Publications co-authored by SARomics Biostructures' team
Recent highlights
Skladanowska K, Bloch Y, Strand J, White K, Hua J, Aldridge D, Welin M, Logan DT, Soete A, Merceron R, Murphy C, Provost M, Bazan JF, Hunter C, Hill J & Savvides SN. Structural basis of activation and antagonism of receptor signaling mediated by interleukin-27.
Cell Reports, 41, 111490. doi:https://doi.org/10.1016/j.celrep.2022.111490
Cell Reports, 41, 111490. doi:https://doi.org/10.1016/j.celrep.2022.111490
Interleukin-27 (IL-27) uniquely assembles p28 and EBI3 subunits to a heterodimeric cytokine that signals via IL-27Rα and gp130. To provide the structural framework for receptor activation by IL-27 and its emerging therapeutic targeting, the crystal structures of mouse IL-27 in complex with IL-27Rα and human IL-27 in complex with SRF388, a monoclonal antibody undergoing clinical trials with oncology indications, were determined.
Zhang Y, Towers CG, Liu J, Håkansson M, Logan DT, Donini O & Kutateladze TG (2022).
Dusquetide modulates innate immune response through binding to p62.
Structure 30, 1055-1061e7. doi: 10.1016/j.str.2022.05.003
Dusquetide modulates innate immune response through binding to p62.
Structure 30, 1055-1061e7. doi: 10.1016/j.str.2022.05.003
SQSTM1/p62 is an autophagic receptor that plays a major role in mediating stress and innate immune responses. Preclinical studies identified p62 as a target of the prototype innate defense regulator (IDR); however, the molecular mechanism of this process remains unclear. The paper describes the structural basis and biological consequences of the interaction of p62 with the next generation of IDRs, dusquetide.
Don't miss our blog post telling the exciting story behind this publication!
Maurer MF, Lewis JL, Ardour D, Gudgeon CJ, Chandrasekaran S, Mudri S, Kleist, KN, Navas C, Wolfson MF, Rixon MW, Swanson R, Dillon SR, Levin SD, Kimbung YR, Akutsu M, Logan DT, Walse B, Swiderek K & Peng SL (2022).
The engineered CD80 variant fusion therapeutic davoceticept combines checkpoint antagonism with conditional CD28 co-stimulation for anti-tumor immunity.
Nature Commun. 13, 1790. doi:10.1038/s41467-022-29286-5
The engineered CD80 variant fusion therapeutic davoceticept combines checkpoint antagonism with conditional CD28 co-stimulation for anti-tumor immunity.
Nature Commun. 13, 1790. doi:10.1038/s41467-022-29286-5
The CD80 vIgD from ALPN-202 was co-crystallized with WT PD-L1 ECD and used to determine the structure of the CD80 vIgD:PD-L1 complex. The paper shows that a therapeutic ALPN-202 enhances T cell activation and anti-tumor efficacy in cell-based assays and mouse tumor models more potently than checkpoint blockade alone and thus has the potential to generate potent, clinically meaningful anti-tumor immunity in humans.
Huang S, Xu P, Shen DD, Simon IA, Mao C, Tan Y, Zhang H, Harpsøe K, Li H, Zhang Y, You C, Yu X, Jiang Y, Zhang Y, Gloriam DE, Xu HE (2022).
GPCRs steer Gi and Gs selectivity via TM5-TM6 switches as revealed by structures of serotonin receptors.
Mol Cell. 82(14):2681-2695.e6. doi:10.1016/j.molcel.2022.05.031.
GPCRs steer Gi and Gs selectivity via TM5-TM6 switches as revealed by structures of serotonin receptors.
Mol Cell. 82(14):2681-2695.e6. doi:10.1016/j.molcel.2022.05.031.
