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  • 1.
    Karalius, Antanas
    et al.
    KTH Royal Institute of Technology, Sweden.
    Zhang, Yang
    KTH Royal Institute of Technology, Sweden.
    Kravchenko, Oleksandr
    KTH Royal Institute of Technology, Sweden.
    Elofsson, Ulla
    RISE Research Institutes of Sweden, Bioeconomy and Health, Chemical processes and Pharmaceutical Development.
    Szabó, Zoltan
    KTH Royal Institute of Technology, Sweden.
    Yan, Mingdi
    KTH Royal Institute of Technology, Sweden; University of Massachusetts Lowell, US.
    Ramström, Olof
    KTH Royal Institute of Technology, Sweden, University of Massachusetts Lowell, US; Linnaeus University, Sweden.
    Formation and Out-of-Equilibrium, High/Low State Switching of a Nitroaldol Dynamer in Neutral Aqueous Media2020In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773Article in journal (Refereed)
    Abstract [en]

    The nitroaldol reaction is demonstrated as an efficient dynamic covalent reaction in phosphate buffers at neutral pH. Rapid equilibration was recorded with pyridine-based aldehydes, and dynamic oligomerization could be achieved, leading to nitroaldol dynamers of up to 17 repeating units. The dynamers were applied in a coherent stimuli-responsive molecular system in which larger dynamers transiently existed out-of-equilibrium in a neutral aqueous system rich in formaldehyde, controlled by nitromethane.

  • 2.
    Paulraj, T
    et al.
    KTH Royal Institute of Technology, Sweden.
    Wennmalm, S
    KTH Royal Institute of Technology, Sweden.
    Wieland, D
    Helmholtz-Zentrum Geesthacht, Germany.
    Riazanova, A V
    KTH Royal Institute of Technology, Sweden.
    Dėdinaitė, Andra
    RISE Research Institutes of Sweden, Bioeconomy and Health, Chemical Process and Pharmaceutical Development. KTH Royal Institute of Technology, Sweden.
    Günther Pomorski, T.
    Ruhr University Bochum, Germany; University of Copenhagen, Denmark.
    Cárdenas, M.
    Malmö University, Sweden.
    Svagan, A. J.
    KTH Royal Institute of Technology, Sweden.
    Primary cell wall inspired micro containers as a step towards a synthetic plant cell2020In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 11, no 1, article id 958Article in journal (Refereed)
    Abstract [en]

    The structural integrity of living plant cells heavily relies on the plant cell wall containing a nanofibrous cellulose skeleton. Hence, if synthetic plant cells consist of such a cell wall, they would allow for manipulation into more complex synthetic plant structures. Herein, we have overcome the fundamental difficulties associated with assembling lipid vesicles with cellulosic nanofibers (CNFs). We prepare plantosomes with an outer shell of CNF and pectin, and beneath this, a thin layer of lipids (oleic acid and phospholipids) that surrounds a water core. By exploiting the phase behavior of the lipids, regulated by pH and Mg2+ ions, we form vesicle-crowded interiors that change the outer dimension of the plantosomes, mimicking the expansion in real plant cells during, e.g., growth. The internal pressure enables growth of lipid tubules through the plantosome cell wall, which paves the way to the development of hierarchical plant structures and advanced synthetic plant cell mimics. © 2020, The Author(s).

