Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Kathrin Motzny"'
Autor:
Samuel Naudi-Fabra, Carlos A. Elena-Real, Ida Marie Vedel, Maud Tengo, Kathrin Motzny, Pin-Lian Jiang, Peter Schmieder, Fan Liu, Sigrid Milles
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract The early phases of clathrin mediated endocytosis are organized through a highly complex interaction network mediated by clathrin associated sorting proteins (CLASPs) that comprise long intrinsically disordered regions (IDRs). AP180 is a CLA
Externí odkaz:
https://doaj.org/article/0a7886336eb3462eb8da4dd6206dfce4
Autor:
Jiang Ren, Judith Bruns, Peter Lindemann, Kathrin Motzny, Ronald Kühne, Slim Chiha, Matthias M. Müller, Monika Beerbaum, Robert Opitz, Stephan Dohmen, Matthias Barone, Arne Soicke, Marco Tobias Klein, Dominik Albat, Peter Schmieder, Udo Heinemann, Hartmut Oschkinat, Yvette Roske, Marc Nazaré, Hans-Günther Schmalz, Peter ten Dijke, Rudolf Volkmer, Maarten van Dinther
Publikováno v:
Proceedings of the National Academy of Sciences, 117(47), 29684-29690. NATL ACAD SCIENCES
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America
Significance Protein–protein interactions mediated by proline-rich motifs are involved in regulation of many important signaling cascades. These motifs belong to the most abundant recognition motifs in the eukaryotic genome and preferentially adopt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f3f020fdbbb67aa9a4b024f1290a866
https://hdl.handle.net/1887/3185199
https://hdl.handle.net/1887/3185199
Publikováno v:
Molecularcellular proteomics : MCP. 4(11)
GYF domains are conserved eukaryotic adaptor domains that recognize proline-rich sequences. Although the structure and function of the prototypic GYF domain from the human CD2BP2 protein have been characterized in detail, very little is known about G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ee88d5555ad5099a3e6595e29462cbb
https://pubmed.ncbi.nlm.nih.gov/16120600
https://pubmed.ncbi.nlm.nih.gov/16120600
Publikováno v:
The Journal of biological chemistry. 280(39)
The GYF domain of CD2BP2 serves as an adapter that recognizes proline-rich sequences in intracellular proteins. Although the T cell adhesion molecule CD2 and the core splicing protein SmB/B' were previously shown to interact with CD2BP2-GYF, we are n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c99c0d314e05930a42f5a88101b8f7fa
https://pubmed.ncbi.nlm.nih.gov/16000308
https://pubmed.ncbi.nlm.nih.gov/16000308