Serotonin (or 5-hydroxytryptamine, 5-HT) is an important neurotransmitter that activates 12 different G protein-coupled receptors (GPCRs) through selective coupling of Gs, Gi, or Gq proteins. The structural basis for G protein subtype selectivity by these GPCRs remains elusive. The paper reports the structures of the serotonin receptors 5-HT4, 5-HT6, and 5-HT7 with Gs, and 5-HT4 with Gi1. The structures reveal that transmembrane helices TM5 and TM6 alternate lengths as a macro-switch to determine receptor's selectivity for Gs and Gi, respectively.
Xu P, Huang S, Zhang H, Mao C, Zhou X E, Cheng X, Simon I A, Shen D-D, Yen H-Y, Robinson C V, Harpsøe K, Svensson B, Guo J, Jiang H, Gloriam D E, Melcher K, Jiang Y, Zhang Y, Xu H E (2021).
Structural insights into the lipid and ligand regulation of serotonin receptors.
Nature 592, 469–473, https://doi.org/10.1038/s41586-021-03376-8
Structural insights into the lipid and ligand regulation of serotonin receptors.
Nature 592, 469–473, https://doi.org/10.1038/s41586-021-03376-8
Serotonin, or 5-hydroxytryptamine (5-HT), is a neurotransmitter that activates the largest subtype family of G-protein-coupled receptors (GPCR). Drugs that target 5-HT1A, 5-HT1D, 5-HT1E and other 5-HT receptors are used to treat numerous disorders. The paper reports five structures of 5-HT receptor–G-protein complexes: 5-HT1A in the apo state, bound to 5-HT or bound to the antipsychotic drug aripiprazole; 5-HT1D bound to 5-HT; and 5-HT1E in complex with a 5-HT1E- and 5-HT1F-selective agonist, BRL-54443.
Full list
- 2022 Skladanowska K, Bloch Y, Strand J, White K, Hua J, Aldridge D, Welin M, Logan DT, Soete A, Merceron R, Murphy C, Provost M, Bazan JF, Hunter C, Hill J & Savvides SN. Structural basis of activation and antagonism of receptor signaling mediated by interleukin-27.
Cell Reports, 41, 111490. doi:https://doi.org/10.1016/j.celrep.2022.111490
Zhang Y, Towers CG, Liu J, Håkansson M, Logan DT, Donini O & Kutateladze TG. Dusquetide modulates innate immune response through binding to p62.
Structure 30, 1055-1061e7. doi: 10.1016/j.str.2022.05.003
Maurer MF, Lewis JL, Ardour D, Gudgeon CJ, Chandrasekaran S, Mudri S, Kleist, KN, Navas C, Wolfson MF, Rixon MW, Swanson R, Dillon SR, Levin SD, Kimbung YR, Akutsu M, Logan DT, Walse B, Swiderek K & Peng SL (2022). The engineered CD80 variant fusion therapeutic davoceticept combines checkpoint antagonism with conditional CD28 co-stimulation for anti-tumor immunity.
Nature Commun. 13, 1790. doi: 10.1038/s41467-022-29286-5
Huang S, Xu P, Shen DD, Simon IA, Mao C, Tan Y, Zhang H, Harpsøe K, Li H, Zhang Y, You C, Yu X, Jiang Y, Zhang Y, Gloriam DE, Xu HE. GPCRs steer Gi and Gs selectivity via TM5-TM6 switches as revealed by structures of serotonin receptors.
Mol Cell. 2022 Jul 21;82(14):2681-2695.e6. doi: 10.1016/j.molcel.2022.05.031.
Ahlqvist J, Linares-Pastén JA, Håkansson M, Jasilonis A, Kwiatkow K, Fridjonsson, OH, Kaczarowska, A-K, Dabrowski, S, Aevarsson, A, Hreggvidsson, GO, Al-Karadaghi S, Kaczorowska, T, Nordberg Karlsson E. (2022). Crystal structure and initial characterization of a novel archeal-like Holiday junction-resolving enzyme from Thermus thermophilus phage Tth 15-6.
Acta Cryst. D78, 212.
Dandare SU, Håkansson M, Svensson LA, Timson DJ, Allen CRC (2022). Expression, purification and crystallization of a novel metagenome-derived salicylaldehyde dehydrogenase from Apline soil.
