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Publications Derek Logan

Logan group publications

ResearcherID: http://www.researcherid.com/rid/A-1114-2011

Google Scholar: http://scholar.google.com/citations?user=7Um2bwQAAAAJ&hl=en

In refereed journals

 

2019

  1. Ruggieri F, Campillo Brocal J, 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., in press.
  2. Grãve K, Lambert W, Berggren G, Griese JJ, Bennett, MD, Logan DT & Högbom M (2019) Redox-induced structural changes in the di-iron and di-manganese forms of Bacillus anthracis ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access. J. Biol. Inorg. Chem. 24, 849-861. doi: 10.1007/s00775-019-01703-z
  3. Rozman Grinberg I, Berglund S, Hasan M, Lundin D, Ho FM, Magnuson A, Logan DT, Sjöberg BM & Berggren G (2019) Class Id ribonucleotide reductase utilizes a Mn2(IV,III) cofactor and undergoes large conformational changes on metal loading. J. Biol. Inorg. Chem., 24, 863-877. doi: 10.1007/s00775-019-01697-8
  4. Caldararu O, Kumar R, Oksanen E, Logan DT & Ryde U (2019) Are crystallographic B-factors suitable for calculating protein conformational entropy? Phys Chem Chem Phys 21, 18149-18160. doi: 10.1039/c9cp02504a 
  5. Kumar R, Misini Ignjatovic M, Peterson K, Olsson M, Leffler H, Ryde U, Nilsson UJ & Logan DT (2019) Structure and energetics of ligand–fluorine interactions with galectin-3 backbone and side-chain amides – insight into solvation effects and multipolar interactions. ChemMedChem4,1528-1536. doi: 10.1002/cmdc.201900293
  6. Bågenholm V, Wiemann M, Reddy SK, Bhattacharya A, Rosengren A, Logan DT & Stålbrand H (2019) A surface exposed GH26 β-mannanase from Bacteroides ovatus: structure, role and phylogenetic analysis of BoMan26B. J. Biol. Chem. 294, 9100-9117. doi: 10.1074/jbc.RA118.007171
  7. Korkmaz B, Lesner A, Wysocka M, Gieldon A, Håkansson M, Gauthier F, Logan DT, Jenne D, 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. doi: 10.1016/j.bcp.2019.04.006
  8. Kracht ON, Correia Cordeiro RS, Håkansson M, Stockmann J, Sander D, Bandow JE, Senges CHR, Logan DT & Kourist R. Discovery of three novel sesquiterpene syntheses from Streptomyces chartreusis NRRL 3882 and crystal structure of an α-eudesmol synthase. Biotech. J. 297, 71–77.doi: 10.1016/j.jbiotec.2019.03.006
  9. Casaletto JB, Geddie M, Abu-Yousif AO, Masson K, Fulgham A, Boudot A, Maiwald T, Kearns JD, Kohli N, Su S, Razlog M, Raue A, Klara A, Håkansson M, Logan DT, Welin M, Chattopadhyay S, Harms BD, Nielsen U, 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. USA 116, 7533–7542. doi: 10.1073/pnas.1819085116.
  10. Awad W, Al-Eryani Y, Ekström S, Logan DT & von Wachenfeldt C (2019) Structural basis for YjbH-mediated recognition of transcription factor Spx. Structure 27, 923–936. doi: 10.1016/j.str.2019.03.009
  11. Caldararu O, Manzoni F, Oksanen E, Logan DT & Ryde U (2019) Refinement of protein structures using a combination of quantum mechanical calculations with neutron and X-ray crystallographic data. Acta Crystallogr. D Biol. Crystallogr., 75, 368–380 doi: 10.1107/ S205979831900175X
  12. Kumar R, Peterson K, Misini Ignjatovic M, Leffler H, Ryde U, Nilsson UJ & Logan DT (2019) Substituted polyfluoroaryl interactions with an arginine side chain in galectin-3 are governed by steric, desolvation and electronic conjugation effects. Org. Biomol. Chem. 17, 1081–1089. doi: 0.1039/c8ob02888e
  13. Verteramo ML, Stenström O, Misini Ignjatovic , Caldararu O, Olsson M, Manzoni F, Leffler H, Oksanen E, Logan DT, Nilsson U, Ryde, U, Akke, M (2019) Interplay between conformational entropy and solvation entropy in protein–ligand binding. J. Am. Chem. Soc. 141, 2012-2026.doi:10.1021/jacs.8b11099.

