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Frank Wien

Wikidata Item | Scholia Profile [curation] | Reasonator | SQID

Listed Publications

49 publications found

TitleAuthors (identified)Published InIdentifier(s)TopicPublished Date
Amyloid-like Hfq interaction with single-stranded DNA: involvement in recombination and replication in Escherichia coli[1]Krzysztof Kubiak, [2]Frank Wien, [3]Indresh Yadav, [4]Nykola C. Jones, [5]Søren Vrønning Hoffmann, [6]Eric Le Cam, [7]Antoine Cossa, [8]Frederic Geinguenaud, [9]Johan Rc Van Der Maarel, [10]Grzegorz Węgrzyn, [11]Véronique Arluison [Full author list]QRB Discovery [curation]DOI: 10.1017/QRD.2022.15
Escherichia coli [curation]2022-01-01
Crucial Role of the C-Terminal Domain of Hfq Protein in Genomic Instability[1]Virali J Parekh, [2]Frank Wien, [3]Wilfried Grange, [4]Thomas A De Long, [5]Véronique Arluison, [6]Richard R Sinden [Full author list]Microorganisms [curation]DOI: 10.3390/MICROORGANISMS8101598
PubMed: 33080799
2020-10-17
Interactions between DNA and the Hfq Amyloid-like Region Trigger a Viscoelastic Response[1]Omar El Hamoui, [2]Indresh Yadav, [3]Milad Radiom, [4]Frank Wien, [5]Jean-Francois Berret, [6]Johan Rc Van Der Maarel, [7]Véronique Arluison [Full author list]Biomacromolecules [curation]DOI: 10.1021/ACS.BIOMAC.0C00747
PubMed: 32786728
2020-08-10
In Situ Analysis of Weakly Bound Proteins Reveals Molecular Basis of Soft Corona Formation[1]Daniel Sanchez-Guzman, [2]Gaël Giraudon-Colas, [3]Laurent Marichal, [4]Yves Boulard, [5]Frank Wien, [6]Jéril Degrouard, [7]Armelle Baeza-Squiban, [8]Serge Pin, [9]Jean Philippe Renault, [10]Stéphanie Devineau [Full author list]ACS Nano [curation]DOI: 10.1021/ACSNANO.0C04165
PubMed: 32633939
2020-07-07
Human Serum Albumin in the Presence of AGuIX Nanoagents: Structure Stabilisation without Direct Interaction[1]Xiaomin Yang, [1-Q91440067]Xiaomin Yang, [10]Frank Wien, [10-Q51557662]Frank Wien, [2]Marta Bolsa-Ferruz, [3]Laurent Marichal, [4]Erika Porcel, [5]Daniela Salado-Leza, [6]François Lux, [7]Olivier Tillement, [8]Jean-Philippe Renault, [11]Sandrine Lacombe, [2-Q97411429]Marta Bolsa-Ferruz, [3-Q88205659]Laurent Marichal, [4-Q89975519]Erika Porcel, [5-Q87888740]Daniela Salado-Leza, [9]Serge Pin [Full author list]International Journal of Molecular Sciences [curation]DOI: 10.3390/IJMS21134673
PubMed: 32630060
2020-06-30
Albumin-driven disassembly of lipidic nanoparticles: the specific case of the squalene-adenosine nanodrug[1]Frédéric Gobeaux, [2]Joëlle Bizeau, [3]Firmin Samson, [4]Laurent Marichal, [5]Isabelle Grillo, [6]Frank Wien, [7]Semen O. Yesylevskyy, [8]Christophe Ramseyer, [9]Marie Rouquette, [10]Sinda Lepêtre-Mouelhi, [11]Didier Desmaële, [12]Patrick Couvreur, [13]Patrick Guenoun, [14]Jean-Philippe Renault, [15]Fabienne Testard [Full author list]Nanoscale [curation]DOI: 10.1039/C9NR06485K
PubMed: 31961354
2020-01-21
Application of Synchrotron Radiation Circular Dichroism for RNA Structural Analysis[1]Etienne Le Brun, [2]Véronique Arluison, [3]Frank Wien [Full author list]Methods in Molecular Biology [curation]DOI: 10.1007/978-1-0716-0278-2_11
PubMed: 32006313
synchrotron radiation [curation]; RNA analysis [curation]2020-01-01
