Glutamate receptor ion channels: structure, regulation, and function
The mammalian ionotropic glutamate receptor family encodes 18 gene products that
coassemble to form ligand-gated ion channels containing an agonist recognition site, a …
coassemble to form ligand-gated ion channels containing an agonist recognition site, a …
MMPs in learning and memory and neuropsychiatric disorders
Matrix metalloproteinases (MMPs) are a group of over twenty proteases, operating chiefly
extracellularly to cleave components of the extracellular matrix, cell adhesion molecules as …
extracellularly to cleave components of the extracellular matrix, cell adhesion molecules as …
Synaptic circuit remodelling by matrix metalloproteinases in health and disease
GW Huntley - Nature Reviews Neuroscience, 2012 - nature.com
Matrix metalloproteinases (MMPs) are extracellularly acting enzymes that have long been
known to have deleterious roles in brain injury and disease. In particular, widespread and …
known to have deleterious roles in brain injury and disease. In particular, widespread and …
Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases
B Cauwe, G Opdenakker - Critical reviews in biochemistry and …, 2010 - Taylor & Francis
Matrix metalloproteinases (MMPs), originally discovered to function in the breakdown of
extracellular matrix proteins, have gained the status of regulatory proteases in signaling …
extracellular matrix proteins, have gained the status of regulatory proteases in signaling …
Matrix metalloproteinase-9 controls NMDA receptor surface diffusion through integrin β1 signaling
P Michaluk, L Mikasova, L Groc… - Journal of …, 2009 - Soc Neuroscience
Matrix metalloproteinase-9 (MMP-9) has emerged as a physiological regulator of NMDA
receptor (NMDAR)-dependent synaptic plasticity and memory. The pathways by which MMP …
receptor (NMDAR)-dependent synaptic plasticity and memory. The pathways by which MMP …
The human ether-a-go-go-related gene (hERG) potassium channel represents an unusual target for protease-mediated damage
SM Lamothe, J Guo, W Li, T Yang, S Zhang - Journal of Biological …, 2016 - ASBMB
The human ether-a-go-go-related gene (hERG) encodes the pore-forming subunit of the
rapidly activating delayed rectifier potassium channel (I Kr), which is important for cardiac …
rapidly activating delayed rectifier potassium channel (I Kr), which is important for cardiac …
Matrix metalloproteases as influencers of the cells' social media
Matrix metalloproteinases (MMPs) have been studied in the context of cancer due to their
ability to increase cell invasion, and were initially thought to facilitate metastasis solely …
ability to increase cell invasion, and were initially thought to facilitate metastasis solely …
Matrix metalloproteinase-dependent shedding of intercellular adhesion molecule-5 occurs with long-term potentiation
K Conant, Y Wang, A Szklarczyk, A Dudak, MP Mattson… - Neuroscience, 2010 - Elsevier
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that can
be released or activated in a neuronal activity dependent manner. Although pathologically …
be released or activated in a neuronal activity dependent manner. Although pathologically …
Extracellular metalloproteinases in the plasticity of excitatory and inhibitory synapses
G Wiera, JW Mozrzymas - Cells, 2021 - mdpi.com
Long-term synaptic plasticity is shaped by the controlled reorganization of the synaptic
proteome. A key component of this process is local proteolysis performed by the family of …
proteome. A key component of this process is local proteolysis performed by the family of …
Matrix metalloproteinases regulate the formation of dendritic spine head protrusions during chemically induced long-term potentiation
Dendritic spines are are small membranous protrusions that extend from neuronal dendrites
and harbor the majority of excitatory synapses. Increasing evidence has shown that matrix …
and harbor the majority of excitatory synapses. Increasing evidence has shown that matrix …