    2018

  14. Yang F, Wang H, Logan DT, Mu X, Danielsson J & Oliveberg M (2018) The cost of long catalytic loops in folding and stability of the ALS-associated protein SOD1. J. Am. Chem. Soc. 140, 16570-16579. doi: 10.1021/jacs.8b08141
  15. Ruggieri F, van Langen L, Logan DT, Walse B & Berglund P (2018) Transaminase-catalyzed racemization with potential for dynamic kinetic resolutions. ChemCatChem 10, 5012-5018. doi: 10.1021/jacs.8b08141
  16. Manzoni F, Wallerstein J, Schrader T, Ostermann A, Coates L, Akke M, Oksanen E & Logan DT (2018) Elucidation of hydrogen bonding patterns in ligand-free, lactose- and glycerol-bound galectin-3 by neutron crystallography to guide drug design. J. Med. Chem. 61, 4412-4420. doi: 10.1021/acs.jmedchem.8b00081
  17. Awad W, Kjellström S, Svensson Birkedal G, Mani K & Logan DT (2018) Structural and biophysical characterization of human EXTL3: domain organisation, glycosylation and solution structure. Biochemistry 57, 1166-1177. doi: 10.1021/acs.biochem.7b00557
  18. Andersen MCF, Boos I, Kinnaert C, Awan S, Pedersen H, Kracun SK, Lanz G, Rydahl MG, Kjærulff L, Håkansson M, Kimbung R, Logan DT, Gotfredsen C, Willats WGT and Clausen MHH (2018) Synthesis of branched and linera 1,4-linked galactan oligosaccharides Org. Biomol. Chem. 16, 1158-1162.doi: 10.1039/C7OB03035E.
  19. Rozman Grinberg I, Lundin D, Hasan H, Crona M, Jonna CR, Loderer C, Sahlin M, Markova N, Borovok I, Berggren G, Hofer A,Logan DT & Sjöberg BM (2018) Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit. eLife7,e31529  doi: 10.7554/eLife.31529
  20. 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.
  21. Noresson AL, Aurelius O, Öberg CT, Engström O, Sundin AP, Håkansson M, Stenström O, Akke M, Logan DT, Leffler H & Nilsson UJ (2018) Designing interactions by control of protein-ligand complex conformation: tuning arginine-arene interaction geometry for enhanced electrostatic protein-ligand interactions. Chemical Science 9, 1014-1021.doi: 10.1039/C7SC04749E

    2017

  22. Zetterberg FR, Peterson K, Johnsson R, Brimert T, Håkansson M, Logan DT, Leffler H & Nilsson UJ (2017) 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
  23. Linares-Pastén JA, Falck P, Albasri K, Kjellström S, Adlercreutz P, Logan DT & Nordberg Karlsson E (2017) Three-dimensional structures and functional studies of two GH43 arabinofuranosidases from Weissella sp. strain 142 and Lactobacillus brevis. FEBS J. 284, 2019-2036. doi: 10.1111/febs.14101
  24. Kulkarni TS ,Khan S, Villagomez R, Mahmood T, Lindahl S, Logan DT, Linares-Pastén JA & Nordberg Karlsson E (2017)  Crystal structure of β-glucosidase 1A from Thermotoga neapolitana and comparison of active site mutants for hydrolysis of flavonoid glucosides (2017) Proteins85, 872-884. doi:10.1002/prot.25256
  25. Rämisch S, Tillgren V, Aspberg A & Logan DT (2017) Crystal structure of chondroadherin: solving a difficult molecular replacement problem using de novo models. Acta Crystallogr. D. Biol. Crystallogr.,73, 53–63. doi: 10.1107/S205979831601980X 