Role of Hfq in Genome Evolution: Instability of G-Quadruplex Sequences in E. coli[1]Virali J Parekh, [2]Brittany A Niccum, [3]Rachna Shah, [4]Marisa A Rivera, [5]Mark J Novak, [6]Frederic Geinguenaud, [7]Frank Wien, [8]Véronique Arluison, [9]Richard R Sinden [Full author list]Microorganisms [curation]DOI: 10.3390/MICROORGANISMS8010028
PubMed: 31877879
Escherichia coli [curation]2019-12-22
The Bacterial Amyloid-Like Hfq Promotes In Vitro DNA Alignment[1]Frank Wien, [2]Denis Martinez, [3]Etienne Le Brun, [4]Nykola C. Jones, [5]Søren Vrønning Hoffmann, [6]Jehan Waeytens, [7]Melanie Berbon, [8]Birgit Habenstein, [9]Véronique Arluison [Full author list]Microorganisms [curation]DOI: 10.3390/MICROORGANISMS7120639
PubMed: 31816864
2019-12-03
Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization[1]François Auvray, [2]David Dennetiere, [3]Alexandre Giuliani, [4]Frédéric Jamme, [5]Frank Wien, [6]Bastien Nay, [7]Séverine Zirah, [8]François Polack, [9]Claude Menneglier, [10]Bruno Lagarde, [11]Jonathan D. Hirst, [12]Matthieu Réfrégiers [Full author list]Structural dynamics (Melville, N.Y.) [curation]DOI: 10.1063/1.5120346
PubMed: 31700943
2019-09-01
In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study[1]David Partouche, [2]Valeria Militello, [3]Andrea Gómez-Zavaglia, [4]Frank Wien, [5]Christophe Sandt, [6]Véronique Arluison [Full author list]Pathogens [curation]DOI: 10.3390/PATHOGENS8010036
PubMed: 30889801
infrared spectroscopy [curation]; FTIR [curation]2019-03-18
Epigallocatechin Gallate Remodelling of Hfq Amyloid-Like Region Affects Survival[1]David Partouche, [2]Florian Turbant, [3]Omar El Hamoui, [4]Camille Campidelli, [5]Marianne Bombled, [6]Sylvain Trépout, [7]Frank Wien, [8]Véronique Arluison [Full author list]Pathogens [curation]DOI: 10.3390/PATHOGENS7040095
PubMed: 30513780
2018-12-01
Reversible Assembly of a Drug Peptide into Amyloid Fibrils: A Dynamic Circular Dichroism Study[1]Frédéric Gobeaux, [2]Frank Wien [Full author list]Langmuir [curation]DOI: 10.1021/ACS.LANGMUIR.8B00094
PubMed: 29772895
2018-06-05
Techniques to Analyze sRNA Protein Cofactor Self-Assembly In Vitro[1]David Partouche, [2]Antoine Malabirade, [3]Thomas Bizien, [4]Marisela Velez, [5]Sylvain Trépout, [6]Sergio Marco, [7]Valeria Militello, [8]Christophe Sandt, [9]Frank Wien, [10]Véronique Arluison [Full author list]Methods in Molecular Biology [curation]DOI: 10.1007/978-1-4939-7634-8_18
PubMed: 29484601
2018-01-01
Conversion of NOX2 into a constitutive enzyme in vitro and in living cells, after its binding with a chimera of the regulatory subunits[1]Rawand Masoud, [2]Xavier Serfaty, [3]Marie Erard, [4]Paul Machillot, [5]Gilda Karimi, [6]Elodie Hudik, [7]Frank Wien, [8]Laura Baciou, [9]Chantal Houée-Levin, [10]Tania Bizouarn [Full author list]Free Radical Biology and Medicine [curation]DOI: 10.1016/J.FREERADBIOMED.2017.10.376
PubMed: 29079525
2017-10-24
Structural proteomics: Topology and relative accessibility of plant lipid droplet associated proteins[1]Pascale Jolivet, [2]Laure Aymé, [3]Alexandre Giuliani, [4]Frank Wien, [5]Thierry Chardot, [6]Yann Gohon [Full author list]Journal of Proteomics [curation]DOI: 10.1016/J.JPROT.2017.09.005
PubMed: 28918933
2017-09-14
Membrane association of the bacterial riboregulator Hfq and functional perspectives[1]Antoine Malabirade, [2]Javier Morgado-Brajones, [3]Sylvain Trépout, [4]Frank Wien, [5]Ileana Marquez, [6]Jérôme Seguin, [7]Sergio Marco, [8]Marisela Velez, [9]Véronique Arluison [Full author list]Scientific Reports [curation]DOI: 10.1038/S41598-017-11157-5
