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Structure-Guided Design and Optimization of Small Molecules Targeting the Protein–Protein Interaction between the von Hippel–Lindau (VHL) E3 Ubiquitin Ligase and the Hypoxia Inducible Factor (HIF) Alpha Subunit with in Vitro Nanomolar AffinitiesChloroplasts assemble the major subunit FaeG of Escherichia coli F4 (K88) fimbriae to strand-swapped dimersThe F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfacesStructural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeGSmall-Molecule Inhibitors of the Interaction between the E3 Ligase VHL and HIF1αDissecting Fragment-Based Lead Discovery at the von Hippel-Lindau Protein:Hypoxia Inducible Factor 1α Protein-Protein InterfaceTargeting the von Hippel–Lindau E3 Ubiquitin Ligase Using Small Molecules To Disrupt the VHL/HIF-1α InteractionIs NMR Fragment Screening Fine-Tuned to Assess Druggability of Protein–Protein Interactions?The active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE
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hulumtuese
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onderzoeker
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researcher
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հետազոտող
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name
Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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type
label
Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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Inge Van Molle
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