Streptavidin
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Subject Areas on Research
- A colorimetric gold nanoparticle sensor to interrogate biomolecular interactions in real time on a surface.
- Astatine-211-labeled biotin conjugates resistant to biotinidase for use in pretargeted radioimmunotherapy.
- Binding and signaling of surface-immobilized reagentless fluorescent biosensors derived from periplasmic binding proteins.
- Control of protein-ligand recognition using a stimuli-responsive polymer.
- Cutting edge: C3d functions as a molecular adjuvant in the absence of CD21/35 expression.
- DNA-templated self-assembly of protein and nanoparticle linear arrays.
- DNA-templated self-assembly of protein arrays and highly conductive nanowires.
- Differential osteopontin expression in phenotypically distinct subclones of murine breast cancer cells mediates metastatic behavior.
- Direct force measurements of the streptavidin-biotin interaction.
- Direct observation of multimer stabilization in the mechanical unfolding pathway of a protein undergoing oligomerization.
- Distinct MutS DNA-binding modes that are differentially modulated by ATP binding and hydrolysis.
- Dual-order snapshot spectral imaging of plasmonic nanoparticles.
- Dynamic seeding of perfusing human umbilical vein endothelial cells (HUVECs) onto dual-function cell adhesion ligands: Arg-Gly-Asp (RGD)-streptavidin and biotinylated fibronectin.
- Effect of streptavidin RGD mutant on the adhesion of endothelial cells.
- Effect of streptavidin affinity mutants on the integrin-independent adhesion of biotinylated endothelial cells.
- Effect of streptavidin-biotin on endothelial vasoregulation and leukocyte adhesion.
- Electrochemical biosensor of nanocube-augmented carbon nanotube networks.
- Engineered chimeric streptavidin tetramers as novel tools for bioseparations and drug delivery.
- Enhanced TOF-SIMS imaging of a micropatterned protein by stable isotope protein labeling.
- Founder's Award, Society for Biomaterials. Sixth World Biomaterials Congress 2000, Kamuela, HI,May 15-20, 2000. Really smart bioconjugates of smart polymers and receptor proteins.
- High-affinity augmentation of endothelial cell attachment: long-term effects on focal contact and actin filament formation.
- High-throughput screen for inhibitors of 1-deoxy-d-xylulose 5-phosphate reductoisomerase by surrogate ligand competition.
- Label-free plasmonic detection of biomolecular binding by a single gold nanorod.
- Molecular engineering of proteins and polymers for targeting and intracellular delivery of therapeutics.
- Nanomechanics of streptavidin hubs for molecular materials.
- Plasmonic detection of a model analyte in serum by a gold nanorod sensor.
- Preparation and characterization of anti-tenascin monoclonal antibody-streptavidin conjugates for pretargeting applications.
- Rational selection of gold nanorod geometry for label-free plasmonic biosensors.
- Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120.
- Streptavidin binding and endothelial cell adhesion to biotinylated fibronectin.
- Streptavidin-biotin binding energetics.
- Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex.
- Synergistic effect of shear stress and streptavidin-biotin on the expression of endothelial vasodilator and cytoskeleton genes.
- Synthesis and preliminary biological evaluation of (3-iodobenzoyl)norbiotinamide and ((5-iodo-3-pyridinyl)carbonyl)norbiotinamide: two radioiodinated biotin conjugates with improved stability.
- The motion of a single molecule, the lambda-receptor, in the bacterial outer membrane.
- The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy.
- Two-dimensional protein crystallization via metal-ion coordination by naturally occurring surface histidines.
- X-ray crystallographic studies of streptavidin mutants binding to biotin.
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Keywords of People
- Bennett, Vann, George Barth Geller Distinguished Professor of Molecular Biology, Duke Cancer Institute