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21 results for author:"Wieruszeski J.-M." in Literature citations

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Differential contribution of the repeats to heparin binding of HBHA, a major adhesin of Mycobacterium tuberculosis.

Lebrun P., Raze D., Fritzinger B., Wieruszeski J.M., Biet F., Dose A., Carpentier M., Schwarzer D., Allain F., Lippens G. et al.

PLoS ONE 7:e32421-e32421(2012) · UniProtKB (1)

Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.

Smet-Nocca C., Broncel M., Wieruszeski J.M., Tokarski C., Hanoulle X., Leroy A., Landrieu I., Rolando C., Lippens G., Hackenberger C.P.

Mol. Biosyst. 7:1420-1429(2011) · UniProtKB (1) · Mapped (5)

SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity.

Smet-Nocca C., Wieruszeski J.M., Leger H., Eilebrecht S., Benecke A.

BMC Biochem. 12:4-4(2011) · Mapped (3)

Spectroscopic studies of GSK3{beta} phosphorylation of the neuronal tau protein and its interaction with the N-terminal domain of apolipoprotein E.

Leroy A., Landrieu I., Huvent I., Legrand D., Codeville B., Wieruszeski J.M., Lippens G.

J. Biol. Chem. 285:33435-33444(2010) · Mapped (9)

NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease.

Landrieu I., Leroy A., Smet-Nocca C., Huvent I., Amniai L., Hamdane M., Sibille N., Buee L., Wieruszeski J.M., Lippens G.

Biochem. Soc. Trans. 38:1006-1011(2010) · Mapped (6)

Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B.

Hanoulle X., Badillo A., Wieruszeski J.M., Verdegem D., Landrieu I., Bartenschlager R., Penin F., Lippens G.

J. Biol. Chem. 284:13589-13601(2009) · Mapped (1)

Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded.

Hanoulle X., Verdegem D., Badillo A., Wieruszeski J.M., Penin F., Lippens G.

Biochem. Biophys. Res. Commun. 381:634-638(2009) · Mapped (154)

NMR investigation of the interaction between the neuronal protein tau and the microtubules.

Sillen A., Barbier P., Landrieu I., Lefebvre S., Wieruszeski J.M., Leroy A., Peyrot V., Lippens G.

Biochemistry 46:3055-3064(2007) · Mapped (6)

Structural impact of heparin binding to full-length Tau as studied by NMR spectroscopy.

Sibille N., Sillen A., Leroy A., Wieruszeski J.M., Mulloy B., Landrieu I., Lippens G.

Biochemistry 45:12560-12572(2006) · Mapped (6)

Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein.

Smet C., Wieruszeski J.M., Buee L., Landrieu I., Lippens G.

FEBS Lett. 579:4159-4164(2005) · Mapped (2)

Characterization of the Arabidopsis thaliana Arath;CDC25 dual-specificity tyrosine phosphatase.

Landrieu I., Hassan S., Sauty M., Dewitte F., Wieruszeski J.-M., Inze D., de Veylder L., Lippens G.

Biochem. Biophys. Res. Commun. 322:734-739(2004) · UniProtKB (1)

A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana.

Landrieu I., da Costa M., de Veylder L., Dewitte F., Vandepoele K., Hassan S., Wieruszeski J.-M., Corellou F., Faure J.-D., Van Montagu M. et al.

Proc. Natl. Acad. Sci. U.S.A. 101:13380-13385(2004) · UniProtKB (1) · Mapped (3)

The peptidyl prolyl cis/trans-isomerase Pin1 recognizes the phospho-Thr212-Pro213 site on Tau.

Smet C., Sambo A.V., Wieruszeski J.M., Leroy A., Landrieu I., Buee L., Lippens G.

Biochemistry 43:2032-2040(2004) · Mapped (10)

Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana.

Landrieu I., Wieruszeski J.-M., Wintjens R., Inze D., Lippens G.

J. Mol. Biol. 320:321-332(2002) · UniProtKB (1)

All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.

Messens J., Martins J.C., Van Belle K., Brosens E., Desmyter A., De Gieter M., Wieruszeski J.-M., Willem R., Wyns L., Zegers I.

Proc. Natl. Acad. Sci. U.S.A. 99:8506-8511(2002) · UniProtKB (1)

1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides.

Wintjens R., Wieruszeski J.-M., Drobecq H., Rousselot-Pailley P., Buee L., Lippens G., Landrieu I.

J. Biol. Chem. 276:25150-25156(2001) · UniProtKB (1) · Mapped (2)

Sequence-specific 1H, 13C and 15N chemical shift backbone NMR assignment and secondary structure of the Arabidopsis thaliana PIN1At protein.

Landrieu I., Wieruszeski J.-M., Odaert B., Inze D., Grzesiek S., Lippen G.

J. Biomol. NMR 17:271-272(2000) · UniProtKB (1)

Characterization of a new family of toxin-like peptides from the venom of the scorpion Leiurus quinquestriatus hebraeus. 1H-NMR structure of leiuropeptide II.

Buisine E., Wieruszeski J.-M., Lippens G., Wouters D., Tartar A., Sautiere P.

J. Pept. Res. 49:545-555(1997) · UniProtKB (3)

Change in glycosylation of chicken transferrin glycans biosynthesized during embryogenesis and primary culture of embryo hepatocytes.

Jacquinot P.-M., Leger D., Wieruszeski J.-M., Coddeville B., Montreuil J., Spik G.

Glycobiology 4:617-624(1994) · UniProtKB (1)

Rat mammary-gland transferrin: nucleotide sequence, phylogenetic analysis and glycan structure.

Escriva H., Pierce A., Coddeville B., Gonzalez F., Benaissa M., Leger D., Wieruszeski J.-M., Spik G., Pamblanco M.

Biochem. J. 307:47-55(1995) · UniProtKB (1) · Mapped (2)

The glycan moiety of human pancreatic lithostathine. Structure characterization and possible pathophysiological implications.

De Reggi M., Capon C., Gharib B., Wieruszeski J.-M., Michel R., Fournet B.

Eur. J. Biochem. 230:503-510(1995) · UniProtKB (1)

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