Schertler Group Research

Class A G protein-coupled receptor (GPCRs) transduce extracellular signals across the cell membrane by activating cytoplasmic-bound heterotrimeric GTP binding proteins (G proteins), which, in turn, modulate the activity of downstream effector proteins. Despite the physiological and pharmacological relevance of GPCRs, the structural basis of ligand efficacy and receptor activation, and how these elements translate into cytoplasmic trafficking and cellular response still remain elusive. In my group we integrate data from structural biology, molecular biology, cellular biology and structural bioinformatics to study the molecular basis of GPCR function. Specifically, we aim to obtain the crystal structure of the complexes between GPCRs and their cytoplasmic partners, the centre-pieces that connect extracellular stimuli to intracellular signals. In addition, we compare the profile of activated signalling molecules with their dynamic intracellular localisation pattern to learn how receptor activation translates into specific pathways of cellular signalling. Combination of the data resulting from the study of different Class A GPCRs will allow us to obtain a global picture of GPCR signalling. Our goal is to link receptor structure, cellular biological data and pharmacological results to physiological function.
I have long-standing expertise with light-activated GPCRs, in particular mammalian rhodopsin and, more recently, invertebrate rhodopsins, for example Jumping Spider Rhodopsin. In collaboration with partners with expertise in spectroscopic analysis of retinal proteins and in vivo applications of these proteins, we aim to understand in atomic detail the structure-function relationship between the retinal binding pocket and i) the spectroscopic properties of the protein, ii) the molecular basis of mono- versus instability and iii) molecular determinants of G-protein selectivity. Together, this will allow for the design of next-generation of optogenetic tools, allowing for photon-mediated control of major signalling pathways in any cell type. 

Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit
Tsai CJ, Marino J, Adaixo R, Pamula F, Muehle J, Maeda S, Flock T, Taylor NM, Mohammed I, Matile H, Dawson RJ, Deupi X, Stahlberg H, Schertler GF.
Elife. 2019;18:e46041.

Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR
Varma N, Mutt E, Mühle J, Panneels V, Terakita A, Deupi X, Nogly P, Schertler GF, Lesca E.
PNAS. 2019;116(29):14547-14556.

Crystal structure of rhodopsin in complex with a mini-G o sheds light on the principles of G protein selectivity
Tsai CJ, Pamula F, Nehmé R, Mühle J, Weinert T, Flock T, Nogly P, Edwards PC, Carpenter B, Gruhl T, Ma P, Deupi X, Standfuss J, Tate CG, Schertler GFX.
Sci Adv 2018;4(9):eaat7052

Molecular signatures of G-protein-coupled receptors
Venkatakrishnan AJ, Deupi X, Lebon G, Tate CG, Schertler GF, Babu MM.
Nature 2013;494(7436):185-94

The structural basis for agonist and partial agonist action on a β(1)-adrenergic receptor.
Warne T, Moukhametzianov R, Baker JG, Nehmé R, Edwards PC, Leslie AG, Schertler GF, Tate CG.
Nature. 2011;469(7329):241-4.




2024

  • Tejero O, Pamula F, Koyanagi M, Nagata T, Afanasyev P, Das I, et al.
    Active state structures of a bistable visual opsin bound to G proteins
    Nature Communications. 2024; 15(1): 8928 (13 pp.). https://doi.org/10.1038/s41467-024-53208-2
    DORA PSI
  • Bonifer C, Hanke W, Mühle J, Löhr F, Becker-Baldus J, Nagel J, et al.
    Structural response of G protein binding to the cyclodepsipeptide inhibitor FR900359 probed by NMR spectroscopy
    Chemical Science. 2024; 15(32): 12939-12956. https://doi.org/10.1039/d4sc01950d
    DORA PSI
  • Rodrigues MJ, Tejero O, Mühle J, Pamula F, Das I, Tsai CJ, et al.
    Activating an invertebrate bistable opsin with the all-trans 6.11 retinal analog
    Proceedings of the National Academy of Sciences of the United States of America PNAS. 2024; 121(31): e2406814121 (3 pp.). https://doi.org/10.1073/pnas.2406814121
    DORA PSI
  • Gotthard G, Mous S, Weinert T, Maia RNA, James D, Dworkowski F, et al.
    Capturing the blue-light activated state of the Phot-LOV1 domain from Chlamydomonas reinhardtii using time-resolved serial synchrotron crystallography
    IUCrJ. 2024; 11(5): (17 pp.). https://doi.org/10.1107/S2052252524005608
    DORA PSI
  • Bertalan É, Rodrigues MJ, Schertler GFX, Bondar AN
    Graph-based algorithms to dissect long-distance water-mediated H-bond networks for conformational couplings in GPCRs
    British Journal of Pharmacology. 2024. https://doi.org/10.1111/bph.16387
    DORA PSI

