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2008
CandelAM, van NulandNA, Martin-SierraFM, MartinezJC, Conejero-LaraF.  2008.  Analysis of the thermodynamics of binding of an SH3 domain to proline-rich peptides using a chimeric fusion protein. 377(1):117-135. Abstract
2007
Van MolleI, JoensuuJJ, ButsL, PanjikarS, KotiahoM, BouckaertJ, WynsL, Niklander-TeeriV, De Greve H.  2007.  Chloroplasts assemble the major subunit FaeG of Escherichia coli F4 (K88) fimbriae to strand-swapped dimers. Journal Molecular Biology. 368(3):791-799. Abstract
RoosG, Garcia-PinoA, VanBelle K, BrosensE, WahniK, VandenbusscheG, WynsL, LorisR, MessensJ.  2007.  The conserved active site proline determines the reducing power of Staphylococcus aureus thioredoxin. J. Mol. Biol.. 368(3):800-811. Abstract
2006
SibilleN, FavierA, AzuagaAI, GanshawG, BottR, BonvinAM, BoelensR, van NulandNA.  2006.  Comparative NMR study on the impact of point mutations on protein stability of Pseudomonas mendocina lipase. 15(8):1915-1927. Abstract
RoosG, ButsL, VanBelle K, BrosensE, GeerlingsP, LorisR, WynsL, MessensJ.  2006.  Interplay between ion binding and catalysis in the thioredoxin-coupled arsenate reductase family. J. Mol. Biol.. 360(4):826-838. Abstract
RoosG, LoverixS, BrosensE, VanBelle K, WynsL, GeerlingsP, MessensJ.  2006.  The activation of electrophile, nucleophile and leaving group during the reaction catalysed by pI258 arsenate reductase. Chembiochem.. 7(6):981-989. Abstract
2005
Dao-ThiMH, VanMelderen L, DeGenst E, AfifH, ButsL, WynsL, LorisR.  2005.  Molecular basis of gyrase poisoning by the addiction toxin CcdB. 348(5):1091-1102. Abstract
TielkerD, HackerS, LorisR, StrathmannM, WingenderJ, WilhelmS, RosenauF, JaegerKE.  2005.  Pseudomonas aeruginosa lectin LecB is located in the outer membrane and is involved in biofilm formation. 151(Pt 5):1313-1323. Abstract
DumoulinM, CanetD, LastAM, PardonE, ArcherDB, MuyldermansS, WynsL, MatagneA, RobinsonCV, RedfieldC, DobsonCM.  2005.  Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations. Nature. 346(3):773-788. Abstract
2003
DumoulinM, LastAM, DesmyterA, DecanniereK, CanetD, LarssonG, SpencerA, ArcherDB, SasseJ, MuyldermansS, WynsL, RedfieldC, MatagneA, RobinsonCV, DobsonCM.  2003.  A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. 424(6950):783-788. Abstract
LorisR, MarianovskyI, LahJ, LaeremansT, Engelberg-KulkaH, GlaserG, MuyldermansS, WynsL.  2003.  Crystal structure of the intrinsically flexible addiction antidote MazE. 278(30):28252-28257. Abstract
2001
DesmyterA, DecanniereK, MuyldermansS, WynsL.  2001.  Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody. 276(28):26285-26290. Abstract
DeswarteJ, DeVos S, LanghorstU, SteyaertJ, LorisR.  2001.  The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution. 268(14):3993-4000. Abstract
2000
LanghorstU, BackmannJ, LorisR, SteyaertJ.  2000.  Analysis of a water mediated protein-protein interactions within RNase T1. Biochemistry. 39(22):6586-6593. Abstract
1999
Huyghues-DespointesBM, LanghorstU, SteyaertJ, PaceCN, ScholtzJM.  1999.  Hydrogen-exchange stabilities of RNase T1 and variants with buried and solvent-exposed Ala --> Gly mutations in the helix. Biochemistry. 38(50):16481-16490. Abstract
BahassiEM, O'DeaMH, AllaliN, MessensJ, GellertM, CouturierM.  1999.  Interactions of CcdB with DNA gyrase. Inactivation of Gyra, poisoning of the gyrase-DNA complex, and the antidote action of CcdA. J. Biol. Chem.. 274(16):10936-10944. Abstract
LanghorstU, LorisR, DenisovVP, DoumenJ, RooseP, MaesD, HalleB, SteyaertJ.  1999.  Dissection of the structural and functional role of a conserved hydration site in RNase T1. 8(4):722-730. Abstract
1998
ChitiF, TaddeiN, van NulandNA, MagheriniF, StefaniM, RamponiG, DobsonCM.  1998.  Structural characterization of the transition state for folding of muscle acylphosphatase. 283(4):893-903. Abstract
1997
LoverixS, DoumenJ, SteyaertJ.  1997.  Additivity of protein-guanine interactions in ribonuclease T1. 272(15):9635-9639. Abstract
1994
SteyaertJ, HaikalAF, WynsL.  1994.  Investigation of the functional interplay between the primary site and the subsite of RNase T1: kinetic analysis of single and multiple mutants for modified substrates. 18(4):318-323. Abstract
SteyaertJ, HaikalAF, WynsL.  1994.  Investigation of the functional interplay between the primary site and the subsite of RNase T1: kinetic analysis of single and multiple mutants for modified substrates. 18(4):318-323. Abstract
PletinckxJ, SteyaertJ, ZegersI, ChoeHW, HeinemannU, WynsL.  1994.  Crystallographic study of Glu58Ala RNase T1 x 2'-guanosine monophosphate at 1.9-A resolution. Biochemistry. 33(7):1654-1662. Abstract
PletinckxJ, SteyaertJ, ZegersI, ChoeHW, HeinemannU, WynsL.  1994.  Crystallographic study of Glu58Ala RNase T1 x 2'-guanosine monophosphate at 1.9-A resolution. 33(7):1654-1662. Abstract
1993
SteyaertJ, WynsL.  1993.  Functional interactions among the His40, Glu58 and His92 catalysts of ribonuclease T1 as studied by double and triple mutants. 229(3):770-781. Abstract
1992
ZegersI, VerhelstP, ChoeHW, SteyaertJ, HeinemannU, SaengerW, WynsL.  1992.  Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant. Biochemistry. 31(46):11317-11325. Abstract