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1. Microsecond time-resolved X-ray scattering by utilizing MHz repetition rate at second-generation XFELs

Author

Konold, Patrick E., Monrroy, Leonardo, Bellisario, Alfredo, Filipe, Diogo, Adams, Patrick, Alvarez, Roberto, Bean, Richard, Bielecki, Johan, Bódizs, Szabolcs, Ducrocq, Gabriel, Grubmueller, Helmut, Kirian, Richard A., Kloos, Marco, Koliyadu, Jayanath C. P., Koua, Faisal H. M., Larkiala, Taru, Letrun, Romain, Lindsten, Fredrik, Maihöfer, Michael, Martin, Andrew V., Mészáros, Petra, Mutisya, Jennifer, Nimmrich, Amke, Okamoto, Kenta, Round, Adam, Sato, Tokushi, Valerio, Joana, Westphal, Daniel, Wollter, August, Yenupuri, Tej Varma, You, Tong, Maia, Filipe, and Westenhoff, Sebastian

Published
2024
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2. Neutralizing RGMa with Elezanumab Promotes Cerebroprotection and Recovery in Rabbit Middle Cerebral Artery Occlusion

Author

Jacobson, Peer B., Mothe, Andrea, Levy, Aharon, Krakovsky, Michael, Hooker, Bradley A., Zhang, Xiaomeng, Mollon, Jennifer, Mordashova, Yulia, Droescher, Mathias, Weiss, Sabine, Barghorn, Stefan, Dreher, Ingeborg, Awwad, Khader, Nimmrich, Volker, Huang, Lili, Fung, Emma, Buck, Wayne R., Pfleeger, Kimberly, Ziemann, Adam, Smith, Elaine, Fox, Gerard B., Tator, Charles H., and Gold, Michael

Published
2024
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3. 3D-Printed Sheet Jet for Stable Megahertz Liquid Sample Delivery at X-ray Free Electron Lasers

Author

Konold, Patrick E., You, Tong, Bielecki, Johan, Valerio, Joana, Kloos, Marco, Westphal, Daniel, Bellisario, Alfredo, Varma, Tej, Wolter, August, Koliyadu, Jayanath C. P., Koua, Faisal H. M., Letrun, Romain, Round, Adam, Sato, Tokushi, Mésźaros, Petra, Monrroy, Leonardo, Mutisya, Jennifer, Bódizs, Szabolcs, Larkiala, Taru, Nimmrich, Amke, Alvarez, Roberto, Bean, Richard, Ekeberg, Tomas, Kirian, Richard A., Westenhoff, Sebastian, and Maia, Filipe R. N. C.

Subjects
Physics - Instrumentation and Detectors, Physics - Applied Physics, Physics - Biological Physics
Abstract

X-ray Free Electron Lasers (XFELs) can probe chemical and biological reactions as they unfold with unprecedented spatial and temporal resolution. A principal challenge in this pursuit is the delivery of samples to the X-ray interaction point in a way that produces data of the highest possible quality and efficiency. This is hampered by constraints posed by the light source and operation within a beamline environment. For liquid samples, the solution typically involves a high-speed liquid jet, capable of keeping up with the rate of X-ray pulses. However, conventional jets are not ideal because of radiation-induced explosions of the jet, as well as their cylindrical geometry combined with the X-ray pointing instability of many beamlines causes the interaction volume to differ for every pulse. This complicates data analysis and contributes to measurement errors. An alternative geometry is a liquid sheet jet which, with its constant thickness over large areas, eliminates the X-ray pointing related problems. Since liquid sheets can be made very thin, the radiation-induced explosion is reduced, boosting their stability. They are especially attractive for experiments which benefit from small interaction volumes such as fluctuation X-ray scattering and several types of spectroscopy. Although they have seen increasing use for soft X-ray applications in recent years, there has not yet been wide-scale adoption at XFELs. Here, we demonstrate liquid sheet jet sample injection at the European XFEL. We evaluate several aspects of its performance relative to a conventional liquid jet including thickness profile, stability, and radiation-induced explosion dynamics at high repetition rates. The sheet jet exhibits superior performance across these critical experimental parameters. Its minute thickness also suggests ultrafast single-particle solution scattering is a possibility.

Published
2023
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4. Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography

Author

Cellini, Andrea, Shankar, Madan Kumar, Nimmrich, Amke, Hunt, Leigh Anna, Monrroy, Leonardo, Mutisya, Jennifer, Furrer, Antonia, Beale, Emma V., Carrillo, Melissa, Malla, Tek Narsingh, Maj, Piotr, Vrhovac, Lidija, Dworkowski, Florian, Cirelli, Claudio, Johnson, Philip J. M., Ozerov, Dmitry, Stojković, Emina A., Hammarström, Leif, Bacellar, Camila, Standfuss, Jörg, Maj, Michał, Schmidt, Marius, Weinert, Tobias, Ihalainen, Janne A., Wahlgren, Weixiao Yuan, and Westenhoff, Sebastian

Published
2024
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5. 3D-printed sheet jet for stable megahertz liquid sample delivery at X-ray free-electron lasers

Author

Patrick E. Konold, Tong You, Johan Bielecki, Joana Valerio, Marco Kloos, Daniel Westphal, Alfredo Bellisario, Tej Varma Yenupuri, August Wollter, Jayanath C. P. Koliyadu, Faisal H.M. Koua, Romain Letrun, Adam Round, Tokushi Sato, Petra Mészáros, Leonardo Monrroy, Jennifer Mutisya, Szabolcs Bódizs, Taru Larkiala, Amke Nimmrich, Roberto Alvarez, Patrick Adams, Richard Bean, Tomas Ekeberg, Richard A. Kirian, Andrew V. Martin, Sebastian Westenhoff, and Filipe R. N. C. Maia

Subjects
free-electron lasers, injectors, single particles, fast sax, time-resolved studies, fast wax, sample delivery, xfels, Crystallography, QD901-999
Abstract

X-ray free-electron lasers (XFELs) can probe chemical and biological reactions as they unfold with unprecedented spatial and temporal resolution. A principal challenge in this pursuit involves the delivery of samples to the X-ray interaction point in such a way that produces data of the highest possible quality and with maximal efficiency. This is hampered by intrinsic constraints posed by the light source and operation within a beamline environment. For liquid samples, the solution typically involves some form of high-speed liquid jet, capable of keeping up with the rate of X-ray pulses. However, conventional jets are not ideal because of radiation-induced explosions of the jet, as well as their cylindrical geometry combined with the X-ray pointing instability of many beamlines which causes the interaction volume to differ for every pulse. This complicates data analysis and contributes to measurement errors. An alternative geometry is a liquid sheet jet which, with its constant thickness over large areas, eliminates the problems related to X-ray pointing. Since liquid sheets can be made very thin, the radiation-induced explosion is reduced, boosting their stability. These are especially attractive for experiments which benefit from small interaction volumes such as fluctuation X-ray scattering and several types of spectroscopy. Although their use has increased for soft X-ray applications in recent years, there has not yet been wide-scale adoption at XFELs. Here, gas-accelerated liquid sheet jet sample injection is demonstrated at the European XFEL SPB/SFX nano focus beamline. Its performance relative to a conventional liquid jet is evaluated and superior performance across several key factors has been found. This includes a thickness profile ranging from hundreds of nanometres to 60 nm, a fourfold increase in background stability and favorable radiation-induced explosion dynamics at high repetition rates up to 1.13 MHz. Its minute thickness also suggests that ultrafast single-particle solution scattering is a possibility.