2023

  • Casadei CM, Hosseinizadeh A, Bliven S, Weinert T, Standfuss J, Fung R, et al.
    Low-pass spectral analysis of time-resolved serial femtosecond crystallography data
    Structural Dynamics. 2023; 10(3): 034101 (18 pp.). https://doi.org/10.1063/4.0000178
    DORA PSI
  • Barret DCA, Schuster D, Rodrigues MJ, Leitner A, Picotti P, Schertler GFX, et al.
    Structural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel
    Proceedings of the National Academy of Sciences of the United States of America PNAS. 2023; 120(15): e2300309120 (10 pp.). https://doi.org/10.1073/pnas.2300309120
    DORA PSI
  • Gruhl T, Weinert T, Rodrigues MJ, Milne CJ, Ortolani G, Nass K, et al.
    Ultrafast structural changes direct the first molecular events of vision
    Nature. 2023; 615: 939-944. https://doi.org/10.1038/s41586-023-05863-6
    DORA PSI
  • Rodrigues MJ, Casadei CM, Weinert T, Panneels V, Schertler GFX
    Correction of rhodopsin serial crystallography diffraction intensities for a lattice-translocation defect
    Acta Crystallographica Section D: Structural Biology. 2023; 79(3): D79 (10 pp.). https://doi.org/10.1107/S2059798323000931
    DORA PSI
  • Emmenegger M, De Cecco E, Lamparter D, Jacquat RPB, Riou J, Menges D, et al.
    Continuous population-level monitoring of SARS-CoV-2 seroprevalence in a large European metropolitan region
    iScience. 2023; 26(2): 105928 (34 pp.). https://doi.org/10.1016/j.isci.2023.105928
    DORA PSI

2022

  • Casadei CM, Hosseinizadeh A, Schertler GFX, Ourmazd A, Santra R
    Dynamics retrieval from stochastically weighted incomplete data by low-pass spectral analysis
    Structural Dynamics. 2022; 9(4): 044101 (9 pp.). https://doi.org/10.1063/4.0000156
    DORA PSI
  • Mous S, Gotthard G, Ehrenberg D, Sen S, Weinert T, Johnson PJM, et al.
    Dynamics and mechanism of a light-driven chloride pump
    Science. 2022; 375(6583): 845-851. https://doi.org/10.1126/science.abj6663
    DORA PSI
  • Barret DCA, Schertler GFX, Benjamin Kaupp U, Marino J
    The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods
    Nature Structural and Molecular Biology. 2022; 29(1): 32-39. https://doi.org/10.1038/s41594-021-00700-8
    DORA PSI
  • Barret DCA, Schertler GFX, Kaupp UB, Marino J
    Structural basis of the partially open central gate in the human CNGA1/CNGB1 channel explained by additional density for calmodulin in cryo-EM map
    Journal of Structural Biology. 2022; 214(1): 107828 (5 pp.). https://doi.org/10.1016/j.jsb.2021.107828
    DORA PSI


2021

  • Casadei CM, Hosseinizadeh A, Schertler GFX, Ourmazd A, Santra R
    Dynamics retrieval from stochastically weighted incomplete data by low-pass spectral analysis
    Structural Dynamics. 2022; 9(4): 044101 (9 pp.). https://doi.org/10.1063/4.0000156
    DORA PSI
  • Mous S, Gotthard G, Ehrenberg D, Sen S, Weinert T, Johnson PJM, et al.
    Dynamics and mechanism of a light-driven chloride pump
    Science. 2022; 375(6583): 845-851. https://doi.org/10.1126/science.abj6663
    DORA PSI
  • Barret DCA, Schertler GFX, Benjamin Kaupp U, Marino J
    The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods
    Nature Structural and Molecular Biology. 2022; 29(1): 32-39. https://doi.org/10.1038/s41594-021-00700-8
    DORA PSI
  • Barret DCA, Schertler GFX, Kaupp UB, Marino J
    Structural basis of the partially open central gate in the human CNGA1/CNGB1 channel explained by additional density for calmodulin in cryo-EM map
    Journal of Structural Biology. 2022; 214(1): 107828 (5 pp.). https://doi.org/10.1016/j.jsb.2021.107828
    DORA PSI
  • Romantini N, Alam S, Dobitz S, Spillmann M, De Foresta M, Schibli R, et al.
    Exploring the signaling space of a GPCR using bivalent ligands with a rigid oligoproline backbone
    Proceedings of the National Academy of Sciences of the United States of America PNAS. 2021; 118(48): e2108776118 (8 pp.). https://doi.org/10.1073/pnas.2108776118
    DORA PSI
  • Bertalan É, Lesca E, Schertler GFX, Bondar A-N
    C-Graphs tool with graphical user interface to dissect conserved hydrogen-bond networks: applications to visual rhodopsins
    Journal of Chemical Information and Modeling. 2021; 61(11): 5692-5707. https://doi.org/10.1021/acs.jcim.1c00827
    DORA PSI
  • Wu N, Olechwier AM, Brunner C, Edwards PC, Tsai C-J, Tate CG, et al.
    High-mass MALDI-MS unravels ligand-mediated G protein-coupling selectivity to GPCRs
    Proceedings of the National Academy of Sciences of the United States of America PNAS. 2021; 118(31): e2024146118 (9 pp.). https://doi.org/10.1073/pnas.2024146118
    DORA PSI
  • Panneels V, Diaz A, Imsand C, Guizar-Sicairos M, Müller E, Bittermann AG, et al.
    Imaging of retina cellular and subcellular structures using ptychographic hard X-ray tomography
    Journal of Cell Science. 2021; 134(19): jcs258561 (8 pp.). https://doi.org/10.1242/jcs.258561
    DORA PSI
  • Isaikina P, Tsai C-J, Dietz N, Pamula F, Grahl A, Goldie KN, et al.
    Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist
    Science Advances. 2021; 7(25): eabg8685 (11 pp.). https://doi.org/10.1126/sciadv.abg8685
    DORA PSI
  • Marino J, Schertler GFX
    A set of common movements within GPCR-G-protein complexes from variability analysis of cryo-EM datasets
    Journal of Structural Biology. 2021; 213(2): 107699 (7 pp.). https://doi.org/10.1016/j.jsb.2021.107699
    DORA PSI
  • Abiko LA, Rogowski M, Gautier A, Schertler G, Grzesiek S
    Efficient production of a functional G protein-coupled receptor in E. coli for structural studies
    Journal of Biomolecular NMR. 2021; 75(1): 25-38. https://doi.org/10.1007/s10858-020-00354-6
    DORA PSI


