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The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism.
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1999
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1.44
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2
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FEBS Lett
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1.30
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3
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The conformational effects of N-glycosylation on the tailpiece from serum IgM.
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1.28
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4
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Solution structure of human calcitonin gene-related peptide by 1H NMR and distance geometry with restrained molecular dynamics.
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1991
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1.28
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5
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Sensitivity enhancement of a two-dimensional experiment for the measurement of heteronuclear long-range coupling constants, by a new scheme of coherence selection by gradients.
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2001
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6
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The metal binding site of the hepatitis C virus NS3 protease. A spectroscopic investigation.
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1998
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7
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Structural characterization of the interactions of optimized product inhibitors with the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein by NMR and modelling studies.
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J Mol Biol
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1999
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8
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1990
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9
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Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain.
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10
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11
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Uncertainties in structural determinations of oligosaccharide conformation, using measurements of nuclear Overhauser effects.
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1990
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0.89
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12
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A conformationally homogeneous combinatorial peptide library.
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13
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Primary sequence dependence of conformation in oligomannose oligosaccharides.
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14
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15
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Resonance assignment and secondary structure determination and stability of the recombinant human uteroglobin with heteronuclear multidimensional NMR.
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1997
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0.75
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16
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Measurement of homonuclear three-bond J(H(N)Halpha) coupling constants in unlabeled peptides complexed with labeled proteins: application to a decapeptide inhibitor bound to the proteinase domain of the NS3 protein of hepatitis C virus (HCV).
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J Biomol NMR
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2001
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17
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High-resolution solution structure of two members of a conformationally homogeneous combinatorial peptide library based on the classical zinc-finger motif.
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1996
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0.75
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