Acta Crystallographic Secition F: Structural Biology Communications 78 (4). - 2021 Mujtaba H, van Klaveren S, Håkansson M, Diehl C, Kovačič R, Baussière F, Sundin A P, Dernovšek J, Walse B, Zetterberg F, Leffler H, Anderluh M, Tomašič T, Jakopin Ž, Nilsson U J (2021). Benzimidazole–galactosides bind selectively to the Galectin-8 N-Terminal domain: Structure-based design and optimisation.
Eu. J. Med. Chem. 223, 113664. https://doi.org/10.1016/j.ejmech.2021.113664
Beckmann R, Jensen K, Fenn S, Speck J, Krause K, Meier A, Röth M, Fauser S, Kimbung R, Logan DT, Steegmaier M & Kettenberger H. (2021). DutaFabs: A novel platform of bispecific therapeutic Fab fragments which can simultaneously bind two targets with high affinity.
Nature Communications 12, 708. https://doi.org/10.1038/s41467-021-20949-3
Stenström O, Diehl C, Modig K, Nilsson U J, and Akke M. (2021). Mapping the energy landscape of protein–ligand binding via linear free energy relationships determined by protein NMR relaxation dispersion.
RSC Chem. Biol. 2, 259-265. https://doi.org/10.1039/D0CB00229A
Durcik M, et al. and Welin M, Kimbung R, Focht D et al. and Tomašiča T. (2021). New dual ATP-competitive inhibitors of bacterial DNA gyrase and topoisomerase IV active against ESKAPE pathogens.
Eur J Med Chem 213, 113200. https://doi.org/10.1016/j.ejmech.2021.113200
Goebel EJ, Kattamuri C, Gipson GR, Krishnan L, Chavez M, Czepnik M, Maguire MC, Grenha R, Håkansson M, Logan DT, Grinberg AV, Sako D, Castonguay R, Kumar R, Thompson TB (2021). Structures of activin ligand traps using natural sets of type I and type II TGFβ receptors.
iScience 25, 103590. doi: 10.1016/j.isci.2021.103590 - 2020-2019 Nyerges A, et al. and Welin M, Kimbung R, Focht D, Peterlin Mašič L, and Pal C. (2020). Rational design of balanced dual-targeting antibiotics with limited resistance.
PLoS Biol 18(10):e3000819. https://doi.org/10.1371/journal.pbio.3000819
Karczewski J, Krasucki S P, Asare-Okai P N, Diehl C, Friedman A, Brown C M, Maezato Y, and Streatfield S J. (2020). Isolation, Characterization and Structure Elucidation of a Novel Lantibiotic From Paenibacillus sp.
Front. Microbiol. 24. https://doi.org/10.3389/fmicb.2020.598789
Sanchez-Fernandez A, Diehl C, Houston J E, Leung A E, Tellam J P, Rogers S E, Prevost S, Ulvenlund S, Sjögren H, and Wahlgren M. (2020). An integrative toolbox to unlock the structure and dynamics of protein–surfactant complexes.
Nanoscale Adv 2, 4011-4023. https://doi.org/10.1039/D0NA00194E
Schneider, P., Welin, M., Svensson, B., Walse, B. and Schneider, G. (2020). Virtual screening and design with machine intelligence applied to Pim‐1 kinase inhibitors.
Mol. Inf., 39, 2000109. https://doi.org/10.1002/minf.202000109
Telzerow A, Paris J, Håkansson M, González‐Sabín J, Ríos‐Lombardía N, Gröger H, Morís F, Schürmann M, Schwab H, Steiner K. (2020). Expanding the Toolbox of R‐Selective Amine Transaminases by Identification and Characterization of New Members.
ChemBioChem 2020 21, 1–12. https://doi.org/10.1002/cbic.202000692
Ladds M J G W, Popova G, Pastor-Fernández A, Kannan S, van Leeuwen I M M, Håkansson M, Walse B, Tholander F, Ravi Bhatia, Verma C S, Lane D P, Laín S. (2020). Exploitation of dihydroorotate dehydrogenase (DHODH) and p53 activation as therapeutic targets: A case study in polypharmacology.