2020

  • Tsai C-J, Schertler GFX
    Membrane protein crystallization
    In: Renaud J-P, ed. Structural biology in drug discovery. Methods, techniques, and practices. Hoboken: John Wiley & Sons, Inc.; 2020:187-210. https://doi.org/10.1002/9781118681121.ch9
    DORA PSI
  • Romantini N, Alam S, Dobitz S, Spillmann M, De Foresta M, Schibli R, et al.
    Exploring the signaling space of a GPCR using bivalent ligands with a rigid oligoproline backbone
    Proceedings of the National Academy of Sciences of the United States of America PNAS. 2021; 118(48): e2108776118 (8 pp.). https://doi.org/10.1073/pnas.2108776118
    DORA PSI
  • Bertalan É, Lesca E, Schertler GFX, Bondar A-N
    C-Graphs tool with graphical user interface to dissect conserved hydrogen-bond networks: applications to visual rhodopsins
    Journal of Chemical Information and Modeling. 2021; 61(11): 5692-5707. https://doi.org/10.1021/acs.jcim.1c00827
    DORA PSI
  • Wu N, Olechwier AM, Brunner C, Edwards PC, Tsai C-J, Tate CG, et al.
    High-mass MALDI-MS unravels ligand-mediated G protein-coupling selectivity to GPCRs
    Proceedings of the National Academy of Sciences of the United States of America PNAS. 2021; 118(31): e2024146118 (9 pp.). https://doi.org/10.1073/pnas.2024146118
    DORA PSI
  • Panneels V, Diaz A, Imsand C, Guizar-Sicairos M, Müller E, Bittermann AG, et al.
    Imaging of retina cellular and subcellular structures using ptychographic hard X-ray tomography
    Journal of Cell Science. 2021; 134(19): jcs258561 (8 pp.). https://doi.org/10.1242/jcs.258561
    DORA PSI
  • Isaikina P, Tsai C-J, Dietz N, Pamula F, Grahl A, Goldie KN, et al.
    Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist
    Science Advances. 2021; 7(25): eabg8685 (11 pp.). https://doi.org/10.1126/sciadv.abg8685
    DORA PSI
  • Marino J, Schertler GFX
    A set of common movements within GPCR-G-protein complexes from variability analysis of cryo-EM datasets
    Journal of Structural Biology. 2021; 213(2): 107699 (7 pp.). https://doi.org/10.1016/j.jsb.2021.107699
    DORA PSI
  • Abiko LA, Rogowski M, Gautier A, Schertler G, Grzesiek S
    Efficient production of a functional G protein-coupled receptor in E. coli for structural studies
    Journal of Biomolecular NMR. 2021; 75(1): 25-38. https://doi.org/10.1007/s10858-020-00354-6
    DORA PSI
  • Rößler P, Mayer D, Tsai C-J, Veprintsev DB, Schertler GFX, Gossert AD
    GPCR activation states induced by nanobodies and mini-G proteins compared by NMR spectroscopy
    Molecules. 2020; 25(24): 5984 (17 pp.). https://doi.org/10.3390/molecules25245984
    DORA PSI
  • Henzi A, Senatore A, Lakkaraju AKK, Scheckel C, Mühle J, Reimann R, et al.
    Soluble dimeric prion protein ligand activates Adgrg6 receptor but does not rescue early signs of demyelination in PrP-deficient mice
    PLoS One. 2020; 15(11): e0242137 (22 pp.). https://doi.org/10.1371/journal.pone.0242137
    DORA PSI
  • Nass K, Cheng R, Vera L, Mozzanica A, Redford S, Ozerov D, et al.
    Advances in long-wavelength native phasing at X-ray free-electron lasers
    IUCrJ. 2020; 7: 965-975. https://doi.org/10.1107/S2052252520011379
    DORA PSI
  • Avsar SY, Kapinos LE, Schoenenberger C-A, Schertler GFX, Mühle J, Meger B, et al.
    Immobilization of arrestin-3 on different biosensor platforms for evaluating GPCR binding
    Physical Chemistry Chemical Physics. 2020; 22(41): 24086-24096. https://doi.org/10.1039/d0cp01464h
    DORA PSI
  • Karathanou K, Lazaratos M, Bertalan É, Siemers M, Buzar K, Schertler GFX, et al.
    A graph-based approach identifies dynamic H-bond communication networks in spike protein S of SARS-CoV-2
    Journal of Structural Biology. 2020; 212(2): 107617 (19 pp.). https://doi.org/10.1016/j.jsb.2020.107617
    DORA PSI
  • Spillmann M, Thurner L, Romantini N, Zimmermann M, Meger B, Behe M, et al.
    New insights into arrestin recruitment to GPCRs
    International Journal of Molecular Sciences. 2020; 21(14): 4949 (14 pp.). https://doi.org/10.3390/ijms21144949
    DORA PSI
  • Skopintsev P, Ehrenberg D, Weinert T, James D, Kar RK, Johnson PJM, et al.
    Femtosecond-to-millisecond structural changes in a light-driven sodium pump
    Nature. 2020; 583: 314-318. https://doi.org/10.1038/s41586-020-2307-8
    DORA PSI