Published
2023
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7. Eliminating finite-size effects on the calculation of x-ray scattering from molecular dynamics simulations.

Author

Dohn, A. O., Markmann, V., Nimmrich, A., Haldrup, K., Møller, K. B., and Nielsen, M. M.

Subjects
MOLECULAR dynamics, SOLVATION, RADIAL distribution function, TRANSITION metal complexes, STRUCTURAL reliability, CELL size, X-ray scattering, RENORMALIZATION (Physics)
Abstract

Structural studies using x-ray scattering methods for investigating molecules in solution are shifting focus toward describing the role and effects of the surrounding solvent. However, forward models based on molecular dynamics (MD) simulations to simulate structure factors and x-ray scattering from interatomic distributions such as radial distribution functions (RDFs) face limitations imposed by simulations, particularly at low values of the scattering vector q. In this work, we show how the value of the structure factor at q = 0 calculated from RDFs sampled from finite MD simulations is effectively dependent on the size of the simulation cell. To eliminate this error, we derive a new scheme to renormalize the sampled RDFs based on a model of the excluded volume of the particle-pairs they were sampled from, to emulate sampling from an infinite system. We compare this new correction method to two previous RDF-correction methods, developed for Kirkwood–Buff theory applications. We present a quantitative test to assess the reliability of the simulated low-q scattering signal and show that our RDF-correction successfully recovers the correct q = 0 limit for neat water. We investigate the effect of MD-sampling time on the RDF-corrections, before advancing to a molecular example system, comprised of a transition metal complex solvated in a series of water cells with varying densities. We show that our correction recovers the correct q = 0 behavior for all densities. Furthermore, we employ a simple continuum scattering model to dissect the total scattering signal from the solvent–solvent structural correlations in a solute–solvent model system to find two distinct contributions: a non-local density-contribution from the finite, fixed cell size in NVT simulations, and a local contribution from the solvent shell. We show how the second contribution can be approximated without also including the finite-size contribution. Finally, we provide a "best-practices"-checklist for experimentalists planning to incorporate explicit solvation MD simulations in future work, offering guidance for improving the accuracy and reliability of structural studies using x-ray scattering methods in solution. [ABSTRACT FROM AUTHOR]

Published
2023
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9. Microsecond time-resolved X-ray scattering by utilizing MHz repetition rate at second-generation XFELs

Author

Westenhoff, Sebastian, primary, Konold, Patrick, additional, Monrroy, Leonardo, additional, Bellisario, Alfredo, additional, Filipe, Diogo, additional, Adams, Patrick, additional, Alvarez, Roberto, additional, Bean, Richard, additional, Bielecki, Johan, additional, Bódizs, Szabolcs, additional, Ducroq, Gabriel, additional, Grubmueller, Helmut, additional, Kirian, Richard, additional, Kloos, Marco, additional, Koliyadu, Jayanat, additional, Koua, Faisal, additional, Larkiala, Taru, additional, Letrun, Romain, additional, Lindsten, Fredrik, additional, Maihöfer, Michael, additional, Martin, Andrew, additional, Mészáros, Petra, additional, Mutisya, Jennifer, additional, Nimmrich, Amke, additional, Okamoto, Kenta, additional, Round, Adam, additional, Sato, Tokushi, additional, Valerio, Joana, additional, Westphal, Daniel, additional, Wolter, August, additional, Yenupuri, Tej, additional, You, Tong, additional, and Maia, Filipe, additional

Published
2023
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10. Calpain

Author

Nimmrich, Volker, Bespalov, Anton, Möller, Achim, and Choi, Sangdun, editor

Published
2018
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11. 3D-printed sheet jet for stable megahertz liquid sample delivery at X-ray free-electron lasers

Author

Konold, Patrick E., primary, You, Tong, additional, Bielecki, Johan, additional, Valerio, Joana, additional, Kloos, Marco, additional, Westphal, Daniel, additional, Bellisario, Alfredo, additional, Varma Yenupuri, Tej, additional, Wollter, August, additional, Koliyadu, Jayanath C. P., additional, Koua, Faisal H.M., additional, Letrun, Romain, additional, Round, Adam, additional, Sato, Tokushi, additional, Mészáros, Petra, additional, Monrroy, Leonardo, additional, Mutisya, Jennifer, additional, Bódizs, Szabolcs, additional, Larkiala, Taru, additional, Nimmrich, Amke, additional, Alvarez, Roberto, additional, Adams, Patrick, additional, Bean, Richard, additional, Ekeberg, Tomas, additional, Kirian, Richard A., additional, Martin, Andrew V., additional, Westenhoff, Sebastian, additional, and Maia, Filipe R. N. C., additional

Published
2023
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12. The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

Author

Elin Claesson, Weixiao Yuan Wahlgren, Heikki Takala, Suraj Pandey, Leticia Castillon, Valentyna Kuznetsova, Léocadie Henry, Matthijs Panman, Melissa Carrillo, Joachim Kübel, Rahul Nanekar, Linnéa Isaksson, Amke Nimmrich, Andrea Cellini, Dmitry Morozov, Michał Maj, Moona Kurttila, Robert Bosman, Eriko Nango, Rie Tanaka, Tomoyuki Tanaka, Luo Fangjia, So Iwata, Shigeki Owada, Keith Moffat, Gerrit Groenhof, Emina A Stojković, Janne A Ihalainen, Marius Schmidt, and Sebastian Westenhoff

Subjects
phytochromes, SFX, Deinococcus radiodurans, initial photorespons, Medicine, Science, Biology (General), QH301-705.5
Abstract

Phytochrome proteins control the growth, reproduction, and photosynthesis of plants, fungi, and bacteria. Light is detected by a bilin cofactor, but it remains elusive how this leads to activation of the protein through structural changes. We present serial femtosecond X-ray crystallographic data of the chromophore-binding domains of a bacterial phytochrome at delay times of 1 ps and 10 ps after photoexcitation. The data reveal a twist of the D-ring, which leads to partial detachment of the chromophore from the protein. Unexpectedly, the conserved so-called pyrrole water is photodissociated from the chromophore, concomitant with movement of the A-ring and a key signaling aspartate. The changes are wired together by ultrafast backbone and water movements around the chromophore, channeling them into signal transduction towards the output domains. We suggest that the observed collective changes are important for the phytochrome photoresponse, explaining the earliest steps of how plants, fungi and bacteria sense red light.

