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index medicus (9) 9
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intracellular (3) 3
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membran (3) 3
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peptides (3) 3
protein (3) 3
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antiporters - chemistry (2) 2
aqueous-solutions (2) 2
arabidopsis proteins - chemistry (2) 2
beta-arrestins - chemistry (2) 2
binding sites (2) 2
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clathrin adapter (2) 2
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detergens (2) 2
elektronenmikroskopie (2) 2
endocytosis (2) 2
facial amphiphiles (2) 2
general chemistry (2) 2
gtp-binding protein alpha subunits, gs - metabolism (2) 2
guanine nucleotide-binding protein (2) 2
ion-channel (2) 2
mechanism (2) 2
membrane proteins - chemistry (2) 2
molecular biology (2) 2
multiprotein complexes (2) 2
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peptide-1 receptor (2) 2
pharmacology (2) 2
phosphorylation (2) 2
physical sciences (2) 2
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protein conformation (2) 2
protein domains (2) 2
protein stability (2) 2
receptors, g-protein-coupled - chemistry (2) 2
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signaling (2) 2
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transmission electron microscopy (2) 2
washing-materials (2) 2
aaa atpase vps4 (1) 1
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1. Full Text Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein
by Zhang, Yan and Sun, Bingfa and Feng, Dan and Hu, Hongli and Chu, Matthew and Qu, Qianhui and Tarrasch, Jeffrey T and Li, Shane and Sun Kobilka, Tong and Kobilka, Brian K and Skiniotis, Georgios
Nature, ISSN 0028-0836, 06/2017, Volume 546, Issue 7657, pp. 248 - 253
Glucagon-like peptide 1 (GLP-1) is a hormone with essential roles in regulating insulin secretion, carbohydrate metabolism and appetite. GLP-1 effects are... 
VISUALIZATION | PEPTIDE-1 RECEPTOR | DYNAMIC PROCESS | DOMAIN | GLUCAGON RECEPTOR | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | COUPLED RECEPTORS | BINDING | EXTRACELLULAR LOOP | FAMILY | GTP-Binding Protein alpha Subunits, Gs - metabolism | Rabbits | GTP-Binding Protein alpha Subunits, Gs - chemistry | Glucagon-Like Peptide 1 - metabolism | GTP-Binding Protein alpha Subunits, Gs - ultrastructure | Glucagon-Like Peptide-1 Receptor - chemistry | Models, Molecular | Glucagon-Like Peptide 1 - chemistry | Cryoelectron Microscopy | Glucagon-Like Peptide-1 Receptor - metabolism | Animals | Glucagon-Like Peptide-1 Receptor - ultrastructure | Protein Domains | Glucagon-Like Peptide-1 Receptor - classification | Physiological aspects | Hormone receptors | G proteins | Structure | Appetite | Carbohydrates | Atomic force microscopy | G protein-coupled receptors | Peptides | Glucagon | Secretion | Carbohydrate metabolism | Activation | Ras protein | Hormones | Glucose | Metabolism | Electron microscopy | Guanine nucleotide-binding protein | Insulin | Proteins | Receptors | Transmission electron microscopy | Pivots | Intracellular | Atomic structure | Glucagon-like peptide 1 | Crystal structure
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2. Full Text Phase-plate cryo-EM structure of a class B GPCR-G-protein complex
by Liang, Yi-Lynn and Khoshouei, Maryam and Radjainia, Mazdak and Zhang, Yan and Glukhova, Alisa and Tarrasch, Jeffrey and Thal, David M and Furness, Sebastian G. B and Christopoulos, George and Coudrat, Thomas and Danev, Radostin and Baumeister, Wolfgang and Miller, Laurence J and Christopoulos, Arthur and Kobilka, Brian K and Wootten, Denise and Skiniotis, Georgios and Sexton, Patrick M
Nature, ISSN 0028-0836, 06/2017, Volume 546, Issue 7656, pp. 118 - 123
Class B G-protein-coupled receptors are major targets for the treatment of chronic diseases, such as osteoporosis, diabetes and obesity. Here we report the... 