 

2019

  • Tsai C-J, Marino J, Adaixo R, Pamula F, Muehle J, Maeda S, et al.
    Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit
    eLife. 2019; 8: e46041 (19 pp.). https://doi.org/10.7554/eLife.46041
    DORA PSI
  • Varma N, Mutt E, Mühle J, Panneels V, Terakita A, Deupi X, et al.
    Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR
    Proceedings of the National Academy of Sciences of the United States of America PNAS. 2019; 116(29): 14547-14556. https://doi.org/10.1073/pnas.1902192116
    DORA PSI
  • Nagata T, Koyanagi M, Tsukamoto H, Mutt E, Schertler GFX, Deupi X, et al.
    The counterion–retinylidene Schiff base interaction of an invertebrate rhodopsin rearranges upon light activation
    Communications Biology. 2019; 2: 180 (9 pp.). https://doi.org/10.1038/s42003-019-0409-3
    DORA PSI
  • Ehrenberg D, Varma N, Deupi X, Koyanagi M, Terakita A, Schertler GFX, et al.
    The two-photon reversible reaction of the bistable jumping spider rhodopsin-1
    Biophysical Journal. 2019; 116(7): 1248-1258. https://doi.org/10.1016/j.bpj.2019.02.025
    DORA PSI
  • Mayer D, Damberger FF, Samarasimhareddy M, Feldmueller M, Vuckovic Z, Flock T, et al.
    Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation
    Nature Communications. 2019; 10: 1261 (14 pp.). https://doi.org/10.1038/s41467-019-09204-y
    DORA PSI
  • Haider RS, Wilhelm F, Rizk A, Mutt E, Deupi X, Peterhans C, et al.
    Arrestin-1 engineering facilitates complex stabilization with native rhodopsin
    Scientific Reports. 2019; 9(1): 439 (13 pp.). https://doi.org/10.1038/s41598-018-36881-4
    DORA PSI


2018

  • Convergent evolution of tertiary structure in rhodopsin visual proteins from vertebrates and box jellyfish Gerrard E, Mutt E, Nagata T, Koyanagi M, Flock T, Lesca E, Schertler Gebhard FX, Terakita A, Deupi X, Lucas Robert J
    Proceedings of the National Academy of Sciences 115, 6201 (2018).
    DOI: 10.1073/pnas.1721333115
  • Crystal structure of rhodopsin in complex with a mini-G o sheds light on the principles of G protein selectivity Tsai C, Pamula F, Nehmé R, Mühle J, Weinert T, Flock T, Nogly P, Edwards Patricia C, Carpenter B, Gruhl T, Ma P, Deupi X, Standfuss J, Tate Christopher G, Schertler Gebhard FX
    Science Advances 4, eaat7052 (2018).
    DOI: 10.1126/sciadv.aat7052
  • Development of an antibody fragment that stabilizes GPCR/G-protein complexes Maeda S, Koehl A, Matile H, Hu H, Hilger D, Schertler Gebhard FX, Manglik A, Skiniotis G, Dawson Roger JP, Kobilka Brian K
    NATURE COMMUNICATIONS 9, 3712 (2018).
    DOI: 10.1038/s41467-018-06002-w
  • Ligand channel in pharmacologically stabilized rhodopsin. Mattle D, Kuhn B, Aebi J, Bedoucha M, Kekilli D, Grozinger N, Alker A, Rudolph MG, Schmid G, Schertler GFX, Hennig M, Standfuss J, Dawson RJP
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 115, 3640 (2018).
  • Light induced charge and energy transport in nucleic acids and proteins: general discussion Chattopadhyay A, Cogdell R, Crespo-Hernández Carlos E, Datta A, De A, Haacke S, Hariharan M, Helliwell J, Hughes A, Improta R, Jones M, Joseph J, Karsili T, Kohler B, Krishnan R, Kuriakose A, L M, Markovitsi D, Medhi H, Periyasamy G, Pradeepkumar PI, Roy Chowdhury P, Sarangi M, Schapiro I, Schertler Gebhard FX, Schlichting I, Segarra-Martí J, Swaminathan R, V V, van Grondelle R, Venkatraman R, Venkatramani R, Watts A
    FARADAY DISCUSSIONS 207, 153 (2018).
    DOI: 10.1039/c8fd90004c
  • Photocrosslinking between nucleic acids and proteins: general discussion Bhat V, Cogdell R, Crespo-Hernández Carlos E, Datta A, De A, Haacke S, Helliwell J, Improta R, Joseph J, Karsili T, Kohler B, Krishnan R, L M, Lewis F, Mandal I, Markovitsi D, Mishra Padmaja P, Paul S, Periyasamy G, Pradeepkumar PI, Roy Chowdhury P, Sarangi M, Sasikumar D, Schapiro I, Schertler Gebhard FX, Schlichting I, Segarra-Martí J, Swaminathan R, V V, van Grondelle R, Varghese R, Venkatramani R
    FARADAY DISCUSSIONS 207, 283 (2018).
    DOI: 10.1039/c8fd90005a
  • Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser Nogly P, Weinert T, James D, Carbajo S, Ozerov D, Furrer A, Gashi D, Borin V, Skopintsev P, Jaeger K, Nass K, Båth P, Bosman R, Koglin J, Seaberg M, Lane T, Kekilli D, Brünle S, Tanaka T, Wu W, Milne C, White T, Barty A, Weierstall U, Panneels V, Nango E, Iwata S, Hunter M, Schapiro I, Schertler G, Neutze R, Standfuss J
    SCIENCE 361, 145 (2018).
    DOI: 10.1126/science.aat0094
  • Structure of the µ-opioid receptor?Gi protein complex Koehl A, Hu H, Maeda S, Zhang Y, Qu Q, Paggi Joseph M, Latorraca Naomi R, Hilger D, Dawson R, Matile H, Schertler Gebhard FX, Granier S, Weis William I, Dror Ron O, Manglik A, Skiniotis G, Kobilka Brian K
    NATURE -, - (2018).
    DOI: 10.1038/s41586-018-0219-7
  • The role of water molecules in phototransduction of retinal proteins and G protein-coupled receptors Lesca E, Panneels V, Schertler Gebhard FX
    FARADAY DISCUSSIONS 207, 27 (2018).
    DOI: 10.1039/c7fd00207f


