1. Selective, rapid and optically switchable regulation of protein function in live mammalian cells.

    Nature Chemistry 7(7):554 (2015) PMID 26100803

    The rapid and selective regulation of a target protein within living cells that contain closely related family members is an outstanding challenge. Here we introduce genetically directed bioorthogonal ligand tethering (BOLT) and demonstrate selective inhibition (iBOLT) of protein function. In iB...
  2. Biophysical mechanism of T-cell receptor triggering in a reconstituted system.

    Nature 487(7405):64 (2012) PMID 22763440 PMCID PMC3393772

    A T-cell-mediated immune response is initiated by the T-cell receptor (TCR) interacting with peptide-bound major histocompatibility complex (pMHC) on an infected cell. The mechanism by which this interaction triggers intracellular phosphorylation of the TCR, which lacks a kinase domain, remains ...
  3. Biophysical mechanism of T-cell receptor triggering in a reconstituted system.

    Nature 487(7405):64 (2012) PMID 22763440 PMCID PMC3393772

    A T-cell-mediated immune response is initiated by the T-cell receptor (TCR) interacting with peptide-bound major histocompatibility complex (pMHC) on an infected cell. The mechanism by which this interaction triggers intracellular phosphorylation of the TCR, which lacks a kinase domain, remains ...
  4. The T cell receptor triggering apparatus is composed of monovalent or monomeric proteins.

    Journal of Biological Chemistry 286(37):31993 (2011) PMID 21757710 PMCID PMC3173209

    Understanding the component stoichiometry of the T cell antigen receptor (TCR) triggering apparatus is essential for building realistic models of signal initiation. Recent studies suggesting that the TCR and other signaling-associated proteins are preclustered on resting T cells relied on measur...
  5. The T cell receptor triggering apparatus is composed of monovalent or monomeric proteins.

    Journal of Biological Chemistry 286(37):31993 (2011) PMID 21757710 PMCID PMC3173209

    Understanding the component stoichiometry of the T cell antigen receptor (TCR) triggering apparatus is essential for building realistic models of signal initiation. Recent studies suggesting that the TCR and other signaling-associated proteins are preclustered on resting T cells relied on measur...
  6. The T cell receptor triggering apparatus is composed of monovalent or monomeric proteins.

    Journal of Biological Chemistry 286(37):31993 (2011) PMID 21757710 PMCID PMC3173209

    Understanding the component stoichiometry of the T cell antigen receptor (TCR) triggering apparatus is essential for building realistic models of signal initiation. Recent studies suggesting that the TCR and other signaling-associated proteins are preclustered on resting T cells relied on measur...
  7. The T cell receptor triggering apparatus is composed of monovalent or monomeric proteins.

    Journal of Biological Chemistry 286(37):31993 (2011) PMID 21757710 PMCID PMC3173209

    Understanding the component stoichiometry of the T cell antigen receptor (TCR) triggering apparatus is essential for building realistic models of signal initiation. Recent studies suggesting that the TCR and other signaling-associated proteins are preclustered on resting T cells relied on measur...
  8. A new pathway of CD5 glycoprotein-mediated T cell inhibition dependent on inhibitory phosphorylation of Fyn kinase.

    Journal of Biological Chemistry 286(35):30324 (2011) PMID 21757751 PMCID PMC3162391

    Triggering of the T cell receptor initiates a signaling cascade resulting in the activation of the T cell. These signals are integrated alongside those resulting from the triggering of other receptors whose function is to modulate the overall response. CD5 is an immunotyrosine-based inhibition m...
  9. A new pathway of CD5 glycoprotein-mediated T cell inhibition dependent on inhibitory phosphorylation of Fyn kinase.

    Journal of Biological Chemistry 286(35):30324 (2011) PMID 21757751 PMCID PMC3162391

    Triggering of the T cell receptor initiates a signaling cascade resulting in the activation of the T cell. These signals are integrated alongside those resulting from the triggering of other receptors whose function is to modulate the overall response. CD5 is an immunotyrosine-based inhibition m...
  10. Distinctive properties of the hyaluronan-binding domain in the lymphatic endothelial receptor Lyve-1 and their implications for receptor function.

    Journal of Biological Chemistry 285(14):10724 (2010) PMID 19887450 PMCID PMC2856280

    The lymphatic endothelial hyaluronan (HA) receptor Lyve-1 is a member of the Link protein superfamily most similar to the leukocyte HA receptor CD44. However, the structure of Lyve-1 and the nature of its interaction with ligand are obscure. Here we present new evidence that Lyve-1 is functional...
  11. Distinctive properties of the hyaluronan-binding domain in the lymphatic endothelial receptor Lyve-1 and their implications for receptor function.