    2016

  26. Bågenholm V, Reddy SK, Bouraoui H, Morrill J, Kulcinskaja E, Bahr CM, Aurelius O, Rogerts T, Xiao Y, Logan DT, Martens EC, Koropatkin NM & Stålbrand H (2016) Galactomannan catabolism conferred by a polysaccharide utilisation locus of Bacteroides ovatus: enzyme synergy and crystal structure of a β-mannanase. J. Biol. Chem.292, 229-243 doi: jbc.M116.746438
  27. Wang H, Lang L, Logan DT, Danielsson J & Oliveberg M (2016) Tricking a protein to swap strands. J. Am. Chem. Soc. 138, 15571-15579doi: 10.1021/jacs.6b05151
  28. Manzoni F, Saraboji K, Sprenger J, Noresson A-L, Nilsson U, Leffler H, Fisher Z, Schrader T, Ostermann A, Coates L, Blakeley MP, Oksanen O & Logan DT (2016) Perdeuteration, crystallisation, data collection and comparison of five neutron diffraction datasets of human galectin-3C. Acta Crystallogr. D. Biol. Crystallogr.72, 1194-1202. doi: 10.1107/S2059798316015540
  29. 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 dimerisation-induced conformation of the LukGH leukocidin of Staphylococcus aureus for the generation of neutralising antibodies. mAbs8, 1347–1360 doi: 10.1080/19420862.2016.1215791
  30. Lizatovic R, Aurelius O, Stenström O, Drakenberg T, Akke M, Logan DT & André I (2016)  A de novo designed coiled-coil peptide with a reversible pH-induced oligomerization switch. Structure 24, 946–55. doi: 10.1016/j.str.2016.03.027
  31. Johansson R, Jonna VR, Kumar R, Nayeri N, Lundin D, Sjöberg B-M, Hofer A & Logan DT (2016) A novel mode of allosteric activity regulation in a ribonucleotide reductase with double ATP cones. Structure 24, 906–17. doi: 10.1016/j.str.2016.03.025
  32. Nilsson LM, Green LC, Muralidharan SV, Demir D, Welin M, Bhadury J, Logan DT, Walse B & Nilsson JA (2016) Cancer differentiation agent hexametylene bisacetamide inhibits BET bromodomain proteins. Cancer Research 76, 2376–2383 doi: 10.1158/0008-5472.CAN-15-2721

    2015

  33. 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. Biochemistry54, 6435–6438. doi: 10.1021/acs.biochem.5b01058
  34. Danielsson J, Mu X, Lang L, Wang H, Binolfi A, Theillet FX, Bekei B, Logan DT, Selenko P, Wennerström H & Oliveberg M (2015) Thermodynamics of protein destabilisation in live cells. Proc. Natl. Acad. Sci. USA112, 12402–12407. doi: 10.1073/pnas.1511308112
  35. Ohlin M, von Schantz L, Schrader TE, Ostermann A, Logan DT & Fisher SZ (2015) Crystallization, neutron data collection, initial structure refinement and analysis of a xyloglucan heptamer bound to an engineered carbohydrate-binding module from xylanase. Acta Crystallogr. F Struct. Biol. Commun.71, 1072-1077. doi: 10.1107/S2053230X15011383
  36. Awad W, Adamczyk B, Örnros J, Karlsson NG, Mani K, Logan DT (2015) Structural aspects of N-glycosylations and the C-terminal region in human glypican-1. J. Biol. Chem.290, 22991-23008. doi: 10.1074/jbc.M115.660878
  37. Aurelius O, Johansson R, Bågenholm V, Lundin D, Tholander F, Balhuizen A, Beck T, Sahlin M, Sjöberg BM, Mulliez E & Logan DT (2015) The crystal structure of Thermotoga maritima class III ribonucleotide reductase lacks a radical cysteine pre-positioned in the active site. PLoS One10, e0128199. doi: 10.1371/journal.pone.0128199
  38. Lundin D, Berggren G, Logan DT & Sjöberg B-M (2015) The origin and evolution of ribonucleotide reduction. Life (Basel) 5, 604-636. doi: 10.3390/life5010604
  39. Logan DT, Appio R, Fredslund F, Haase D, Martinez F, Nan J, Nardella A, Norén K, Sigfridsson K, Thomas D, Unge J, Balmes O, Carlson S, Ursby T & Thunnissen MMGM (2015) Status of the crystallography beamlines at the MAX IV Laboratory. European Physical Journal: EPJ Plus 130, 1-9. doi: 10.1140/epjp/i2015-15049-9
  40. Badarau A, Rouha H, Malafa S, Logan DT, Håkansson M, Stulik L, Dolezilkova I, Teubenbacher A, Gross K, Maierhofer B, Weber S, Jägerhofer M, Hoffman 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

    2014

  41. von Schantz L, Håkansson M, Logan DT, Nordberg Karlsson E & Ohlin M (2014) Carbohydrate binding module recognition of xyloglucan defined by polar contacts with branching xyloses and CH‐Π interactions. Proteins82, 3466-3475. doi: 10.1002/prot.24700
  42. Rosengren A, Reddy SK, Svantesson Sjöberg J, Aurelius O, Logan DT, Kolenová K & Stålbrand H (2014) An Aspergillus nidulans β-mannanase with high transglycosylation capacity revealed through comparative studies within glycosidase family 5. Appl. Microbiol. Biotechnol.98, 10091-10104; doi: 10.1107/S0907444913025250