2017

  • Comprehensive Analysis of the Role of Arrestin Residues in Receptor Binding Haider Raphael S, Rizk A, Schertler G, Ostermaier M
    Springer International Publishing -, 83 (2017).
    DOI: 10.1007/978-3-319-57553-7_7
  • Perspective: Opportunities for ultrafast science at SwissFEL Abela Rafael, Beaud Paul, van Bokhoven Jeroen A, Chergui Majed, Feurer Thomas, Haase Johannes, Ingold Gerhard, Johnson Steven L, Knopp Gregor, Lemke Henrik, Milne Chris J, Pedrini Bill, Radi Peter, Schertler Gebhard, Standfuss Jorg, Staub Urs, Patthey Luc
    STRUCTURAL DYNAMICS 4, 061602 (2017).
    DOI: 10.1063/1.4997222
  • Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons Weinert T, Olieric N, Cheng R, Brünle S, James D, Ozerov D, Gashi D, Vera L, Marsh M, Jaeger K, Dworkowski F, Panepucci E, Basu S, Skopintsev P, Doré Andrew S, Geng T, Cooke Robert M, Liang M, Prota Andrea E, Panneels V, Nogly P, Ermler U, Schertler G, Hennig M, Steinmetz Michel O, Wang M, Standfuss J
    NATURE COMMUNICATIONS 8, 542 (2017).
    DOI: 10.1038/s41467-017-00630-4


2016

  • A three-dimensional movie of structural changes in bacteriorhodopsin Nango Eriko, Royant Antoine, Kubo Minoru, Nakane Takanori, Wickstrand Cecilia, Kimura Tetsunari, Tanaka Tomoyuki, Tono Kensuke, Song Changyong, Tanaka Rie, Arima Toshi, Yamashita Ayumi, Kobayashi Jun, Hosaka Toshiaki, Mizohata Eiichi, Nogly Przemyslaw, Sugahara Michihiro, Nam Daewoong, Nomura Takashi, Shimamura Tatsuro, Im Dohyun, Fujiwara Takaaki, Yamanaka Yasuaki, Jeon Byeonghyun, Nishizawa Tomohiro, Oda Kazumasa, Fukuda Masahiro, Andersson Rebecka, Bath Petra, Dods Robert, Davidsson Jan, Matsuoka Shigeru, Kawatake Satoshi, Murata Michio, Nureki Osamu, Owada Shigeki, Kameshima Takashi, Hatsui Takaki, Joti Yasumasa, Schertler Gebhard, Yabashi Makina, Bondar AnaNicoleta, Standfuss Jorg, Neutze Richard, Iwata So
    SCIENCE 354, 1552-1557 (2016).
    DOI: 10.1126/science.aah3497
  • Addendum to Three-dimensional mass density mapping of cellular ultrastructure by ptychographic X-ray nanotomography [J. Struct. Biol. 192 (2015) 461-469] Diaz A, Malkova B, Holler M, Guizar-Sicairos M, Lima E, Panneels V, Pigino G, Bittermann A, Wettstein L, Tomizaki T, Bunk O, Schertler G, Ishikawa T, Wepf R, Menzel A
    JOURNAL OF STRUCTURAL BIOLOGY 193, 83 (2016).
    DOI: 10.1016/j.jsb.2015.12.003
  • Backbone NMR reveals allosteric signal transduction networks in the beta1-adrenergic receptor Isogai S, Deupi X, Opitz C, Heydenreich Franziska M, Tsai C, Brueckner F, Schertler Gebhard FX, Veprintsev Dmitry B, Grzesiek S
    NATURE 530, 237 (2016).
    DOI: 10.1038/nature16577
  • Conformational Selection in a Protein-Protein Interaction Revealed by Dynamic Pathway Analysis Chakrabarti Kalyan S, Agafonov Roman V, Pontiggia F, Otten R, Higgins Matthew K, Schertler Gebhard FX, Oprian Daniel D, Kern D
    CELL REPORTS 14, 32 (2016).
    DOI: 10.1016/j.celrep.2015.12.010
  • Diverse activation pathways in class A GPCRs converge near the G-protein-coupling region Venkatakrishnan AJ, Deupi X, Lebon G, Heydenreich Franziska M, Flock T, Miljus T, Balaji S, Bouvier M, Veprintsev Dmitry B, Tate Christopher G, Schertler G FX, Babu MMadan
    NATURE 536, 484 (2016).
    DOI: 10.1038/nature19107
  • Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography Nogly P, Panneels V, Nelson G, Gati C, Kimura T, Milne C, Milathianaki D, Kubo M, Wu W, Conrad C, Coe J, Bean R, Zhao Y, Båth P, Dods R, Harimoorthy R, Beyerlein Kenneth R, Rheinberger J, James D, DePonte D, Li C, Sala L, Williams Garth J, Hunter Mark S, Koglin Jason E, Berntsen P, Nango E, Iwata S, Chapman Henry N, Fromme P, Frank M, Abela R, Boutet S, Barty A, White Thomas A, Weierstall U, Spence J, Neutze R, Schertler G, Standfuss J
    NATURE COMMUNICATIONS 7, 12314 (2016).
    DOI: 10.1038/ncomms12314
  • Structural role of the T94I rhodopsin mutation in congenital stationary night blindness Singhal Ankita, Guo Ying, Matkovic Milos, Schertler Gebhard, Deupi Xavier, Yan Elsa C Y, Standfuss Joerg
    EMBO REPORTS 17, 1431-1440 (2016).
    DOI: 10.15252/embr.201642671
  • Three-dimensional mass density mapping of cellular ultrastructure by ptychographic X-ray nanotomography (vol 192, pg 461, 2015) Diaz Ana, Malkova Barbora, Holler Mirko, Guizar-Sicairos Manuel, Lima Enju, Panneels Valerie, Pigino Gaia, Bittermann Anne Greet, Wettstein Larissa, Tomizaki Takashi, Bunk Oliver, Schertler Gebhard, Ishikawa Takashi, Wepf Roger, Menzel Andreas
    JOURNAL OF STRUCTURAL BIOLOGY 193, 83-83 (2016).
    DOI: 10.1016/j.jsb.2015.12.003