PubMed: 28878270
2017-09-06
A Reactive Eremophilane and Its Antibacterial 2(1H)-Naphthalenone Rearrangement Product, Witnesses of a Microbial Chemical Warfare[1]Séverine Amand, [2]Marine Vallet, [3]Laura Guedon, [4]Grégory Genta-Jouve, [5]Frank Wien, [6]Stéphane Mann, [7]Joëlle Dupont, [8]Soizic Prado, [9]Bastien Nay [Full author list]Organic Letters [curation]DOI: 10.1021/ACS.ORGLETT.7B01788
PubMed: 28737947
Paraconiothyrium variabile [curation]; Didymosphaeria variabile [curation]; Variabilone [curation]; 4-Epi-microsphaeropsisin [curation]2017-07-24
Chiroptical properties of cryptophane-111[1]Thierry Buffeteau, [2]Delphine Pitrat, [3]Nicolas Daugey, [4]Nathalie Calin, [5]Marion Jean, [6]Nicolas Vanthuyne, [7]Laurent Ducasse, [8]Frank Wien, [9]Thierry Brotin [Full author list]Physical Chemistry Chemical Physics [curation]DOI: 10.1039/C7CP02045G
PubMed: 28676874
2017-07-01
Unusual Chiroptical Properties of the Cryptophane-222 Skeleton[1]Delphine Pitrat, [2]Nicolas Daugey, [3]Marion Jean, [4]Nicolas Vanthuyne, [5]Frank Wien, [6]Laurent Ducasse, [7]Nathalie Calin, [8]Thierry Buffeteau, [9]Thierry Brotin [Full author list]Journal of Physical Chemistry B [curation]DOI: 10.1021/ACS.JPCB.6B09771
PubMed: 27973824
2016-11-30
Refolding of Aggregation-Prone ScFv Antibody Fragments Assisted by Hydrophobically Modified Poly(sodium acrylate) Derivatives.[1]Nicolas Martin, [2]Narciso Costa, [3]Frank Wien, [4]Françoise Winnik, [5]Céline Ortega, [6]Amaury Herbet, [7]Didier Boquet, [8]Christophe Tribet [Full author list]Macromolecular Bioscience [curation]DOI: 10.1002/MABI.201600213
PubMed: 27548824
refolding [curation]; hydrophobicity [curation]2016-08-22
The physicochemical properties of membranes correlate with the NADPH oxidase activity[1]Hager Souabni, [2]Frank Wien, [3]Tania Bizouarn, [4]Chantal Houée-Levin, [5]Matthieu Réfrégiers, [6]Laura Baciou [Full author list]BBA - General Subjects [curation]DOI: 10.1016/J.BBAGEN.2016.06.028
PubMed: 27378459
2016-07-02
Structure Change from β-Strand and Turn to α-Helix in Histone H2A-H2B Induced by DNA Damage Response[1]Yudai Izumi, [2]Kentaro Fujii, [3]Frank Wien, [4]Chantal Houée-Lévin, [5]Sandrine Lacombe, [6]Daniela Salado-Leza, [7]Erika Porcel, [8]Rawand Masoud, [9]Satoshi Yamamoto, [10]Matthieu Réfrégiers, [11]Marie-Anne Hervé du Penhoat, [12]Akinari Yokoya [Full author list]Biophysical Journal [curation]DOI: 10.1016/J.BPJ.2016.06.002
PubMed: 27410735
DNA damage [curation]2016-07-01
Exploring the arachidonic acid-induced structural changes in phagocyte NADPH oxidase p47(phox) and p67(phox) via thiol accessibility and SRCD spectroscopy.[1]Tania Bizouarn, [2]Gilda Karimi, [3]Rawand Masoud, [4]Hager Souabni, [5]Paul Machillot, [6]Xavier Serfaty, [7]Frank Wien, [8]Matthieu Réfrégiers, [9]Chantal Houée-Levin, [10]Laura Baciou [Full author list]FEBS Journal [curation]DOI: 10.1111/FEBS.13779
PubMed: 27284000
2016-06-10
Can Changes in Temperature or Ionic Conditions Modify the DNA Organization in the Full Bacteriophage Capsid?[1]Marta de Frutos, [2]Amélie Leforestier, [3]Jéril Degrouard, [4]Nebraska Zambrano, [5]Frank Wien, [6]Pascale Boulanger, [7]Sandrine Brasilès, [8]Madalena Renouard, [9]Dominique Durand, [10]Françoise Livolant [Full author list]Journal of Physical Chemistry B [curation]DOI: 10.1021/ACS.JPCB.6B01783