    Journal of Biological Chemistry 285(14):10724 (2010) PMID 19887450 PMCID PMC2856280

    The lymphatic endothelial hyaluronan (HA) receptor Lyve-1 is a member of the Link protein superfamily most similar to the leukocyte HA receptor CD44. However, the structure of Lyve-1 and the nature of its interaction with ligand are obscure. Here we present new evidence that Lyve-1 is functional...
  12. Distinctive properties of the hyaluronan-binding domain in the lymphatic endothelial receptor Lyve-1 and their implications for receptor function.

    Journal of Biological Chemistry 285(14):10724 (2010) PMID 19887450 PMCID PMC2856280

    The lymphatic endothelial hyaluronan (HA) receptor Lyve-1 is a member of the Link protein superfamily most similar to the leukocyte HA receptor CD44. However, the structure of Lyve-1 and the nature of its interaction with ligand are obscure. Here we present new evidence that Lyve-1 is functional...
  13. Distinctive properties of the hyaluronan-binding domain in the lymphatic endothelial receptor Lyve-1 and their implications for receptor function.

    Journal of Biological Chemistry 285(14):10724 (2010) PMID 19887450 PMCID PMC2856280

    The lymphatic endothelial hyaluronan (HA) receptor Lyve-1 is a member of the Link protein superfamily most similar to the leukocyte HA receptor CD44. However, the structure of Lyve-1 and the nature of its interaction with ligand are obscure. Here we present new evidence that Lyve-1 is functional...
  14. Distinctive properties of the hyaluronan-binding domain in the lymphatic endothelial receptor Lyve-1 and their implications for receptor function.

    Journal of Biological Chemistry 285(14):10724 (2010) PMID 19887450 PMCID PMC2856280

    The lymphatic endothelial hyaluronan (HA) receptor Lyve-1 is a member of the Link protein superfamily most similar to the leukocyte HA receptor CD44. However, the structure of Lyve-1 and the nature of its interaction with ligand are obscure. Here we present new evidence that Lyve-1 is functional...
  15. Distinctive properties of the hyaluronan-binding domain in the lymphatic endothelial receptor Lyve-1 and their implications for receptor function.

    Journal of Biological Chemistry 285(14):10724 (2010) PMID 19887450 PMCID PMC2856280

    The lymphatic endothelial hyaluronan (HA) receptor Lyve-1 is a member of the Link protein superfamily most similar to the leukocyte HA receptor CD44. However, the structure of Lyve-1 and the nature of its interaction with ligand are obscure. Here we present new evidence that Lyve-1 is functional...
  16. Distinctive properties of the hyaluronan-binding domain in the lymphatic endothelial receptor Lyve-1 and their implications for receptor function.

    Journal of Biological Chemistry 285(14):10724 (2010) PMID 19887450 PMCID PMC2856280

    The lymphatic endothelial hyaluronan (HA) receptor Lyve-1 is a member of the Link protein superfamily most similar to the leukocyte HA receptor CD44. However, the structure of Lyve-1 and the nature of its interaction with ligand are obscure. Here we present new evidence that Lyve-1 is functional...
  17. Distinctive properties of the hyaluronan-binding domain in the lymphatic endothelial receptor Lyve-1 and their implications for receptor function.

    Journal of Biological Chemistry 285(14):10724 (2010) PMID 19887450 PMCID PMC2856280

    The lymphatic endothelial hyaluronan (HA) receptor Lyve-1 is a member of the Link protein superfamily most similar to the leukocyte HA receptor CD44. However, the structure of Lyve-1 and the nature of its interaction with ligand are obscure. Here we present new evidence that Lyve-1 is functional...
  18. Distinctive properties of the hyaluronan-binding domain in the lymphatic endothelial receptor Lyve-1 and their implications for receptor function.

    Journal of Biological Chemistry 285(14):10724 (2010) PMID 19887450 PMCID PMC2856280

    The lymphatic endothelial hyaluronan (HA) receptor Lyve-1 is a member of the Link protein superfamily most similar to the leukocyte HA receptor CD44. However, the structure of Lyve-1 and the nature of its interaction with ligand are obscure. Here we present new evidence that Lyve-1 is functional...
  19. Distinctive properties of the hyaluronan-binding domain in the lymphatic endothelial receptor Lyve-1 and their implications for receptor function.

    Journal of Biological Chemistry 285(14):10724 (2010) PMID 19887450 PMCID PMC2856280

    The lymphatic endothelial hyaluronan (HA) receptor Lyve-1 is a member of the Link protein superfamily most similar to the leukocyte HA receptor CD44. However, the structure of Lyve-1 and the nature of its interaction with ligand are obscure. Here we present new evidence that Lyve-1 is functional...
  20. The platelet receptor CLEC-2 is active as a dimer.

    Biochemistry (Washington) 48(46):10988 (2009) PMID 19824697

    The platelet receptor CLEC-2 binds to the snake venom toxin rhodocytin and the tumor cell surface protein podoplanin. Binding of either of these ligands promotes phosphorylation of a single tyrosine residue in the YXXL motif in the intracellular domain of CLEC-2. Phosphorylation of this tyrosine...