Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module

Middle East Respiratory Syndrome Coronavirus: Update for Clinicians

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The hepatitis E virus ORF1 ‘X-domain’ residues form a putative macrodomain protein/Appr-1″-pase catalytic-site, critical for viral RNA replication

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Middle East Respiratory Syndrome Coronavirus “MERS-CoV”: Current Knowledge Gaps

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Laboratory Investigation and Phylogenetic Analysis of an Imported Middle East Respiratory Syndrome Coronavirus Case in Greece

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South Korea scrambles to contain MERS virus

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South Korea scrambles to contain MERS virus

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Structures of theMiddle East respiratory syndrome coronavirus3C-like protease reveal insights into substrate specificity

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Spread of MERS to South Korea and China

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Crystal structure of the papain-like protease of MERS coronavirus reveals unusual, potentially druggable active-site features

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A novel human coronavirus: Middle East respiratory syndrome human coronavirus

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Isolation of a Novel Coronavirus from a Man with Pneumonia in Saudi Arabia

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Overview of theCCP4 suite and current developments

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LigPlot+: Multiple Ligand–Protein Interaction Diagrams for Drug Discovery

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The ADP-ribose-1''-monophosphatase domains of severe acute respiratory syndrome coronavirus and human coronavirus 229E mediate resistance to antiviral interferon responses

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MolProbity: all-atom structure validation for macromolecular crystallography

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Differential Activities of Cellular and Viral Macro Domain Proteins in Binding of ADP-Ribose Metabolites

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Crystal Structures of Two Coronavirus ADP-Ribose-1''-Monophosphatases and Their Complexes with ADP-Ribose: a Systematic Structural Analysis of the Viral ADRP Domain

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Proteomics Analysis Unravels the Functional Repertoire of Coronavirus Nonstructural Protein 3

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Mouse Hepatitis Virus Liver Pathology Is Dependent on ADP-Ribose-1''-Phosphatase, a Viral Function Conserved in the Alpha-Like Supergroup

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