PEPTIDE-1 RECEPTOR | SALMON-CALCITONIN | ACTIVATION | MECHANISM | SPECIFICITY | PHARMACOLOGY | MULTIDISCIPLINARY SCIENCES | CONSEQUENCES | MICROSCOPY | BINDING | MODULATION | Receptors, Calcitonin - metabolism | Humans | Receptors, Calcitonin - classification | Receptors, Calcitonin - ultrastructure | Models, Molecular | Heterotrimeric GTP-Binding Proteins - metabolism | Cryoelectron Microscopy | Heterotrimeric GTP-Binding Proteins - ultrastructure | Conserved Sequence | Heterotrimeric GTP-Binding Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | Ligands | Protein Conformation | Receptors, Calcitonin - agonists | Cell Membrane - metabolism | Binding Sites | G protein-coupled receptors | Peptides | Molecular structure | Medical services | Helices | Hydrophobicity | Guanine nucleotide-binding protein | Proteins | Osteoporosis | Receptors | Biomedical materials | Functional anatomy | Calcitonin | Biocompatibility | Coupling | Coordination compounds | Obesity | Stability | Diabetes mellitus | Electron microscopy | Diseases | Bundling | Transmission electron microscopy | Plates (structural members) | Intracellular | Molecular biology
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3. Full Text Extended surface for membrane association in Zika virus NS1 structure
by Brown, W Clay and Akey, David L and Konwerski, Jamie R and Tarrasch, Jeffrey T and Skiniotis, Georgios and Kuhn, Richard J and Smith, Janet L and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature Structural and Molecular Biology, ISSN 1545-9993, 09/2016, Volume 23, Issue 9, pp. 865 - 867
The Zika virus, which has been implicated in an increase in neonatal microcephaly and Guillain-Barre syndrome, has spread rapidly through tropical regions of... 
BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOPHYSICS | CELL BIOLOGY | Zika Virus - ultrastructure | Sf9 Cells | Viral Nonstructural Proteins - chemistry | Animals | Surface Properties | Protein Structure, Quaternary | Virus Attachment | Models, Molecular | Crystallography, X-Ray | Protein Interaction Domains and Motifs | Spodoptera | Proteins | Viral proteins | Genetic aspects | Virulence (Microbiology) | Properties | Structure | Observations | Membrane proteins | Zika virus | Guillain-Barre syndrome | Molecular biology | Microcephaly | Virology | Crystal structure
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4. Full Text Structures of two distinct conformations of holo-non-ribosomal peptide synthetases
by Drake, Eric J and Miller, Bradley R and Shi, Ce and Tarrasch, Jeffrey T and Sundlov, Jesse A and Leigh Allen, C and Skiniotis, Georgios and Aldrich, Courtney C and Gulick, Andrew M and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature, ISSN 0028-0836, 01/2016, Volume 529, Issue 7585, pp. 235 - 238
Many important natural products are produced by multidomain non-ribosomal peptide synthetases (NRPSs)(1-4). During synthesis, intermediates are covalently... 
ADENYLATION | MODULE | ENZYME | MECHANISM | MULTIDISCIPLINARY SCIENCES | GENES | CONDENSATION DOMAIN | CRYSTAL | CARRIER PROTEIN | Protein Structure, Tertiary | Biocatalysis | Escherichia coli - enzymology | Models, Molecular | Crystallography, X-Ray | Holoenzymes - chemistry | Acinetobacter baumannii - enzymology | Peptide Synthases - metabolism | Coenzymes - metabolism | Carrier Proteins - metabolism | Holoenzymes - metabolism | Peptide Synthases - chemistry | Pantetheine - analogs & derivatives | Pantetheine - metabolism | Post-translational modification | Influence | Research | Catalysis | Peptides | Analysis | Proteins | Enzymes | Hydrogen bonds | Amino acids | Ligands | Crystal structure
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5. Full Text Structural insights into the activation of metabotropic glutamate receptors
by Koehl, Antoine and Hu, Hongli and Feng, Dan and Sun, Bingfa and Zhang, Yan and Robertson, Michael J and Chu, Matthew and Kobilka, Tong Sun and Laermans, Toon and Steyaert, Jan and Tarrasch, Jeffrey and Dutta, Somnath and Fonseca, Rasmus and Weis, William I and Mathiesen, Jesper M and Skiniotis, Georgios and Kobilka, Brian K and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Nature, ISSN 0028-0836, 02/2019, Volume 566, Issue 7742, pp. 79 - 84
Metabotropic glutamate receptors are family C G-protein-coupled receptors. They form obligate dimers and possess extracellular ligand-binding Venus flytrap... 
