Ion channel modulation as a drug discovery target in inflammatory diseases

1996 ◽  
Vol 45 (9) ◽  
pp. 435-437 ◽  
Author(s):  
D. C. Hanson ◽  
K. Koch
Keyword(s):  
Drug Discovery ◽  
Ion Channel ◽  
Inflammatory Diseases ◽  
Channel Modulation ◽  
Ion Channel Modulation ◽  
Drug Discovery Target

Ion Channel Modulation as a Therapeutic Approach in Multiple Sclerosis

2015 ◽  
Vol 22 (38) ◽  
pp. 4366-4378 ◽  
Author(s):  
R. Arnold ◽  
W. Huynh ◽  
M.C. Kiernan ◽  
A.V. Krishnan
Keyword(s):  
Multiple Sclerosis ◽  
Ion Channel ◽  
Therapeutic Approach ◽  
Channel Modulation ◽  
Ion Channel Modulation

FV-009 candidate drug: Novel and selective P/Q-type Ca2+ and voltage-gated Na+ ion channel modulation for epilepsy and pain

2015 ◽  
Vol 46 ◽  
pp. 57
Author(s):  
Malik Slassi ◽  
Peter Dove ◽  
Shane Climie ◽  
David O'Neill ◽  
Zezhou Wang ◽  
...  
Keyword(s):  
Ion Channel ◽  
Channel Modulation ◽  
Voltage Gated ◽  
Candidate Drug ◽  
Ion Channel Modulation

Structures of the AMPA receptor in complex with its auxiliary subunit cornichon

Science ◽  
2019 ◽  
Vol 366 (6470) ◽  
pp. 1259-1263 ◽  
Author(s):  
Terunaga Nakagawa
Keyword(s):  
Ion Channel ◽  
Membrane Topology ◽  
Auxiliary Subunits ◽  
Channel Modulation ◽  
Protein Protein Interaction ◽  
Cryo Electron Microscopy ◽  
Ion Channel Modulation ◽  
Interaction Interface ◽  
Excitatory Neurotransmission ◽  
Membrane Spanning

In the brain, AMPA-type glutamate receptors (AMPARs) form complexes with their auxiliary subunits and mediate the majority of fast excitatory neurotransmission. Signals transduced by these complexes are critical for synaptic plasticity, learning, and memory. The two major categories of AMPAR auxiliary subunits are transmembrane AMPAR regulatory proteins (TARPs) and cornichon homologs (CNIHs); these subunits share little homology and play distinct roles in controlling ion channel gating and trafficking of AMPAR. Here, I report high-resolution cryo–electron microscopy structures of AMPAR in complex with CNIH3. Contrary to its predicted membrane topology, CNIH3 lacks an extracellular domain and instead contains four membrane-spanning helices. The protein-protein interaction interface that dictates channel modulation and the lipids surrounding the complex are revealed. These structures provide insights into the molecular mechanism for ion channel modulation and assembly of AMPAR/CNIH3 complexes.

scholarly journals Towards understanding the molecular basis of ion channel modulation by lipids: Mechanistic models and current paradigms

2017 ◽  
Vol 1859 (9) ◽  
pp. 1507-1516 ◽  
Author(s):  
José A. Poveda ◽  
A. Marcela Giudici ◽  
M. Lourdes Renart ◽  
Andrés Morales ◽  
José M. González-Ros
Keyword(s):  
Ion Channel ◽  
Molecular Basis ◽  
Mechanistic Models ◽  
Channel Modulation ◽  
Ion Channel Modulation

scholarly journals Ion Channel Modulation in Spinal/Trigeminal Synaptic Plasticity

2014 ◽  
Vol 2014 ◽  
pp. 1-3
Author(s):  
Dong-ho Youn ◽  
Gábor Gerber ◽  
William A. Sather
Keyword(s):  
Synaptic Plasticity ◽  
Ion Channel ◽  
Channel Modulation ◽  
Ion Channel Modulation
Sign in / Sign up

Export Citation Format

Share Document