Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Livia Otte"'
Publikováno v:
Journal of Molecular Recognition. 19:49-59
The onset of autoimmune diseases is proposed to involve binding promiscuity of antibodies (Abs) and T-cells, an often reported yet poorly understood phenomenon. Here, we attempt to approach two questions: first, is binding promiscuity a general featu
Autor:
Livia Otte, Peter Schmieder, Rudolf Volkmer-Engert, Urs Wiedemann, Jens Schneider-Mergener, Gerd Krause, José R. Pires, Hartmut Oschkinat, Brigitte Schlegel, Michael Beyermann
Publikováno v:
Protein science, 12(3): 491-500
Cellular processes depend on finely tuned protein–protein interactions, which together form complex interaction networks. These interactions are often mediated by noncatalytic protein domains. One of these protein interaction modules, the WW domain
Autor:
Livia Otte, Christa Scholz, Patrick Scheerer, Norbert Krauss, Achim Kramer, Martina Seifert, Jens Schneider-Mergener, Wolfgang Höhne, Helga Wessner
Publikováno v:
Journal of molecular recognition : JMR. 20(4)
The structure of a complex of the anti-cholera toxin antibody TE33 Fab (fragment antibody) with the D-peptide vpGsqhyds was solved to 1.78 A resolution. The D-peptide was derived from the linear L-peptide epitope VPGSQHIDS by a stepwise transformatio
Autor:
Christoph Parthier, Hartmut Oschkinat, Urs Wiedemann, Rainer Rudolph, Rodolpho do Aido-Machado, Gerald Böhm, José R. Pires, Livia Otte
Publikováno v:
Journal of molecular biology. 348(2)
WW domains are small protein-protein interaction modules that recognize proline-rich stretches in proteins. The class II tandem WW domains of the formin binding protein 11 (FBP11) recognize specifically proteins containing PPLPp motifs as present in
Autor:
Gerd Krause, Rebecca C. Wade, Ting Wang, Hartmut Oschkinat, Urs Wiedemann, Livia Otte, Karin Schleinkofer
Publikováno v:
Journal of molecular biology. 344(3)
WW domains are small globular protein interaction modules found in a wide spectrum of proteins. They recognize their target proteins by binding specifically to short linear peptide motifs that are often proline-rich. To infer the determinants of the
Autor:
Josef Brock, Jens Schneider-Mergener, Michael Wright, Livia Otte, Thomas Bittorf, Robert Jaster, Tilo Sasse
Publikováno v:
Cellular signalling. 12(11-12)
The transcription factor STAT5 is activated by multiple hematopoietic cytokine receptors and has been implicated in the induction of cellular processes such as differentiation, proliferation and antiapoptotic activities. Here, we report cloning of th
Publikováno v:
Peptides: The Wave of the Future ISBN: 9789401039055
The complexity of peptide conformational space poses a great obstacle for the correct prediction of three-dimensional peptide structures in complex with proteins. We have investigated the predictability of linear and cyclic peptides that were derived
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::63cae80339e819223de991bcd3205412
https://doi.org/10.1007/978-94-010-0464-0_195
https://doi.org/10.1007/978-94-010-0464-0_195