Zobrazeno 1 - 10
of 51
pro vyhledávání: '"M, Federwisch"'
Autor:
Jörg Köhl, Wilfried Bautsch, Andreas Klos, T. Melcher, M. Federwisch, Monica Emde, Axel Wollmer, T. Stühmer
Publikováno v:
Biophysical Chemistry. 46:237-248
Three mutants of the anaphylatoxin C5a were prepared with positions 2, 64 and 70, respectively, substituted by tryptophan. The last mutant was additionally labelled at Cys27 for fluorescence energy transfer (FET) measurements. The structural integrit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::678e464aaf1fab7c8a913d55a1e5d5f7
https://doi.org/10.1016/0301-4622(93)80017-d
https://doi.org/10.1016/0301-4622(93)80017-d
Publikováno v:
Insulin & Related Proteins-Structure to Function and Pharmacology ISBN: 9781402006555
The association/dissociation behaviour in the presence of co-ordinating metal ions and T-R transforming ligands is too complex for rigorous analysis. In the present study equimolar mixtures of insulin labelled with a fluorescence donor and with an ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c8071c14f8256738d82b3741e0270074
https://doi.org/10.1007/0-306-47582-0_4
https://doi.org/10.1007/0-306-47582-0_4
Autor:
R R, Flörke, K, Schnaith, W, Passlack, M, Wichert, L, Kuehn, M, Fabry, M, Federwisch, H, Reinauer
Publikováno v:
The Biochemical journal. 360(Pt 1)
Interaction between two alphabeta half-receptors within the (alphabeta)(2) holoreceptor complex is required for insulin binding with high affinity and for insulin-triggered changes of size and shape. To understand the underlying structure-function re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::475d8dd5f466e3ea87de52ac7d7c2f54
https://pubmed.ncbi.nlm.nih.gov/11696007
https://pubmed.ncbi.nlm.nih.gov/11696007
Autor:
K, Schleinkofer, A, Dingley, I, Tacken, M, Federwisch, G, Müller-Newen, P C, Heinrich, P, Vusio, Y, Jacques, J, Grötzinger
Publikováno v:
Journal of molecular biology. 306(2)
The interleukin-11 receptor (IL-11R) belongs to the hematopoietic receptor superfamily. The functional receptor complex comprises IL-11, IL-11R and the signal-transducing subunit gp130. The extracellular part of the IL-11R consists of three domains:
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1e36acd4423436cf0ebdd229b39590e7
https://pubmed.ncbi.nlm.nih.gov/11237599
https://pubmed.ncbi.nlm.nih.gov/11237599
Autor:
G, De Wilde, J, Murray-Rust, E, Boone, D, Olerenshaw, N Q, McDonald, C, Ibanez, G, Haegeman, A, Wollmer, M, Federwisch
Publikováno v:
European journal of biochemistry. 268(5)
Upon stimulation with tumor necrosis factor (TNF), the TNF receptor (TNFR55) mediates a multitude of effects both in normal and in tumor cells. Clustering of the intracellular domain of the receptor, the so-called death domain (DD), is responsible fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a739b7ec493767e407075ee3e30b8162
https://pubmed.ncbi.nlm.nih.gov/11231290
https://pubmed.ncbi.nlm.nih.gov/11231290
Publikováno v:
Journal of molecular biology. 302(1)
FADD (also known as MORT-1) is an essential adapter protein that couples the transmembrane receptors Fas (CD95) and tumor necrosis factor receptor-1 (TNF-R1) to intracellular cysteine proteases known as caspases, which propagate and execute the progr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a1158076b8faea33c9918abb44988555
https://pubmed.ncbi.nlm.nih.gov/10964568
https://pubmed.ncbi.nlm.nih.gov/10964568
Autor:
Brandenburg D, Hans-Gregor Gattner, V.J. Lenz, U Hassiepen, Axel Wollmer, M Federwisch, Hartwig Höcker
Publikováno v:
Biochemistry. 34(18)
Insulin is a proteohormone with amphipathic three-dimensional structure and the ligand of a receptor, which itself spans the plasma membrane of glucose-metabolizing cells. In this study, the possible impact of amphiphiles on structural and dynamic pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bed4f804e1cb6677d0407019bb325640
https://pubmed.ncbi.nlm.nih.gov/7742317
https://pubmed.ncbi.nlm.nih.gov/7742317
Publikováno v:
The Journal of biological chemistry. 267(32)
To provide an experimental system amenable to a detailed biochemical and structural investigation of the extracellular (ligand binding) domain of the insulin receptor, we developed a mammalian heterologous cell expression system from which tens of mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bba16ea3517491cf2101f0e9e73a094a
https://pubmed.ncbi.nlm.nih.gov/1385419
https://pubmed.ncbi.nlm.nih.gov/1385419
Publikováno v:
Biophysical chemistry. 44(3)
The biological activity of oligopeptide analogues of C3a is markedly increased by N-terminal attachment of a hydrophobic group as, for instance, 9-fluorenylmethoxycarbonyl (Fmoc), either direct or via a flexible 6-aminohexanoyl (Ahx) spacer. This stu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ef00b298d1213bb9f6dd665172f37d6
https://pubmed.ncbi.nlm.nih.gov/1420945
https://pubmed.ncbi.nlm.nih.gov/1420945
Autor:
M D, Waterfield, C, Greenfield, I, Hiles, M, Federwisch, A, Wollmer, T L, Blundell, N, McDonald
Publikováno v:
Advances in second messenger and phosphoprotein research. 24
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a285210d31a2b86546a655ffe175fb09
https://pubmed.ncbi.nlm.nih.gov/2119642
https://pubmed.ncbi.nlm.nih.gov/2119642