Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Elena Vazquez-Sarandeses"'
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:
Leona Berndt, Elena Vazquez-Sarandeses, Arthur Alves de Melo, Kazuki Teranishi, Ralf Langen, Mark R. Ambroso, Michael Lammers, Daniel Merken, Oliver Daumke, Ian S. Haworth, Joo-Yeun Lee, Alan K Okada, Jose Mario Isas, Karen Chang, Priyatama Pandey
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications
Nature Communications
Lysine acetylation regulates the function of soluble proteins in vivo, yet it remains largely unexplored whether lysine acetylation regulates membrane protein function. Here, we use bioinformatics, biophysical analysis of recombinant proteins, live-c
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