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Profil

Evrard Christine

See author's contact details
Main Referenced Co-authors
Declercq, Jean-Paul (15)
Fastrez, Jacques (5)
Knoops, Bernard (4)
Martial, Joseph  (4)
Van de Weerdt, Cécile  (4)
Main Referenced Keywords
microgravity (3); peroxiredoxin (3); thioredoxin fold (3); thioredoxin peroxidase (3); antioxidant enzyme (2);
Main Referenced Unit & Research Centers
Giga-Development and Stem Cells - ULiège (1)
Giga-Systems Biology and Chemical Biology - ULiège (1)
Main Referenced Disciplines
Biochemistry, biophysics & molecular biology (22)
Chemistry (1)
Physics (1)

Publications (total 23)

The most downloaded
783 downloads
Claus, H., Akça, E., Debaerdemaeker, T., Evrard, C., Declercq, J.-P., Harris, J. R., Schlott, B., & König, H. (2005). Molecular organization of selected prokaryotic S-Iayer proteins. Canadian Journal of Microbiology, 51, 731-743. doi:10.1139/W05-093 https://hdl.handle.net/2268/57472

The most cited

278 citations (OpenAlex)

Declercq, J.-P., Evrard, C., Clippe, A., Vander Stricht, D., Bernard, A., & Knoops, B. (2001). Crystal Structure of Human Peroxiredoxin 5, a Novel Type of Mammalian Peroxiredoxin at 1.5 Ǻ Resolution. Journal of Molecular Biology, 311, 751-759. doi:10.1006/jmbi.2001.4853 https://hdl.handle.net/2268/59241

Urbach, C., Evrard, C., Pudzaitis, V., Fastrez, J., Soumillion, P., & Declercq, J.-P. (2009). Structure of PBP-A from Thermosynechococcus elongatus, a Penicillin-Binding Protein Closely Related to Class A β-Lactamases. Journal of Molecular Biology, 386, 109-120. doi:10.1016/j.jmb.2008.12.001
Peer Reviewed verified by ORBi

Sleutel, M., Willaert, R., Gillespie, C., Evrard, C., Wyns, L., & Maes, D. (2009). Kinetics and Thermodynamics of Glucose Isomerase Crystallization. Crystal Growth and Design, 9, 497-504. doi:10.1021/cg800756h
Peer Reviewed verified by ORBi

Maes, D., Evrard, C., Gavira, J., Sleutel, M., Van de Weerdt, C., Otalora, F., Garcia-Ruiz, J. M., Nicolis, G., Martial, J., & Decanniere, K. (2008). Toward a Definition of X-ray Crystal Quality. Crystal Growth and Design, 8 (12), 4284-4290. doi:10.1021/cg800699e
Peer Reviewed verified by ORBi

Evrard, C., Maes, D., Zegers, I., Declercq, J. P., Vanhee, C., Martial, J., Wyns, L., & Van de Weerdt, C. (November 2007). TIM crystals grown by capillary counterdiffusion: Statistical evidence of quality improvement in microgravity. Crystal Growth and Design, 7 (11), 2161-2166. doi:10.1021/cg700687t
Peer Reviewed verified by ORBi

MAES, D., DECANNIERE, K., ZEGERS, I., VANHEE, SLEUTEL, M., WILLAERT, R., Van de Weerdt, C., Martial, J., DECLERCQ, J.-P., Evrard, C., OTALORA, F., & GARCIA-RUIZ, J.-M. (2007). Protein crystallisation under microgravity conditions: What did we learn on TIM crystallisation from the Soyuz missions? Microgravity Science and Technology, XIX (5/6), 90-94.
Peer Reviewed verified by ORBi

Zegers, I., Carotenuto, L., Evrard, C., Garcia-Ruiz, J., De Gieter, P., Gonzales- Ramires, L., Istasse, E., Legros, J.-C., Martial, J., Minetti, C., Otalora, F., Queeckers, P., Schockeart, C., Van de Weerdt, C., Willaert, R., Wyns, L., Yourassowsky, C., & Dubois, F. (2006). Counterdiffusion protein crystallisation in microgravity and its observation with PromISS (Protein Microscope for the International Space Station). Microgravity Science and Technology, XVIII, 165-169. doi:10.1007/BF02870402
Peer Reviewed verified by ORBi

Claus, H., Akça, E., Debaerdemaeker, T., Evrard, C., Declercq, J.-P., Harris, J. R., Schlott, B., & König, H. (2005). Molecular organization of selected prokaryotic S-Iayer proteins. Canadian Journal of Microbiology, 51, 731-743. doi:10.1139/W05-093
Peer Reviewed verified by ORBi

Smeets, A., Evrard, C., Landtmeters, M., Marchand, C., Knoops, B., & Declercq, J.-P. (2005). Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2. Protein Science: A Publication of the Protein Society, 14, 2610-2621. doi:10.1110/ps.051632905
Peer Reviewed verified by ORBi

Evrard, C., Smeets, A., Knoops, B., & Declercq, J.-P. (2004). Crystal structure of the C47S mutant of human peroxiredoxin 5. Journal of Chemical Crystallography, 34, 553-558. doi:10.1023/B:JOCC.0000042025.08082.6c
Peer Reviewed verified by ORBi

