Noncanonical thyroid hormone signaling mediates cardiometabolic effects in vivo

Autor: Lars C. Moeller, Sören Latteyer, Janina Gassen, Lars Grøntved, Xiao Hui Liao, David L. Armstrong, Martin Hrabé de Angelis, Graham R. Williams, Eddy Rijntjes, Majken S. Siersbæk, J. H. Duncan Bassett, Karl Heinz Strucksberg, Helena Rakov, Dagmar Führer, Petra Kleinbongard, Kathrin Engels, John G. Logan, Eugenie Werbenko, Josef Köhrle, Jan Rozman, Andrea S. Pollard, Samuel Refetoff, Ludger Klein-Hitpass, Denise Zwanziger, Valerie Gailus-Durner, G. Sebastian Hönes, Helmut Fuchs, Stine M. Præstholm

Publikováno v: Proc. Natl. Acad. Sci. U.S.A. 114, E11323-E11332 (2017)
E11332
E11323
Hönes, G S, Rakov, H, Logan, J, Liao, X H, Werbenko, E, Pollard, A S, Præstholm, S M, Siersbæk, M S, Rijntjes, E, Gassen, J, Latteyer, S, Engels, K, Strucksberg, K H, Kleinbongard, P, Zwanziger, D, Rozman, J, Gailus-Durner, V, Fuchs, H, De Angelis, M H, Klein-Hitpass, L, Köhrle, J, Armstrong, D L, Grøntved, L, Bassett, J H D, Williams, G R, Refetoff, S, Führer, D & Moeller, L C 2017, ' Noncanonical thyroid hormone signaling mediates cardiometabolic effects in vivo ', Proceedings of the National Academy of Sciences of the United States of America, vol. 114, no. 52, pp. E11323-E11332 . https://doi.org/10.1073/pnas.1706801115

Thyroid hormone (TH) and TH receptors (TRs) α and β act by binding to TH response elements (TREs) in regulatory regions of target genes. This nuclear signaling is established as the canonical or type 1 pathway for TH action. Nevertheless, TRs also

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8feff2a52973e4132443bd02c28c6438
https://pubmed.ncbi.nlm.nih.gov/29229863

Protein phosphatase 5 protects neurons against amyloid-β toxicity

Autor: Efrain Sanchez-Ortiz, Byoung Kwon Hahm, David L. Armstrong, Sandra Rossie

Publikováno v: Journal of Neurochemistry. 111:391-402

Amyloid-beta (Abeta) is thought to promote neuronal cell loss in Alzheimer's disease, in part through the generation of reactive oxygen species (ROS) and subsequent activation of mitogen-activated protein kinase (MAPK) pathways. Protein phosphatase 5

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f58d5232dd52f062b9bffd86000590d
https://doi.org/10.1111/j.1471-4159.2009.06337.x

Orai proteins interact with TRPC channels and confer responsiveness to store depletion

Autor: Eda Yildirim, Christian Erxleben, Lutz Birnbaumer, Joel Abramowitz, Yanhong Liao, David L. Armstrong

Publikováno v: Proceedings of the National Academy of Sciences. 104:4682-4687

The TRPC (C-type transient receptor potential) class of ion channels has been hypothesized to participate in store-operated Ca 2+ entry (SOCE). Recently, however, STIM1 and Orai1 proteins have been proposed to form SOCE channels. Whether TRPCs partic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40bde2dfd0829fef5da518d7ad98db77
https://doi.org/10.1073/pnas.0611692104

Cyclosporin and Timothy syndrome increase mode 2 gating of CaV1.2 calcium channels through aberrant phosphorylation of S6 helices

Autor: Saverio Gentile, Claudio Gómez-Alegría, David T. Chin, Christian Erxleben, David L. Armstrong, Lutz Birnbaumer, Yanhong Liao, Yasuo Mori

Publikováno v: Proceedings of the National Academy of Sciences. 103:3932-3937

Calcium channels in the plasma membrane rarely remain open for much more than a millisecond at any one time, which avoids raising intracellular calcium to toxic levels. However, the dihydropyridine-sensitive calcium channels of the CaV1 family, which

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a56a91ded87771f6c046f75e66bc2e29
https://doi.org/10.1073/pnas.0511322103

Leucine Zipper Domain Targets cAMP-dependent Protein Kinase to Mammalian BK Channels

Autor: Lijun Tian, David L. Armstrong, Lorraine S. Coghill, Michael J. Shipston, Stephen H.-F. MacDonald

Publikováno v: Journal of Biological Chemistry. 278:8669-8677

Large conductance, calcium- and voltage-activated potassium (BK) channels control excitability in many tissues and are regulated by several protein kinases and phosphatases that remain associated with the channels in cell-free patches of membrane. He

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46582c9a968abdd2fa6009360a84799c
https://doi.org/10.1074/jbc.m211661200