Published
2020
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13. Primary conformational changes of the chromophore and the surroundings after photoexcitation of bacteriophytochrome

Author

Shankar, Madan Kumar, primary, Wahlgren, Weixiao Yuan, additional, Nimmrich, Amke, additional, Kurttila, Moona, additional, Cellini, Andrea, additional, Maj, Piotr, additional, Claesson, Elin, additional, Luo, Fangjia, additional, Tosha, Takehiko, additional, Ninawan, Nuemket, additional, Owada, Shigeki, additional, Tanaka, Rie, additional, Takala, Heikki, additional, Ihalainen, Janne A., additional, and Westenhoff, Sebastian, additional

Published
2023
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16. Solvent-Dependent Structural Dynamics in the Ultrafast Photodissociation Reaction of Triiodide Observed with Time-Resolved X-ray Solution Scattering

Author

Nimmrich, Amke, primary, Panman, Matthijs R., additional, Berntsson, Oskar, additional, Biasin, Elisa, additional, Niebling, Stephan, additional, Petersson, Jonas, additional, Hoernke, Maria, additional, Björling, Alexander, additional, Gustavsson, Emil, additional, van Driel, Tim B., additional, Dohn, Asmus O., additional, Laursen, Mads, additional, Zederkof, Diana B., additional, Tono, Kensuke, additional, Katayama, Tetsuo, additional, Owada, Shigeki, additional, Nielsen, Martin M., additional, Davidsson, Jan, additional, Uhlig, Jens, additional, Hub, Jochen S., additional, Haldrup, Kristoffer, additional, and Westenhoff, Sebastian, additional

Published
2023
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17. Supplementary Table S2 from Association of DNA Methylation of Phosphoserine Aminotransferase with Response to Endocrine Therapy in Patients with Recurrent Breast Cancer

Author

Martens, John W.M., primary, Nimmrich, Inko, primary, Koenig, Thomas, primary, Look, Maxime P., primary, Harbeck, Nadia, primary, Model, Fabian, primary, Kluth, Antje, primary, Bolt-de Vries, Joan, primary, Sieuwerts, Anieta M., primary, Portengen, Henk, primary, Meijer-Van Gelder, Marion E., primary, Piepenbrock, Christian, primary, Olek, Alexander, primary, Höfler, Heinz, primary, Kiechle, Marion, primary, Klijn, Jan G.M., primary, Schmitt, Manfred, primary, Maier, Sabine, primary, and Foekens, John A., primary

Published
2023
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18. Solvent-Dependent Structural Dynamics in the Ultrafast Photodissociation Reaction of Triiodide Observed with Time-Resolved X-ray Solution Scattering

Author

Nimmrich, Amke, Panman, Matthijs R., Berntsson, Oskar, Biasin, Elisa, Niebling, Stephan, Petersson, Jonas, Hoernke, Maria, Björling, Alexander, Gustavsson, Emil, van Driel, Tim B., Dohn, Asmus O., Laursen, Mads, Zederkof, Diana B., Tono, Kensuke, Katayama, Tetsuo, Owada, Shigeki, Nielsen, Martin M., Davidsson, Jan, Uhlig, Jens, Hub, Jochen S., Haldrup, Kristoffer, Westenhoff, Sebastian, Nimmrich, Amke, Panman, Matthijs R., Berntsson, Oskar, Biasin, Elisa, Niebling, Stephan, Petersson, Jonas, Hoernke, Maria, Björling, Alexander, Gustavsson, Emil, van Driel, Tim B., Dohn, Asmus O., Laursen, Mads, Zederkof, Diana B., Tono, Kensuke, Katayama, Tetsuo, Owada, Shigeki, Nielsen, Martin M., Davidsson, Jan, Uhlig, Jens, Hub, Jochen S., Haldrup, Kristoffer, and Westenhoff, Sebastian

Abstract

Resolving the structural dynamics of bond breaking, bond formation, and solvation is required for a deeper understanding of solutionphase chemical reactions. In this work, we investigate the photodissociation of triiodide in four solvents using femtosecond time-resolved X-ray solution scattering following 400 nm photoexcitation. Structural analysis of the scattering data resolves the solvent-dependent structural evolution during the bond cleavage, internal rearrangements, solvent-cage escape, and bond reformation in real time. The nature and structure of the reaction intermediates during the recombination are determined, elucidating the full mechanism of photodissociation and recombination on ultrafast time scales. We resolve the structure of the precursor state for recombination as a geminate pair. Further, we determine the size of the solvent cages from the refined structures of the radical pair. The observed structural dynamics present a comprehensive picture of the solvent influence on structure and dynamics of dissociation reactions.

Published
2023
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19. Finite-size Effects on the Calculation of X-ray Scattering from Molecular Dynamics Simulations

Author

Asmus Ougaard Dohn, Verena Isabell Markmann, Amke Nimmrich, Kristoffer Haldrup, Klaus Braagaard Møller, and Martin Meedom Nielsen

Abstract

Structural studies using x-ray scattering methods to investigate molecules in solution are shifting focus towards including the role and effects of the surrounding solvent. However, forward models based on molecular dynamics (MD) simulations to simulate structure factors and x-ray scattering from interatomic distributions such as radial distribution functions (RDFs) face limitations imposed by simulations, particularly at low values of the scattering vector q. In this work, we show how the value of the structure factor at q = 0 calculated from RDFs sampled from finite MD simulations is entirely dependent on the size of the simulation cell. We derive a new, simple method to correct the RDFs to eliminate this error, and compare it to two other RDF- correction methods developed for Kirkwood-Buff theory applications. We present a quantitative test to assess the reliability of the simulated low-q scattering signal, and show that our RDF- correction successfully recovers the correct q = 0 limit for neat water. We investigate the effect of MD-sampling time on the RDF-corrections, before advancing to a more realistic example system comprised of a solvated transition metal complex, sampled in a series of water cells with increasing density. We show that our correction recovers the correct q = 0 behaviour for increasing density. Furthermore, we employ a simple continuum scattering model to dissect the total scattering signal from the solvent-solvent structural correlations in a solute-solvent model system to find two distinct contributions: a non-local ’density’-contribution and a local contribution from the solvent shell. We show how the second contribution can be approximated without also including the density-contribution. Finally, we provide a ’best-practices’-checklist for experimentalists planning to incorporate explicit solvation MD simulations in future work, offering guidance for improving the accuracy and reliability of structural studies using x-ray scattering methods in solution.