Evrard, C., Capron, A., Marchand, C., Clippe, A., Wattiez, R., Soumillion, P., Knoops, B., & Declercq, J.-P. (2004). Crystal structure of a dimeric oxidized form of human peroxiredoxin 5. Journal of Molecular Biology, 337, 1079-1090. doi:10.1016/j.jmb.2004.02.017
Peer Reviewed verified by ORBi

Claus, H., Akça, E., Debaerdemaeker, T., Evrard, C., Declercq, J.-P., & König, H. (2002). Primary Structure of Selected Archaeal Mesophilic and Extremely Thermophilic Outer Surface Layer Proteins. Systematic and Applied Microbiology, 25, 3-12. doi:10.1078/0723-2020-00100
Peer Reviewed verified by ORBi

Declercq, J.-P., Evrard, C., Clippe, A., Vander Stricht, D., Bernard, A., & Knoops, B. (2001). Crystal Structure of Human Peroxiredoxin 5, a Novel Type of Mammalian Peroxiredoxin at 1.5 Ǻ Resolution. Journal of Molecular Biology, 311, 751-759. doi:10.1006/jmbi.2001.4853
Peer Reviewed verified by ORBi

Declercq, J.-P., & Evrard, C. (2001). A twinned monoclinic crystal form of human peroxiredoxin 5 with eight molecules in the asymmetric unit. Acta Crystallographica. Section D, Biological Crystallography, D57, 1829-1835. doi:10.1107/S0907444901015475
Peer Reviewed verified by ORBi

Evrard, C., Declercq, J.-P., Debaerdemaeker, T., & König, H. (1999). The first successful crystallization of a prokaryotic extremely thermophilic outer surface layer glycoprotein. Zeitschfrift für Kristallographie, 214, 427-429. doi:10.1524/zkri.1999.214.8.427
Peer Reviewed verified by ORBi

Declercq, J.-P., Evrard, C., Carter, D., Wright, B., Etienne, G., & Parello, J. (1999). A crystal of a typical EF-hand protein grown under microgravity diffracts X-rays beyond 0.9 Å resolution. Journal of Crystal Growth, 196, 595-601. doi:10.1016/S0022-0248(98)00829-X
Peer Reviewed verified by ORBi

Evrard, C., Fastrez, J., & Soumillion, P. (1999). Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme. FEBS Letters, 460, 442-446. doi:10.1016/S0014-5793(99)01395-2
Peer Reviewed verified by ORBi

Declercq, J.-P., Evrard, C., Lamzin, V., & Parello, J. (1999). Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 Å) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core. Protein Science: A Publication of the Protein Society, 8, 2194-2204. doi:10.1110/ps.8.10.2194
Peer Reviewed verified by ORBi

Evrard, C., Fastrez, J., & Declercq, J.-P. (1999). The incorporation of a non-natural amino acid (aza-tryptophan) may help to crystallize a protein and to solve its crystal structure. Application to bacteriophage lambda lysozyme. Acta Crystallographica. Section D, Biological Crystallography, D55, 430-435. doi:10.1107/S0907444998011901
Peer Reviewed verified by ORBi

Carter, D., Wright, B., Miller, T., Chapman, J., Twigg, P., Keeling, K., Moody, K., White, M., Click, J., Ruble, J., Ho, J., Adcock-Downey, L., Dowling, T., Chang, C.-H., Ala, P., Rose, J., Wang, B. C., Declercq, J.-P., Evrard, C., ... Stevens, A. (1999). PCAM: a multi-user facility-based protein crystallization apparatus for microgravity. Journal of Crystal Growth, 196, 610-622. doi:10.1016/S0022-0248(98)00858-6
Peer Reviewed verified by ORBi

Evrard, C., Fastrez, J., & Declercq, J.-P. (1998). Crystal Structure of the Lysozyme from Bacteriophage Lambda and its Relationship with V and C-type Lysozymes. Journal of Molecular Biology, 276, 151-164. doi:10.1006/jmbi.1997.1499
Peer Reviewed verified by ORBi

Evrard, C., Declercq, J.-P., & Fastrez, J. (1997). Crystallization and preliminary X-ray analysis of bacteriophage lambda lysozyme in which all tryptophans have been replaced by aza-tryptophans. Acta Crystallographica. Section D, Biological Crystallography, D53, 217-219. doi:10.1107/S0907444996011523
Peer Reviewed verified by ORBi

Creuven, I., Evrard, C., Olivier, A., Evrard, G., Van Aerschot, A., Wigerinck, P., Herdewijn, P., & Durant, F. (1996). Relationship between structural properties and affinity for herpes simplex virus type 1 thymidine kinase of bromine substituted 5-heteroaromatic 2'-deoxyuridines. Antiviral Research, 30, 63-74. doi:10.1016/0166-3542(95)00838-1
Peer Reviewed verified by ORBi

Olivier, A., Creuven, I., Evrard, C., Evrard, G., Dory, M., van Aerschot, A., Wigerinck, P., Herdewijn, P., & Durant, F. (1994). Stereoelectronic properties of five anti-HSV-1 2′-deoxynucleosides analogues with heterocyclic substituents in the 5-position: A comparison with BVDU. Antiviral Research, 24, 289-304. doi:10.1016/0166-3542(94)90076-0
Peer Reviewed verified by ORBi

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