1. Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling.

    Cell 161(5):1101 (2015) PMID 25981665 PMCID PMC4441853

    G-protein-coupled receptors (GPCRs) transduce signals from the extracellular environment to intracellular proteins. To gain structural insight into the regulation of receptor cytoplasmic conformations by extracellular ligands during signaling, we examine the structural dynamics of the cytoplasmi...
  2. Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.

    Biochemistry (Washington) 53(46):7160 (2014) PMID 25268658 PMCID PMC4245987

    Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic ...
  3. Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.

    Biochemistry (Washington) 53(46):7160 (2014) PMID 25268658 PMCID PMC4245987

    Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic ...
  4. Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.

    Biochemistry (Washington) 53(46):7160 (2014) PMID 25268658 PMCID PMC4245987

    Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic ...
  5. Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.

    Biochemistry (Washington) 53(46):7160 (2014) PMID 25268658 PMCID PMC4245987

    Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic ...
  6. Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.

    Biochemistry (Washington) 53(46):7160 (2014) PMID 25268658 PMCID PMC4245987

    Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic ...
  7. High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population.

    Journal of Biological Chemistry 289(18):12566 (2014) PMID 24627492 PMCID PMC4007448

    In recent years, there has been a vast increase in structural and functional understanding of VDAC1, but VDAC2 and -3 have been understudied despite having many unique phenotypes. One reason for the paucity of structural and biochemical characterization of the VDAC2 and -3 isoforms stems from th...
  8. High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population.

    Journal of Biological Chemistry 289(18):12566 (2014) PMID 24627492 PMCID PMC4007448

    In recent years, there has been a vast increase in structural and functional understanding of VDAC1, but VDAC2 and -3 have been understudied despite having many unique phenotypes. One reason for the paucity of structural and biochemical characterization of the VDAC2 and -3 isoforms stems from th...
  9. High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population.

    Journal of Biological Chemistry 289(18):12566 (2014) PMID 24627492 PMCID PMC4007448

    In recent years, there has been a vast increase in structural and functional understanding of VDAC1, but VDAC2 and -3 have been understudied despite having many unique phenotypes. One reason for the paucity of structural and biochemical characterization of the VDAC2 and -3 isoforms stems from th...
  10. Self-association of arrestin family members.

    Handbook of experimental pharmacology 219:205 (2014) PMID 24292832 PMCID PMC4512752

    Mammals express four arrestin subtypes, three of which have been shown to self-associate. Cone photoreceptor-specific arrestin-4 is the only one that is a constitutive monomer. Visual arrestin-1 forms tetramers both in crystal and in solution, but the shape of its physiologically relevant soluti...
  11. Self-association of arrestin family members.

    Handbook of experimental pharmacology 219:205 (2014) PMID 24292832

    Mammals express four arrestin subtypes, three of which have been shown to self-associate. Cone photoreceptor-specific arrestin-4 is the only one that is a constitutive monomer. Visual arrestin-1 forms tetramers both in crystal and in solution, but the shape of its physiologically relevant soluti...
  12. Self-association of arrestin family members.

    Handbook of experimental pharmacology 219:205 (2014) PMID 24292832

    Mammals express four arrestin subtypes, three of which have been shown to self-associate. Cone photoreceptor-specific arrestin-4 is the only one that is a constitutive monomer. Visual arrestin-1 forms tetramers both in crystal and in solution, but the shape of its physiologically relevant soluti...
  13. Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant.

    Cellular Signalling 25(12):2613 (2013) PMID 24012956 PMCID PMC3833262

    Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell ...
  14. Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant.

    Cellular Signalling 25(12):2613 (2013) PMID 24012956 PMCID PMC3833262

    Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell ...
  15. Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant

    Cellular Signalling 25(12):2613 (2013)

    Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-ind...
  16. Conformational selection and adaptation to ligand binding in T4 lysozyme cavity mutants.

    PNAS 110(46):E4306 (2013) PMID 24167295 PMCID PMC3832024

    The studies presented here explore the relationship between protein packing and molecular flexibility using ligand-binding cavity mutants of T4 lysozyme. Although previously reported crystal structures of the mutants investigated show single conformations that are similar to the WT protein, site...
  17. Conformational selection and adaptation to ligand binding in T4 lysozyme cavity mutants.

    PNAS 110(46):E4306 (2013) PMID 24167295 PMCID PMC3832024

    The studies presented here explore the relationship between protein packing and molecular flexibility using ligand-binding cavity mutants of T4 lysozyme. Although previously reported crystal structures of the mutants investigated show single conformations that are similar to the WT protein, site...
  18. Technological advances in site-directed spin labeling of proteins.

    Current Opinion in Structural Biology 23(5):725 (2013) PMID 23850140 PMCID PMC3805720

    Molecular flexibility over a wide time range is of central importance to the function of many proteins, both soluble and membrane. Revealing the modes of flexibility, their amplitudes, and time scales under physiological conditions is the challenge for spectroscopic methods, one of which is site...
  19. Technological advances in site-directed spin labeling of proteins.

    Current Opinion in Structural Biology 23(5):725 (2013) PMID 23850140 PMCID PMC3805720

    Molecular flexibility over a wide time range is of central importance to the function of many proteins, both soluble and membrane. Revealing the modes of flexibility, their amplitudes, and time scales under physiological conditions is the challenge for spectroscopic methods, one of which is site...
  20. Technological advances in site-directed spin labeling of proteins

    Current Opinion in Structural Biology 23(5):725 (2013)

    • New spin labels extend the capability of site-directed spin labeling. • Inter-spin distances can be measured to 100Å, along with the associated distributions. ...