PubMed: 27152667
bacteriophage [curation]2016-05-06
Combination of acoustic levitation with small angle scattering techniques and synchrotron radiation circular dichroism. Application to the study of protein solutions[1]Viviana Cristiglio, [2]Isabelle Grillo, [3]Margarita Fomina, [4]Frank Wien, [5]Evgenyi Shalaev, [6]Alexey N. Novikov, [7]Séverine Brassamin, [8]Matthieu Réfrégiers, [9]Javier Pérez, [10]Louis Hennet [Full author list]Biochimica et Biophysica Acta [curation]DOI: 10.1016/J.BBAGEN.2016.04.026
PubMed: 27155578
synchrotron radiation [curation]2016-05-04
Titanium Dioxide Nanoparticles Increase Superoxide Anion Production by Acting on NADPH Oxidase[1]Rawand Masoud, [2]Tania Bizouarn, [3]Sylvain Trépout, [4]Frank Wien, [5]Laura Baciou, [6]Sergio Marco, [7]Chantal Houée Levin [Full author list]PLOS One [curation]DOI: 10.1371/JOURNAL.PONE.0144829
PubMed: 26714308
titanium [curation]; nanoparticle [curation]2015-12-29
Neurodegenerative disease-associated mutants of a human mitochondrial aminoacyl-tRNA synthetase present individual molecular signatures[1]Claude Sauter, [2]Bernard Lorber, [3]Agnès Gaudry, [4]Loukmane Karim, [5]Hagen Schwenzer, [6]Frank Wien, [7]Pierre Roblin, [8]Catherine Florentz, [9]Marie Sissler [Full author list]Scientific Reports [curation]DOI: 10.1038/SREP17332
PubMed: 26620921
neurodegeneration [curation]2015-12-01
Structural Basis of IgE Binding to α- and γ-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains.[1]Hamza Mameri, [2]Chantal Brossard, [3]Jean-Charles Gaudin, [4]Yann Gohon, [5]Evelyne Paty, [6]Etienne Beaudouin, [7]Denise-Anne Moneret-Vautrin, [8]Martine Drouet, [9]Véronique Solé, [10]Frank Wien, [11]Roberta Lupi, [12]Colette Larré, [13]Jacques Snégaroff, [14]Sandra Denery-Papini [Full author list]Journal of Agricultural and Food Chemistry [curation]DOI: 10.1021/ACS.JAFC.5B01922
PubMed: 26186140
2015-07-17
Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy[1]András Micsonai, [2]Frank Wien, [3]Linda Kernya, [4]Young-Ho Lee, [5]Yuji Goto, [6]Matthieu Réfrégiers, [7]József Kardos [Full author list]Proceedings of the National Academy of Sciences of the United States of America [curation]DOI: 10.1073/PNAS.1500851112
PubMed: 26038575
spectroscopy [curation]2015-06-02
RRP6 from Trypanosoma brucei: crystal structure of the catalytic domain, association with EAP3 and activity towards structured and non-structured RNA substrates[1]Rosicler L Barbosa, [2]Pierre Legrand, [3]Frank Wien, [4]Blandine Pineau, [5]Andrew Thompson, [6]Beatriz G Guimarães [Full author list]PLOS One [curation]DOI: 10.1371/JOURNAL.PONE.0089138
PubMed: 24558481
Trypanosoma brucei [curation]; crystal structure [curation]2014-02-18
Fold of an oleosin targeted to cellular oil bodies[1]Jean-David Vindigni, [2]Frank Wien, [3]Alexandre Giuliani, [4]Zoi Erpapazoglou, [5]Roselyne Tache, [6]Franjo Jagic, [7]Thierry Chardot, [8]Yann Gohon, [9]Marine Froissard [Full author list]Biochimica et Biophysica Acta [curation]DOI: 10.1016/J.BBAMEM.2013.04.009
PubMed: 23603223
2013-04-17