2015

  • Batch crystallization of rhodopsin for structural dynamics using an X-ray free-electron laser Wu W, Nogly P, Rheinberger J, M Kick L, Gati C, Nelson G, Deupi X, Standfuss J, Schertler G, Panneels V
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS 71, 856 (2015).
    DOI: 10.1107/S2053230X15009966
  • Conformational activation of visual rhodopsin in native disc membranes Malmerberg E, Bovee-Geurts PHM, Katona G, Deupi X, Arnlund D, Wickstrand C, Johansson LC, Westenhoff S, Nazarenko E, Schertler GFX, Menzel A, de Grip WJ, Neutze R
    Science Signaling 8, ra26 (2015).
    DOI: 10.1126/scisignal.2005646
  • GPCR structure, function, drug discovery and crystallography: report from Academia-Industry International Conference (UK Royal Society) Chicheley Hall, 1?2 September 2014 Heifetz A, Schertler Gebhard FX, Seifert R, Tate Christopher G, Sexton Patrick M, Gurevich Vsevolod V, Fourmy D, Cherezov V, Marshall Fiona H, Storer RIan, Moraes I, Tikhonova Irina G, Tautermann Christofer S, Hunt P, Ceska T, Hodgson S, Bodkin Mike J, Singh S, Law Richard J, Biggin Philip C
    Naunyn-Schmiedeberg's Archives of Pharmacology 388, 883 (2015).
    DOI: 10.1007/s00210-015-1111-8
  • Large scale expression and purification of the rat 5-HT2c receptor He X, Robertson N, Jazayeri A, Gasperina A, Schertler G, Li X
    PROTEIN EXPRESSION AND PURIFICATION 106, 1 (2015).
    DOI: 10.1016/j.pep.2014.10.010
  • Lipidic cubic phase serial millisecond crystallography using synchrotron radiation Nogly Przemyslaw, James Daniel, Wang Dingjie, White Thomas A, Zatsepin Nadia, Shilova Anastasya, Nelson Garrett, Liu Haiguang, Johansson Linda, Heymann Michael, Jaeger Kathrin, Metz Markus, Wickstrand Cecilia, Wu Wenting, Bath Petra, Berntsen Peter, Oberthuer Dominik, Panneels Valerie, Cherezov Vadim, Chapman Henry, Schertler Gebhard, Neutze Richard, Spence John, Moraes Isabel, Burghammer Manfred, Standfuss Joerg, Weierstall Uwe
    IUCRJ 2, 168-176 (2015).
    DOI: 10.1107/S2052252514026487
  • Membrane protein structural biology using X-ray free electron lasers Neutze R, Brändén G, Schertler G
    CURRENT OPINION IN STRUCTURAL BIOLOGY 33, 115 (2015).
    DOI: 10.1016/j.sbi.2015.08.006
  • Probing Galpha_i1 protein activation at single?amino acid resolution Sun D, Flock T, Deupi X, Maeda S, Matkovic M, Mendieta S, Mayer D, Dawson R, Schertler G, Babu M, Veprintsev D
    NATURE STRUCTURAL & MOLECULAR BIOLOGY 22, 686 (2015).
    DOI: 10.1038/nsmb.3070
  • Rhodopsin on Tracks: New Ways to Go in Signaling Schertler Gebhard FX
    STRUCTURE 23, 606 (2015).
    DOI: 10.1016/j.str.2015.03.008
  • Three-dimensional mass density mapping of cellular ultrastructure by ptychographic X-ray nanotomography Diaz A, Malkova B, Holler M, Guizar-Sicairos M, Lima E, Panneels V, Pigino G, Bittermann A, Wettstein L, Tomizaki T, Bunk O, Schertler G, Ishikawa T, Wepf R, Menzel A
    JOURNAL OF STRUCTURAL BIOLOGY 192, 461 (2015).
    DOI: 10.1016/j.jsb.2015.10.008
  • Time-resolved structural studies with serial crystallography: A new light on retinal proteins Panneels Valerie, Wu Wenting, Tsai ChingJu, Nogly Przemek, Rheinberger Jan, Jaeger Kathrin, Cicchetti Gregor, Gati Cornelius, Kick Leonhard M, Sala Leonardo, Capitani Guido, Milne Chris, Padeste Celestino, Pedrini Bill, Li XiaoDan, Standfuss Joerg, Abela Rafael, Schertler Gebhard
    STRUCTURAL DYNAMICS 2, 041718 (2015).
    DOI: 10.1063/1.4922774


