A crystal structure of the Dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replication - Test2 - elhamkhani - TriplyDB

A crystal structure of the Dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replication

A crystal structure of the Dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replication

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ZIKA-How fast does this virus mutate?Predicting Zika virus structural biology: Challenges and opportunities for intervention Potent Allosteric Dengue Virus NS5 Polymerase Inhibitors: Mechanism of Action and Resistance Profiling Flaviviral Replication Complex: Coordination between RNA Synthesis and 5'-RNA Capping The C-terminal 18 Amino Acid Region of Dengue Virus NS5 Regulates its Subcellular Localization and Contains a Conserved Arginine Residue Essential for Infectious Virus Production Analysis of worldwide sequence mutations in Zika virus proteins E, NS1, NS3 and NS5 from a structural point of view The many faces of the flavivirus NS5 protein in antagonism of type I interferon signaling Intrinsically Disordered Side of the Zika Virus Proteome Looking for inhibitors of the dengue virus NS5 RNA-dependent RNA-polymerase using a molecular docking approach The Zika virus methyltransferase: structure and functions for drug design perspectives Purification of Zika virus RNA-dependent RNA polymerase and its use to identify small-molecule Zika inhibitors Sequence-Specific Fidelity Alterations Associated with West Nile Virus Attenuation in Mosquitoes A Structural Overview of RNA-Dependent RNA Polymerases from the Flaviviridae Family The structure of Zika virus NS5 reveals a conserved domain conformation Dengue Virus Non-Structural Protein 5 Unstructural biology of the Dengue virus proteins.Isotope Labeling of Biomolecules: Structural Analysis of Viruses by HDX-MS.Identification of a Pyridoxine-Derived Small-Molecule Inhibitor Targeting Dengue Virus RNA-Dependent RNA Polymerase Dengue Virus Nonstructural Protein 5 (NS5) Assembles into a Dimer with a Unique Methyltransferase and Polymerase Interface Flexibility of NS5 Methyltransferase-Polymerase Linker Region Is Essential for Dengue Virus Replication.Structural insight and flexible features of NS5 proteins from all four serotypes of Dengue virus in solution Molecular basis for specific viral RNA recognition and 2'-O-ribose methylation by the dengue virus nonstructural protein 5 (NS5)Suppression of Drug Resistance in Dengue Virus.Dynamic Nucleolar Targeting of Dengue Virus Polymerase NS5 in Response to Extracellular pH Crystal structure of full-length Zika virus NS5 protein reveals a conformation similar to Japanese encephalitis virus NS5.The conformational changes of Zika virus methyltransferase upon converting SAM to SAH.Organization of the Flavivirus RNA replicase complex.Serotype-specific interactions among functional domains of dengue virus 2 nonstructural proteins (NS) 5 and NS3 are crucial for viral RNA replication.Interactions between the Dengue Virus Polymerase NS5 and Stem-Loop A.New developments in flavivirus drug discovery.Genomics, proteomics and evolution of dengue virus.A Conserved Pocket in the Dengue Virus Polymerase Identified through Fragment-based Screening.Identification of the critical linker residues conferring differences in the compactness of NS5 from Dengue virus serotype 4 and NS5 from Dengue virus serotypes 1-3.Zika virus hijacks stress granule proteins and modulates the host stress response.Evaluation of Sofosbuvir (β-D-2'-deoxy-2'-α-fluoro-2'-β-C-methyluridine) as an inhibitor of Dengue virus replication.Conformational Ensemble of the Poliovirus 3CD Precursor Observed by MD Simulations and Confirmed by SAXS: A Strategy to Expand the Viral Proteome?Peptides as Therapeutic Agents for Dengue Virus.Middle East Respiratory Syndrome Coronavirus Nonstructural Protein 16 Is Necessary for Interferon Resistance and Viral Pathogenesis.Structural and Functional Basis of the Fidelity of Nucleotide Selection by Flavivirus RNA-Dependent RNA Polymerases.Structure and function of Zika virus NS5 protein: perspectives for drug design.

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A crystal structure of the Dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replication

http://www.wikidata.org/entity/Q27321114

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2015 nî lūn-bûn

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2015 թուականի Մարտին հրատարակուած գիտական յօդուած

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2015 թվականի մարտին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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A crystal structure of the Den ...... xibility and virus replication

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A crystal structure of the Den ...... xibility and virus replication

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A crystal structure of the Den ...... xibility and virus replication

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A crystal structure of the Den ...... xibility and virus replication

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A crystal structure of the Den ...... xibility and virus replication

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A crystal structure of the Den ...... xibility and virus replication

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Chin Chin Lee

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Jie Zheng

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Kitti Wing Ki Chan

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Moon Y F Tay

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Subhash G Vasudevan

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Tingjin Sherryl Soh

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Tobias C Cornvik

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Wint Wint Phoo

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Yongqian Zhao

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P2860

Structure and functionality in flavivirus NS-proteins: perspectives for drug design

The global distribution and burden of dengue

NS5 of dengue virus mediates STAT2 binding and degradation

MolProbity: all-atom structure validation for macromolecular crystallography

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Serotype-specific detection of dengue viruses in a fourplex real-time reverse transcriptase PCR assay.

An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization

West Nile Virus 5'-Cap Structure Is Formed by Sequential Guanine N-7 and Ribose 2'-O Methylations by Nonstructural Protein 5

Structure and Function of Flavivirus NS5 Methyltransferase

Crystal Structure of the Dengue Virus RNA-Dependent RNA Polymerase Catalytic Domain at 1.85-Angstrom Resolution

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Kunchithapadam Swaminathan

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