The single T65S mutation generates brighter cyan fluorescent proteins with increased photostability and pH insensitivity[1]Asma Fredj, [2]Hélène Pasquier, [3]Isabelle Demachy, [4]Gabriella Jonasson, [5]Bernard Levy, [6]Valérie Derrien, [7]Yasmina Bousmah, [8]Gallia Manoussaris, [9]Frank Wien, [10]Jacqueline Ridard, [11]Marie Erard, [12]Fabienne Merola [Full author list]PLOS One [curation]DOI: 10.1371/JOURNAL.PONE.0049149
PubMed: 23133673
2012-11-02
Immunoglobulin-E reactivity and structural analysis of wheat low-molecular-weight glutenin subunits and their repetitive and nonrepetitive halves[1]Hamza Mameri, [2]Jacques Snégaroff, [3]Yann Gohon, [4]Catherine Pecquet, [5]Dominique Choudat, [6]Nadia Raison-Peyron, [7]Sandra Denery-Papini, [8]Frank Wien, [9]Pierre Briozzo [Full author list]Journal of Agricultural and Food Chemistry [curation]DOI: 10.1021/JF3007568
PubMed: 22747247
wheat [curation]2012-07-17
New insights into pb5, the receptor binding protein of bacteriophage T5, and its interaction with its Escherichia coli receptor FhuA[1]Ali Flayhan, [2]Frank Wien, [3]Maïté Paternostre, [4]Pascale Boulanger, [5]Cécile Breyton [Full author list]Biochimie [curation]DOI: 10.1016/J.BIOCHI.2012.05.021
PubMed: 22659573
Escherichia coli [curation]; bacteriophage [curation]2012-05-29
Anisotropy spectra of amino acids[1]Cornelia Meinert, [2]Jan Hendrik Bredehöft, [3]Jean-Jacques Filippi, [4]Yannick Baraud, [5]Laurent Nahon, [6]Frank Wien, [7]Nykola C. Jones, [8]Søren Vrønning Hoffmann, [9]Uwe Meierhenrich [Full author list]Angewandte Chemie International Edition [curation]DOI: 10.1002/ANIE.201108997
PubMed: 22438137
catalysis [curation]; general chemistry [curation]2012-03-21
Amphipols from A to Z[1]J-L Popot, [2]Thorsten Althoff, [3]Dominique Bagnard, [4]J-L Banères, [5]P Bazzacco, [6]E Billon-Denis, [7]L J Catoire, [8]P Champeil, [9]D Charvolin, [10]M J Cocco, ..., [27]Christophe Tribet, [28]Carine van Heijenoort, [29]Frank Wien, [30]Francesca Zito, [31]M Zoonens [Full author list]Annual Review of Biophysics [curation]DOI: 10.1146/ANNUREV-BIOPHYS-042910-155219
PubMed: 21545287
2011-01-01
High water solubility and fold in amphipols of proteins with large hydrophobic regions: oleosins and caleosin from seed lipid bodies[1]Yann Gohon, [2]Jean-David Vindigni, [3]Agnès Pallier, [4]Frank Wien, [5]Hervé Celia, [6]Alexandre Giuliani, [7]Christophe Tribet, [8]Thierry Chardot, [9]Pierre Briozzo [Full author list]Biochimica et Biophysica Acta [curation]DOI: 10.1016/J.BBAMEM.2010.12.002
PubMed: 21146495
protein folding [curation]; hydrophobicity [curation]2010-12-10
Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural context[1]Luc Bousset, [2]Jonathan Bonnefoy, [3]Yannick Sourigues, [4]Frank Wien, [5]Ronald Melki [Full author list]PLOS One [curation]DOI: 10.1371/JOURNAL.PONE.0009760
PubMed: 20339590
prion protein family [curation]2010-03-22
Spatio-temporal radiation biology: new insights and biomedical perspectives[1]S Lacombe, [2]Laure Sabatier, [3]Frank Wien, [4]Y A Gauduel [Full author list]Cell Death and Disease [curation]DOI: 10.1038/CDDIS.2009.5
PubMed: 21364623
radiobiology [curation]2010-01-01
DISCO: a low-energy multipurpose beamline at synchrotron SOLEIL.[1]Alexandre Giuliani, [2]Frédéric Jamme, [3]Valérie Rouam, [4]Frank Wien, [5]Jean-Luc Giorgetta, [6]Bruno Lagarde, [7]Oleg Chubar, [8]Stéphane Bac, [9]Isabelle Yao, [10]Solène Rey, [11]Christian Herbeaux, [12]Jean-Louis Marlats, [13]Daniel Zerbib, [14]François Polack, [15]Matthieu Réfrégiers [Full author list]Journal of Synchrotron Radiation [curation]DOI: 10.1107/S0909049509034049