REFINEMENT | ANTAGONIST | PHARMACOLOGY | MULTIDISCIPLINARY SCIENCES | POSITIVE ALLOSTERIC MODULATORS | DIMERIZATION | COOPERATIVITY | HEPTAHELICAL DOMAIN | G-PROTEIN | SUBTYPE 5 | DISCOVERY | Metabotropic glutamate receptors | Observations | Structure | Enzyme activation | Methods | Binding | Plants (botany) | Cysteine | Automation | G protein-coupled receptors | Activation | Glutamic acid receptors | Electron microscopy | Crystallography | X-ray crystallography | Domains | Proteins | Signaling | Receptors | Microscopy | Signal processing | Ligands | Transmembrane domains | Dimers | Glutamic acid receptors (metabotropic) | Binding sites
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6. Full Text Accessible Mannitol‐Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation
by Hussain, Hazrat and Du, Yang and Scull, Nicola J and Mortensen, Jonas S and Tarrasch, Jeffrey and Bae, Hyoung Eun and Loland, Claus J and Byrne, Bernadette and Kobilka, Brian K and Chae, Pil Seok
Chemistry – A European Journal, ISSN 0947-6539, 05/2016, Volume 22, Issue 21, pp. 7068 - 7073
Integral membrane proteins are amphipathic molecules crucial for all cellular life. The structural study of these macromolecules starts with protein extraction... 
electron microscopy | membrane proteins | amphiphile design | novel detergents | protein stabilization | CRYSTALLIZATION | AQUEOUS-SOLUTIONS | COMPLEX | CRYSTAL-STRUCTURE | COUPLED RECEPTOR | FACIAL AMPHIPHILES | CHEMISTRY, MULTIDISCIPLINARY | MNG AMPHIPHILES | ION-CHANNEL | GLYCOL GNG AMPHIPHILES | INSIGHTS | Receptors, Adrenergic, beta-2 - isolation & purification | Membrane Proteins - isolation & purification | Arabidopsis - chemistry | Antiporters - chemistry | Humans | Bacterial Proteins - chemistry | Solubility | Antiporters - isolation & purification | Light-Harvesting Protein Complexes - isolation & purification | Rhodobacter capsulatus - chemistry | Receptors, Adrenergic, beta-2 - chemistry | Arabidopsis Proteins - isolation & purification | Arabidopsis Proteins - chemistry | Membrane Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | Mannitol - chemistry | Surface-Active Agents - chemistry | Protein Stability | Bacterial Proteins - isolation & purification | Light-Harvesting Protein Complexes - chemistry | Detergents, Synthetic | G proteins | Analysis | Mannitol | Membrane proteins | Proteins | Membranes | Purification | Effectiveness | Aggregates | Accessibility | Crystallization | Electron microscopy
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7. Full Text GPCR-G Protein-β-Arrestin Super-Complex Mediates Sustained G Protein Signaling
by Thomsen, Alex R.B and Plouffe, Bianca and Cahill, Thomas J and Shukla, Arun K and Tarrasch, Jeffrey T and Dosey, Annie M and Kahsai, Alem W and Strachan, Ryan T and Pani, Biswaranjan and Mahoney, Jacob P and Huang, Liyin and Breton, Billy and Heydenreich, Franziska M and Sunahara, Roger K and Skiniotis, Georgios and Bouvier, Michel and Lefkowitz, Robert J
Cell, ISSN 0092-8674, 08/2016, Volume 166, Issue 4, pp. 907 - 919
Classically, G protein-coupled receptor (GPCR) stimulation promotes G protein signaling at the plasma membrane, followed by rapid β-arrestin-mediated... 