Published
2023

20. Solvent-Dependent Structural Dynamics in the Ultrafast Photodissociation Reaction of Triiodide Observed with Time-Resolved X-ray Solution Scattering

Author

Amke Nimmrich, Matthijs R. Panman, Oskar Berntsson, Elisa Biasin, Stephan Niebling, Jonas Petersson, Maria Hoernke, Alexander Björling, Emil Gustavsson, Tim B. van Driel, Asmus O. Dohn, Mads Laursen, Diana B. Zederkof, Kensuke Tono, Tetsuo Katayama, Shigeki Owada, Martin M. Nielsen, Jan Davidsson, Jens Uhlig, Jochen S. Hub, Kristoffer Haldrup, and Sebastian Westenhoff

Subjects
Colloid and Surface Chemistry, General Chemistry, Biochemistry, Catalysis
Published
2023

21. Supplementary Table S1 from Association of DNA Methylation of Phosphoserine Aminotransferase with Response to Endocrine Therapy in Patients with Recurrent Breast Cancer

Author

John A. Foekens, Sabine Maier, Manfred Schmitt, Jan G.M. Klijn, Marion Kiechle, Heinz Höfler, Alexander Olek, Christian Piepenbrock, Marion E. Meijer-Van Gelder, Henk Portengen, Anieta M. Sieuwerts, Joan Bolt-de Vries, Antje Kluth, Fabian Model, Nadia Harbeck, Maxime P. Look, Thomas Koenig, Inko Nimmrich, and John W.M. Martens

Abstract

Supplementary Table S1 from Association of DNA Methylation of Phosphoserine Aminotransferase with Response to Endocrine Therapy in Patients with Recurrent Breast Cancer

Published
2023

22. Data from Association of DNA Methylation of Phosphoserine Aminotransferase with Response to Endocrine Therapy in Patients with Recurrent Breast Cancer

Author

John A. Foekens, Sabine Maier, Manfred Schmitt, Jan G.M. Klijn, Marion Kiechle, Heinz Höfler, Alexander Olek, Christian Piepenbrock, Marion E. Meijer-Van Gelder, Henk Portengen, Anieta M. Sieuwerts, Joan Bolt-de Vries, Antje Kluth, Fabian Model, Nadia Harbeck, Maxime P. Look, Thomas Koenig, Inko Nimmrich, and John W.M. Martens

Abstract

To understand the biological basis of resistance to endocrine therapy is of utmost importance in patients with steroid hormone receptor–positive breast cancer. Not only will this allow us prediction of therapy success, it may also lead to novel therapies for patients resistant to current endocrine therapy. DNA methylation in the promoter regions of genes is a prominent epigenetic gene silencing mechanism that contributes to breast cancer biology. In the current study, we investigated whether promoter DNA methylation could be associated with resistance to endocrine therapy in patients with recurrent breast cancer. Using a microarray-based technology, the promoter DNA methylation status of 117 candidate genes was studied in a cohort of 200 steroid hormone receptor–positive tumors of patients who received the antiestrogen tamoxifen as first-line treatment for recurrent breast cancer. Of the genes analyzed, the promoter DNA methylation status of 10 genes was significantly associated with clinical outcome of tamoxifen therapy. The association of the promoter hypermethylation of the strongest marker, phosphoserine aminotransferase (PSAT1) with favorable clinical outcome was confirmed by an independent quantitative DNA methylation detection method. Furthermore, the extent of DNA methylation of PSAT1 was inversely associated with its expression at the mRNA level. Finally, also at the mRNA level, PSAT1 was a predictor of tamoxifen therapy response. Concluding, our work indicates that promoter hypermethylation and mRNA expression of PSAT1 are indicators of response to tamoxifen-based endocrine therapy in steroid hormone receptor–positive patients with recurrent breast cancer.

Published
2023

23. Femtosecond conformational changes in a photolyase guide long-range electron transfer as resolved by serial crystallography

Author

Cellini, Andrea, primary, Shankar, Madan Kumar, additional, Nimmrich, Amke, additional, Mutisya, Jennifer, additional, Furrer, Antonia, additional, Beale, Emma, additional, Carrillo, Melissa, additional, Malla, Tek Narsingh, additional, Maj, Piotr, additional, Vrhovac, Lidija, additional, Dworkowskic, Florian, additional, Cirelli, Claudio, additional, Johnson, Philip, additional, Ozerov, Dmitry, additional, Bacellar, Camila, additional, Standfuss, Jörg, additional, Schmidt, Marius, additional, Weinert, Tobias, additional, Ihalainen, Janne, additional, Wahlgren, Weixiao, additional, and Westenhoff, Sebastian, additional

Published
2023
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24. The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature

Author

Eriko Nango, Weixiao Yuan Wahlgren, Marius Schmidt, Swagatha Ghosh, So Iwata, Amke Nimmrich, Andrea Cellini, Sebastian Westenhoff, Shigeki Owada, Joachim Kübel, Janne A. Ihalainen, Léocadie Henry, Elin Claesson, Suraj Pandey, Valentyna Kuznetsova, Leticia Castillon, Heikki Takala, Emina A. Stojković, Medicum, and Department of Anatomy

Subjects
MECHANISM, Materials science, Absorption spectroscopy, DNA repair, fotobiologia, 02 engineering and technology, Crystal structure, REPAIR ACTIVITY, 03 medical and health sciences, COLI DNA PHOTOLYASE, X-RAY-DIFFRACTION, Cryptochrome, Structural Biology, Animals, serial crystallography, CRYSTAL-STRUCTURE, CRYPTOCHROME, Photolyase, SERIAL FEMTOSECOND CRYSTALLOGRAPHY, 030304 developmental biology, 0303 health sciences, Crystallography, flavoproteins, FAD, Resolution (electron density), Temperature, banaanikärpänen, DNA, kidetiede, (6-4) photolyase, 021001 nanoscience & nanotechnology, Research Papers, RADICAL TRANSFER, (6–4) photolyase, room-temperature structure, photolyases, Drosophila melanogaster, RECONSTITUTION, X-ray crystallography, 1182 Biochemistry, cell and molecular biology, lämpötila, proteiinit, 0210 nano-technology, Deoxyribodipyrimidine Photo-Lyase, PHOTOACTIVATION, Visible spectrum
Abstract

A crystal structure of a photolyase at room temperature confirms the structural information obtained from cryogenic crystallography and paves the way for time-resolved studies of the photolyase at an X-ray free-electron laser., (6–4) photolyases are flavoproteins that belong to the photolyase/cryptochrome family. Their function is to repair DNA lesions using visible light. Here, crystal structures of Drosophila melanogaster (6–4) photolyase [Dm(6–4)photolyase] at room and cryogenic temperatures are reported. The room-temperature structure was solved to 2.27 Å resolution and was obtained by serial femtosecond crystallography (SFX) using an X-ray free-electron laser. The crystallization and preparation conditions are also reported. The cryogenic structure was solved to 1.79 Å resolution using conventional X-ray crystallo­graphy. The structures agree with each other, indicating that the structural information obtained from crystallography at cryogenic temperature also applies at room temperature. Furthermore, UV–Vis absorption spectroscopy confirms that Dm(6–4)photolyase is photoactive in the crystals, giving a green light to time-resolved SFX studies on the protein, which can reveal the structural mechanism of the photoactivated protein in DNA repair.