J Biol Chem 295, 17935-17949. https://doi.org/10.1074/jbc.RA119.012056
Shilova A, Lebrette H, Aurelius, O, Nan J, Welin M, Kovacic R, Ghosh S, Safari C, Friel R J, Milas M, Matej Z, Högbom M, Brändén G, Kloos M, Shoeman R L, Doak B, Ursby, T M. Håkansson T M, Logan D T, and Mueller U. (2020). Current status and future opportunities for serial crystallography at MAX IV Laboratory
J. Synchrotron Rad. 27, 1095-1102. https://doi.org/10.1107/S1600577520008735
Plotka M, Szadkowska M, Håkansson M, Kovačič R, Al-Karadaghi S, Walse B, Werbowy O, Kaczorowska A-K, and Kaczorowski T. (2020). Molecular Characterization of a Novel Lytic Enzyme LysC from Clostridium intestinale URNW and Its Antibacterial Activity Mediated by Positively Charged N-Terminal Extension.
Int J Mol Sci. 21, 4894; https://doi.org/10.3390/ijms21144894
Baggio C, Udompholkul P, Gambini L, Jossart J, Salem AF, Håkansson M, Perry JJP, Pellecchia M. (2020). N-locking stabilization of covalent helical peptides: Application to Bfl-1 antagonists.
Chem Biol Drug Des. 95, 412-426. doi: 10.1111/cbdd.13661
Telzerow A, Paris J, Håkansson M, Gonzalez-Sabin J, Rios-Lombardía N, Schürmann M, Gröger H, Morís F, Kourist R, Schwab H and Steiner K (2019). Amine Transaminase from Exophiala Xenobiotica - Crystal Structure and Engineering of a Fold IV Transaminase that Naturally Converts Biaryl Ketones.
ACS Catal. 9, 1140−1148. https://doi.org/10.1021/acscatal.8b04524
Dahlqvist A, Mandal S, Peterson K, Håkansson M, Logan DT, Zetterberg FR, Leffler H, Nilsson UJ (2019). 3-Substituted 1-Naphthamidomethyl-C-galactosyls Interact with Two Unique Sub-sites for High-Affinity and High-Selectivity Inhibition of Galectin-3.
Molecules. 24 (24), 4554. https://doi.org/10.3390/molecules24244554
Ruggieri F, Campillo-Brocal JC, Chen S, Humble MS, Walse B, Logan DT, Berglund P (2019). Insight into the dimer dissociation process of the Chromobacterium violaceum (S)-selective amine transaminase.
Sci Rep. 9, 16946. DOI: 10.1093/nar/25.17.3389
Freitag-Pohl S, Jasilionis A, Håkansson M, Svensson LA, Kovačič R, Welin M, Watzlawick H, Wang L, Altenbuchner J, Płotka M, Kaczorowska AK, Kaczorowski T, Nordberg Karlsson E, Al-Karadaghi S, Walse B, Aevarsson A, Pohl E (2019). Crystal structures of the Bacillus subtilis prophage lytic cassette proteins XepA and YomS.
Acta Crystallogr D Struct Biol., 75(Pt 11):1028-1039. https://doi.org/10.1107/S2059798319013330
Korkmaz B, Lesner A, Wysocka M, Gieldon A, Håkansson M, Gauthier F, Logan DT, Jenne DE, Lauritzen C, Pedersen J (2019). Structure-based design and in vivo anti-arthritic activity evaluation of a potent dipeptidyl cyclopropyl nitrile inhibitor of cathepsin C.
Biochem Pharmacol. 164, 349-367. https://doi.org/10.1016/j.bcp.2019.04.006
Kracht ON, Correia Cordeiro RS, Håkansson M, Stockmann J, Sander D, Bandow J, Senges CHR, Logan DT, Kourist R (2019). Discovery of three novel sesquiterpene synthases from Streptomyces chartreusis NRRL 3882 and crystal structure of an α-eudesmol synthase.
