Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Carla Glasser"'
Publikováno v:
eLife, Vol 6 (2017)
Ion conductivity and the gating characteristics of tetrameric glutamate receptor ion channels are determined by their subunit composition. Competitive homo- and hetero-dimerization of their amino-terminal domains (ATDs) is a key step controlling asse
Externí odkaz:
https://doaj.org/article/78527d336bf84b1d96eea10e51153c51
Autor:
Huaying Zhao, Yan Fu, Carla Glasser, Eric J Andrade Alba, Mark L Mayer, George Patterson, Peter Schuck
Publikováno v:
eLife, Vol 5 (2016)
The dynamic assembly of multi-protein complexes underlies fundamental processes in cell biology. A mechanistic understanding of assemblies requires accurate measurement of their stoichiometry, affinity and cooperativity, and frequently consideration
Externí odkaz:
https://doaj.org/article/07db3e12ea6b4d9d81a7cec3f59ba488
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e83439 (2013)
Sedimentation velocity analytical ultracentrifugation (SV) is a powerful first-principle technique for the study of protein interactions, and allows a rigorous characterization of binding stoichiometry and affinities. A recently introduced commercial
Externí odkaz:
https://doaj.org/article/8d8b5c9d28d84b0fbfb21f9efbd19110
Publikováno v:
eLife
eLife, Vol 6 (2017)
eLife, Vol 6 (2017)
Ion conductivity and the gating characteristics of tetrameric glutamate receptor ion channels are determined by their subunit composition. Competitive homo- and hetero-dimerization of their amino-terminal domains (ATDs) is a key step controlling asse
Autor:
Yan Fu, Mark L. Mayer, Peter Schuck, Eric J Andrade Alba, Carla Glasser, George H. Patterson, Huaying Zhao
Publikováno v:
eLife
eLife, Vol 5 (2016)
eLife, Vol 5 (2016)
The dynamic assembly of multi-protein complexes underlies fundamental processes in cell biology. A mechanistic understanding of assemblies requires accurate measurement of their stoichiometry, affinity and cooperativity, and frequently consideration
Publikováno v:
Biophysical Journal. 114:126a
Publikováno v:
The Journal of General Physiology
The pores of glutamate receptors and K+ channels share sequence homology, suggesting a conserved secondary structure. Scanning mutagenesis with substitution of alanine and tryptophan in GluR6 channels was performed based on the structure of KcsA. Our
1. The effect on polyamine block of mutations at the Q/R site and the conserved negative charge +4 site in AMPA and kainate receptors was studied using the rat glutamate receptor GluR6 expressed in Xenopus oocytes and human embryonic kidney (HEK) cel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94ef015183e956168b0b87306ac8a85f
https://europepmc.org/articles/PMC2269595/
https://europepmc.org/articles/PMC2269595/