Published
2021

25. Structural basis of the radical pair state in photolyases and cryptochromes

Author

Andrea Cellini, Madan Kumar Shankar, Weixiao Yuan Wahlgren, Amke Nimmrich, Antonia Furrer, Daniel James, Maximilian Wranik, Sylvain Aumonier, Emma V. Beale, Florian Dworkowski, Jörg Standfuss, Tobias Weinert, and Sebastian Westenhoff

Subjects
Metals and Alloys, Biochemistry and Molecular Biology, Tryptophan, General Chemistry, Catalysis, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, Cryptochromes, Materials Chemistry, Ceramics and Composites, Flavin-Adenine Dinucleotide, Animals, Amino Acids, Deoxyribodipyrimidine Photo-Lyase, Biokemi och molekylärbiologi
Abstract

We present the structure of a photoactivated animal (6-4) photolyase in its radical pair state, captured by serial crystallography. We observe how a conserved asparigine moves towards the semiquinone FAD chromophore and stabilizes it by hydrogen bonding. Several amino acids around the final tryptophan radical rearrange, opening it up to the solvent. The structure explains how the protein environment stabilizes the radical pair state, which is crucial for function of (6-4) photolyases and cryptochromes.

Published
2022

26. Structural basis of the radical pair state in photolyases and cryptochromes

Author

Cellini, Andrea, Shankar, Madan Kumar, Wahlgren, Weixiao Yuan, Nimmrich, Amke, Furrer, Antonia, James, Daniel, Wranik, Maximilian, Aumonier, Sylvain, Beale, Emma, V, Dworkowski, Florian, Standfuss, Jorg, Weinert, Tobias, Westenhoff, Sebastian, Cellini, Andrea, Shankar, Madan Kumar, Wahlgren, Weixiao Yuan, Nimmrich, Amke, Furrer, Antonia, James, Daniel, Wranik, Maximilian, Aumonier, Sylvain, Beale, Emma, V, Dworkowski, Florian, Standfuss, Jorg, Weinert, Tobias, and Westenhoff, Sebastian

Abstract

We present the structure of a photoactivated animal (6-4) photolyase in its radical pair state, captured by serial crystallography. We observe how a conserved asparigine moves towards the semiquinone FAD chromophore and stabilizes it by hydrogen bonding. Several amino acids around the final tryptophan radical rearrange, opening it up to the solvent. The structure explains how the protein environment stabilizes the radical pair state, which is crucial for function of (6-4) photolyases and cryptochromes.

Published
2022
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29. Higher efficacy of letrozole in combination with trastuzumab compared to letrozole monotherapy as first-line treatment in patients with HER2-positive, hormone-receptor-positive metastatic breast cancer – Results of the eLEcTRA trial

Author

Huober, J., Fasching, P.A., Barsoum, M., Petruzelka, L., Wallwiener, D., Thomssen, C., Reimer, T., Paepke, S., Azim, H.A., Ragosch, V., Kubista, E., Baumgärtner, A.K., Beckmann, M.W., May, C., Nimmrich, I., and Harbeck, N.

Published
2012
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31. Structural basis of the radical pair state in photolyases and cryptochromes

Author

Cellini, Andrea, primary, Shankar, Madan Kumar, additional, Wahlgren, Weixiao Yuan, additional, Nimmrich, Amke, additional, Furrer, Antonia, additional, James, Daniel, additional, Wranik, Maximilian, additional, Aumonier, Sylvain, additional, Beale, Emma V., additional, Dworkowski, Florian, additional, Standfuss, Jörg, additional, Weinert, Tobias, additional, and Westenhoff, Sebastian, additional

Published
2022
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35. Discovery of ABT-957: 1-Benzyl-5-oxopyrrolidine-2-carboxamides as selective calpain inhibitors with enhanced metabolic stability

Author

Marjoleen Nijsen, Wilfried Hornberger, Achim Moeller, Volker Nimmrich, Helmut Mack, Andreas Kling, Katja Jantos, and Yanbin Lao

Subjects
Pyrrolidines, biology, 010405 organic chemistry, Chemistry, Organic Chemistry, Clinical Biochemistry, Carbonyl reduction, Pharmaceutical Science, Calpain, Metabolic stability, Highly selective, 01 natural sciences, Biochemistry, 0104 chemical sciences, Calpain inhibitors, Structure-Activity Relationship, 010404 medicinal & biomolecular chemistry, Drug Discovery, biology.protein, Humans, Molecular Medicine, Molecular Biology, Glycoproteins
Abstract

Aberrant activation of calpain has been observed in various pathophysiological disorders including neurodegenerative diseases such as Alzheimer's Disease. Here we describe our efforts on ketoamide-based 1-benzyl-5-oxopyrrolidine-2-carboxamides as a novel series of highly selective calpain inhibitors mitigating the metabolic liability of carbonyl reduction. The most advanced compound from this new series, namely A-1212805 (ABT-957, Alicapistat) proceeded to clinical phase I studies.

Published
2019

36. The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature

Author

Cellini, Andrea, primary, Yuan Wahlgren, Weixiao, additional, Henry, Léocadie, additional, Pandey, Suraj, additional, Ghosh, Swagatha, additional, Castillon, Leticia, additional, Claesson, Elin, additional, Takala, Heikki, additional, Kübel, Joachim, additional, Nimmrich, Amke, additional, Kuznetsova, Valentyna, additional, Nango, Eriko, additional, Iwata, So, additional, Owada, Shigeki, additional, Stojković, Emina A., additional, Schmidt, Marius, additional, Ihalainen, Janne A., additional, and Westenhoff, Sebastian, additional

Published
2021
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38. Nimmrich, Amke

Author

Nimmrich, Amke and Nimmrich, Amke

Published
2021

40. DNA hypermethylation of PITX2 is a marker of poor prognosis in untreated lymph node-negative hormone receptor-positive breast cancer patients

Author

Nimmrich, Inko, Sieuwerts, Anieta M., Meijer-van Gelder, Marion E., Schwope, Ina, Bolt-de Vries, Joan, Harbeck, Nadia, Koenig, Thomas, Hartmann, Oliver, Kluth, Antje, Dietrich, Dimo, Magdolen, Viktor, Portengen, Henk, Look, Maxime P., Klijn, Jan G. M., Lesche, Ralf, Schmitt, Manfred, Maier, Sabine, Foekens, John A., and Martens, John W. M.