J Biotechnol. 297, 71-77. https://doi.org/10.1016/j.jbiotec.2019.03.006
Casaletto JB, Geddie ML, Abu-Yousif AO, Masson K, Fulgham A, Boudot A, Maiwald T, Kearns JD, Kohli N, Su S, Razlog M, Raue A, Kalra A, Håkansson M, Logan DT, Welin M, Chattopadhyay S, Harms BD, Nielsen UB, Schoeberl B, Lugovskoy AA, MacBeath G (2019). MM-131, a bispecific anti-Met/EpCAM mAb, inhibits HGF-dependent and HGF-independent Met signaling through concurrent binding to EpCAM.
Proc Natl Acad Sci U S A 116, 7533-7542. https://doi.org/10.1073/pnas.1819085116 - 2018-2017 Ruggieri F, van Langen LM, Logan DT, Walse B, Berglund P. (2018). Transaminase-Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions.
ChemCatChem, 10, 1-8. https://doi.org/10.1002/cctc.201801049
Gustafsson NMS, Färnegårdh K, Bonagas N, Ninou AH, Groth P, Wiita E, Jönsson M, Hallberg K, Lehto J, Pennisi R, Martinsson J, Norström C, Hollers J, Schultz J, Andersson M, Markova N, Marttila P, Kim B, Norin M, Olin T, Helleday T (2018). Targeting PFKFB3 radiosensitizes cancer cells and suppresses homologous recombination.
Nat Commun. 9, 3872. DOI: 10.1038/s41467-018-06287-x
Abdillahi SM, Maaß T, Kasetty G, Strömstedt AA, Baumgarten M, Tati R, Nordin SL, Walse B, Wagener R, Schmidtchen A, Mörgelin M (2018)
Collagen VI Contains Multiple Host Defense Peptides with Potent In Vivo Activity.
J Immunol., 201, 1007-1020. https://doi.org/10.4049/jimmunol.1700602
Ladds MJGW, van Leeuwen IMM, Drummond CJ, Chu S, Healy AR, Popova G, Pastor Fernández A, Mollick T, Darekar S, Sedimbi SK, Nekulova M, Sachweh MCC, Campbell J, Higgins M, Tuck C, Popa M, Safont MM, Gelebart P, Fandalyuk Z, Thompson AM, Svensson R, Gustavsson AL, Johansson L, Färnegårdh K, Yngve U, Saleh A, Haraldsson M, D'Hollander ACA, Franco M, Zhao Y, Håkansson M, Walse B, Larsson K, Peat EM, Pelechano V, Lunec J, Vojtesek B, Carmena M, Earnshaw WC, McCarthy AR, Westwood NJ, Arsenian-Henriksson M, Lane DP, Bhatia R, McCormack E, Laín S. A (2018). A DHODH inhibitor increases p53 synthesis and enhances tumor cell killing by p53 degradation blockage.
Nat Commun. 9, 1107. DOI: 10.1038/s41467-018-03441-3
Andersen MCF, Boos I, Kinnaert C, Awan SI, Pedersen HL, Kračun SK, Lanz G,Rydahl MG, Kjærulff L, Håkansson M, Kimbung R, Logan DT, Gotfredsen CH, Willats WGT, Clausen MH (2018). Synthesis of branched and linear 1,4-linked galactan oligosaccharides.
Org Biomol Chem. 16, 1157-1162. DOI: 10.1039/c7ob03035e
Peterson K, Kumar R, Stenström O, Verma P, Verma PR, Håkansson M, Kahl-Knutsson B, Zetterberg F, Leffler H, Akke M, Logan DT, Nilsson UJ (2018). Systematic tuning of fluoro-galectin-3 interactions provides thiodigalactoside derivatives with single digit nM affinity and high selectivity.
J Med Chem 61, 1164–1175. DOI: 10.1021/acs.jmedchem.7b01626.
