate specificity for interferon-stimulated gene 15Progressive Hearing Loss in Mice Carrying a Mutation in Usp53.Enhancement of proteasome activity by a small-molecule inhibitor of USP14HyperISGylation of Old World monkey ISG15 in human cells.Deubiquitylase, deSUMOylase, and deISGylase activity microarrays for assay of substrate preference and functional modifiersBlockade of the ubiquitin protease UBP43 destabilizes transcription factor PML/RARα and inhibits the growth of acute promyelocytic leukemiaSelective inactivation of USP18 isopeptidase activity in vivo enhances ISG15 conjugation and viral resistanceUbiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control.Evolutionary Loss of Activity in De-Ubiquitylating Enzymes of the OTU Family.Evidence for the ubiquitin protease UBP43 as an antineoplastic target.Characterization of ubiquitin and ubiquitin-like-protein isopeptidase activities.Poison domains block transit of translocated substrates via the Legionella pneumophila Icm/Dot systemISG15 inhibits IFN-α-resistant liver cancer cell growth.Emerging roles for immunomodulatory functions of free ISG15.The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome.Antiviral activity of innate immune protein ISG15.Interferon-stimulated gene 15 and the protein ISGylation system.Identification and Validation of ISG15 Target Proteins.Interferon response and viral evasion by members of the family rhabdoviridae.The antiviral activities of ISG15.Antiviral Properties of ISG15.Identification of candidate substrates of ubiquitin-specific protease 13 using 2D-DIGEStructural basis of the specificity of USP18 toward ISG15.Selective Dual Inhibitors of the Cancer-Related Deubiquitylating Proteases USP7 and USP47.Nucleophosmin/B23 regulates ubiquitin dynamics in nucleoli by recruiting deubiquitylating enzyme USP36.Thiopurine analogue inhibitors of severe acute respiratory syndrome-coronavirus papain-like protease, a deubiquitinating and deISGylating enzyme.How USP18 deals with ISG15-modified proteins: structural basis for the specificity of the protease.The ISG15 conjugation system.
P2860
Q21136036-2D4E5E47-16FA-4F3C-ACB6-43B6526034C7Q21245043-5D371F61-5B2B-45A1-BAC7-CA49D94656C5Q24301017-12CC4A99-600C-4D2E-9E34-A4B743847778Q24306252-5C247E49-ED0B-49AB-A9C7-50221F83CE6EQ24316174-AD155EA0-AB22-4C8D-83F3-76FE7420C2C2Q24645701-ED48B469-B591-4EED-BCF3-5EB03E1BB8ECQ26795621-1F6235AD-682D-4E9A-9173-ECAF6659FD98Q27334789-99AF72B0-7178-49B5-9A14-DE6A67DEF8CFQ27486790-2ED57F30-2871-46F5-8C73-B07F01436D03Q27667261-1FB4A875-23D1-47A6-BB31-85CD55E5F6A2Q28505547-FA035EF9-9077-4CCA-9C18-A2EFE9FD514DQ28506642-302122FC-4505-417F-A1AE-AA4276334623Q29616735-336A85BD-2FD1-4B3B-9C40-D3E01BD28642Q33344443-8EA88470-40F4-4A28-8F54-8B01A4C0AEAFQ33721740-FB53D193-7421-476F-A87F-FA21334537C9Q34393733-99F7D183-0821-4E06-A328-A1B6490DC2EEQ34458906-4BD8E939-0ACC-48A7-B8F7-1F952F9B9D51Q35021872-17F06304-11D7-4851-A254-29DDD60F816EQ35847223-F9ABB9CC-D441-4896-8515-EB4E1946907BQ36223149-998A41D3-F895-4D49-AC32-A39AFB32ABCEQ36662171-60271EC4-0522-40AA-9F6D-285A1EEEA4EEQ37123778-996EB9E2-B5F9-484F-B8C2-BDDD2F117430Q37145183-27630C16-121F-479A-9E58-9DB5F966FD32Q37404247-9FC185D3-2725-4D17-A50D-FC4A01E886FDQ37467606-73658AE6-4A91-4177-8105-F2BF86F6615BQ37579660-EF0B8009-7315-4F0E-B9E1-1682E5EE05A4Q37824472-CC96DBF0-4652-4045-9336-7B8D355CB009Q37827468-E2CA363C-CE5E-4098-8F11-F995363885B5Q37945180-9B5D9EB1-7461-467F-B41D-2BBFE0877867Q38149665-046C9108-FAEE-4249-8E8A-7933674EC963Q38614093-AF9218E7-3266-4F48-8888-AF1D4979DE15Q38789396-96784D79-4CC8-4672-9EAF-150B420C417BQ38976984-31B34D90-29F4-4456-9071-A18C85347EE1Q39730830-E1362A6B-CBDE-4947-AF65-EFA0E18E6BE6Q42126825-0D99D0CC-84BD-41AE-B3BE-29C723EE6B1BQ44246327-8777AEF7-A88C-4062-AECE-D79EF701B83DQ47841496-061E7A52-9972-49C3-BC77-81B071B8BCCDQ55244542-300E394D-6632-4B17-B7B0-4CB7BF163090
P2860
description
2007 nî lūn-bûn
@nan
2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Screen for ISG15-crossreactive deubiquitinases.
@ast
Screen for ISG15-crossreactive deubiquitinases.
@en
type
label
Screen for ISG15-crossreactive deubiquitinases.
@ast
Screen for ISG15-crossreactive deubiquitinases.
@en
prefLabel
Screen for ISG15-crossreactive deubiquitinases.
@ast
Screen for ISG15-crossreactive deubiquitinases.
@en
P2093
P2860
P1433
P1476
Screen for ISG15-crossreactive deubiquitinases.
@en
P2093
André Catic
Daniël Blom
Edda Fiebiger
Gregory A Korbel
Hidde L Ploegh
Paul J Galardy
P2860
P356
10.1371/JOURNAL.PONE.0000679
P407
P577
2007-07-25T00:00:00Z