[NMR paper] 1H, 13C, 15N backbone resonance assignment of apo and ADP-ribose bound forms of the macro domain of Hepatitis E virus through solution NMR spectroscopy
1H, 13C, 15N backbone resonance assignment of apo and ADP-ribose bound forms of the macro domain of Hepatitis E virus through solution NMR spectroscopy
The genome of Hepatitis E virus (HEV) is 7.2 kilobases long and has three open reading frames. The largest one is ORF1, encoding a non-structural protein involved in the replication process, and whose processing is ill-defined. The ORF1 protein is a multi-modular protein which includes a macro domain (MD). MDs are evolutionarily conserved structures throughout all kingdoms of life. MDs participate in the recognition and removal of...
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[NMR paper] Dimer organization of membrane-associated NS5A of hepatitis C virus as determined by highly sensitive*1H-detected solid-state NMR.
Dimer organization of membrane-associated NS5A of hepatitis C virus as determined by highly sensitive*1H-detected solid-state NMR.
Related Articles Dimer organization of membrane-associated NS5A of hepatitis C virus as determined by highly sensitive*1H-detected solid-state NMR.
Angew Chem Int Ed Engl. 2020 Nov 18;:
Authors: Jirasko V, Lends A, Lakomek NA, Fogeron ML, Weber M, Malär A, Penzel S, Bartenschlager R, Meier BH, Böckmann A
Abstract
The Hepatitis C virus nonstructural protein 5A (NS5A) is a membrane-associated protein...
[NMR paper] The casein kinase 2-dependent phosphorylation of NS5A domain 3 from hepatitis C virus followed by time-resolved NMR.
The casein kinase 2-dependent phosphorylation of NS5A domain 3 from hepatitis C virus followed by time-resolved NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles The casein kinase 2-dependent phosphorylation of NS5A domain 3 from hepatitis C virus followed by time-resolved NMR.
Chembiochem. 2015 Dec 18;
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[NMR paper] Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR.
Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR.
Related Articles Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR.
Biochim Biophys Acta. 2014 Aug 7;
Authors: Shalom-Elazari H, Zazrin-Greenspon H, Shaked H, Chill JH
Abstract
E1 and E2 are two hepatitis C viral envelope glycoproteins that assemble into a heterodimer that is essential for membrane fusion and penetration into the target cell. Both...
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[NMR paper] Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR.
Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR.
Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR.
Biochim Biophys Acta. 2013 Nov 2;
Authors: Zazrin H, Shaked H, Chill JH
Abstract
Oligomerization of hepatitis C viral envelope proteins E1 and E2 is essential to virus fusion and assembly. Although interactions within the transmembrane (TM) domains of these glycoproteins have proven contributions to the E1/E2 heterodimerization process and consequent...
Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR - ScienceDirect.com
Linear Mode
