Zobrazeno 1 - 10
of 110
pro vyhledávání: '"Oliver, Daumke"'
Autor:
Trendelina Rrustemi, Katrina Meyer, Yvette Roske, Bora Uyar, Altuna Akalin, Koshi Imami, Yasushi Ishihama, Oliver Daumke, Matthias Selbach
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024)
Abstract Despite their lack of a defined 3D structure, intrinsically disordered regions (IDRs) of proteins play important biological roles. Many IDRs contain short linear motifs (SLiMs) that mediate protein-protein interactions (PPIs), which can be r
Externí odkaz:
https://doaj.org/article/36c66039d80545849583a72a85603f51
Autor:
Nikolai Schleussner, Pierre Cauchy, Vedran Franke, Maciej Giefing, Oriol Fornes, Naveen Vankadari, Salam A. Assi, Mariantonia Costanza, Marc A. Weniger, Altuna Akalin, Ioannis Anagnostopoulos, Thomas Bukur, Marco G. Casarotto, Frederik Damm, Oliver Daumke, Benjamin Edginton-White, J. Christof M. Gebhardt, Michael Grau, Stephan Grunwald, Martin-Leo Hansmann, Sylvia Hartmann, Lionel Huber, Eva Kärgel, Simone Lusatis, Daniel Noerenberg, Nadine Obier, Ulrich Pannicke, Anja Fischer, Anja Reisser, Andreas Rosenwald, Klaus Schwarz, Srinivasan Sundararaj, Andre Weilemann, Wiebke Winkler, Wendan Xu, Georg Lenz, Klaus Rajewsky, Wyeth W. Wasserman, Peter N. Cockerill, Claus Scheidereit, Reiner Siebert, Ralf Küppers, Rudolf Grosschedl, Martin Janz, Constanze Bonifer, Stephan Mathas
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-18 (2023)
Abstract Disease-causing mutations in genes encoding transcription factors (TFs) can affect TF interactions with their cognate DNA-binding motifs. Whether and how TF mutations impact upon the binding to TF composite elements (CE) and the interaction
Externí odkaz:
https://doaj.org/article/89617bbfc2d9437a8c22b2474e5ec08c
Autor:
Saif Mohd, Andreas Oder, Edgar Specker, Martin Neuenschwander, Jens Peter Von Kries, Oliver Daumke
Publikováno v:
PLoS ONE, Vol 19, Iss 7, p e0302704 (2024)
Eps15 (epidermal growth factor receptor pathway substrate 15) homology domain-containing proteins (EHDs) comprise a family of eukaryotic dynamin-related ATPases that participate in various endocytic membrane trafficking pathways. Dysregulation of EHD
Externí odkaz:
https://doaj.org/article/bc1fb18899bc4379a14d127bddc963a0
Autor:
Arthur A. Melo, Thiemo Sprink, Jeffrey K. Noel, Elena Vázquez-Sarandeses, Chris van Hoorn, Saif Mohd, Justus Loerke, Christian M. T. Spahn, Oliver Daumke
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
Eps15-homology domain containing proteins comprise a family of dynamin-related ATPases. Here, Melo et al. use cryo-electron tomography to determine the membrane-bound EHD4 structure, therefore clarifying the membrane binding and oligomerization mode.
Externí odkaz:
https://doaj.org/article/90f05469303e46aabea102fe1018d3c7
Autor:
Alan K. Okada, Kazuki Teranishi, Mark R. Ambroso, Jose Mario Isas, Elena Vazquez-Sarandeses, Joo-Yeun Lee, Arthur Alves Melo, Priyatama Pandey, Daniel Merken, Leona Berndt, Michael Lammers, Oliver Daumke, Karen Chang, Ian S. Haworth, Ralf Langen
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Lysine acetylation regulates the function of soluble proteins in vivo, yet it remains largely unexplored whether lysine acetylation regulates the function of membrane proteins. Here, the authors map lysine acetylation predominantly in membrane-intera
Externí odkaz:
https://doaj.org/article/969a6247f4f548d799fa269799855a27
Autor:
Stephan Grunwald, Linus V. M. Hopf, Tobias Bock-Bierbaum, Ciara C. M. Lally, Christian M. T. Spahn, Oliver Daumke
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
The conserved eukaryotic heterotrimeric NatC complex co-translationally acetylates the N-termini of numerous target proteins. Here, the authors provide insights into the catalytic mechanism of NatC by determining the crystal structures of Saccharomyc
Externí odkaz:
https://doaj.org/article/600264e4d8b44389bdb8c8442cd3c649
Autor:
Ilka Wilhelmi, Stephan Grunwald, Niclas Gimber, Oliver Popp, Gunnar Dittmar, Anup Arumughan, Erich E. Wanker, Thomas Laeger, Jan Schmoranzer, Oliver Daumke, Annette Schürmann
Publikováno v:
Molecular Metabolism, Vol 45, Iss , Pp 101151- (2021)
Objective: Hormone secretion from metabolically active tissues, such as pancreatic islets, is governed by specific and highly regulated signaling pathways. Defects in insulin secretion are among the major causes of diabetes. The molecular mechanisms
Externí odkaz:
https://doaj.org/article/1448fb0556da4f3e9a968b2dfe04626d
Publikováno v:
Cell Reports, Vol 31, Iss 7, Pp - (2020)
Summary: Human guanylate binding protein 1 (hGBP1) belongs to the dynamin superfamily of GTPases and conveys host defense against intracellular bacteria and parasites. During infection, hGBP1 is recruited to pathogen-containing vacuoles, such as Chla
Externí odkaz:
https://doaj.org/article/7380fbad5d71493faa5a410fa2e30574
Autor:
Manuel Hessenberger, Ralf M. Zerbes, Heike Rampelt, Séverine Kunz, Audrey H. Xavier, Bettina Purfürst, Hauke Lilie, Nikolaus Pfanner, Martin van der Laan, Oliver Daumke
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
The MICOS complex has an essential role in crista junction formation and mitochondrial inner membrane morphology. Here, the authors show that one of its components, Mic60, known to form contact sites between inner and outer membranes, also displays m
Externí odkaz:
https://doaj.org/article/7b4425f4e601401a96034bbaf18029f4
Publikováno v:
Frontiers in Medicine, Vol 6 (2019)
Caveolae, flask-shaped cholesterol-, and glycosphingolipid-rich membrane microdomains, contain caveolin 1, 2, 3 and several structural proteins, in particular Cavin 1–4, EHD2, pacsin2, and dynamin 2. Caveolae participate in several physiological pr
Externí odkaz:
https://doaj.org/article/53bd258f886645a6bbca46dd23965a8a