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A General Amino Acid Synthesis Enabled by Innate Radical Cross‐Coupling.
- Published in:
- Angewandte Chemie, 2018, v. 130, n. 44, p. 14768, doi. 10.1002/ange.201809310
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- Article
Chemical genetics strategy identifies an HCV NS5A inhibitor with a potent clinical effect.
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- Nature, 2010, v. 465, n. 7294, p. 96, doi. 10.1038/nature08960
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- Article
The crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HCV inhibitors.
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- Protein Science: A Publication of the Protein Society, 2014, v. 23, n. 6, p. 723, doi. 10.1002/pro.2456
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- Article
Lattice engineering enables definition of molecular features allowing for potent small-molecule inhibition of HIV-1 entry.
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- Nature Communications, 2019, v. 10, n. 1, p. 1, doi. 10.1038/s41467-018-07851-1
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- Article
A General Amino Acid Synthesis Enabled by Innate Radical Cross‐Coupling.
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- Angewandte Chemie International Edition, 2018, v. 57, n. 44, p. 14560, doi. 10.1002/anie.201809310
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- Article
Genotypic correlates of susceptibility to HIV-1 attachment inhibitor BMS-626529, the active agent of the prodrug BMS-663068.
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- Journal of Antimicrobial Chemotherapy (JAC), 2014, v. 69, n. 3, p. 573, doi. 10.1093/jac/dkt412
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- Article
Mechanistic Characterization and Molecular Modeling of Hepatitis B Virus Polymerase Resistance to Entecavir.
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- PLoS ONE, 2010, v. 5, n. 2, p. 1, doi. 10.1371/journal.pone.0009195
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- Article
Resensitizing daclatasvir-resistant hepatitis C variants by allosteric modulation of NS5A.
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- Nature, 2015, v. 527, n. 7577, p. 245, doi. 10.1038/nature15711
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- Article
Homology models of the HIV-1 attachment inhibitor BMS-626529 bound to gp120 suggest a unique mechanism of action.
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- Proteins, 2015, v. 83, n. 2, p. 331, doi. 10.1002/prot.24726
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- Article
Expanding GPCR homology model binding sites via a balloon potential: A molecular dynamics refinement approach.
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- Proteins, 2008, v. 71, n. 4, p. 1919, doi. 10.1002/prot.21906
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- Article