Zetterberg FR, Peterson K, Johnsson R, Brimert T, Håkansson M, Logan DT, Leffler H, Nilsson UJ (2018). Monosaccharide derivatives with low nM lectin affinity and high selectivity based on combined fluorine-amide, phenyl-arginine, sulfur-π, and halogen bond interactions.
ChemMedChem 13, 133-137. DOI: 10.1002/cmdc.201700744.
Takemoto Y, Slough DP, Meinke G, Katnik C, Graziano ZA, Chidipi B, Reiser M, Alhadidy MM, Ramirez R, Salvador-Montañés O, Ennis S, Guerrero-Serna G, Haburcak M, Diehl C, Cuevas J, Jalife J, Bohm A, Lin YS, Noujaim SF (2017). Structural basis for the antiarrhythmic blockade of a potassium channel with a small molecule.
FASEB J pii: fj.201700349R. DOI: 10.1096/fj.201700349R.
Anderson LC, Håkansson M, Walse B and Nilsson CL (2017). Intact Protein Analysis at 21 Tesla and X-Ray Crystallography Define Structural Differences in Single Amino Acid Variants of Human Mitochondrial Branched-Chain Amino Acid Aminotransferase 2 (BCAT2).
J Am Soc Mass Spectrom 28, 1796-1804. DOI: 10.1007/s13361-017-1705-0
Walse B, Turnbull AP and Boyd SM (2017). Tailoring Hit Identification and Qualification Methods for Targeting Protein–Protein Interactions.
In Applied Biophysics for Drug Discovery (Huddler, D. and Zartler, E.R., ed.) pp. 29-59, John Wiley & Sons, Inc, Hoboken, NJ, USA.
Noresson AL, Aurelius O, Öberg CT, Engström O, Sundin AP, Håkansson M, Stenström O, Akke M, Logan DT, Leffler H, Nilsson UJ (2017).
Designing interactions by control of protein-ligand complex conformation: tuning arginine-arene interaction geometry for enhanced electrostatic protein-ligand interactions.
Chem Sci. 9, 1014-1021. DOI: 10.1039/c7sc04749e - 2016-2015 Nilsson LM, Green LC, Veppil Muralidharan S, Demir D, Welin M, Bhadury J, Logan D, Walse B and Nilsson JA (2016). Cancer differentiating agent hexamethylene bisacetamide inhibits BET bromodomain proteins.
Cancer Res. 76, 2376-2383. DOI: 10.1158/0008-5472.CAN-15-2721
Badarau A, Rouha H, Malafa S, Battles MB, Walker L, Nielson N, Dolezilkova I, Teubenbacher A, Banerjee S, Maierhofer B, Weber S, Stulik L, Logan DT, Welin M, Mirkina I, Pleban C, Zauner G, Gross K, Jägerhofer M, Magyarics Z & Nagy E (2016). Context matters: The importance of dimerization-induced conformation of the LukGH leukocidin of Staphylococcus aureus for the generation of neutralizing antibodies.
MAbs. 8, 1347-1360. DOI: 10.1080/19420862.2016.1215791
Badarau A, Rouha H, Malafa S, Logan DT, Håkansson M, Stulik L, Dolezilkova I, Teubenbacher A, Gross K, Maierhofer B, Weber S, Jägerhofer M, Hoffmann D, Nagy E (2015). Structure-Function Analysis of Heterodimer Formation, Oligomerization, and Receptor Binding of the Staphylococcus aureus Bi-component Toxin LukGH.
J. Biol. Chem. 290, 142-156. DOI: 10.1074/jbc.M114.598110
Rodrigues T, Reker, D, Welin M, Caldera M, Brunner C, Gabernet G,Schneider P, Walse B and Schneider G (2015). De Novo Fragment Design for Drug Discovery and Chemical Biology.
Angewandte Chemie International Edition, DOI: 10.1002/anie.201508055.
Fisher SZ, von Schantz L, Håkansson M, Logan DT & Ohlin M. (2015). Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand.