    2013

  43. Awad W, Svensson Birkedal G, Thunnissen MMGM, Mani K & Logan DT (2013) Improvements of the order, isotropy and electron density of glypican-1 crystals by controlled dehydration. Acta Crystallogr. Biol. Crystallogr. D69, 2524–2533. doi: 10.1107/S0907444913025250
  44. Ursby T, Unge J, Appio R, Logan DT, Fredslund F, Svensson C, Larsson K, Labrador A & Thunnissen MM (2013) The macromolecular crystallography beamline I911-3 at the MAX IV Laboratory. J. Synchr. Rad. 20, 648–653. doi: 10.1107/S0909049513011734
  45. Thunnissen MMGM, Sondhauss PM, Wallén E, Theodor K, Logan DT, Labrador A, Unge J, Appio R, Fredslund F & Ursby T (2013) BIOMAX: The future macromolecular crystallography beamline at MAX IV. Journal of Physics: Conference Series 425, 072012 doi:10.1088/1742-6596/425/7/072012
  46. Danielsson J, Awad W, Saraboji K, Kurnik M, Lang L, Leinartaité L, Marklund SL, Logan DT & Oliveberg M (2013) Global structural motions from the strain of a single hydrogen bond. Proc. Natl. Acad. Sci. USA110, 3829–34. doi: 10.1073/pnas.1217306110

    2012

  47. von Schantz L, Håkansson M, Logan DT, Walse B, Österlin J, Nordberg Karlsson E & Ohlin M (2012) Structural basis for carbohydrate binding specificity - a comparative assessment of two engineered carbohydrate binding modules. Glycobiology 22, 948-61. doi: 10.1093/glycob/cws063
  48. Svensson G, Awad W, Håkansson M, Mani K & Logan DT (2012) Crystal structure of N-glycosylated human glypican-1 core protein: structure of two loops evolutionarily conserved in vertebrate glypican-1. J. Biol. Chem. 287, 14040–51. doi. 10.1074/jbc.M111.322487
  49. Svedendahl Humble M, Engelmark Cassimjee K, Håkansson M, Kimbung YR, Walse B, Abedi V, Federsel HJ, 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. doi: 10.1111/j.1742-4658.2012.08468.x
  50. Haglund E, Danielsson D, K Saraboji, Lindberg MO, Logan DT & Oliveberg M (2012) Trimming down a protein structure to its bare foldons: spatial organisation of the cooperative unit. J. Biol. Chem. 287, 2731–2738. doi: 10.1074/jbc.M111.312447
  51. 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 pre-organized to recognize a sugar-like framework of oxygens: ultra-high resolution structures and water dynamics. Biochemistry 51, 296–306. doi: 10.1021/bi201459p

