Zobrazeno 1 - 10
of 54
pro vyhledávání: '"Bernd Gutte"'
Autor:
Mouhssin Oufir, Leslie R. Bisset, Stefan R. K. Hoffmann, Gongda Xue, Stephan Klauser, Bianca Bergamaschi, Alain Gervaix, Jürg Böni, Jörg Schüpbach, Bernd Gutte
Publikováno v:
Advances in Virology, Vol 2011 (2011)
An artificial HIV-1 enhancer-binding peptide was extended by nine consecutive arginine residues at the C-terminus and by the nuclear localization signal of SV40 large T antigen at the N-terminus. The resulting synthetic 64-residue peptide was found t
Externí odkaz:
https://doaj.org/article/92fc98ba0c004ad3bd069b5d19189400
Autor:
Yaroslav Nikolaev, Christine Deillon, Stefan R K Hoffmann, Laurent Bigler, Sebastian Friess, Renato Zenobi, Konstantin Pervushin, Peter Hunziker, Bernd Gutte
Publikováno v:
PLoS ONE, Vol 5, Iss 5, p e10765 (2010)
Basic-region leucine zipper (bZIP) proteins are one of the largest transcription factor families that regulate a wide range of cellular functions. Owing to the stability of their coiled coil structure leucine zipper (LZ) domains of bZIP factors are w
Externí odkaz:
https://doaj.org/article/45692af13e28481b9fb07bc0be0f2bd2
Autor:
Bernd Gutte, Stephan Klauser
The first part of this review article lists examples of complete, empirical de novo design that made important contributions to the development of the field and initiated challenging projects. The second part of this article deals with computational
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89368b768ba1861ad1276ae045e5c09f
https://www.zora.uzh.ch/id/eprint/174731/
https://www.zora.uzh.ch/id/eprint/174731/
Autor:
Niankun Liu, Lloyd C. Trotman, Stephan Klauser, Georg Caderas, Thomas Hehlgans, André Hiltpold, Kurt Städler, Bernd Gutte
Publikováno v:
International Journal of Peptide and Protein Research. 46:333-340
We have designed and synthesized HIV-1 enhancer-binding polypeptides that were derived from bacteriophage 434 repressor. These peptides were 39-54 residues long and contained either the recognition helix or the entire helix-turn-helix motif of the DN
Autor:
Christine Deillon, Niankun Liu, Bernd Gutte, Stephan Klauser, Stefan R. K. Hoffmann, T. Cui, Georg Caderas
Publikováno v:
Current Protein & Peptide Science. 2:107-121
The purpose of preparing fusion proteins from designed and natural sequences is mainly twofold; it aims at the stabilization of structure and at the modification of biological activity. Fusion with beta-galactosidase, for example, can increase the in
Autor:
Markus G. Grütter, Richard Thomas, David F. Sargent, Peer R. E. Mittl, Christine Deillon, Bernd Gutte, Stephan Klauser, Niankun Liu
Publikováno v:
Proceedings of the National Academy of Sciences. 97:2562-2566
The question of whether a protein whose natural sequence is inverted adopts a stable fold is still under debate. We have determined the 2.1-Å crystal structure of the retro -GCN4 leucine zipper. In contrast to the two-stranded helical coiled-coil G
Publikováno v:
European Journal of Biochemistry. 266:599-607
An artificial HIV-1 enhancer-binding 42-residue peptide (R42) that had been derived from bacteriophage 434 repressor inhibited the cell-free in vitro transcription of HIV-1 enhancer-containing plasmids [Hehlgans, T., Stolz, M., Klauser, S., Cui, T.,
Publikováno v:
Journal of Biotechnology. 66:225-228
A 96-bp DNA fragment containing the bacteriophage SP6 promoter was covalently coupled to EAH-Sepharose 4B in an orientation-specific manner. Here we show that the immobilized DNA was able to serve as template in in vitro transcription of RNA. This so
Autor:
Jörg Schüpbach, Stefan R. K. Hoffmann, Leslie R. Bisset, Alain Gervaix, Mouhssin Oufir, Gongda Xue, Jürg Böni, Bernd Gutte, Bianca Bergamaschi, Stephan Klauser
Publikováno v:
Advances in Virology
Advances in Virology, Vol 2011 (2011)
Advances in Virology, Vol. 2011, No 165871 (2011) pp. 1-13
Advances in Virology, Vol 2011 (2011)
Advances in Virology, Vol. 2011, No 165871 (2011) pp. 1-13
An artificial HIV-1 enhancer-binding peptide was extended by nine consecutive arginine residues at the C-terminus and by the nuclear localization signal of SV40 large T antigen at the N-terminus. The resulting synthetic 64-residue peptide was found t
Autor:
Laurent Bigler, Peter Hunziker, Sebastian D. Friess, Renato Zenobi, Stefan R. K. Hoffmann, Konstantin Pervushin, Bernd Gutte, Yaroslav Nikolaev, Christine Deillon
Publikováno v:
PLoS ONE
PLoS ONE, Vol 5, Iss 5, p e10765 (2010)
PLoS ONE, 5 (5)
PLoS ONE, Vol 5, Iss 5, p e10765 (2010)
PLoS ONE, 5 (5)
Basic-region leucine zipper (bZIP) proteins are one of the largest transcription factor families that regulate a wide range of cellular functions. Owing to the stability of their coiled coil structure leucine zipper (LZ) domains of bZIP factors are w