ReviewNeurochemical research2008
Modulation by clamping: Kv4 and KChIP interactions.
Review in Neurochemical research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Review
- Inducing IJournal of molecular and cellular cardiology · 2022Article
- Transcriptomes of electrophysiologically recorded Dbx1-derived respiratory neurons of the preBötzinger complex in neonatal mice.Scientific reports · 2022Article
- Article
- β Subunits Functionally Differentiate Human Kv4.3 Potassium Channel Splice Variants.Frontiers in physiology · 2017Article
- β Subunits Control the Effects of Human Kv4.3 Potassium Channel Phosphorylation.Frontiers in physiology · 2017Article
- The stoichiometry and biophysical properties of the Kv4 potassium channel complex with K+ channel-interacting protein (KChIP) subunits are variable, depending on the relative expression level.The Journal of biological chemistry · 2014Article
- Auxiliary KChIP4a suppresses A-type K+ current through endoplasmic reticulum (ER) retention and promoting closed-state inactivation of Kv4 channels.The Journal of biological chemistry · 2013Article
- Contribution of the γ-secretase subunits to the formation of catalytic pore of presenilin 1 protein.The Journal of biological chemistry · 2012Article
- Negative modulation of NMDA receptor channel function by DREAM/calsenilin/KChIP3 provides neuroprotection?Frontiers in molecular neuroscience · 2012Article
- Interactions of the proteins of neuronal ceroid lipofuscinosis: clues to function.Cellular and molecular life sciences : CMLS · 2011Review
- Expression and distribution of Kv4 potassium channel subunits and potassium channel interacting proteins in subpopulations of interneurons in the basolateral amygdala.Neuroscience · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rapidly inactivating (A-type) potassium channels regulate membrane excitability that defines the fundamental mechanism of neuronal functions such as pain signaling. Cytosolic Kv channel-interacting proteins KChIPs that belong to neuronal calcium sensor (NCS) family of calcium binding EF-hand proteins co-assemble with Kv4 (Shal) alpha subunits to form a native complex that encodes major components of neuronal somatodendritic A-type K+ current, I(SA), in neurons and transient outward current, I(TO), in cardiac myocytes. The specific binding of auxiliary KChIPs to the Kv4 N-terminus results in modulation of gating properties, surface expression and subunit assembly of Kv4 channels. Here, I attempt to emphasize the interaction between KChIPs and Kv4 based on recent progress made in understanding the structure complex in which a single KChIP1 molecule laterally clamps two neighboring Kv4.3 N-termini in a 4:4 manner. Greater insights into molecular mechanism between KChIPs and Kv4 interaction may provide therapeutic potentials of designing compounds aimed at disrupting the protein-protein interaction for treatment of membrane excitability-related disorders.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.