    2011 and earlier

  52. Ofer A, Yanku M, Gorovitz-Harris B, Kreft J, Logan DT, Cohen G, Borovok I & Aharonowitz A (2011) Listeria monocytogenes EGD-e is unable to grow anaerobically due to a deletion in the class III NrdD ribonucleotide reductase: implications for its use as a model laboratory strain. J. Bacteriol. 193,2931–2940. doi: 10.1128/JB.01405-10
  53. Wang E, Ikonen TP, Knaapila M, Svergun D, Logan DT & von Wachenfeldt C (2011) Small angle X-ray scattering study of the transcriptional repressor Rex from Bacillus subtilis. Conformational response to NADH and NAD+ binding in solution. J. Mol. Biol. 408, 670–83. doi: doi: 10.1016/j.jmb.2011.02.050
  54. Leinartaité L, Saraboji K, Nordlund A, Logan DT & Oliveberg M (2010) Folding catalysis by transient coordination of Zn2+ to the the Cu ligands of the ALS-associated enzyme SOD1. J. Am. Chem. Soc. 132, 13495–13504. doi:10.1021/ja1057136
  55. Johansson R, Torrents E, Lundin D, Sprenger J, Sahlin M, Sjöberg B-M & Logan DT (2010) High resolution structures of the flavoprotein NrdI in oxidised and reduced states: an unusual flavoxodin. FEBS J. 277, 4265–4277. doi: 10.1111/j.1742-4658.2010.07815.x
  56. Larsson KM, Logan DT & Nordlund P (2010) Structural basis for adenosylcobalamin activation in AdoCbl-dependent ribonucleotide reductases. ACS Chem. Biol. 5, 933–942. doi: 10.1021/cb1000845 
  57. Pozzo T, Linares-Pasten J, Nordberg Karlsson E & Logan DT (2010) Structural and functional analyses of β-glucosidase 3B from Thermotoga neapolitana: a thermostable three-domain representative of glycoside hydrolase 3. J. Mol. Biol.397, 724–739. doi: 10.1021/cb1000845
  58. Krintel C, Mörgelin M, Logan DT & Holm C (2009) Phosphorylation of hormone-sensitive lipase by protein kinase A in vitro promotes an increase in its hydrophobic surface area. FEBS J. 276, 4752–4762. doi: 10.1111/j.1742-4658.2009.07172.x
  59. Nordlund A, Leinartaité L, Saraboji K, Aisenbrey C, Gröbner G, Danielsson J, Logan DT & Oliveberg M (2009) Functional features cause misfolding of the ALS-provoking enzyme SOD1. Proc. Natl. Acad. Sci. U.S.A. 106, 9667–9672. doi: 10.1073/pnas.0812046106
  60. Krintel C, Osmark P, Larsen MR, Resjö S, Logan DT & Holm C (2008) Ser 649 and Ser650 are the major determinants of protein kinase A-mediated activation of human hormone-sensitive lipase against lipid substrates. PLoS ONE 3:e3756. doi: 10.1371/journal.pone.0003756
  61. Pramhed A, Addis L, Tillgren V, Wenglén C, Heinegård D & Logan DT (2008) Purification, crystallisation and preliminary diffraction analysis of human chondroadherin. Acta Cryst. F64, 516–9. doi: 10.1107/S1744309108012141
  62. Wang E, Bauer M, Rogstam A, Linse S, Logan DT & von Wachenfeldt C (2008) Structure and functional properties of the Bacillus subtilis transcriptional repressor Rex. Mol. Microbiol. 69, 466–478. doi: 10.1111/j.1365-2958.2008.06295.x
  63. Turner P, Pramhed A, Kanders E, Hedström M, Nordberg-Karlsson E & Logan DT (2007) Expression, purification, crystallization and preliminary X-ray diffraction analysis of Thermotoga maritima β-glucosidase B. Acta Cryst. F63, 702–706. doi: 10.1107/S1744309108012141
  64. Olofsson M, Hansson S, Hedberg L, Logan DT & Oliveberg M (2007) Folding of S6 structures with divergent amino-acid composition:  pathway flexibility within the bounds of partly overlapping foldons. J. Mol. Biol, 365, 237–248. doi: 10.1016/j.jmb.2006.09.016
  65. Hörnberg A, Logan DT, Marklund SL & Oliveberg M (2007) The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase. J. Mol. Biol. 365, 333–342. doi: 10.1016/j.jmb.2006.09.048
  66. Hansson S, Singh R, Gudkov AT, Liljas A & Logan DT (2005) Crystal structure of a mutant elongation factor G trapped with a GTP analogue. FEBS Letters579, 4492–4497. doi: 10.1016/j.febslet.2005.07.016
  67. Hansson S, Singh R, Gudkov AT, Liljas A & Logan DT (2005) Structural insights into fusidic acid sensitivity and resistance in EF-G. J. Mol. Biol.348, 939–949. doi: 10.1016/j.jmb.2005.02.066
  68. Poole AM & Logan DT (2005): Modern mRNA proofreading and repair: proof that the last universal common ancestor (LUCA) had an RNA genome? Mol. Biol. Evol. 22, 1444–1455. doi: 10.1093/molbev/msi132
  69. Kolberg M, Logan DT, Bleifuss G, Potsch S, Sjöberg BM, Gräslund A, Lubitz W, Lassmann G & Lendzian F (2005) A new tyrosyl radical on F208 as ligand to the diiron center in E. coli ribonucleotide reductase, mutant R2-Y122H: Combined X-ray diffraction, and EPR/ENDOR studies. J. Biol. Chem,280, 11233–11246. doi: 10.1074/jbc.M414634200
