1. In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures.

    Acta Crystallogr D Struct Biol 72(Pt 1):93 (2016) PMID 26894538 PMCID PMC4756617

    Here, a method for presenting crystals of soluble and membrane proteins growing in the lipid cubic or sponge phase for in situ diffraction data collection at cryogenic temperatures is introduced. The method dispenses with the need for the technically demanding and inefficient crystal-harvesting ...
  2. Q&A: Brian Kobilka. Stuck on structure.

    Nature 514(7522):S12 (2014) PMID 25317590

  3. Nanoscale high-content analysis using compositional heterogeneities of single proteoliposomes.

    Nature Methods 11(9):931 (2014) PMID 25086504 PMCID PMC4485457

    Proteoliposome reconstitution is a standard method to stabilize purified transmembrane proteins in membranes for structural and functional assays. Here we quantified intrareconstitution heterogeneities in single proteoliposomes using fluorescence microscopy. Our results suggest that compositiona...
  4. The role of protein dynamics in GPCR function: insights from the β2AR and rhodopsin.

    Current Opinion in Cell Biology 27:136 (2014) PMID 24534489 PMCID PMC3986065

    G protein-coupled receptors (GPCRs) are versatile signaling proteins that mediate complex cellular responses to hormones and neurotransmitters. Recent advances in GPCR crystallography have provided inactive and active state structures for rhodopsin and the β2 adrenergic receptor (β2AR). Although...
  5. The structural basis of G-protein-coupled receptor signaling (Nobel Lecture).

    Angewandte Chemie. International edition in Eng... 52(25):6380 (2013) PMID 23650120 PMCID PMC4031317

  6. Brian Kobilka: chipping away at the β2-adrenergic receptor. Interview by Ruth Williams.

    Circulation Research 112(12):1538 (2013) PMID 23743226

  7. Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study.

    Chemical Communications 49(23):2287 (2013) PMID 23165475 PMCID PMC3578972

    The development of a new class of surfactants for membrane protein manipulation, "GNG amphiphiles", is reported. These amphiphiles display promising behavior for membrane proteins, as demonstrated recently by the high resolution structure of a sodium-pumping pyrophosphatase reported by Kellosalo...
  8. Membrane Curvature Regulates the Oligomerization of Human β2-Adrenergic Receptors

    Biophysical Journal 104(2):42a (2013)

  9. A new era of GPCR structural and chemical biology.

    Nature Chemical Biology 8(8):670 (2012) PMID 22810761 PMCID PMC4031315

    G protein-coupled receptors (GPCRs) are versatile molecular machines that regulate the majority of physiological responses to chemically diverse hormones and neurotransmitters. Recent breakthroughs in structural studies have advanced our understanding of GPCR signaling, particularly the selectiv...
  10. Highly Accurate Quantification of the Oligomerization of the β2 Adrenergic Receptor using FRET

    Biophysical Journal 102(3):232a (2012)

  11. Tandem facial amphiphiles for membrane protein stabilization.

    Journal of the American Chemical Society 132(47):16750 (2010) PMID 21049926 PMCID PMC3050673

    We describe a new type of synthetic amphiphile that is intended to support biochemical characterization of intrinsic membrane proteins. Members of this new family displayed favorable behavior with four of five membrane proteins tested, and these amphiphiles formed relatively small micelles.
  12. Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins.

    Nature Methods 7(12):1003 (2010) PMID 21037590 PMCID PMC3063152

    The understanding of integral membrane protein (IMP) structure and function is hampered by the difficulty of handling these proteins. Aqueous solubilization, necessary for many types of biophysical analysis, generally requires a detergent to shield the large lipophilic surfaces of native IMPs. M...
  13. International Workshop at the Nobel Forum, Karolinska Institutet on G protein-coupled receptors: finding the words to describe monomers, oligomers, and their molecular mechanisms and defining their meaning. Can a consensus be reached?

    Journal of Receptors and Signal Transduction 30(5):284 (2010) PMID 20858022

    A meeting was held May 19, 2010 at the Karolinski Institute on Nomenclature in Pharmacology. This meeting occurred in conjunction with the Symposium The Changing World of G Protein Coupled Receptors: From Monomers to Dimers and Receptor Mosaics (Higher-order Oligomers) held the previous day at t...
  14. Regulation of G-protein coupled receptor traffic by an evolutionary conserved hydrophobic signal.

    Traffic 11(4):560 (2010) PMID 20059747 PMCID PMC2919199

    Plasma membrane (PM) expression of G-protein coupled receptors (GPCRs) is required for activation by extracellular ligands; however, mechanisms that regulate PM expression of GPCRs are poorly understood. For some GPCRs, such as alpha2c-adrenergic receptors (alpha(2c)-ARs), heterologous expressio...
  15. The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex.

    PNAS 106(23):9501 (2009) PMID 19470481 PMCID PMC2685739

    G protein-coupled receptors (GPCRs) mediate the majority of physiologic responses to hormones and neurotransmitters. However, many GPCRs exhibit varying degrees of agonist-independent G protein activation. This phenomenon is referred to as basal or constitutive activity. For many of these GPCRs,...
  16. Structure and Dynamics of the Human beta 2 Adrenergic Receptor

    Biophysical Journal 96(3):373a (2009)

  17. Understanding the ligand-receptor-G protein ternary complex for GPCR drug discovery.

    Methods in Molecular Biology 552:67 (2009) PMID 19513642

    Understanding the ternary complex between G protein-coupled receptors (GPCRs), cognate G proteins, and their ligands is an important landmark for drug discovery. Yet, little is known about the specific interactions between GPCRs and G proteins. For a better perspective on the ternary complex dyn...
  18. New G-protein-coupled receptor crystal structures: insights and limitations.

    Trends in Pharmacological Sciences 29(2):79 (2008) PMID 18194818

    G-protein-coupled receptors (GPCRs) constitute a large family of structurally similar proteins that respond to a chemically diverse array of physiological and environmental stimulants. Until recently, high-resolution structural information was limited to rhodopsin, a naturally abundant GPCR that...
  19. Signaling from beta1- and beta2-adrenergic receptors is defined by differential interactions with PDE4.

    EMBO Journal 27(2):384 (2008) PMID 18188154 PMCID PMC2196435

    Beta1- and beta2-adrenergic receptors (betaARs) are highly homologous, yet they play clearly distinct roles in cardiac physiology and pathology. Myocyte contraction, for instance, is readily stimulated by beta1AR but not beta2AR signaling, and chronic stimulation of the two receptors has opposin...
  20. Structure and conformational changes in the C-terminal domain of the beta2-adrenoceptor: insights from fluorescence resonance energy transfer studies.

    Journal of Biological Chemistry 282(18):13895 (2007) PMID 17347144

    The C terminus of the beta(2)-adrenoceptor (AR) interacts with G protein-coupled receptor kinases and arrestins in an agonist-dependent manner, suggesting that conformational changes induced by ligands in the transmembrane domains are transmitted to the C terminus. We used fluorescence resonance...
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