PubMed: 19844021
2009-09-10
A reference database for circular dichroism spectroscopy covering fold and secondary structure space[1]Jonathan G Lees, [2]Andrew J. Miles, [3]Frank Wien, [4]Bonnie Ann Wallace [Full author list]Bioinformatics [curation]DOI: 10.1093/BIOINFORMATICS/BTL327
PubMed: 16787970
database [curation]; spectroscopy [curation]2006-06-20
VUV irradiation effects on proteins in high-flux synchrotron radiation circular dichroism spectroscopy[1]Frank Wien, [2]Miles AJ, [3]Lees JG, [4]Vrønning Hoffmann S, [5]Bonnie Ann Wallace [Full author list]Journal of Synchrotron Radiation [curation]DOI: 10.1107/S0909049505006953
PubMed: 15968132
synchrotron radiation [curation]2005-06-15
Redetermination of the extinction coefficient of camphor-10-sulfonic acid, a calibration standard for circular dichroism spectroscopy[1]Andrew J. Miles, [2]Frank Wien, [3]Bonnie Ann Wallace [Full author list]Analytical Biochemistry [curation]DOI: 10.1016/J.AB.2004.08.035
PubMed: 15556575
2004-12-01
Biomedical applications of synchrotron radiation circular dichroism spectroscopy: identification of mutant proteins associated with disease and development of a reference database for fold motifs[1]Bonnie Ann Wallace, [2]Frank Wien, [3]Andrew J. Miles, [4]Jonathan G Lees, [5]Soren Vronning Hoffmann, [6]Paul Evans, [7]Graeme J Wistow, [8]Christine Slingsby [Full author list]Faraday Discussions [curation]DOI: 10.1039/B306055C
PubMed: 14992410
database [curation]; synchrotron radiation [curation]; protein folding [curation]2004-01-01
Database searching for thymidine and thymidylate kinase inhibitors using three-dimensional structure-based methods[1]David T Manallack, [2]Will R Pitt, [3]Piet Herdewijn, [4]Jan Balzarini, [5]Erik De Clercq, [6]Mark R Sanderson, [7]Maninder Sohi, [8]Frank Wien, [9]Helene Munier-Lehmann, [10]Ahmed Haouz, [11]Marc Delarue [Full author list]Journal of Enzyme Inhibition and Medicinal Chemistry [curation]DOI: 10.1080/14756360290032949
PubMed: 12443042
2002-06-01
A DNA-porphyrin minor-groove complex at atomic resolution: the structural consequences of porphyrin ruffling[1]M Bennett, [2]A Krah, [3]Frank Wien, [4]Elspeth Garman, [5]R McKenna, [6]M Sanderson, [7]S Neidle [Full author list]Proceedings of the National Academy of Sciences of the United States of America [curation]DOI: 10.1073/PNAS.160271897
PubMed: 10920199
2000-08-01
Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir[1]M S Bennett, [2]Frank Wien, [3]J N Champness, [4]T Batuwangala, [5]T Rutherford, [6]W C Summers, [7]H Sun, [8]G Wright, [9]M R Sanderson [Full author list]FEBS Letters [curation]DOI: 10.1016/S0014-5793(98)01619-6
PubMed: 9989588
aciclovir [curation]1999-01-01
Exploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands[1]J N Champness, [2]M S Bennett, [3]Frank Wien, [4]R Visse, [5]W C Summers, [6]Piet Herdewijn, [7]E de Clerq, [8]Tomasz Ostrowski, [9]R L Jarvest, [10]M R Sanderson [Full author list]Proteins [curation]DOI: 10.1002/(SICI)1097-0134(19980815)32:3<350::AID-PROT10>3.0.CO;2-8
PubMed: 9715911
aciclovir [curation]; X-ray crystallography [curation]1998-08-01
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