  70. Ursby T, Mammen CB, Cerenius Y, Svensson C, Sommarin B, Fodje, MN, Kvick, Å, Logan DT, Als-Nielsen J, Thunnissen, MMGM, Larsen S & Liljas A (2004) The new macromolecular crystallography stations at MAX-lab: The MAD Station. AIP Conference Proceedings, 705, 1241-1246. doi: 10.1063/1.1758025
  71. Larsson K-M, Eliasson R, Jordan A, Reichard P, Logan DT& Nordlund P (2004) Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase. Nat. Struct. Mol. Biol.11, 1142–1149. doi: 10.1038/nsmb838
  72. Lundell A, Olin AI, al-Karadaghi S, Mörgelin M, Aspberg A & Logan DT (2004) Structural basis for the interactions between tenascins and lectican C-type lectin domains: evidence for a cross-linking role for tenascins. Structure12, 1495–1506. doi:10.1016/j.str.2004.05.021
  73. Logan DT, Mulliez E, Larsson K-M, Bodevin S, Atta M, Garnaud PE, Sjöberg BM & Fontecave M (2003) A metal binding site in the catalytic subunit of anaerobic ribonucleotide reductase. Proc. Natl. Acad. Sci. U.S.A 100, 3826–3831. DOI: 10.1073/pnas.0736456100
  74. Poole AM, Logan DT & Sjöberg B-M(2002)Evolution of the ribonucleotide reductases: much ado about oxygen. J. Mol. Evolution55, 180–96. DOI: 10.1007/s00239-002-2315-3
  75. Larsson K-M, Andersson J, Sjöberg B-M, Nordlund P & Logan DT (2001) Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases. Structure9, 739–750. doi: 10.1016/S0969-2126(01)00627-X
  76. Logan DT, Andersson J, Sjöberg, BM & Nordlund P (1999) A glycyl radical site in the crystal structure of a class III anaerobic ribonucleotide reductase. Science 283, 1499–1504. DOI: 10.1126/science.283.5407.1499
  77. Logan DT, Persson BO, deMaré F, Slaby A, & Nordlund P (1998) Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: Structural basis for the oxygen insertion step of hydroxylation reactions catalysed by diiron proteins. Biochemistry37, 10798–10807. DOI: 10.1021/bi9806403 
  78. Mazauric M-H, Keith G, Logan DT, Kreutzer R, Giegé R & Kern D (1998) Glycyl-tRNA synthetase from Thermus thermophilus. Wide structural divergence with other prokaryotic glycyl-tRNA synthetases and functional inter-relation with prokaryotic and eukaryotic glycylation systems. Eur. J. Biochem. 251, 744–757. DOI: 10.1046/j.1432-1327.1998.2510744.x
  79. Katterle B, Sahlin M, Schmidt PP, Pötsch S, Logan D, Gräslund A & Sjöberg B-M (1997) Kinetics of transient radicals in Escherichia coli ribonucleotide reductase: Formation of a new tyrosyl radical in mutant protein R2 J. Biol. Chem.272 10414–10421. DOI: 10.1074/jbc.272.16.10414
  80. Gauss D, Logan DT & Freist, W (1996) Glycyl-tRNA synthetase. Biological Chemistry Hoppe-Seyler377, 343–356.
  81. Logan DT, Su XD, Åberg A, Regnström K, Hajdu J, Eklund H & Nordlund P (1996) Structure of the reduced protein R2 of ribonucleotide reductase: structural basis for activation at a di-iron site. Structure4, 1053–1064. DOI: S0969-2126(96)00112-8
  82. Logan DT, Mazauric MH, Kern D & Moras D (1995) Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus. EMBO J.14, 4145–4167. DOI: 1460-2075.1995.tb00089.x
  83. Lea S, Abu-Ghazaleh R, Blakemore W, Curry S, Fry E, Jackson T, King A, Logan D, Newman J & Stuart D (1995) Structural comparison of two strains of foot-and-mouth disease virus subtype O1 and a laboratory antigenic variant, G67. Structure3, 571–580. DOI: 10.1016/S0969-2126(01)00191-5
  84. Logan DT, Cura V, Touzel  JP, Kern D & Moras D (1994)  Crystallisation of the glycyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data. J. Mol. Biol. 241, 732–735. DOI: 10.1006/jmbi.1994.1547
  85. Logan D, Abu-Ghazaleh R, Blakemore W, Curry S, Jackson T, King A, Lea S, Lewis R, Newman J, Parry N, Rowlands D, Stuart D & Fry E (1993) Structure of a major immunogenic site on foot-and-mouth disease virus. Nature362, 566–568. DOI: 10.1038/362566a0
  86. Curry S, Abu-Ghazaleh R, Blakemore W, Fry E, Jackson T, King A, Lea S, Logan D, Newman J &  Stuart D (1992) Crystallization and preliminary X-ray analysis of three serotypes of foot-and-mouth disease virus. J. Mol. Biol. 228, 1263–1268. DOI: 10.1016/0022-2836(92)90332-e
  87. Davey RJ, Black SN, Logan D, Maginn SJ, Fairbrother JE & Grant DJW (1992) Structural and kinetic features of crystal-growth inhibition - adipic acid growing in the presence of n-alkanoic acids. J. Chem. Soc Faraday Trans.88, 3461–3466. DOI: 10.1039/FT9928803461
  88. Parry N, Fox G, Rowlands D, Brown F, Fry E, Acharya R, Logan D & Stuart D (1990) Structural and serological evidence for a novel mechanism of antigenic variation in foot-and-mouth disease virus. Nature347, 569–572. DOI: 10.1038/347569a0

