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Quantum Dot-Based Concentric FRET Configuration for the Parallel Detection of Protease Activity and Concentration

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Structure-function relationships in the interaction of alpha-thrombin with blood platelets.

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Cell Death

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Fluorogenic substrates for proteases based on intramolecular fluorescence energy transfer (IFETS)

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Multiplexed Tracking of Protease Activity Using a Single Color of Quantum Dot Vector and a Time-Gated Förster Resonance Energy Transfer Relay

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Quantum Dots as Simultaneous Acceptors and Donors in Time-Gated Förster Resonance Energy Transfer Relays: Characterization and Biosensing

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Proteolytic Activity at Quantum Dot-Conjugates: Kinetic Analysis Reveals Enhanced Enzyme Activity and Localized Interfacial “Hopping”

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Assembly of a Concentric Förster Resonance Energy Transfer Relay on a Quantum Dot Scaffold: Characterization and Application to Multiplexed Protease Sensing

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Understanding the Self-Assembly of Proteins onto Gold Nanoparticles and Quantum Dots Driven by Metal-Histidine Coordination

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Proteolytic activity monitored by fluorescence resonance energy transfer through quantum-dot–peptide conjugates

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HD1, a Thrombin-directed Aptamer, Binds Exosite 1 on Prothrombin with High Affinity and Inhibits Its Activation by Prothrombinase

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Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry

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Regulation of Proteolytic Activity in Tissues

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Analysis of Protease Activity Using Quantum Dots and Resonance Energy Transfer

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