  • 3.
    Rudd, Sean
    et al.
    Karolinska Institute, Sweden.
    Tsesmetzis, Nikolaos
    Karolinska Institute, Sweden.
    Sanjiv, Kumar
    Karolinska Institute, Sweden.
    Paulin, Cynthia
    RISE Research Institutes of Sweden, Bioeconomy and Health, Chemical processes and Pharmaceutical Development. Karolinska Institute, Sweden.
    Sandhow, Lakshmi
    Karolinska Institute, Sweden.
    Kutzner, Juliane
    University Hospital Heidelberg, Germany.
    Hed Myrberg, Ida
    Karolinska Institute, Sweden.
    Bunten, Sarah
    University Hospital Heidelberg, Germany.
    Axelsson, Hanna
    Karolinska Institute, Sweden.
    Zhang, Si
    Karolinska Institute, Sweden.
    Rasti, Azita
    Karolinska Institute, Sweden.
    Mäkelä, Petri
    Karolinska Institute, Sweden.
    Coggins, SiAna
    Emory University School of Medicine, US.
    Tao, Sijia
    Emory University School of Medicine, US.
    Suman, Sharda
    Karolinska Institute, Sweden.
    Branca, Rui
    Karolinska Institute, Sweden.
    Mermelekas, Georgios
    Karolinska Institute, Sweden.
    Wiita, Elisee
    Karolinska Institute, Sweden.
    Lee, Sun
    Karolinska Institute, Sweden.
    Walfridsson, Julian
    Karolinska Institute, Sweden.
    Schinazi, Raymond
    Emory University School of Medicine, US.
    Kim, Baek
    Emory University School of Medicine, US; Kyung-Hee University, South Korea.
    Lehtiö, Janne
    Karolinska Institute, Sweden.
    Rassidakis, Georgis
    Karolinska Institute, Sweden.
    Pokrovskaja Tamm, Katja
    Karolinska Institute, Sweden.
    Warpman-Berglund, Ulrika
    Karolinska Institute, Sweden.
    Heyman, Mats
    Karolinska Institute, Sweden.
    Grandér, Dan
    Karolinska Institute, Sweden.
    Lehmann, Sören
    Karolinska Institute, Sweden; Uppsala University, Sweden.
    Lundbäck, Thomas
    AstraZeneca, Sweden.
    Qian, Hong
    Karolinska Institute, Sweden.
    Henter, Jan-Inge
    Karolinska Institute, Sweden.
    Schaller, Torsten
    University Hospital Heidelberg, Germany; Heidelberg ImmunoTherapeutics GmbH, Germany.
    Helleday, Thomas
    Karolinska Institute, Sweden; University of Sheffield, UK.
    Herold, Nikolas
    Karolinska Institute, Sweden.
    Ribonucleotide reductase inhibitors suppress SAMHD1 ara-CTPase activity enhancing cytarabine efficacy2020In: EMBO Molecular Medicine, ISSN 1757-4676, E-ISSN 1757-4684, article id e10419Article in journal (Refereed)
    Abstract [en]

    The deoxycytidine analogue cytarabine (ara-C) remains the backbone treatment of acute myeloid leukaemia (AML) as well as other haematological and lymphoid malignancies, but must be combined with other chemotherapeutics to achieve cure. Yet, the underlying mechanism dictating synergistic efficacy of combination chemotherapy remains largely unknown. The dNTPase SAMHD1, which regulates dNTP homoeostasis antagonistically to ribonucleotide reductase (RNR), limits ara-C efficacy by hydrolysing the active triphosphate metabolite ara-CTP. Here, we report that clinically used inhibitors of RNR, such as gemcitabine and hydroxyurea, overcome the SAMHD1-mediated barrier to ara-C efficacy in primary blasts and mouse models of AML, displaying SAMHD1-dependent synergy with ara-C. We present evidence that this is mediated by dNTP pool imbalances leading to allosteric reduction of SAMHD1 ara-CTPase activity. Thus, SAMHD1 constitutes a novel biomarker for combination therapies of ara-C and RNR inhibitors with immediate consequences for clinical practice to improve treatment of AML. © 2020 The Authors. Published under the terms of the CC BY 4.0 license

  • 4.
    Sonderby, P.
    et al.
    DTU Technical University of Denmark, Denmark.
    Soderberg, Christopher
    RISE Research Institutes of Sweden, Bioeconomy and Health, Chemical Process and Pharmaceutical Development. Lund University, Sweden.
    Frankaer, C. G.
    University of Copenhagen, Denmark.
    Peters, G.
    DTU Technical University of Denmark, Denmark.
    Bukrinski, J. T.
    CMC Assist Aps, Denmark.
    Labrador, A.
    Lund University, Sweden.
    Plivelic, T. S.
    Lund University, Sweden.
    Harris, P.
    DTU Technical University of Denmark, Denmark.
    Concentrated protein solutions investigated using acoustic levitation and small-Angle X-ray scattering2020In: Journal of Synchrotron Radiation, ISSN 0909-0495, E-ISSN 1600-5775, Vol. 27, p. 396-404Article in journal (Refereed)
    Abstract [en]

    An acoustically levitated droplet has been used to collect synchrotron SAXS data on human serum albumin protein solutions up to a protein concentration of 400mgml-1. A careful selection of experiments allows for fast data collection of a large amount of data, spanning a protein concentration/solvent concentration space with limited sample consumption (down to 3μL per experiment) and few measurements. The data analysis shows data of high quality that are reproducible and comparable with data from standard flow-Through capillary-based experiments. Furthermore, using this methodology, it is possible to achieve concentrations that would not be accessible by conventional cells. The protein concentration and ionic strength parameter space diagram may be covered easily and the amount of protein sample is significantly reduced (by a factor of 100 in this work). Used in routine measurements, the benefits in terms of protein cost and time spent are very significant. 

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