2014

  • 7 angstrom resolution in protein two-dimensional-crystal X-ray diffraction at Linac Coherent Light Source Pedrini Bill, Tsai Ching-Ju, Capitani Guido, Padeste Celestino, Hunter Mark S, Zatsepin Nadia A, Barty Anton, Benner W Henry, Boutet Sebastien, Feld Geoffrey K, Hau-Riege Stefan P, Kirian Richard A, Kupitz Christopher, Messerschmitt Marc, Ogren John I, Pardini Tommaso, Segelke Brent, Williams Garth J, Spence John C H, Abela Rafael, Coleman Matthew, Evans James E, Schertler Gebhard F X, Frank Matthias, Li Xiao-Dan
    PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES 369, UNSP 20130500 (2014).
    DOI: 10.1098/rstb.2013.0500
  • Crystallization Scale Preparation of a Stable GPCR Signaling Complex between Constitutively Active Rhodopsin and G-Protein Garriga P, Maeda S, Sun D, Singhal A, Foggetta M, Schmid G, Standfuss J, Hennig M, Dawson Roger JP, Veprintsev Dmitry B, Schertler Gebhard FX
    PLOS ONE 9, e98714 (2014).
    DOI: 10.1371/journal.pone.0098714
  • Femtosecond X-ray diffraction from two-dimensional protein crystals Frank Matthias, Carlson David B, Hunter Mark S, Williams Garth J, Messerschmidt Marc, Zatsepin Nadia A, Barty Anton, Benner W Henry, Chu Kaiqin, Graf Alexander T, Hau-Riege Stefan P, Kirian Richard A, Padeste Celestino, Pardini Tommaso, Pedrini Bill, Segelke Brent, Seibert M Marvin, Spence John C H, Tsai ChingJu, Lane Stephen M, Li XiaoDan, Schertler Gebhard, Boutet Sebastien, Coleman Matthew, Evans James E
    IUCRJ 1, 95-100 (2014).
    DOI: 10.1107/S2052252514001444
  • Molecular mechanism of phosphorylation-dependent arrestin activation Ostermaier M, Schertler G, Standfuss J
    CURRENT OPINION IN STRUCTURAL BIOLOGY 29, 143 (2014).
    DOI: 10.1016/j.sbi.2014.07.006
  • Retinal proteins - You can teach an old dog new tricks Foreword Heberle Joachim, Deupi Xavier, Schertler Gebhard
    BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1837, 531-532 (2014).
    DOI: 10.1016/j.bbabio.2014.02.019
  • Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A Benoit Roger M, Frey Daniel, Hilbert Manuel, Kevenaar Josta T, Wieser Mara M, Stirnimann Christian U, McMillan David, Ceska Tom, Lebon Florence, Jaussi Rolf, Steinmetz Michel O, Schertler Gebhard F X, Hoogenraad Casper C, Capitani Guido, Kammerer Richard A
    NATURE 505, 108-+ (2014).
    DOI: 10.1038/nature12732
  • The 2.1 Å Resolution Structure of Cyanopindolol-Bound ?1-Adrenoceptor Identifies an Intramembrane Na+ Ion that Stabilises the Ligand-Free Receptor van Veen Hendrik W, Miller-Gallacher Jennifer L, Nehmé R, Warne T, Edwards Patricia C, Schertler Gebhard FX, Leslie Andrew GW, Tate Christopher G
    PLOS ONE 9, e92727 (2014).
    DOI: 10.1371/journal.pone.0092727


2013

  • Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding Vishnivetskiy SergeyA, Ostermaier Martin K, Singhal A, Panneels V, Homan Kristoff T, Glukhova A, Sligar Stephen G, Tesmer John JG, Schertler Gebhard FX, Standfuss J, Gurevich Vsevolod V
    CELLULAR SIGNALLING 25, 2155 (2013).
    DOI: 10.1016/j.cellsig.2013.07.009
  • Insights into congenital stationary night blindness based on the structure of G90D rhodopsin Singhal Ankita, Ostermaier Martin K, Vishnivetskiy Sergey A, Panneels Valerie, Homan Kristoff T, Tesmer John J G, Veprintsev Dmitry, Deupi Xavier, Gurevich Vsevolod V, Schertler Gebhard F X, Standfuss Joerg
    EMBO REPORTS 14, 520-526 (2013).
    DOI: 10.1038/embor.2013.44
  • Molecular signatures of G-protein-coupled receptors Venkatakrishnan A J, Deupi Xavier, Lebon Guillaume, Tate Christopher G, Schertler Gebhard F, Babu M Madan
    NATURE 494, 185-194 (2013).
    DOI: 10.1038/nature11896
  • Production of GPCR and GPCR complexes for structure determination Maeda S, Schertler G
    CURRENT OPINION IN STRUCTURAL BIOLOGY 23, 381 (2013).
    DOI: 10.1016/j.sbi.2013.04.006
  • Structure of beta-Adrenergic Receptors Brueckner Florian, Piscitelli Chayne L, Tsai Ching-Ju, Standfuss Joerg, Deupi Xavier, Schertler Gebhard F X
    G PROTEIN COUPLED RECEPTORS: STRUCTURE 520, 117-151 (2013).
    DOI: 10.1016/B978-0-12-391861-1.00006-X
  • Two Alternative Conformations of a Voltage-Gated Sodium Channel Tsai C, Tani K, Irie K, Hiroaki Y, Shimomura T, McMillan Duncan G, Cook Gregory M, Schertler Gebhard FX, Fujiyoshi Y, Li X
    JOURNAL OF MOLECULAR BIOLOGY 425, 4074 (2013).
    DOI: 10.1016/j.jmb.2013.06.036


