Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Urs Wiedemann"'
Publikováno v:
Molecular Endocrinology. 21:574-580
Comparison between wild-type and mutated glycoprotein hormone receptors (GPHRs), TSH receptor, FSH receptor, and LH-chorionic gonadotropin receptor is established to identify determinants involved in molecular activation mechanism. The basic aims of
Autor:
Urs Wiedemann, Prisca Boisguerin, Gerd Krause, Dietmar Leitner, Rainer Leben, Karin Moelling, Rudolf Volkmer-Engert, Hartmut Oschkinat
Publikováno v:
Journal of Molecular Biology. 343:703-718
Transient macromolecular complexes are often formed by protein-protein interaction domains (e.g. PDZ, SH2, SH3, WW) which recognize linear sequence motifs with in vitro affinities typically in the micromolar range. The analysis of the resulting inter
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
Publikováno v:
Proceedings of the National Academy of Sciences. 99:11405-11410
The VirB/D4 type IV secretion system of Agrobacterium tumefaciens translocates virulence factors (VirE2, VirF, and the VirD2-T-DNA complex) to plant cells. The membrane-bound translocation machinery consists of 12 proteins (VirB1–11 and VirD4) requ
Publikováno v:
Protein Science Encyclopedia ISBN: 3527610758
Protein Science Encyclopedia
Protein Science Encyclopedia
Originally published in: Modular Protein Domains. Edited by Giovanni Cesareni, Mario Gimona, Marius Sudol and Michael Yaffe. Copyright © 2005 Wiley-VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3-527-30813-2 The sections in this article are Intro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a21bb344bb9c592411efeeaaffdb059
https://doi.org/10.1002/9783527610754.pp06
https://doi.org/10.1002/9783527610754.pp06
Autor:
Federico Antinori, Urs Wiedemann
Publikováno v:
Journal of Physics G: Nuclear and Particle Physics. 32
Autor:
Dietmar Leitner, Peter Schmieder, Anne Diehl, Dirk Labudde, Martin Wahl, José R. Pires, Michele Fossi, Martina Leidert, Urs Wiedemann, Gerd Krause, Hartmut Oschkinat
Publikováno v:
FEBS letters. 579(17)
Phox and Bem1 (PB1) domains mediate protein-pro- tein interactions via the formation of homo- or hetero-dimers. The C-terminal PB1 domain of yeast cell division cycle 24 (CDC24p), a guanine-nucleotide exchange factor involved in cell polarity establi
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