Structural Analysis of a Viral Ovarian Tumor Domain Protease from the Crimean-Congo Hemorrhagic Fever Virus in Complex with Covalently Bonded Ubiquitin
about
Genetic Characterization of Archived Bunyaviruses and their Potential for Emergence in AustraliaMolecular Insights into Crimean-Congo Hemorrhagic Fever VirusViral OTU deubiquitinases: a structural and functional comparisonGenomic Characterization of the Genus Nairovirus (Family Bunyaviridae)Diversity of Ubiquitin and ISG15 Specificity among Nairoviruses' Viral Ovarian Tumor Domain ProteasesAn ankyrin-repeat ubiquitin-binding domain determines TRABID's specificity for atypical ubiquitin chainsOn Terminal Alkynes That Can React with Active-Site Cysteine Nucleophiles in ProteasesDeubiquitinase function of arterivirus papain-like protease 2 suppresses the innate immune response in infected host cellsThe mechanism of OTUB1-mediated inhibition of ubiquitinationA Compact Viral Processing Proteinase/Ubiquitin Hydrolase from the OTU FamilyStructural Basis for the Ubiquitin-Linkage Specificity and deISGylating Activity of SARS-CoV Papain-Like ProteaseGenomic Characterization of Yogue, Kasokero, Issyk-Kul, Keterah, Gossas, and Thiafora Viruses: Nairoviruses Naturally Infecting Bats, Shrews, and TicksComparative analysis of the L, M, and S RNA segments of Crimean-Congo haemorrhagic fever virus isolates from southern Africa.Inhibition of interferon induction and action by the nairovirus Nairobi sheep disease virus/Ganjam virus.Architecture and regulation of negative-strand viral enzymatic machineryThe human otubain2-ubiquitin structure provides insights into the cleavage specificity of poly-ubiquitin-linkages.Antibodies to the core proteins of Nairobi sheep disease virus/Ganjam virus reveal details of the distribution of the proteins in infected cells and tissuesArterivirus and nairovirus ovarian tumor domain-containing Deubiquitinases target activated RIG-I to control innate immune signaling.Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease.The vOTU domain of highly-pathogenic porcine reproductive and respiratory syndrome virus displays a differential substrate preference.Interferon-induced ISG15 pathway: an ongoing virus-host battle.The molecular biology of nairoviruses, an emerging group of tick-borne arboviruses.Manipulation of viral infection by deubiquitinating enzymes: new players in host-virus interactions.Crimean-Congo Hemorrhagic Fever Virus Suppresses Innate Immune Responses via a Ubiquitin and ISG15 Specific Protease.Fluorometric CCHFV OTU protease assay with potent inhibitors.Inherent dynamics within the Crimean-Congo Hemorrhagic fever virus protease are localized to the same region as substrate interactions.Emergence of a novel highly pathogenic porcine reproductive and respiratory syndrome virus in China.A viral deubiquitylating enzyme targets viral RNA-dependent RNA polymerase and affects viral infectivity.A general chemical ligation approach towards isopeptide-linked ubiquitin and ubiquitin-like assay reagents.
P2860
Q26315475-B9EBCC14-E0AC-4DEA-A451-01A11DC1795AQ26750548-69863ED9-14DA-4131-B5AF-3FBCE0435CC6Q27026446-3911A608-477F-4050-8A3E-C6307260B4CDQ27469076-D9DBD360-3D95-477C-84D4-87CE34513AADQ27675985-E085C8A4-3F43-4945-8E42-6370488FE6C5Q27676107-57B0B547-2AE1-467F-8228-4890B9756166Q27676208-FEC58E89-7710-4E4D-B104-54D8FC22EC53Q27676341-248A343C-A31A-4DB3-9DC4-D9DAE2265637Q27677504-55B62639-D529-4DE8-A2EF-B8D92F11F3C6Q27679781-75DEE54B-CA8E-4228-AA0F-EC98015C1286Q27683898-70F4D8F6-B3B2-4C09-8FDF-59F00E9F91D1Q28603004-C29D00CC-BC22-49A7-8C6B-051E3A44A78DQ30371883-300700CC-04F5-47B6-A631-8DA64067ACB9Q34097947-A96B6EFE-BD1B-4D89-8FD3-8CF485CBBFD7Q34286309-ADEDEA2F-B52F-4FAD-A566-678419A9CFA6Q35543082-D2100FAB-8906-4BC6-8C6A-9EFBC023A204Q35612527-EBAE8088-C543-43B8-815D-C4106EFFDA96Q35665780-7A12AC59-3EB6-4427-9C1F-8D095CA9EDC3Q36923194-C8246BF3-C6A4-4D55-9A0E-7FCE42C0089FQ37712257-CE3E2F48-37DD-401A-BAE5-444EEDB8F32EQ38082061-09232470-B6D8-45E0-8B4B-6C88334842CAQ38170306-339DCAA7-31C8-466C-87CE-1B247C3683A7Q38803414-5E442F42-1295-4838-9C5F-62D93D1BCE16Q40040506-5C22D594-05DC-48A4-8D62-155F4A27705EQ40148157-9C7B4181-3A06-411C-A14B-8927AC67A2D8Q40174754-1C5E7DDE-8E49-4CFD-85F4-89EEBDE87E47Q40332931-1CE42F34-8512-44DA-88E3-5C6B36A4156DQ40884952-C10A50B0-9953-4F53-8616-F4788BCB4176Q41515742-334AAC7C-23B7-4824-9088-C8FDB7966155
P2860
Structural Analysis of a Viral Ovarian Tumor Domain Protease from the Crimean-Congo Hemorrhagic Fever Virus in Complex with Covalently Bonded Ubiquitin
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Structural Analysis of a Viral ...... th Covalently Bonded Ubiquitin
@ast
Structural Analysis of a Viral ...... th Covalently Bonded Ubiquitin
@en
Structural Analysis of a Viral ...... th Covalently Bonded Ubiquitin
@nl
type
label
Structural Analysis of a Viral ...... th Covalently Bonded Ubiquitin
@ast
Structural Analysis of a Viral ...... th Covalently Bonded Ubiquitin
@en
Structural Analysis of a Viral ...... th Covalently Bonded Ubiquitin
@nl
prefLabel
Structural Analysis of a Viral ...... th Covalently Bonded Ubiquitin
@ast
Structural Analysis of a Viral ...... th Covalently Bonded Ubiquitin
@en
Structural Analysis of a Viral ...... th Covalently Bonded Ubiquitin
@nl
P2093
P2860
P3181
P356
P1433
P1476
Structural Analysis of a Viral ...... th Covalently Bonded Ubiquitin
@en
P2093
Emily M Masters
Erica A Baker
Glenn C Capodagli
Joseph S Brunzelle
Marissa A McKercher
Scott D Pegan
P2860
P304
P3181
P356
10.1128/JVI.02496-10
P577
2011-04-01T00:00:00Z