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Found 20 results

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2007
MessensJ, ColletJF, Van BelleK, BrosensE, LorisR, WynsL.  2007.  The oxidase DsbA folds a protein with a nonconsecutive disulfide. J. Biol. Chem.. 282(43):31302-31307. 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
PauwelsK, LustigA, WynsL, TommassenJ, SavvidesSN, VanGelder P.  2006.  Structure of a membrane-based steric chaperone in complex with its lipase substrate. 13(4):374-375. Abstract
2005
ButsL, LahJ, Dao-ThiMH, WynsL, LorisR.  2005.  Toxin-antitoxin modules as bacterial metabolic stress managers. 30(12):672-679. Abstract
VanWalleI, LastersI, WynsL.  2005.  SABmark--a benchmark for sequence alignment that covers the entire known fold space. 21(7):1267-1268. Abstract
2004
CasaresS, SadqiM, Lopez-MayorgaO, Conejero-LaraF, van NulandNA.  2004.  Detection and characterization of partially unfolded oligomers of the SH3 domain of alpha-spectrin. 86(4):2403-2413. Abstract
2003
VerseesW, SteyaertJ.  2003.  Catalysis by nucleoside hydrolases. Current opinion in structural biology. 13(6):731-738. Abstract
VanWalleI, LastersI, WynsL.  2003.  Consistency matrices: quantified structure alignments for sets of related proteins. 51(1):1-9. Abstract
2002
DumoulinM, ConrathK, VanMeirhaeghe A, MeersmanF, HeremansK, FrenkenLG, MuyldermansS, WynsL, MatagneA.  2002.  Single-domain antibody fragments with high conformational stability. 11(3):500-515. Abstract
2001
ReaderJS, van NulandNA, ThompsonGS, FergusonSJ, DobsonCM, RadfordSE.  2001.  A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding. 10(6):1216-1224. Abstract
1999
ChitiF, TaddeiN, GiannoniE, van NulandNA, RamponiG, DobsonCM.  1999.  Development of enzymatic activity during protein folding. Detection of a spectroscopically silent native-like intermediate of muscle acylphosphatase. 274(29):20151-20158. Abstract
ZegersI, DeswarteJ, WynsL.  1999.  Trimeric domain-swapped barnase. 96(3):818-822. Abstract
1998
BackmannJ, SchaferG, WynsL, BonischH.  1998.  Thermodynamics and kinetics of unfolding of the thermostable trimeric adenylate kinase from the archaeon Sulfolobus acidocaldarius. 284(3):817-833. Abstract
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
ChitiF, van NulandNA, TaddeiN, MagheriniF, StefaniM, RamponiG, DobsonCM.  1998.  Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pH. 37(5):1447-1455. Abstract
van NulandNA, MeijbergW, WarnerJ, ForgeV, ScheekRM, RobillardGT, DobsonCM.  1998.  Slow cooperative folding of a small globular protein HPr. 37(2):622-637. Abstract
1997
BalbachJ, ForgeV, LauWS, JonesJA, van NulandNA, DobsonCM.  1997.  Detection of residue contacts in a protein folding intermediate. 94(14):7182-7185. Abstract
VanDael H, HaezebrouckP, PardonE, JoniauM.  1997.  Conformational stability of LYLA1, a synthetic chimera of human lysozyme and bovine alpha-lactalbumin. 25(3):171-179. Abstract
1996
BalbachJ, ForgeV, LauWS, van NulandNA, BrewK, DobsonCM.  1996.  Protein folding monitored at individual residues during a two-dimensional NMR experiment. 274(5290):1161-1163. Abstract
1995
BalbachJ, ForgeV, van NulandNA, WinderSL, HorePJ, DobsonCM.  1995.  Following protein folding in real time using NMR spectroscopy. 2(10):865-870. Abstract