Zobrazeno 1 - 10
of 94
pro vyhledávání: '"Terence Wagenknecht"'
Publikováno v:
European Journal of Translational Myology, Vol 25, Iss 1, Pp 49-56 (2015)
Cryo-electron tomography (cryo-ET) has emerged as perhaps the only practical technique for revealing nanometer-level three-dimensional structural details of subcellular macromolecular complexes in their native context, inside the cell. As currently p
Externí odkaz:
https://doaj.org/article/f415e8706cb8423da70fbf61e5eeb802
Autor:
Toh-Ming Lu, Rajendra K. Agrawal, Tanvir R. Shaikh, Xing Meng, David Barnard, Terence Wagenknecht, Aymen S. Yassin, Zonghuan Lu
Publikováno v:
Proceedings of the National Academy of Sciences. 111:9822-9827
Association of the two ribosomal subunits during the process of translation initiation is a crucial step of protein synthesis. The two subunits (30S and 50S) of the bacterial 70S ribosome are held together by 12 dynamic bridges involving RNA-RNA, RNA
Publikováno v:
Journal of Structural Biology. 185:32-41
Vitreous freezing offers a way to study cells and tissue in a near-native state by cryo-transmission electron microscopy (cryo-TEM), which is important when structural information at the macromolecular level is required. Many cells -- especially thos
Autor:
Yingjie Liu, Xiaojun Huang, Zheng Liu, Ruiwu Wang, S. R. Wayne Chen, Xiaowei Zhong, Ying Liu, Terence Wagenknecht, Andrea Koop
Publikováno v:
Journal of Cell Science. 126:4527-4535
Summary Calmodulin (CaM), a 16 kDa ubiquitous calcium-sensing protein, is known to bind tightly to the calcium release channel/ryanodine receptor (RyR), and modulate RyR function. CaM binding studies using RyR fragments or synthetic peptides have rev
Autor:
Ying Liu, Terence Wagenknecht, Xixi Tian, Yingjie Liu, Zheng Liu, S. R. Wayne Chen, Ruiwu Wang
Publikováno v:
Journal of Biological Chemistry. 288:4066-4075
Global conformational changes in the three-dimensional structure of the Ca(2+) release channel/ryanodine receptor (RyR) occur upon ligand activation. A number of ligands are able to activate the RyR channel, but whether these structurally diverse lig
Publikováno v:
Journal of Biological Chemistry. 287:30328-30335
Ryanodine receptor types 1 (RyR1) and 2 (RyR2) are calcium release channels that are highly enriched in skeletal and cardiac muscle, respectively, where they play an essential role in excitation-contraction coupling. Apocalmodulin (apo-CaM) weakly ac
Autor:
Terence Wagenknecht, Zheng Liu, Xixi Tian, Xiaowei Zhong, Jaya Gangopadhyay, Ruiwu Wang, Richard W. Cole, S.R. Wayne Chen, Noriaki Ikemoto
Publikováno v:
Journal of Cell Science. 123:1775-1784
Naturally occurring mutations in the cardiac ryanodine receptor (RyR2) have been linked to certain types of cardiac arrhythmias and sudden death. Two mutation hotspots that lie in the N-terminal and central regions of RyR2 are predicted to interact w
Autor:
Toh-Ming Lu, Aymen S. Yassin, Rajendra K. Agrawal, Terence Wagenknecht, Carmen A. Mannella, David Barnard, Hisham Mohamed, Xing Meng, Zonghuan Lu, Tanvir R. Shaikh
Publikováno v:
Journal of Structural Biology. 168:388-395
The goal of time-resolved cryo-electron microscopy is to determine structural models for transient functional states of large macromolecular complexes such as ribosomes and viruses. The challenge of time-resolved cryo-electron microscopy is to rapidl
Autor:
Peter P. Jones, Zheng Liu, Shitian Cai, Bailong Xiao, Terence Wagenknecht, Xing Meng, S. R. Wayne Chen, Jeff Bolstad
Publikováno v:
Biochemical Journal. 410:261-270
PKA (protein kinase A)-dependent phosphorylation of the cardiac Ca 2+ -release channel/RyR2 (type 2 ryanodine receptor) is believed to directly dissociate FKBP12.6 (12.6 kDa FK506-binding protein) from the channel, causing abnormal channel activation
Autor:
Xiaojun Huang, Xing Meng, Zheng Liu, Fei Li, Shitian Cai, Judith A. Airey, Ramon Trujillo, Jeff Bolstad, Bailong Xiao, S.R. Wayne Chen, Terence Wagenknecht
Publikováno v:
Journal of Biological Chemistry. 282:25929-25939
Type 2 ryanodine receptor (RyR2) is the major calcium release channel in cardiac muscle. Phosphorylation of RyR2 by cAMP-dependent protein kinase A and by calmodulin-dependent protein kinase II modulates channel activity. Hyperphosphorylation at a si