Published
2008
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41. Author response: The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

Author

Marius Schmidt, Rahul Nanekar, Melissa Carrillo, Eriko Nango, Robert Bosman, Amke Nimmrich, Sebastian Westenhoff, Linnéa Isaksson, Tomoyuki Tanaka, Moona Kurttila, Valentyna Kuznetsova, Dmitry Morozov, Heikki Takala, Leticia Castillon, Shigeki Owada, Joachim Kübel, Matthijs R. Panman, Elin Claesson, So Iwata, Rie Tanaka, Suraj Pandey, Léocadie Henry, Michał Maj, Luo Fangjia, Janne A. Ihalainen, Gerrit Groenhof, Emina A. Stojković, Andrea Cellini, Weixiao Yuan Wahlgren, and Keith Moffat

Subjects
X-ray laser, Primary (chemistry), Materials science, Phytochrome, business.industry, Femtosecond, Optoelectronics, business
Published
2020

42. Long-lived Excited States in 7- and 9-Methylpurine Probed by fs Time-Resolved Vibrational Absorption Spectroscopy

Author

Hendrik Böhnke, Rebecca Holtmann, Friedrich Temps, and Amke Nimmrich

Subjects
Vibrational absorption, Photoexcitation, Methylpurine, Materials science, Absorption spectroscopy, Excited state, Relaxation (NMR), Spectroscopy, Molecular physics, Blueshift
Abstract

Transient vibrational absorption spectroscopy elucidates common deactivation pathways after UV photoexcitation for 7- and 9-methylpurine. However, 9-methylpurine exhibits an additional relaxation channel revealed by indirect observation of the excited 1ππ* state

Published
2020

43. Observing the Structural Evolution in the Photodissociation of Diiodomethane with Femtosecond Solution X-Ray Scattering

Author

Jan Davidsson, Jochen S. Hub, Kasper S. Kjær, Joachim Kübel, Oskar Berntsson, Emil Gustavsson, Matthijs R. Panman, Kalina Atkovska, Martin Nielsen, Diana B. Zederkof, Markus Hermann, Amke Nimmrich, Kensuke Tono, Sebastian Westenhoff, Elisa Biasin, Shigeki Owada, Tetsuo Katayama, Mads G. Laursen, Asmus Ougaard Dohn, Kristoffer Haldrup, Alireza Honarfar, Stephan Niebling, Tim Brandt van Driel, Jens Uhlig, and Ashley J. Hughes

Subjects
Fysikalisk kemi, Materials science, Scattering, Radical, Atom and Molecular Physics and Optics, Photodissociation, General Physics and Astronomy, 01 natural sciences, Chemical reaction, Physical Chemistry, Rotational energy, chemistry.chemical_compound, chemistry, Chemical physics, 0103 physical sciences, Femtosecond, Physics::Atomic and Molecular Clusters, Molecule, Diiodomethane, Atom- och molekylfysik och optik, Physics::Chemical Physics, 010306 general physics
Abstract

Resolving the structural dynamics of the initial steps of chemical reactions is challenging. We report the femtosecond time-resolved wide-angle x-ray scattering of the photodissociation of diiodomethane in cyclohexane. The data reveal with structural detail how the molecule dissociates into radicals, how the radicals collide with the solvent, and how they form the photoisomer. We extract how translational and rotational kinetic energy is dispersed into the solvent. We also find that 85% of the primary radical pairs are confined to their original solvent cage and discuss how this influences the downstream recombination reactions.

Published
2020

44. Observing the Structural Evolution in the Photodissociation of Diiodomethane with Femtosecond Solution X-Ray Scattering

Author

Panman, Matthijs R., Biasin, Elisa, Berntsson, Oskar, Hermann, Markus, Niebling, Stephan, Hughes, Ashley J., Kübel, Joachim, Atkovska, Kalina, Gustavsson, Emil, Nimmrich, Amke, Dohn, Asmus O., Laursen, Mads, Zederkof, Diana B., Honarfar, Alireza, Tono, Kensuke, Katayama, Tetsuo, Owada, Shigeki, van Driel, Tim B., Kjaer, Kasper, Nielsen, Martin M., Davidsson, Jan, Uhlig, Jens, Haldrup, Kristoffer, Hub, Jochen S., Westenhoff, Sebastian, Panman, Matthijs R., Biasin, Elisa, Berntsson, Oskar, Hermann, Markus, Niebling, Stephan, Hughes, Ashley J., Kübel, Joachim, Atkovska, Kalina, Gustavsson, Emil, Nimmrich, Amke, Dohn, Asmus O., Laursen, Mads, Zederkof, Diana B., Honarfar, Alireza, Tono, Kensuke, Katayama, Tetsuo, Owada, Shigeki, van Driel, Tim B., Kjaer, Kasper, Nielsen, Martin M., Davidsson, Jan, Uhlig, Jens, Haldrup, Kristoffer, Hub, Jochen S., and Westenhoff, Sebastian

Abstract

Resolving the structural dynamics of the initial steps of chemical reactions is challenging. We report the femtosecond time-resolved wide-angle x-ray scattering of the photodissociation of diiodomethane in cyclohexane. The data reveal with structural detail how the molecule dissociates into radicals, how the radicals collide with the solvent, and how they form the photoisomer. We extract how translational and rotational kinetic energy is dispersed into the solvent. We also find that 85% of the primary radical pairs are confined to their original solvent cage and discuss how this influences the downstream recombination reactions.

Published
2020
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46. CDC25L

Author

van Roy, Frans, primary, Nimmrich, Volker, additional, Bespalov, Anton, additional, Möller, Achim, additional, Hara, Hiromitsu, additional, Turowec, Jacob P., additional, St. Denis, Nicole A., additional, Litchfield, David W., additional, Boucher, Dave, additional, Denault, Jean-Bernard, additional, Matsuda, Keiko, additional, Yuzaki, Michisuke, additional, Repeke, Carlos, additional, Garlet, Thiago, additional, Trombone, Ana Paula, additional, Garlet, Gustavo, additional, Silveira, Elcia Maria, additional, Vieira, Andreia, additional, Cunha, Fernando, additional, Kubota, Satoshi, additional, Takigawa, Masaharu, additional, Soares, Helena, additional, Nolasco, Sofia, additional, Gonçalves, João, additional, Bensussan, Armand, additional, Marie-Cardine, Anne, additional, Deswal, Sumit, additional, Schamel, Wolfgang W. A., additional, Santos-Argumedo, Leopoldo, additional, Bishop, Gail A., additional, Decker, Dima A., additional, Hostager, Bruce S., additional, Bravo-Adame, Maria Elena, additional, Sandoval-Hernandez, Monserrat Alba, additional, Migueles-Lozano, Oscar Arturo, additional, Rosenstein, Yvonne, additional, Johnson, Pauline, additional, Samarakoon, Asanga, additional, Saunders, Amy E., additional, Harder, Kenneth W., additional, Roberts, David D., additional, Soto-Pantoja, David R., additional, Isenberg, Jeff S., additional, Lazo, Pedro A., additional, Barcia, Ramiro, additional, Wu, Hsin-Jung, additional, Muthusamy, Natarajan, additional, Bondada, Subbarao, additional, Levy, Shoshana, additional, Pawaria, Sudesh, additional, Binder, Robert J., additional, Masai, Hisao, additional, Hu, Dongli, additional, Lahti, Jill M., additional, Singer, Bernhard B., additional, Horuk, Richard, additional, Miller, Laurence J., additional, Morisset, Jean, additional, Mistry, Anita R., additional, O’Callaghan, Christopher A., additional, Fenton-May, Angharad E., additional, Reschen, Michael, additional, Willment, Janet A., additional, Brown, Gordon D., additional, Rabinow, Leonard, additional, Ness, Scott A., additional, Creutz, Carl E., additional, Yagishita-Kyo, Nan, additional, Inoue, Masatoshi, additional, Nonaka, Mio, additional, Okuno, Hiroyuki, additional, Bito, Haruhiko, additional, Okada, Masato, additional, Cheng, Heung-Chin, additional, Hossain, Mohammed Iqbal, additional, Kamaruddin, Mohd Aizuddin, additional, Chong, Yuh-Ping, additional, Sen, Banibrata, additional, Johnson, Faye M., additional, Pino, Paula A., additional, Cardona, Astrid E., additional, Paroni, Federico, additional, Maedler, Kathrin, additional, and Poon, Randy Y. C., additional

