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8 results for author:"Eliseo T." in Literature citations

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Structural characterization of the Hepatitis C Virus NS3 protease from genotype 3a: the basis of the genotype 1b vs. 3a inhibitor potency shift.

Gallo M., Bottomley M.J., Pennestri M., Eliseo T., Paci M., Koch U., Bazzo R., Summa V., Carfi A., Cicero D.O.

Virology 405:424-438(2010) · Mapped (154)

Binding of a noncovalent inhibitor exploiting the S' region stabilizes the hepatitis C virus NS3 protease conformation in the absence of cofactor.

Gallo M., Pennestri M., Bottomley M.J., Barbato G., Eliseo T., Paci M., Narjes F., De Francesco R., Summa V., Koch U. et al.

J. Mol. Biol. 385:1142-1155(2009) · UniProtKB (1)

NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1.

Verdone G., Corazza A., Colebrooke S.A., Cicero D., Eliseo T., Boyd J., Doliana R., Fogolari F., Viglino P., Colombatti A. et al.

J. Biomol. NMR 43:79-96(2009) · UniProtKB (1)

Structural and dynamic determinants of ligand binding in the ternary complex of chicken liver bile acid binding protein with two bile salts revealed by NMR.

Eliseo T., Ragona L., Catalano M., Assfalg M., Paci M., Zetta L., Molinari H., Cicero D.O.

Biochemistry 46:12557-12567(2007) · Mapped (1)

NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid-binding protein.

Ragona L., Catalano M., Luppi M., Cicero D., Eliseo T., Foote J., Fogolari F., Zetta L., Molinari H.

J. Biol. Chem. 281:9697-9709(2006) · UniProtKB (1)

Solution structure of the HPV-16 E2 DNA binding domain, a transcriptional regulator with a dimeric beta-barrel fold.

Nadra A.D., Eliseo T., Mok Y.K., Almeida C.L., Bycroft M., Paci M., de Prat-Gay G., Cicero D.O.

J. Biomol. NMR 30:211-214(2004) · Mapped (1)

Solution structure of the cyclic peptide contryphan-Vn, a Ca2+-dependent K+ channel modulator.

Eliseo T., Cicero D.O., Romeo C., Schinina M.E., Massilia G.R., Polticelli F., Ascenzi P., Paci M.

Biopolymers 74:189-198(2004) · UniProtKB (1)

Contryphan-Vn: a modulator of Ca2+-dependent K+ channels.

Massilia G.R., Eliseo T., Grolleau F., Lapied B., Barbier J., Bournaud R., Molgo J., Cicero D.O., Paci M., Schinina M.E. et al.

Biochem. Biophys. Res. Commun. 303:238-246(2003) · UniProtKB (1)

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