Biochemistry 54, 6435-6438. DOI: 10.1021/acs.biochem.5b01058
Jong-Eun Kim, Joe Eun Son, Hyein Jeong, Dong Joon Kim, Sang Gwon Seo, Eunjung Lee, Tae Gyu Lim, Jong Rhan Kim, Yengo Raymond Kimbung, Hanyong Chen, Ann M. Bode, Ki Won Lee and Zigang Dong (2015). A Novel Cinnamon-Related Natural Product with Pim-1 Inhibitory Activity Inhibits Leukemia and Skin Cancer.
Cancer Res. 75, 2716-2728. doi: 10.1158/0008-5472.CAN-14-3655 - 2014-2012 von Schantz L, Håkansson M, Logan DT, Nordberg-Karlsson E and Ohlin M (2014). Carbohydrate binding module recognition of xyloglucan defined by polar contacts with branching xyloses and CH-π interactions.
Proteins, 82, 3466-75.
Turnbull AP, Boyd SM & Walse B (2014). Fragment-based drug discovery and protein-protein interactions.
Res. Rep Biochem. 4, 13-26.
Lolli ML, Ducime A, Federico, A Pippione AC, Sainas S, Barge A, Martina K, Boschi D, Lupino E, Piccinini M, Kubbutat M, Schächtele C, Contreras JM, Morice C, Sussman J, Peleg J, Walse B and Al-Kadaraghi S (2014). Towards a Bioisosteric Alkaest: application to the bioisosteric modulation of IMD-0354.
In: Book of Abstracts. p. 234, Lisbon, Portugal, September 7-11. See poster…
Saraboji K, Håkansson M, Genheden S, Diehl C, Qvist J, Weininger U, Nilsson UJ, Leffler H, Ryde U, Akke M & Logan DT. (2012). The Carbohydrate-Binding Site in Galectin-3 Is Preorganized To Recognize a Sugarlike Framework of Oxygens: Ultra-High-Resolution Structures and Water Dynamics.
Biochemistry 2012, 51:296-306.
Humble MS, Cassimjee KE, Håkansson, M, Kimbung YR, Walse B, Abedi V, Federsel H-J, Berglund P & Logan DT (2012). Crystal structures of the Chromobacterium violaceum ω-transaminase reveal major structural rearrangements upon binding of coenzyme PLP.
FEBS J., 279, 779-792.
von Schantz, L., Håkansson, M., Logan, D.T., Walse, B., Osterlin, J., Nordberg-Karlsson, E. and Ohlin, M. (2012). Structural basis for carbohydrate-binding specificity -a comparative assessment of two engineered carbohydrate-binding modules.
Glycobiology, 22, 948-961.
Boyd SM, Turnbull AP and Walse B (2012). Fragment library design considerations.
WIREs Comput. Mol. Sci., 2, 868-885. - 2011-2009 Kasetty G, Papareddy P, Kalle M, Rydengård V, Walse B, Svensson B, Mörgelin M, Malmsten M & Schmidtchen A (2011). The C-terminal sequence of several human serine proteases encodes host defense functions.
J Innate Immun. 3, 471-482.
Svensson SL, Pasupuleti M, Walse B, Malmsten M, Mörgelin M, Sjögren C, Olin AI, Collin M, Schmidtchen A, Palmer R & Egesten A (2010). Midkine and pleiotrophin have bactericidal properties: preserved antibacterial activity in a family of heparin-binding growth factors during evolution.
J Biol Chem. 285, 16105-16115.
Diehl C, Engström O, Delaine T, Håkansson M, Genheden S, Modig K, Leffler H, Ryde U, Nilsson UJ & Akke M (2010). Protein flexibility and conformational entropy in ligand design targeting the carbohydrate recognition domain of galectin-3.
J Am Chem Soc. 132, 14577-1489.
Fritzson I, Svensson B, Al-Karadaghi S, Walse B, Wellmar U, Nilsson UJ, da Graça Thrige D & Jönsson S. (2010).
Inhibition of human DHODH by 4-hydroxycoumarins, fenamic acids, and N-(alkylcarbonyl)anthranilic acids identified by structure-guided fragment selection.
ChemMedChem. 5, 608-617.