VASOPRESSIN RECEPTOR | BETA-ARRESTIN2 | INTERNALIZATION | CLATHRIN ADAPTER | DETERMINANTS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COUPLED RECEPTOR | ENDOCYTOSIS | ASSOCIATION | BETA-ADRENERGIC RECEPTOR | CELL BIOLOGY | GTP-Binding Protein alpha Subunits, Gs - metabolism | Receptors, G-Protein-Coupled - metabolism | Signal Transduction | Humans | Multiprotein Complexes | beta-Arrestins - metabolism | Receptors, G-Protein-Coupled - agonists | Bioluminescence Resonance Energy Transfer Techniques | Microscopy, Electron | Endosomes - metabolism | Microscopy, Confocal | HEK293 Cells | Receptors, G-Protein-Coupled - antagonists & inhibitors | Cyclic AMP - metabolism | beta-Arrestins - chemistry | Receptors, G-Protein-Coupled - chemistry
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8. Full Text Phosphoantigen-induced conformational change of butyrophilin 3A1 (BTN3A1) and its implication on Vγ9Vδ2 T cell activation
by Gu, Siyi and Sachleben, Joseph R and Boughter, Christopher T and Nawrocka, Wioletta I and Borowska, Marta T and Tarrasch, Jeffrey T and Skiniotis, Georgios and Roux, Benoît and Adams, Erin J and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 08/2017, Volume 114, Issue 35, pp. E7311 - E7320
Human Vγ9Vδ2 T cells respond to microbial infections as well as certain types of tumors. The key initiators of Vγ9Vδ2 activation are small,... 
Phosphoantigen | Butyrophilin 3A1 | Conformational change | Human Vγ9Vδ2 T cells | Intraepithelial Lymphocytes - drug effects | Phosphorylation | Magnetic Resonance Spectroscopy - methods | Humans | Butyrophilins - chemistry | Crystallography, X-Ray | Receptors, Antigen, T-Cell, gamma-delta - immunology | Structure-Activity Relationship | Antigens, CD - metabolism | Intraepithelial Lymphocytes - physiology | Lymphocyte Activation - immunology | HEK293 Cells | Protein Binding | Protein Domains | Antigens - immunology | Antigens, CD - physiology | Protein Conformation | T-Lymphocytes - immunology | Antigens, CD - chemistry | Butyrophilins - physiology | Lymphocyte Activation - physiology | Biological Sciences | human Vγ9Vδ2 T cells | PNAS Plus | conformational change | butyrophilin 3A1 | phosphoantigen
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9. Full Text Distinct conformations of GPCR-β-arrestin complexes mediate desensitization, signaling, and endocytosis
by Cahill, Thomas J and Thomsen, Alex R. B and Tarrasch, Jeffrey T and Plouffe, Bianca and Nguyen, Anthony H and Yang, Fan and Huang, Li-Yin and Kahsai, Alem W and Bassoni, Daniel L and Gavino, Bryant J and Lamerdin, Jane E and Triest, Sarah and Shukla, Arun K and Berger, Benjamin and Little, John and Antar, Albert and Blanc, Adi and Qu, Chang-Xiu and Chen, Xin and Kawakami, Kouki and Inoue, Asuka and Aoki, Junken and Steyaert, Jan and Sun, Jin-Peng and Bouvier, Michel and Skiniotis, Georgios and Lefkowitz, Robert J
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 03/2017, Volume 114, Issue 10, pp. 2562 - 2567
beta-Arrestins (beta arrs) interact with G protein-coupled receptors (GPCRs) to desensitize G protein signaling, to initiate signaling on their own, and to... 
