Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Cody S. Freeman"'
Autor:
Mark E. Smolkin, Joseph L. Flanigan, Carol A. Manning, T. Jason Druzgal, Scott A. Sperling, Matthew J. Barrett, Jamie C. Blair, Cody S Freeman
Publikováno v:
Journal of Neurology, Neurosurgery & Psychiatry. 90:1251-1256
ObjectiveA major contributor to dementia in Parkinson disease (PD) is degeneration of the cholinergic basal forebrain. This study determined whether cholinergic nucleus 4 (Ch4) density is associated with cognition in early and more advanced PD.Method
Autor:
Guiying Cui, Chengyu Prince, Taylor L. Knotts, Nael A. McCarty, Cody S. Freeman, Christopher Kuang
Publikováno v:
Journal of Biological Chemistry. 288:20758-20767
Previous studies have identified two salt bridges in human CFTR chloride ion channels, Arg352-Asp993 and Arg347-Asp924, that are required for normal channel function. In the present study, we determined how the two salt bridges cooperate to maintain
Autor:
Robert J. French, Denis McMaster, Christopher H. Thompson, Nael A. McCarty, Matthew D. Fuller, Éva Bakos, Zhi Ren Zhang, Gergely Szakács, Balázs Sarkadi, Julia Kubanek, Eszter Schay, Jan Pohl, Cody S. Freeman
Publikováno v:
Journal of Biological Chemistry. 282:37545-37555
Peptide toxins from animal venom have been used for many years for the identification and study of cation-permeable ion channels. However, no peptide toxins have been identified that interact with known anion-selective channels, including cystic fibr
Autor:
Matthew D. Fuller, Julia Kubanek, Christopher H. Thompson, Jan Pohl, Denis McMaster, Nael A. McCarty, Pedro R. Olivetti, Robert J. French, Cody S. Freeman
The ClC protein family includes voltage-gated chloride channels and chloride/proton exchangers. In eukaryotes, ClC proteins regulate membrane potential of excitable cells, contribute to epithelial transport, and aid in lysosomal acidification. Althou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d63a4ee0679275d6be0af2d3ae789fb1
https://europepmc.org/articles/PMC2758005/
https://europepmc.org/articles/PMC2758005/
Publikováno v:
Biophysical Journal. 96(3)
ClC-2 chloride channels are voltage-gated ion channels that are expressed in neuronal and epithelial cells where they are critical mediators for the passive diffusion of Cl− across the plasma membrane. Although ClC-2 is nearly ubiquitously expresse
Publikováno v:
Biophysical Journal. (3):323a
The pore structure of the CFTR chloride channel is unknown. We showed previously that R352 in TM6 forms a salt bridge with D993 in TM9; charge-destroying mutations at either site destabilized the open state, affecting conductance, selectivity, and po