Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property

Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property

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http://www.wikidata.org/entity/Q27653582
The Crystal Structures of Chikungunya and Venezuelan Equine Encephalitis Virus nsP3 Macro Domains Define a Conserved Adenosine Binding PocketThe SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-QuadruplexesNuclear Magnetic Resonance Structure of the Nucleic Acid-Binding Domain of Severe Acute Respiratory Syndrome Coronavirus Nonstructural Protein 3Pathogenesis of murine coronavirus in the central nervous system.An interaction between the nucleocapsid protein and a component of the replicase-transcriptase complex is crucial for the infectivity of coronavirus genomic RNA.A G-quadruplex-binding macrodomain within the "SARS-unique domain" is essential for the activity of the SARS-coronavirus replication-transcription complex.X-ray Structural and Functional Studies of the Three Tandemly Linked Domains of Non-structural Protein 3 (nsp3) from Murine Hepatitis Virus Reveal Conserved Functions.Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES.Characterization of a critical interaction between the coronavirus nucleocapsid protein and nonstructural protein 3 of the viral replicase-transcriptase complex.Reprogramming cellular events by poly(ADP-ribose)-binding proteinsMurine Coronavirus Cell Type Dependent Interaction with the Type I Interferon ResponseStructural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9.The conserved macrodomains of the non-structural proteins of Chikungunya virus and other pathogenic positive strand RNA viruses function as mono-ADP-ribosylhydrolases.Structural and functional analysis of Oceanobacillus iheyensis macrodomain reveals a network of waters involved in substrate binding and catalysis.The macro domain as fusion tag for carrier-driven crystallization.
P2860

Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property

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http://www.wikidata.org/entity/Q27653582
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2009 nî lūn-bûn
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2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
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2009年論文
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2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Crystal structures of the X-do ...... ay not be a conserved property
@ast
Crystal structures of the X-do ...... ay not be a conserved property
@en
Crystal structures of the X-do ...... ay not be a conserved property
@nl
type
label
Crystal structures of the X-do ...... ay not be a conserved property
@ast
Crystal structures of the X-do ...... ay not be a conserved property
@en
Crystal structures of the X-do ...... ay not be a conserved property
@nl
prefLabel
Crystal structures of the X-do ...... ay not be a conserved property
@ast
Crystal structures of the X-do ...... ay not be a conserved property
@en
Crystal structures of the X-do ...... ay not be a conserved property
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P921
P932
P356
P1433
P1476
Crystal structures of the X-do ...... ay not be a conserved property
@en
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P921
P932