Signaling | GPCR | Endocytosis | Arrestin | Desensitization | RECRUITMENT | CELLS | signaling | CLATHRIN ADAPTER | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | TRAFFICKING | arrestin | desensitization | GRKS | PROTEIN-COUPLED RECEPTOR | ROLES | endocytosis | BETA-ADRENERGIC RECEPTOR | Humans | Molecular Conformation | Multiprotein Complexes | GTP-Binding Protein Regulators - genetics | Mutant Proteins - genetics | Amino Acid Sequence - genetics | beta-Arrestins - genetics | Mutant Proteins - chemistry | HEK293 Cells | Endocytosis - genetics | Receptors, G-Protein-Coupled - genetics | beta-Arrestins - chemistry | Receptors, G-Protein-Coupled - chemistry | Biological Sciences | Physical Sciences
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10. Full Text Highly Branched Pentasaccharide-Bearing Amphiphiles for Membrane Protein Studies
by Ehsan, Muhammad and Du, Yang and Scull, Nicola J and Tikhonova, Elena and Tarrasch, Jeffrey and Mortensen, Jonas S and Loland, Claus J and Skiniotis, Georgios and Guan, Lan and Byrne, Bernadette and Kobilka, Brian K and Chae, Pil Seok
Journal of the American Chemical Society, ISSN 0002-7863, 03/2016, Volume 138, Issue 11, pp. 3789 - 3796
Detergents are essential tools for membrane protein manipulation. Micelles formed by detergent molecules have the ability to encapsulate the hydrophobic... 
CRYSTALLIZATION | STRUCTURAL INSIGHTS | AQUEOUS-SOLUTIONS | COMPLEX | CRYSTAL-STRUCTURE | STABILIZATION | ION-CHANNEL | CRYO-EM | FACIAL AMPHIPHILES | CHEMISTRY, MULTIDISCIPLINARY | BETA-ADRENERGIC RECEPTOR | Carbohydrate Sequence | Oligosaccharides, Branched-Chain - chemistry | Green Fluorescent Proteins - analysis | Detergents - chemistry | Antiporters - chemistry | Recombinant Fusion Proteins - analysis | Antiporters - analysis | Models, Molecular | Spectrometry, Fluorescence | Structure-Activity Relationship | Recombinant Fusion Proteins - chemistry | Detergents - chemical synthesis | Membrane Proteins - analysis | Arabidopsis Proteins - chemistry | Membrane Proteins - chemistry | Micelles | Hydrophobic and Hydrophilic Interactions | Oligosaccharides, Branched-Chain - chemical synthesis | Arabidopsis Proteins - analysis | Green Fluorescent Proteins - chemistry | Usage | Chemical properties | Electron microscopy | Chemical compounds | Analysis | Membrane proteins
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11. Full Text Phosphoantigen-induced conformational change of butyrophilin 3A1 and its implication on V[gamma]9V[delta]2 T cell activation
by Gu, Siyi and Sachleben, Joseph R and Boughter, Christopher T and Nawrocka, Wioletta I and Borowska, Marta T and Tarrasch, Jeffrey T and Skiniotis, Georgios and Roux, Benoit and Adams, Erin J
Proceedings of the National Academy of Sciences of the United States, ISSN 0027-8424, 08/2017, Volume 114, Issue 35, p. E7311
Cell interaction | Antigens | T cells | Health aspects
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12. Phosphoantigen-induced conformational change of butyrophilin 3A1 (BTN3A1) and its implication on Vγ9Vδ2 T cell activation
by Siyi Gu and Joseph R Sachleben and Christopher T Boughter and Wioletta I Nawrocka and Marta T Borowska and Jeffrey T Tarrasch and Georgios Skiniotis and Benoît Roux and Erin J Adams
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 08/2017, Volume 114, Issue 35, p. E7311
Human Vγ9Vδ2 T cells respond to microbial infections as well as certain types of tumors. The key initiators of Vγ9Vδ2 activation are small,... 