Published
2012
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47. Chemokine (C-X-C Motif) Ligand 10

Author

van Roy, Frans, primary, Nimmrich, Volker, additional, Bespalov, Anton, additional, Möller, Achim, additional, Hara, Hiromitsu, additional, Turowec, Jacob P., additional, St. Denis, Nicole A., additional, Litchfield, David W., additional, Boucher, Dave, additional, Denault, Jean-Bernard, additional, Matsuda, Keiko, additional, Yuzaki, Michisuke, additional, Repeke, Carlos, additional, Garlet, Thiago, additional, Trombone, Ana Paula, additional, Garlet, Gustavo, additional, Silveira, Elcia Maria, additional, Vieira, Andreia, additional, Cunha, Fernando, additional, Kubota, Satoshi, additional, Takigawa, Masaharu, additional, Soares, Helena, additional, Nolasco, Sofia, additional, Gonçalves, João, additional, Bensussan, Armand, additional, Marie-Cardine, Anne, additional, Deswal, Sumit, additional, Schamel, Wolfgang W. A., additional, Santos-Argumedo, Leopoldo, additional, Bishop, Gail A., additional, Decker, Dima A., additional, Hostager, Bruce S., additional, Bravo-Adame, Maria Elena, additional, Sandoval-Hernandez, Monserrat Alba, additional, Migueles-Lozano, Oscar Arturo, additional, Rosenstein, Yvonne, additional, Johnson, Pauline, additional, Samarakoon, Asanga, additional, Saunders, Amy E., additional, Harder, Kenneth W., additional, Roberts, David D., additional, Soto-Pantoja, David R., additional, Isenberg, Jeff S., additional, Lazo, Pedro A., additional, Barcia, Ramiro, additional, Wu, Hsin-Jung, additional, Muthusamy, Natarajan, additional, Bondada, Subbarao, additional, Levy, Shoshana, additional, Pawaria, Sudesh, additional, Binder, Robert J., additional, Masai, Hisao, additional, Hu, Dongli, additional, Lahti, Jill M., additional, Singer, Bernhard B., additional, Horuk, Richard, additional, Miller, Laurence J., additional, Morisset, Jean, additional, Mistry, Anita R., additional, O’Callaghan, Christopher A., additional, Fenton-May, Angharad E., additional, Reschen, Michael, additional, Willment, Janet A., additional, Brown, Gordon D., additional, Rabinow, Leonard, additional, Ness, Scott A., additional, Creutz, Carl E., additional, Yagishita-Kyo, Nan, additional, Inoue, Masatoshi, additional, Nonaka, Mio, additional, Okuno, Hiroyuki, additional, Bito, Haruhiko, additional, Okada, Masato, additional, Cheng, Heung-Chin, additional, Hossain, Mohammed Iqbal, additional, Kamaruddin, Mohd Aizuddin, additional, Chong, Yuh-Ping, additional, Sen, Banibrata, additional, Johnson, Faye M., additional, Pino, Paula A., additional, Cardona, Astrid E., additional, Paroni, Federico, additional, Maedler, Kathrin, additional, and Poon, Randy Y. C., additional

Published
2012
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48. Casein Kinase-I

Author

van Roy, Frans, primary, Nimmrich, Volker, additional, Bespalov, Anton, additional, Möller, Achim, additional, Hara, Hiromitsu, additional, Turowec, Jacob P., additional, St. Denis, Nicole A., additional, Litchfield, David W., additional, Boucher, Dave, additional, Denault, Jean-Bernard, additional, Matsuda, Keiko, additional, Yuzaki, Michisuke, additional, Repeke, Carlos, additional, Garlet, Thiago, additional, Trombone, Ana Paula, additional, Garlet, Gustavo, additional, Silveira, Elcia Maria, additional, Vieira, Andreia, additional, Cunha, Fernando, additional, Kubota, Satoshi, additional, Takigawa, Masaharu, additional, Soares, Helena, additional, Nolasco, Sofia, additional, Gonçalves, João, additional, Bensussan, Armand, additional, Marie-Cardine, Anne, additional, Deswal, Sumit, additional, Schamel, Wolfgang W. A., additional, Santos-Argumedo, Leopoldo, additional, Bishop, Gail A., additional, Decker, Dima A., additional, Hostager, Bruce S., additional, Bravo-Adame, Maria Elena, additional, Sandoval-Hernandez, Monserrat Alba, additional, Migueles-Lozano, Oscar Arturo, additional, Rosenstein, Yvonne, additional, Johnson, Pauline, additional, Samarakoon, Asanga, additional, Saunders, Amy E., additional, Harder, Kenneth W., additional, Roberts, David D., additional, Soto-Pantoja, David R., additional, Isenberg, Jeff S., additional, Lazo, Pedro A., additional, Barcia, Ramiro, additional, Wu, Hsin-Jung, additional, Muthusamy, Natarajan, additional, Bondada, Subbarao, additional, Levy, Shoshana, additional, Pawaria, Sudesh, additional, Binder, Robert J., additional, Masai, Hisao, additional, Hu, Dongli, additional, Lahti, Jill M., additional, Singer, Bernhard B., additional, Horuk, Richard, additional, Miller, Laurence J., additional, Morisset, Jean, additional, Mistry, Anita R., additional, O’Callaghan, Christopher A., additional, Fenton-May, Angharad E., additional, Reschen, Michael, additional, Willment, Janet A., additional, Brown, Gordon D., additional, Rabinow, Leonard, additional, Ness, Scott A., additional, Creutz, Carl E., additional, Yagishita-Kyo, Nan, additional, Inoue, Masatoshi, additional, Nonaka, Mio, additional, Okuno, Hiroyuki, additional, Bito, Haruhiko, additional, Okada, Masato, additional, Cheng, Heung-Chin, additional, Hossain, Mohammed Iqbal, additional, Kamaruddin, Mohd Aizuddin, additional, Chong, Yuh-Ping, additional, Sen, Banibrata, additional, Johnson, Faye M., additional, Pino, Paula A., additional, Cardona, Astrid E., additional, Paroni, Federico, additional, Maedler, Kathrin, additional, and Poon, Randy Y. C., additional

