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Inhalt des Dokuments

Publikationen 1990 - 1999


Budisa, N., Minks, C., Alefelder, S., Wenger, W., Dong, F., Mororder, L. and Huber, R. - Toward the experimental codon reassignment in vivo: protein building with an expanded amino acid repertoire [4]. FASEB J., 13, 41-51 (1999)

Link zur Originalpublikation [5]

Minks, C., Huber, R., Moroder, L. and Budisa, N. - Atomic mutations at the single tryptophan residue of human recombinant annexin V: Effects on structure, stability and activity [6]. Biochemistry, 38, 10649-10659 (1999)

Link zur Originalpublikation [7]

Budisa, N., Mororder, L. and Huber, R. - Structure and evolution of the genetic code viewed from the perspective of the experimentally amino acid repertoire in vivo [8]. Cell. Mol. Life Sci., 55, 1626-1635 (1999)

Link zur Originalpublikation [9]


Budisa, N., Minks, C., Medrano, F. J., Lutz, J., Huber, R. and Moroder, L. - Residuespecific bioincorporation of non-natural biologically active amino acids into proteins as possible drug carriers. Structure and stability of per-thiaproline mutant or annexin V [10]. Proc. Natl. Acad. Sci. USA, 95, 455-459 (1998)

Link zur Originalpublikation [11]

Budisa, N. and Pifat, G. - Probing protein stability with non-natural amino acids [12]. Croat. Chem. Acta, 71, 179-187 (1998)

Link zur Originalpublikation [13]

Budisa, N., Huber, R., Minks, C., Golbik, R., Weyher, E. and Moroder, L. - Atomic mutations in annexin V. Thermodynamic studies of isomorphous protein variants [14]. Eur. J. Biochem., 253, 1-9 (1998)

Link zur Originalpublikation [15]


Besse, D., Budisa, N., Karnbock, W. M. C., Musiol, H. J., Pergoraro, S., Siedler, F., Weyher, E. and Moroder, L. - Chalcogen-analogs of amino acids. Their use in X-ray crystallographic and folding studies of peptides and proteins [16]. , 211-218 (1997)

Link zur Originalpublikation [17]

Budisa, N., Karnbock, W., Steinbacher, S., Humm, A., Prade, L., Neuefeind, T., Moroder, L. and Huber, R. - Bioincorporation of telluromehionine into proteins: A promising new approach for X-ray structure analysis of proteins [18]. J. Mol. Biol., 270, 616-623 (1997)

Link zur Originalpublikation [19]

Steinbacher, S., Miller, S., Baxa, U., Budisa, N., Weintraub, A., Seckler, R. and Huber, R. - Phage P22 Tailspike protein: Crystal structure of the head binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage [20]. J. Mol. Biol., 267, 865-880 (1997)

Link zur Originalpublikation [21]

Pieper, M., Betz, M., Budisa, N., Gomis-Ruth, F.-X., Bode, W. and Tschesche, H. - On the role of conserved methionine in metzincins: an active selenomethionine 215-variant of leukocyte collagenase with similar structure as the wild-type form [22]. J. Prot. Chem., 16, 637-650 (1997)

Link zur Originalpublikation [23]


Karnbock, W., Weyher, E., Budisa, N., Huber, R. and Moroder, L. - A new efficient synthesis of acetyltelluro- and acetylselenomethionine and their use in the biosynthesis of heavy-atom protein analogues [24]. J. Am. Chem. Soc., 118, 913-914 (1996)

Link zur Originalpublikation [25]


Budisa, N., Steipe, B., Demange, P., Eckerskorn, C., Kellermann, J. and Huber, R. - High level biosynthetic substitution of methionine in proteins by its analogues 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli [26]. Eur. J. Biochem., 230, 788-796 (1995)

Link zur Originalpublikation [27]


Budisa, N., Benussi, A., Mihokovic, V. and Shinagawa, K. - Enterotoxicity of Staphylococcus aureus strains isolated from foods and clinical materials. [28]. Food Technol. Biotechnol., 30, 79-82 (1992)

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