Binding | Butyrophilin | Antigens | Bacterial infections | Nuclear magnetic resonance--NMR | Computer simulation | Initiators | Tumor cells | Molecular dynamics | T cell receptors | Activation | Lymphocytes T | Crystallography | Cell adhesion & migration | Studies | Magnetic resonance spectroscopy | Interfaces | Spectrometry | Cell activation | Microorganisms | Lymphocytes | Intracellular | Cellular structure | Tumors
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13. Full Text Author Correction: Structural insights into the activation of metabotropic glutamate receptors
by Koehl, Antoine and Hu, Hongli and Feng, Dan and Sun, Bingfa and Zhang, Yan and Robertson, Michael J and Chu, Matthew and Kobilka, Tong Sun and Laeremans, Toon and Steyaert, Jan and Tarrasch, Jeffrey and Dutta, Somnath and Fonseca, Rasmus and Weis, William I and Mathiesen, Jesper M and Skiniotis, Georgios and Kobilka, Brian K and SLAC National Accelerator Lab., Menlo Park, CA (United States)
Nature, ISSN 0028-0836, 03/2019, Volume 567, Issue 7747, pp. E10 - E10
The surname of author Toon Laeremans was misspelled 'Laermans'. This error has been corrected online. 
GENERAL AND MISCELLANEOUS
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14. Full Text Structural Insights into Metabotropic Glutamate Receptor Activation
by Koehl, Antoine and Hu, Hongli and Feng, Dan and Sun, Bingfa and Zhang, Yan and Robertson, Michael J and Chu, Matthew and Kobilka, Tong Sun and Pardon, Els and Steyaert, Jan and Tarrasch, Jeffrey and Dutta, Somnath and Fonseca, Rasmus and Weis, William I and Mathiesen, Jesper M and Skiniotis, Georgios and Kobilka, Brian K
Nature, ISSN 0028-0836, 2/2019, Volume 566, Issue 7742, pp. 79 - 84
Metabotropic glutamate receptors are Family C G protein coupled receptors that form obligate dimers and possess extracellular ligand binding Venus flytrap... 
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15. Full Text Structural insights into the activation of metabotropic glutamate receptors
by Koehl, Antoine and Hu, Hongli and Feng, Dan and Sun, Bingfa and Zhang, Yan and Robertson, Michael J and Chu, Matthew and Kobilka, Tong Sun and Laeremans, Toon and Steyaert, Jan and Tarrasch, Jeffrey and Dutta, Somnath and Fonseca, Rasmus and Weis, William I and Mathiesen, Jesper M and Skiniotis, Georgios and Kobilka, Brian K and SLAC National Accelerator Lab., Menlo Park, CA (United States)
Nature (London), ISSN 0028-0836, 01/2019, Volume 566, Issue 7742
Metabotropic glutamate receptors are family C G-protein-coupled receptors. They form obligate dimers and possess extracellular ligand-binding Venus flytrap... 
BASIC BIOLOGICAL SCIENCES
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16. Full Text Structures of Two Distinct Conformations of holo-Nonribosomal Peptide Synthetases
by Drake, Eric J and Miller, Bradley R and Shi, Ce and Tarrasch, Jeffrey T and Sundlov, Jesse A and Allen, C. Leigh and Skiniotis, Georgios and Aldrich, Courtney C and Gulick, Andrew M
Nature, ISSN 0028-0836, 1/2016, Volume 529, Issue 7585, pp. 235 - 238
Many important natural products are produced by multidomain nonribosomal peptide synthetases (NRPSs) 1 – 4 . During synthesis, intermediates are covalently... 
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17. Full Text Highly branched penta-saccharide-bearing amphiphiles for membrane protein studies
by Ehsan, Muhammad and Du, Yang and Scull, Nicola J and Tikhonova, Elena and Tarrasch, Jeffrey and Mortensen, Jonas S and Loland, Claus J and Skiniotis, Georgios and Guan, Lan and Byrne, Bernadette and Kobilka, Brian K and Chae, Pil Seok
Journal of the American Chemical Society, ISSN 0002-7863, 3/2016, Volume 138, Issue 11, pp. 3789 - 3796
Detergents are essential tools for membrane protein manipulation. Micelles formed by detergent molecules have the ability to encapsulate the hydrophobic... 
penta-saccharide | novel amphiphiles | membrane proteins | molecular design | protein stability
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