 

Reviews/proceedings/invited articles

  1. Logan DT (2019) Hunting down hydrogens: applying neutron crystallography to understand ligand bindin in galectins. Invited article, The Biochemist, April 2019.
  2. Awad W, Logan DT & Mani K (2014) GPC1 (glypican 1), in Atlas of Genetics and Cytogenetics in Oncology and Haematology, ed. J-L Huret, INIST-CNRS, Toulouse, France.
  3. Hofer A, Crona M, Logan DT & Sjöberg B-M (2012) DNA building blocks: keeping control of manufacture. Crit. Rev. Biochem. Mol. Biol. 47, 50–63. DOI: 10.3109/10409238.2011.630372
  4. Logan DT (2011) Closing the circle on ribonucleotide reductases. Nature Struct. Mol. Biol.18, 251–3. DOI: 10.1038/nsmb0311-251
  5. Fontecave M, Mulliez E & Logan DT (2002) Deoxyribonucleotide synthesis in anaerobic organisms: the class III ribonucleotide reductase. Progress in Nucleic Acids Research and Molecular Biology72, 95–127.
  6. Eklund H, Färnegårdh M, Uhlin U, Logan DT & Nordlund  P (2001) Structure and function of the radical enzyme ribonucleotide reductase. Prog. Biochem. Biophys. 77, 177–268. DOI: 10.1016/S0079-6107(01)00014-1
  7. Eklund H, Eriksson M, Uhlin U, Nordlund P & Logan D. (1997) Ribonucleotide reductase - structural studies of a radical enzyme. Biological Chemistry378, 821–825. 
  8. Rowlands, D, Logan D, Abu-Ghazaleh R, Blakemore W, Curry S, Jackson T, King A, Lea S, Lewis R, Newman J, Parry N, Stuart D & Fry E (1994) The structure of an immunodominant loop on foot-and-mouth disease virus, serotype O1, determined under reducing conditions. Arch. Virol. 9, 51–58.
  9. Fry E, Logan D, Acharya R, Fox G, Rowlands D, Brown F & Stuart D (1990) Architecture and topography of an aphthovirus. Seminars in Virology  1, 439–451.

 

Book chapters

  1. Logan DT (2008) Anaerobic ribonucleotide reductases: recent progress in understanding. In "Ribonucleotide reductase (ed. K.K. Andersson), "Molecular Anatomy and Physiology of Proteins" series, Nova Science Publishers, Hauppauge, NY.
  2. Fry E, Logan D & Stuart D (1996) Virus Crystallography, in Methods in Molecular Biology, Volume 56 – Crystallographic methods and protocols, ed. C. Jones, B. Mulloy & M.A. Sanderson. New Jersey: Humana Press Inc.
  3. Acharya R, Fry E, Logan D, Stuart D, Fox G, Rowlands D & Brown F (1990) The structure of foot-and-mouth disease virus, in The use of X-ray Crystallography in the design of anti-viral agents, ed. W.G. Laver & G. Air, Academic Press, Inc.
  4. Acharya R, Fry E, Logan D, Stuart D, Brown F, Fox G & Rowlands D (1990) Some observations on the three-dimensional structure of foot-and-mouth disease virus, in New Aspects of Positive-strand RNA Viruses, ed. MA Brinton & FX Heinz, American Society for Microbiology.