Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Lisa Merklinger"'
Autor:
Lisa Merklinger, Jens Morth
Publikováno v:
Bio-Protocol, Vol 13, Iss 22 (2023)
The lipid bilayers of the cell are composed of various lipid classes and species. These engage in cell signaling and regulation by recruiting cytosolic proteins to the membrane and interacting with membrane-embedded proteins to alternate their activi
Externí odkaz:
https://doaj.org/article/d8d8a14834f347c99616dd600cbb94e3
Autor:
Mattia Deluigi, Lena Morstein, Matthias Schuster, Christoph Klenk, Lisa Merklinger, Riley R. Cridge, Lazarus A. de Zhang, Alexander Klipp, Santiago Vacca, Tasneem M. Vaid, Peer R. E. Mittl, Pascal Egloff, Stefanie A. Eberle, Oliver Zerbe, David K. Chalmers, Daniel J. Scott, Andreas Plückthun
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
This study reports the X-ray structure of the α1B-adrenergic G protein-coupled receptor bound to an inverse agonist, and unveils key determinants of subtype-selective ligand binding that may help the design of aminergic drugs with fewer side-effects
Externí odkaz:
https://doaj.org/article/9eae3c81d8e34aff9e67ac17ad3df5fe
Publikováno v:
Merklinger, L, Bauer, J, Pedersen, P A, Damgaard, R B & Morth, J P 2022, ' Phospholipids alter activity and stability of mitochondrial membrane-bound ubiquitin ligase MARCH5 ', Life Science Alliance, vol. 5, no. 8, e202101309 . https://doi.org/10.26508/lsa.202101309
Mitochondrial homeostasis is tightly controlled by ubiquitination. The mitochondrial integral membrane ubiquitin ligase MARCH5 is a crucial regulator of mitochondrial membrane fission, fusion, and disposal through mitophagy. In addition, the lipid co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9611c052cb58c9188d1dcdd4778dd332
https://curis.ku.dk/portal/da/publications/phospholipids-alter-activity-and-stability-of-mitochondrial-membranebound-ubiquitin-ligase-march5(b659faea-060d-40de-bd4b-1bd9d122937c).html
https://curis.ku.dk/portal/da/publications/phospholipids-alter-activity-and-stability-of-mitochondrial-membranebound-ubiquitin-ligase-march5(b659faea-060d-40de-bd4b-1bd9d122937c).html
Autor:
Mattia, Deluigi, Lena, Morstein, Matthias, Schuster, Christoph, Klenk, Lisa, Merklinger, Riley R, Cridge, Lazarus A, de Zhang, Alexander, Klipp, Santiago, Vacca, Tasneem M, Vaid, Peer R E, Mittl, Pascal, Egloff, Stefanie A, Eberle, Oliver, Zerbe, David K, Chalmers, Daniel J, Scott, Andreas, Plückthun
Publikováno v:
Nature Communications
α-adrenergic receptors (αARs) are G protein-coupled receptors that regulate vital functions of the cardiovascular and nervous systems. The therapeutic potential of αARs, however, is largely unexploited and hampered by the scarcity of subtype-selec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::eed50a140cf35ee5bf914d050863f5f4
https://pubmed.ncbi.nlm.nih.gov/35046410
https://pubmed.ncbi.nlm.nih.gov/35046410
Autor:
Peer R. E. Mittl, Philipp Heine, S.A. Eberle, Santiago Vacca, Lisa Merklinger, Lena Morstein, Pascal Egloff, Mattia Deluigi, Patrick Ernst, Alexander Klipp, Andreas Plückthun, Theodore M. Kamenecka, Yuanjun He, Christoph Klenk, Annemarie Honegger
Publikováno v:
Science Advances
Crystal structures of NTSR1 bound to agonists, inverse agonists, and in the apo state enabled by a novel fusion to DARPin D12.
Neurotensin receptor 1 (NTSR1) and related G protein–coupled receptors of the ghrelin family are clinically unexploi
Neurotensin receptor 1 (NTSR1) and related G protein–coupled receptors of the ghrelin family are clinically unexploi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8377c2e6276b05be462ae72f9c1b9cab
https://doi.org/10.1126/sciadv.abe5504
https://doi.org/10.1126/sciadv.abe5504
Autor:
James Yu, Franz Hagn, Mahmoud L. Nasr, Alan Brown, Lisa Merklinger, Zhen-Yu Sun, Lena Morstein, Zi-Fu Wang, Gerhard Wagner, Hao Wu, Miao Gui, Christoph Klenk, Christoph Gorgulla, Andreas Plückthun, Meng Zhang
Publikováno v:
Nat. Struct. Mol. Biol. 28, 258-267 (2021)
Nat Struct Mol Biol
Nat Struct Mol Biol
G protein coupled receptors (GPCRs) are the largest superfamily of transmembrane proteins and the targets of over 30% of currently marketed pharmaceuticals1,2. Although several structures have been solved for GPCR-G protein complexes3–17, structura
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87e3dfa305bbce4d577593bb87aacee0
https://doi.org/10.21203/rs.3.rs-57572/v1
https://doi.org/10.21203/rs.3.rs-57572/v1