Published
2012
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49. CD72 Antigen

Author

van Roy, Frans, primary, Nimmrich, Volker, additional, Bespalov, Anton, additional, Möller, Achim, additional, Hara, Hiromitsu, additional, Turowec, Jacob P., additional, St. Denis, Nicole A., additional, Litchfield, David W., additional, Boucher, Dave, additional, Denault, Jean-Bernard, additional, Matsuda, Keiko, additional, Yuzaki, Michisuke, additional, Repeke, Carlos, additional, Garlet, Thiago, additional, Trombone, Ana Paula, additional, Garlet, Gustavo, additional, Silveira, Elcia Maria, additional, Vieira, Andreia, additional, Cunha, Fernando, additional, Kubota, Satoshi, additional, Takigawa, Masaharu, additional, Soares, Helena, additional, Nolasco, Sofia, additional, Gonçalves, João, additional, Bensussan, Armand, additional, Marie-Cardine, Anne, additional, Deswal, Sumit, additional, Schamel, Wolfgang W. A., additional, Santos-Argumedo, Leopoldo, additional, Bishop, Gail A., additional, Decker, Dima A., additional, Hostager, Bruce S., additional, Bravo-Adame, Maria Elena, additional, Sandoval-Hernandez, Monserrat Alba, additional, Migueles-Lozano, Oscar Arturo, additional, Rosenstein, Yvonne, additional, Johnson, Pauline, additional, Samarakoon, Asanga, additional, Saunders, Amy E., additional, Harder, Kenneth W., additional, Roberts, David D., additional, Soto-Pantoja, David R., additional, Isenberg, Jeff S., additional, Lazo, Pedro A., additional, Barcia, Ramiro, additional, Wu, Hsin-Jung, additional, Muthusamy, Natarajan, additional, Bondada, Subbarao, additional, Levy, Shoshana, additional, Pawaria, Sudesh, additional, Binder, Robert J., additional, Masai, Hisao, additional, Hu, Dongli, additional, Lahti, Jill M., additional, Singer, Bernhard B., additional, Horuk, Richard, additional, Miller, Laurence J., additional, Morisset, Jean, additional, Mistry, Anita R., additional, O’Callaghan, Christopher A., additional, Fenton-May, Angharad E., additional, Reschen, Michael, additional, Willment, Janet A., additional, Brown, Gordon D., additional, Rabinow, Leonard, additional, Ness, Scott A., additional, Creutz, Carl E., additional, Yagishita-Kyo, Nan, additional, Inoue, Masatoshi, additional, Nonaka, Mio, additional, Okuno, Hiroyuki, additional, Bito, Haruhiko, additional, Okada, Masato, additional, Cheng, Heung-Chin, additional, Hossain, Mohammed Iqbal, additional, Kamaruddin, Mohd Aizuddin, additional, Chong, Yuh-Ping, additional, Sen, Banibrata, additional, Johnson, Faye M., additional, Pino, Paula A., additional, Cardona, Astrid E., additional, Paroni, Federico, additional, Maedler, Kathrin, additional, and Poon, Randy Y. C., additional

Published
2012
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50. Catenin Beta

Author

van Roy, Frans, primary, Nimmrich, Volker, additional, Bespalov, Anton, additional, Möller, Achim, additional, Hara, Hiromitsu, additional, Turowec, Jacob P., additional, St. Denis, Nicole A., additional, Litchfield, David W., additional, Boucher, Dave, additional, Denault, Jean-Bernard, additional, Matsuda, Keiko, additional, Yuzaki, Michisuke, additional, Repeke, Carlos, additional, Garlet, Thiago, additional, Trombone, Ana Paula, additional, Garlet, Gustavo, additional, Silveira, Elcia Maria, additional, Vieira, Andreia, additional, Cunha, Fernando, additional, Kubota, Satoshi, additional, Takigawa, Masaharu, additional, Soares, Helena, additional, Nolasco, Sofia, additional, Gonçalves, João, additional, Bensussan, Armand, additional, Marie-Cardine, Anne, additional, Deswal, Sumit, additional, Schamel, Wolfgang W. A., additional, Santos-Argumedo, Leopoldo, additional, Bishop, Gail A., additional, Decker, Dima A., additional, Hostager, Bruce S., additional, Bravo-Adame, Maria Elena, additional, Sandoval-Hernandez, Monserrat Alba, additional, Migueles-Lozano, Oscar Arturo, additional, Rosenstein, Yvonne, additional, Johnson, Pauline, additional, Samarakoon, Asanga, additional, Saunders, Amy E., additional, Harder, Kenneth W., additional, Roberts, David D., additional, Soto-Pantoja, David R., additional, Isenberg, Jeff S., additional, Lazo, Pedro A., additional, Barcia, Ramiro, additional, Wu, Hsin-Jung, additional, Muthusamy, Natarajan, additional, Bondada, Subbarao, additional, Levy, Shoshana, additional, Pawaria, Sudesh, additional, Binder, Robert J., additional, Masai, Hisao, additional, Hu, Dongli, additional, Lahti, Jill M., additional, Singer, Bernhard B., additional, Horuk, Richard, additional, Miller, Laurence J., additional, Morisset, Jean, additional, Mistry, Anita R., additional, O’Callaghan, Christopher A., additional, Fenton-May, Angharad E., additional, Reschen, Michael, additional, Willment, Janet A., additional, Brown, Gordon D., additional, Rabinow, Leonard, additional, Ness, Scott A., additional, Creutz, Carl E., additional, Yagishita-Kyo, Nan, additional, Inoue, Masatoshi, additional, Nonaka, Mio, additional, Okuno, Hiroyuki, additional, Bito, Haruhiko, additional, Okada, Masato, additional, Cheng, Heung-Chin, additional, Hossain, Mohammed Iqbal, additional, Kamaruddin, Mohd Aizuddin, additional, Chong, Yuh-Ping, additional, Sen, Banibrata, additional, Johnson, Faye M., additional, Pino, Paula A., additional, Cardona, Astrid E., additional, Paroni, Federico, additional, Maedler, Kathrin, additional, and Poon, Randy Y. C., additional

Published
2012
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