Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
about
The ubiquitin-like molecule interferon-stimulated gene 15 (ISG15) is a potential prognostic marker in human breast cancerA MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2Interferon-induced ISG15 conjugation inhibits influenza A virus gene expression and replication in human cellsISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner by blocking Nedd4 ligase activityISG15 modification of filamin B negatively regulates the type I interferon-induced JNK signalling pathwayHuman ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathwaysInfluenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 proteinIdentification of interferon-stimulated gene 15 as an antiviral molecule during Sindbis virus infection in vivo.A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-like domainThe UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like proteinDown-regulation of UCRP and UBE2L6 in BRCA2 knocked-down human breast cellsSWAP pre-mRNA splicing regulators are a novel, ancient protein family sharing a highly conserved sequence motif with the prp21 family of constitutive splicing proteinsConjugates of ubiquitin cross-reactive protein distribute in a cytoskeletal patternISG15 inhibits Nedd4 ubiquitin E3 activity and enhances the innate antiviral responseOrigin and function of ubiquitin-like proteinsProtein ISGylation modulates the JAK-STAT signaling pathwayNegative regulation of ISG15 E3 ligase EFP through its autoISGylationSUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complexISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHPConjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor functionMolecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope associationUbp43 regulates BCR-ABL leukemogenesis via the type 1 interferon receptor signalingThe Regulation of DNA Damage Tolerance by Ubiquitin and Ubiquitin-Like ModifiersInhibition of NEDD8-conjugation pathway by novel molecules: potential approaches to anticancer therapyCrystal Structure of the Human Ubiquitin-activating Enzyme 5 (UBA5) Bound to ATP: MECHANISTIC INSIGHTS INTO A MINIMALISTIC E1 ENZYMEStructural Basis for the Ubiquitin-Linkage Specificity and deISGylating Activity of SARS-CoV Papain-Like ProteaseHERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targetsISG15 Arg151 and the ISG15-conjugating enzyme UbE1L are important for innate immune control of Sindbis virusISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cellsModification of yeast Cdc53p by the ubiquitin-related protein rub1p affects function of the SCFCdc4 complex.A novel protein modification pathway related to the ubiquitin system.Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteinsStage-associated overexpression of the ubiquitin-like protein, ISG15, in bladder cancerUbe1L and protein ISGylation are not essential for alpha/beta interferon signaling.HyperISGylation of Old World monkey ISG15 in human cells.A novel role for ATM in regulating proteasome-mediated protein degradation through suppression of the ISG15 conjugation pathway.ISG15, an interferon-stimulated ubiquitin-like protein, is not essential for STAT1 signaling and responses against vesicular stomatitis and lymphocytic choriomeningitis virus.Induced expression of the endogenous beta interferon gene in adenovirus type 5-transformed rat fibroblastsUbiquitin as a degradation signalStructure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia.
P2860
Q21195217-36190DA8-2661-406E-8555-07B99C415304Q22009372-CA64EBF1-F054-4C25-A5D1-33D72424D4A4Q24314284-B450234F-2615-420B-8E05-72CF148C7326Q24318462-154EF12E-C349-4A4D-ADDA-CEED98657B89Q24318890-056EABCC-B46D-42C7-82B5-8EF3376043D7Q24531725-5D774138-76DE-4D0E-9831-6E4603883B9FQ24536345-5E206CA4-547E-40C1-A18E-5EA421A01A94Q24537289-A9A4D346-D586-455F-8A67-AE7B710F5242Q24558733-98CAE18A-3B67-42D5-8152-396D10258D96Q24562149-626A3BF6-CF23-4C22-9754-0EEA52DA3006Q24603819-A808CA0D-3A76-4011-8867-992AD276FCA7Q24605050-D56649DC-3952-4921-81A8-A1CE7007A3B7Q24607385-B029B6C2-057C-4A12-B30A-7E91A818A6B1Q24648592-ED84FF8A-FAE6-475E-B5C7-FC34ACA1B454Q24651141-02151304-CFB4-4BA1-8581-3ECBD068BD7AQ24672739-04C594C9-74E0-4B6F-83FE-1C6870B44410Q24677656-CC9214F8-E62E-4389-89EC-F17CB76B8914Q24678180-3C5A4FD5-DC7D-4032-8E51-EA6B190409E5Q24681258-74702E1A-1142-4D17-B5EE-D5356250E3BFQ24682460-96F2B5B1-7EFD-4751-A5B8-BB6760F3C407Q24683718-00BF67E2-C4F6-407B-87CE-7347827F9D14Q24685070-10E98446-73DC-4033-93E4-79370ADF9786Q26744520-E37695FC-A117-49CB-9CBA-FD9CB3010C14Q27003218-4A5399A4-8554-40F8-85C7-E287BA56A80AQ27660424-B8FB11AC-9C39-4379-A58F-AA2F6C4BE244Q27683898-9E0B7979-B15D-44B6-8A02-A8F3A2010550Q27863927-DCD87212-42F4-4DEC-B627-C46A509F7098Q27865223-A66807BF-FB55-4CDD-8A64-CCFD81DDF482Q27865244-DA45E6B1-6D56-489C-BEAC-CC0AC87BEB37Q27933259-F1B737E2-DCE5-4AE9-BF5F-4C55CEC6CDEAQ27938072-013D0533-A119-406C-886A-17E09A9184C6Q28087183-B8DBA1D3-EE80-432F-820A-65B575363B98Q28384157-0FCB6DC4-3CCC-4FE1-9211-396E12CCFA8BQ28504645-DBC27258-3597-4996-A41B-640ADD28B63CQ33344443-1E1B587C-D596-4112-A25A-38CE028731DFQ33813351-223ED703-B4EB-47DA-924D-2A6F3CEB9861Q33925311-E0CD1217-A05D-4A79-B6BD-E683652B113DQ33930166-A5CF817F-44BB-47E9-A8AC-2A126675D2B5Q33937351-C252097B-0D29-49BE-B42C-BD9BC3942B6EQ33964599-D5A72FE6-A478-4ED4-BD52-34302AFF3FA6
P2860
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
description
1987 nî lūn-bûn
@nan
1987 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
@ast
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
@en
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
@nl
type
label
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
@ast
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
@en
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
@nl
prefLabel
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
@ast
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
@en
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
@nl
P2093
P1476
Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin.
@en
P2093
P304
11315-11323
P407
P577
1987-08-01T00:00:00Z