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The novel Smad-interacting protein Smicl regulates Chordin expression in the Xenopus embryo. , Collart C , Verschueren K , Rana A, Smith JC , Huylebroeck D ., Development. October 1, 2005; 132 (20): 4575-86.
Loss-of-function mutations in LEMD3 result in osteopoikilosis, Buschke-Ollendorff syndrome and melorheostosis. , Hellemans J, Preobrazhenska O, Willaert A, Debeer P, Verdonk PC, Costa T, Janssens K, Menten B, Van Roy N, Vermeulen SJ, Savarirayan R, Van Hul W, Vanhoenacker F, Huylebroeck D , De Paepe A, Naeyaert JM, Vandesompele J, Speleman F, Verschueren K , Coucke PJ, Mortier GR., Nat Genet. November 1, 2004; 36 (11): 1213-8.
Dynamic regulation of Brachyury expression in the amphibian embryo by XSIP1. , Papin C, van Grunsven LA, Verschueren K , Huylebroeck D , Smith JC ., Mech Dev. February 1, 2002; 111 (1-2): 37-46.
SIP1 (Smad interacting protein 1) and deltaEF1 (delta-crystallin enhancer binding factor) are structurally similar transcriptional repressors. , van Grunsven LA, Schellens A, Huylebroeck D , Verschueren K ., J Bone Joint Surg Am. January 1, 2001; 83-A Suppl 1 (Pt 1): S40-7.
The bone morphogenetic protein 2 signaling mediator Smad1 participates predominantly in osteogenic and not in chondrogenic differentiation in mesenchymal progenitors C3H10T1/2. , Ju W, Hoffmann A, Verschueren K , Tylzanowski P, Kaps C, Gross G, Huylebroeck D ., J Bone Miner Res. October 1, 2000; 15 (10): 1889-99.
New mode of DNA binding of multi-zinc finger transcription factors: deltaEF1 family members bind with two hands to two target sites. , Remacle JE, Kraft H, Lerchner W, Wuytens G , Collart C , Verschueren K , Smith JC , Huylebroeck D ., EMBO J. September 15, 1999; 18 (18): 5073-84.
SIP1, a novel zinc finger/homeodomain repressor, interacts with Smad proteins and binds to 5'-CACCT sequences in candidate target genes. , Verschueren K , Remacle JE, Collart C , Kraft H, Baker BS , Tylzanowski P, Nelles L, Wuytens G , Su MT, Bodmer R, Smith JC , Huylebroeck D ., J Biol Chem. July 16, 1999; 274 (29): 20489-98.
Identification of two amino acids in activin A that are important for biological activity and binding to the activin type II receptors. , Wuytens G , Verschueren K , de Winter JP, Gajendran N, Beek L, Devos K, Bosman F, de Waele P, Andries M, van den Eijnden-van Raaij AJ, Smith JC , Huylebroeck D ., J Biol Chem. April 2, 1999; 274 (14): 9821-7.
The C-terminal domain of Mad-like signal transducers is sufficient for biological activity in the Xenopus embryo and transcriptional activation. , Meersseman G, Verschueren K , Nelles L, Blumenstock C, Kraft H, Wuytens G , Remacle J, Kozak CA, Tylzanowski P, Niehrs C , Huylebroeck D ., Mech Dev. January 1, 1997; 61 (1-2): 127-40.
Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors. , De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D , Verschueren K , Van Den Eijden-Van Raaij AJ., Exp Cell Res. May 1, 1996; 224 (2): 323-34.