2012

  • Conserved activation pathways in G-protein-coupled receptors Deupi X, Standfuss J, Schertler G
    BIOCHEMICAL SOCIETY TRANSACTIONS 40, 383-388 (2012).
    DOI: 10.1042/BST20120001
  • Ligands Stabilize Specific GPCR Conformations: But How? Deupi X, Li XD, Schertler GFX
    STRUCTURE 20, 1289-1290 (2012).
    DOI: 10.1016/j.str.2012.07.009
  • Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II Deupi X, Edwards P, Singhal A, Nickle B, Oprian D, Schertler G, Standfuss J
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 109, 119 (2012).
    DOI: 10.1073/pnas.1114089108


2011

  • ?4D Biology for health and disease? workshop report Abrahams J, Apweiler R, Balling R, Bertero Michela G, Bujnicki Janusz M, Chayen Naomi E, Chène P, Corthals Gary L, Dyl?g T, Förster F, Heck Albert JR, Henderson Peter JF, Herwig R, Jehenson P, Kokalj S, Laue E, Legrain P, Martens L, Migliorini C, Musacchio A, Podobnik M, Schertler Gebhard FX, Schreiber G, Sixma Titia K, Smit August B, Stuart D, Svergun Dmitri I, Taussig Michael J
    New Biotechnology 28, 291 (2011).
    DOI: 10.1016/j.nbt.2010.10.003
  • Adaptation of pineal expressed teleost exo-rod opsin to non-image forming photoreception through enhanced Meta II decay Tarttelin Emma E, Fransen Maikel P, Edwards Patricia C, Hankins Mark W, Schertler Gebhard FX, Vogel R, Lucas Robert J, Bellingham J
    CELLULAR AND MOLECULAR LIFE SCIENCES 68, 3713 (2011).
    DOI: 10.1007/s00018-011-0665-y
  • Membranes Stroud R, Schertler G
    CURRENT OPINION IN STRUCTURAL BIOLOGY 21, 495 (2011).
    DOI: 10.1016/j.sbi.2011.08.001
  • Preparation of an Activated Rhodopsin/Transducin Complex Using a Constitutively Active Mutant of Rhodopsin Xie G, D?Antona Aaron M, Edwards Patricia C, Fransen M, Standfuss J, Schertler Gebhard FX, Oprian Daniel D
    BIOCHEMISTRY 50, 10399 (2011).
    DOI: 10.1021/bi201126r
  • The structural basis for agonist and partial agonist action on a beta(1)-adrenergic receptor Warne T, Moukhametzianov R, Baker JG, Nehme R, Edwards PC, Leslie AGW, Schertler GFX, Tate CG
    NATURE 469, 241 (2011).
    DOI: 10.1038/nature09746
  • The structural basis of agonist-induced activation in constitutively active rhodopsin Standfuss J, Edwards PC, D'Antona A, Fransen M, Xie GF, Oprian DD, Schertler GFX
    NATURE 471, 656 (2011).
    DOI: 10.1038/nature09795
  • Two distinct conformations of helix 6 observed in antagonist-bound structures of a beta(1)-adrenergic receptor Moukhametzianov R, Warne T, Edwards PC, Serrano-Vega MJ, Leslie AGW, Tate CG, Schertler GFX
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 108, 8228 (2011).
    DOI: 10.1073/pnas.1100185108


2010

  • Spial: analysis of subtype-specific features in multiple sequence alignments of proteins Wuster A, Venkatakrishnan AJ, Schertler GFX, Babu MM
    BIOINFORMATICS 26, 2906 (2010).
    DOI: 10.1093/bioinformatics/btq552
  • Tracking G-protein-coupled receptor activation using genetically encoded infrared probes Ye SX, Zaitseva E, Caltabiano G, Schertler GFX, Sakmar TP, Deupi X, Vogel R
    NATURE 464, 1386 (2010).
    DOI: 10.1038/nature08948


2009

  • Engineering G protein-coupled receptors to facilitate their structure determination Tate CG, Schertler GFX
    CURRENT OPINION IN STRUCTURAL BIOLOGY 19, 386 (2009).
    DOI: 10.1016/j.sbi.2009.07.004

Brueckner, Florian Dr.
Postdoc


Cernikova, Lenka
Scientific assistant

Flock, Tilman Dr.
Postdoc

Gautier, Antoine Dr.
Postdoc

Haider, Raphael
Scientific Assistant

Maeda, Shoji Dr.
Postdoc

Matkovic, Milos
Ph.D. Student

Ostermaier, Martin Dr.
Scientific Officer


Piscitelli, Chayne Dr.
Postdoc

Rheinberger, Jan
Ph.D. Student

Wu, Wenting
Ph.D. Student